Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 20:49, 17 November 2007 (UTC)[edit]
Proteins without matches (12)[edit]
Proteins with a High Potential Match (7)[edit]
Redirected Proteins (6)[edit]
Manual Inspection (Page not found) (19)[edit]
Updated (6)[edit]
Protein Status Grid - Date: 20:49, 17 November 2007 (UTC)[edit]
Vebose Log - Date: 20:49, 17 November 2007 (UTC)[edit]
- INFO: Beginning work on ACTR2... {November 17, 2007 12:41:07 PM PST}
- SEARCH REDIRECT: Control Box Found: ACTR2 {November 17, 2007 12:41:25 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:41:26 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:41:26 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:41:26 PM PST}
- UPDATED: Updated protein page: ACTR2 {November 17, 2007 12:41:33 PM PST}
- INFO: Beginning work on C1QBP... {November 17, 2007 12:25:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:26:18 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_C1QBP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1p32.
| PDB = {{PDB2|1p32}}
| Name = Complement component 1, q subcomponent binding protein
| HGNCid = 1243
| Symbol = C1QBP
| AltSymbols =; GC1QBP; HABP1; SF2p32; gC1Q-R; gC1qR; p32
| OMIM = 601269
| ECnumber =
| Homologene = 31023
| MGIid = 1194505
| GeneAtlas_image1 = PBB_GE_C1QBP_214214_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_C1QBP_208910_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005759 |text = mitochondrial matrix}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 708
| Hs_Ensembl = ENSG00000108561
| Hs_RefseqProtein = NP_001203
| Hs_RefseqmRNA = NM_001212
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 5276676
| Hs_GenLoc_end = 5283125
| Hs_Uniprot = Q07021
| Mm_EntrezGene = 12261
| Mm_Ensembl = ENSMUSG00000018446
| Mm_RefseqmRNA = NM_007573
| Mm_RefseqProtein = NP_031599
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 70794002
| Mm_GenLoc_end = 70799169
| Mm_Uniprot = Q8R5L1
}}
}}
'''Complement component 1, q subcomponent binding protein''', also known as '''C1QBP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: C1QBP complement component 1, q subcomponent binding protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=708| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The human complement subcomponent C1q associates with C1r and C1s in order to yield the first component of the serum complement system. The protein encoded by this gene is known to bind to the globular heads of C1q molecules and inhibit C1 activation. This protein has also been identified as the p32 subunit of pre-mRNA splicing factor SF2, as well as a hyaluronic acid-binding protein.<ref name="entrez">{{cite web | title = Entrez Gene: C1QBP complement component 1, q subcomponent binding protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=708| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Krainer AR, Mayeda A, Kozak D, Binns G |title=Functional expression of cloned human splicing factor SF2: homology to RNA-binding proteins, U1 70K, and Drosophila splicing regulators. |journal=Cell |volume=66 |issue= 2 |pages= 383-94 |year= 1991 |pmid= 1830244 |doi= }}
*{{cite journal | author=Busby TF, Ingham KC |title=NH2-terminal calcium-binding domain of human complement C1s- mediates the interaction of C1r- with C1q. |journal=Biochemistry |volume=29 |issue= 19 |pages= 4613-8 |year= 1990 |pmid= 2372546 |doi= }}
*{{cite journal | author=Fridell RA, Harding LS, Bogerd HP, Cullen BR |title=Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins. |journal=Virology |volume=209 |issue= 2 |pages= 347-57 |year= 1995 |pmid= 7778269 |doi= 10.1006/viro.1995.1266 }}
*{{cite journal | author=Luo Y, Yu H, Peterlin BM |title=Cellular protein modulates effects of human immunodeficiency virus type 1 Rev. |journal=J. Virol. |volume=68 |issue= 6 |pages= 3850-6 |year= 1994 |pmid= 8189522 |doi= }}
*{{cite journal | author=Ghebrehiwet B, Lim BL, Peerschke EI, ''et al.'' |title=Isolation, cDNA cloning, and overexpression of a 33-kD cell surface glycoprotein that binds to the globular "heads" of C1q. |journal=J. Exp. Med. |volume=179 |issue= 6 |pages= 1809-21 |year= 1994 |pmid= 8195709 |doi= }}
*{{cite journal | author=Honoré B, Madsen P, Rasmussen HH, ''et al.'' |title=Cloning and expression of a cDNA covering the complete coding region of the P32 subunit of human pre-mRNA splicing factor SF2. |journal=Gene |volume=134 |issue= 2 |pages= 283-7 |year= 1994 |pmid= 8262387 |doi= }}
*{{cite journal | author=Deb TB, Datta K |title=Molecular cloning of human fibroblast hyaluronic acid-binding protein confirms its identity with P-32, a protein co-purified with splicing factor SF2. Hyaluronic acid-binding protein as P-32 protein, co-purified with splicing factor SF2. |journal=J. Biol. Chem. |volume=271 |issue= 4 |pages= 2206-12 |year= 1996 |pmid= 8567680 |doi= }}
*{{cite journal | author=Tange TO, Jensen TH, Kjems J |title=In vitro interaction between human immunodeficiency virus type 1 Rev protein and splicing factor ASF/SF2-associated protein, p32. |journal=J. Biol. Chem. |volume=271 |issue= 17 |pages= 10066-72 |year= 1996 |pmid= 8626563 |doi= }}
*{{cite journal | author=Guo N, Weremowicz S, Lynch N, ''et al.'' |title=Assignment of C1QBP encoding the C1q globular domain binding protein (gC1q-R) to human chromosome 17 band p13.3 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=77 |issue= 3-4 |pages= 283-4 |year= 1997 |pmid= 9284938 |doi= }}
*{{cite journal | author=Majumdar M, Datta K |title=Assignment of cDNA encoding hyaluronic acid-binding protein 1 to human chromosome 17p12-p13. |journal=Genomics |volume=51 |issue= 3 |pages= 476-7 |year= 1998 |pmid= 9721222 |doi= 10.1006/geno.1998.5364 }}
*{{cite journal | author=Petersen-Mahrt SK, Estmer C, Ohrmalm C, ''et al.'' |title=The splicing factor-associated protein, p32, regulates RNA splicing by inhibiting ASF/SF2 RNA binding and phosphorylation. |journal=EMBO J. |volume=18 |issue= 4 |pages= 1014-24 |year= 1999 |pmid= 10022843 |doi= 10.1093/emboj/18.4.1014 }}
*{{cite journal | author=Jiang J, Zhang Y, Krainer AR, Xu RM |title=Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 7 |pages= 3572-7 |year= 1999 |pmid= 10097078 |doi= }}
*{{cite journal | author=Braun L, Ghebrehiwet B, Cossart P |title=gC1q-R/p32, a C1q-binding protein, is a receptor for the InlB invasion protein of Listeria monocytogenes. |journal=EMBO J. |volume=19 |issue= 7 |pages= 1458-66 |year= 2000 |pmid= 10747014 |doi= 10.1093/emboj/19.7.1458 }}
*{{cite journal | author=Beatch MD, Hobman TC |title=Rubella virus capsid associates with host cell protein p32 and localizes to mitochondria. |journal=J. Virol. |volume=74 |issue= 12 |pages= 5569-76 |year= 2000 |pmid= 10823864 |doi= }}
*{{cite journal | author=Storz P, Hausser A, Link G, ''et al.'' |title=Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32. |journal=J. Biol. Chem. |volume=275 |issue= 32 |pages= 24601-7 |year= 2000 |pmid= 10831594 |doi= 10.1074/jbc.M002964200 }}
*{{cite journal | author=Tye AJ, Ghebrehiwet B, Guo N, ''et al.'' |title=The human gC1qR/p32 gene, C1qBP. Genomic organization and promoter analysis. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 17069-75 |year= 2001 |pmid= 11278463 |doi= 10.1074/jbc.M009064200 }}
*{{cite journal | author=Schaerer MT, Kannenberg K, Hunziker P, ''et al.'' |title=Interaction between GABA(A) receptor beta subunits and the multifunctional protein gC1q-R. |journal=J. Biol. Chem. |volume=276 |issue= 28 |pages= 26597-604 |year= 2001 |pmid= 11350968 |doi= 10.1074/jbc.M102534200 }}
*{{cite journal | author=Kobayashi M, Hanai R |title=M phase-specific association of human topoisomerase IIIbeta with chromosomes. |journal=Biochem. Biophys. Res. Commun. |volume=287 |issue= 1 |pages= 282-7 |year= 2001 |pmid= 11549288 |doi= 10.1006/bbrc.2001.5580 }}
*{{cite journal | author=Rozanov DV, Ghebrehiwet B, Postnova TI, ''et al.'' |title=The hemopexin-like C-terminal domain of membrane type 1 matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR. |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 9318-25 |year= 2002 |pmid= 11773076 |doi= 10.1074/jbc.M110711200 }}
*{{cite journal | author=Majumdar M, Meenakshi J, Goswami SK, Datta K |title=Hyaluronan binding protein 1 (HABP1)/C1QBP/p32 is an endogenous substrate for MAP kinase and is translocated to the nucleus upon mitogenic stimulation. |journal=Biochem. Biophys. Res. Commun. |volume=291 |issue= 4 |pages= 829-37 |year= 2002 |pmid= 11866440 |doi= 10.1006/bbrc.2002.6491 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CAPN3... {November 17, 2007 12:26:18 PM PST}
- SEARCH REDIRECT: Control Box Found: CAPN3 {November 17, 2007 12:27:09 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:27:12 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:27:12 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:27:12 PM PST}
- UPDATED: Updated protein page: CAPN3 {November 17, 2007 12:27:21 PM PST}
- INFO: Beginning work on CAST... {November 17, 2007 12:27:21 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:27:51 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Calpastatin
| HGNCid = 1515
| Symbol = CAST
| AltSymbols =; BS-17; MGC9402
| OMIM = 114090
| ECnumber =
| Homologene = 7658
| MGIid = 1098236
| GeneAtlas_image1 = PBB_GE_CAST_212586_at_tn.png
| GeneAtlas_image2 = PBB_GE_CAST_207467_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CAST_208908_s_at_tn.png
| Function = {{GNF_GO|id=GO:0030161 |text = calpain inhibitor activity}}
| Component =
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 831
| Hs_Ensembl = ENSG00000153113
| Hs_RefseqProtein = NP_001035905
| Hs_RefseqmRNA = NM_001042440
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 96023533
| Hs_GenLoc_end = 96136143
| Hs_Uniprot = P20810
| Mm_EntrezGene = 12380
| Mm_Ensembl = ENSMUSG00000021585
| Mm_RefseqmRNA = XM_990139
| Mm_RefseqProtein = XP_995233
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 75160288
| Mm_GenLoc_end = 75274762
| Mm_Uniprot = Q3TTN2
}}
}}
'''Calpastatin''', also known as '''CAST''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CAST calpastatin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=831| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is an endogenous calpain (calcium-dependent cysteine protease) inhibitor. It consists of an N-terminal domain L and four repetitive calpain-inhibition domains (domains 1-4), and it is involved in the proteolysis of amyloid precursor protein. The calpain/calpastatin system is involved in numerous membrane fusion events, such as neural vesicle exocytosis and platelet and red-cell aggregation. The encoded protein is also thought to affect the expression levels of genes encoding structural or regulatory proteins. Several alternatively spliced transcript variants of this gene have been described, but the full-length natures of only some have been determined.<ref name="entrez">{{cite web | title = Entrez Gene: CAST calpastatin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=831| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Murachi T |title=Intracellular regulatory system involving calpain and calpastatin. |journal=Biochem. Int. |volume=18 |issue= 2 |pages= 263-94 |year= 1989 |pmid= 2548504 |doi= }}
*{{cite journal | author=Lee WJ, Ma H, Takano E, ''et al.'' |title=Molecular diversity in amino-terminal domains of human calpastatin by exon skipping. |journal=J. Biol. Chem. |volume=267 |issue= 12 |pages= 8437-42 |year= 1992 |pmid= 1569094 |doi= }}
*{{cite journal | author=Adachi Y, Ishida-Takahashi A, Takahashi C, ''et al.'' |title=Phosphorylation and subcellular distribution of calpastatin in human hematopoietic system cells. |journal=J. Biol. Chem. |volume=266 |issue= 6 |pages= 3968-72 |year= 1991 |pmid= 1995645 |doi= }}
*{{cite journal | author=Inazawa J, Nakagawa H, Misawa S, ''et al.'' |title=Assignment of the human calpastatin gene (CAST) to chromosome 5 at region q14----q22. |journal=Cytogenet. Cell Genet. |volume=54 |issue= 3-4 |pages= 156-8 |year= 1991 |pmid= 2265559 |doi= }}
*{{cite journal | author=Uemori T, Shimojo T, Asada K, ''et al.'' |title=Characterization of a functional domain of human calpastatin. |journal=Biochem. Biophys. Res. Commun. |volume=166 |issue= 3 |pages= 1485-93 |year= 1990 |pmid= 2407243 |doi= }}
*{{cite journal | author=Maki M, Bagci H, Hamaguchi K, ''et al.'' |title=Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene. |journal=J. Biol. Chem. |volume=264 |issue= 32 |pages= 18866-9 |year= 1989 |pmid= 2553724 |doi= }}
*{{cite journal | author=Murachi T, Takano E, Maki M, ''et al.'' |title=Cloning and expression of the genes for calpains and calpastatins. |journal=Biochem. Soc. Symp. |volume=55 |issue= |pages= 29-44 |year= 1990 |pmid= 2559735 |doi= }}
*{{cite journal | author=Asada K, Ishino Y, Shimada M, ''et al.'' |title=cDNA cloning of human calpastatin: sequence homology among human, pig, and rabbit calpastatins. |journal=J. Enzym. Inhib. |volume=3 |issue= 1 |pages= 49-56 |year= 1991 |pmid= 2577276 |doi= }}
*{{cite journal | author=Pontremoli S, Salamino F, Sparatore B, ''et al.'' |title=Characterization of the calpastatin defect in erythrocytes from patients with essential hypertension. |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 3 |pages= 867-74 |year= 1989 |pmid= 2849943 |doi= }}
*{{cite journal | author=Mimori T, Suganuma K, Tanami Y, ''et al.'' |title=Autoantibodies to calpastatin (an endogenous inhibitor for calcium-dependent neutral protease, calpain) in systemic rheumatic diseases. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 16 |pages= 7267-71 |year= 1995 |pmid= 7638179 |doi= }}
*{{cite journal | author=Després N, Talbot G, Plouffe B, ''et al.'' |title=Detection and expression of a cDNA clone that encodes a polypeptide containing two inhibitory domains of human calpastatin and its recognition by rheumatoid arthritis sera. |journal=J. Clin. Invest. |volume=95 |issue= 4 |pages= 1891-6 |year= 1995 |pmid= 7706496 |doi= }}
*{{cite journal | author=Wei SG, Wang LF, Miao SY, ''et al.'' |title=Expression of the calpastatin gene segment during spermiogenesis in human testis: an in situ hybridization study. |journal=Arch. Androl. |volume=34 |issue= 1 |pages= 9-12 |year= 1995 |pmid= 7710300 |doi= }}
*{{cite journal | author=Wang LF, Wei SG, Miao SY, ''et al.'' |title=Calpastatin gene in human testis. |journal=Biochem. Mol. Biol. Int. |volume=33 |issue= 2 |pages= 245-51 |year= 1994 |pmid= 7951045 |doi= }}
*{{cite journal | author=Schwarz-Benmeir N, Glaser T, Barnoy S, Kosower NS |title=Calpastatin in erythrocytes of young and old individuals. |journal=Biochem. J. |volume=304 ( Pt 2) |issue= |pages= 365-70 |year= 1995 |pmid= 7998969 |doi= }}
*{{cite journal | author=Ma H, Yang HQ, Takano E, ''et al.'' |title=Requirement of different subdomains of calpastatin for calpain inhibition and for binding to calmodulin-like domains. |journal=J. Biochem. |volume=113 |issue= 5 |pages= 591-9 |year= 1993 |pmid= 8340353 |doi= }}
*{{cite journal | author=Fujitani K, Kambayashi J, Sakon M, ''et al.'' |title=Identification of mu-, m-calpains and calpastatin and capture of mu-calpain activation in endothelial cells. |journal=J. Cell. Biochem. |volume=66 |issue= 2 |pages= 197-209 |year= 1997 |pmid= 9213221 |doi= }}
*{{cite journal | author=Wang KK, Posmantur R, Nadimpalli R, ''et al.'' |title=Caspase-mediated fragmentation of calpain inhibitor protein calpastatin during apoptosis. |journal=Arch. Biochem. Biophys. |volume=356 |issue= 2 |pages= 187-96 |year= 1998 |pmid= 9705209 |doi= 10.1006/abbi.1998.0748 }}
*{{cite journal | author=Han Y, Weinman S, Boldogh I, ''et al.'' |title=Tumor necrosis factor-alpha-inducible IkappaBalpha proteolysis mediated by cytosolic m-calpain. A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-kappab activation. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 787-94 |year= 1999 |pmid= 9873017 |doi= }}
*{{cite journal | author=Ishikawa H, Nakagawa Y, Shimizu K, ''et al.'' |title=Inflammatory cytokines induced down-regulation of m-calpain mRNA expression in fibroblastic synoviocytes from patients with osteoarthritis and rheumatoid arthritis. |journal=Biochem. Biophys. Res. Commun. |volume=266 |issue= 2 |pages= 341-6 |year= 2000 |pmid= 10600505 |doi= 10.1006/bbrc.1999.1819 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CCL17... {November 17, 2007 12:33:06 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:33:41 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CCL17_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nr2.
| PDB = {{PDB2|1nr2}}, {{PDB2|1nr4}}
| Name = Chemokine (C-C motif) ligand 17
| HGNCid = 10615
| Symbol = CCL17
| AltSymbols =; A-152E5.3; ABCD-2; MGC138271; MGC138273; SCYA17; TARC
| OMIM = 601520
| ECnumber =
| Homologene = 2246
| MGIid = 1329039
| GeneAtlas_image1 = PBB_GE_CCL17_207900_at_tn.png
| Function = {{GNF_GO|id=GO:0008009 |text = chemokine activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6361
| Hs_Ensembl = ENSG00000102970
| Hs_RefseqProtein = NP_002978
| Hs_RefseqmRNA = NM_002987
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 56005294
| Hs_GenLoc_end = 56007475
| Hs_Uniprot = Q92583
| Mm_EntrezGene = 20295
| Mm_Ensembl = ENSMUSG00000031780
| Mm_RefseqmRNA = NM_011332
| Mm_RefseqProtein = NP_035462
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 97699582
| Mm_GenLoc_end = 97701164
| Mm_Uniprot =
}}
}}
'''Chemokine (C-C motif) ligand 17''', also known as '''CCL17''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CCL17 chemokine (C-C motif) ligand 17| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6361| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The CC cytokines are proteins characterized by two adjacent cysteines. The cytokine encoded by this gene displays chemotactic activity for T lymphocytes, but not monocytes or granulocytes. The product of this gene binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.<ref name="entrez">{{cite web | title = Entrez Gene: CCL17 chemokine (C-C motif) ligand 17| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6361| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Saeki H, Tamaki K |title=Thymus and activation regulated chemokine (TARC)/CCL17 and skin diseases. |journal=J. Dermatol. Sci. |volume=43 |issue= 2 |pages= 75-84 |year= 2006 |pmid= 16859899 |doi= 10.1016/j.jdermsci.2006.06.002 }}
*{{cite journal | author=Imai T, Yoshida T, Baba M, ''et al.'' |title=Molecular cloning of a novel T cell-directed CC chemokine expressed in thymus by signal sequence trap using Epstein-Barr virus vector. |journal=J. Biol. Chem. |volume=271 |issue= 35 |pages= 21514-21 |year= 1996 |pmid= 8702936 |doi= }}
*{{cite journal | author=Nomiyama H, Imai T, Kusuda J, ''et al.'' |title=Assignment of the human CC chemokine gene TARC (SCYA17) to chromosome 16q13. |journal=Genomics |volume=40 |issue= 1 |pages= 211-3 |year= 1997 |pmid= 9070951 |doi= 10.1006/geno.1996.4552 }}
*{{cite journal | author=Imai T, Baba M, Nishimura M, ''et al.'' |title=The T cell-directed CC chemokine TARC is a highly specific biological ligand for CC chemokine receptor 4. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 15036-42 |year= 1997 |pmid= 9169480 |doi= }}
*{{cite journal | author=Imai T, Chantry D, Raport CJ, ''et al.'' |title=Macrophage-derived chemokine is a functional ligand for the CC chemokine receptor 4. |journal=J. Biol. Chem. |volume=273 |issue= 3 |pages= 1764-8 |year= 1998 |pmid= 9430724 |doi= }}
*{{cite journal | author=Bernardini G, Hedrick J, Sozzani S, ''et al.'' |title=Identification of the CC chemokines TARC and macrophage inflammatory protein-1 beta as novel functional ligands for the CCR8 receptor. |journal=Eur. J. Immunol. |volume=28 |issue= 2 |pages= 582-8 |year= 1998 |pmid= 9521068 |doi= }}
*{{cite journal | author=Nomiyama H, Imai T, Kusuda J, ''et al.'' |title=Human chemokines fractalkine (SCYD1), MDC (SCYA22) and TARC (SCYA17) are clustered on chromosome 16q13. |journal=Cytogenet. Cell Genet. |volume=81 |issue= 1 |pages= 10-1 |year= 1998 |pmid= 9691168 |doi= }}
*{{cite journal | author=Struyf S, Proost P, Sozzani S, ''et al.'' |title=Enhanced anti-HIV-1 activity and altered chemotactic potency of NH2-terminally processed macrophage-derived chemokine (MDC) imply an additional MDC receptor. |journal=J. Immunol. |volume=161 |issue= 6 |pages= 2672-5 |year= 1998 |pmid= 9743322 |doi= }}
*{{cite journal | author=Loftus BJ, Kim UJ, Sneddon VP, ''et al.'' |title=Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. |journal=Genomics |volume=60 |issue= 3 |pages= 295-308 |year= 1999 |pmid= 10493829 |doi= 10.1006/geno.1999.5927 }}
*{{cite journal | author=Garlisi CG, Xiao H, Tian F, ''et al.'' |title=The assignment of chemokine-chemokine receptor pairs: TARC and MIP-1 beta are not ligands for human CC-chemokine receptor 8. |journal=Eur. J. Immunol. |volume=29 |issue= 10 |pages= 3210-5 |year= 1999 |pmid= 10540332 |doi= }}
*{{cite journal | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |doi= }}
*{{cite journal | author=Ghia P, Transidico P, Veiga JP, ''et al.'' |title=Chemoattractants MDC and TARC are secreted by malignant B-cell precursors following CD40 ligation and support the migration of leukemia-specific T cells. |journal=Blood |volume=98 |issue= 3 |pages= 533-40 |year= 2001 |pmid= 11468146 |doi= }}
*{{cite journal | author=Morita A, Kikuoka S, Horikawa T, ''et al.'' |title=Evaluation of human thymus and activation-regulated chemokine concentrations in blood using a new sandwich ELISA based on monoclonal antibodies. |journal=Clin. Chim. Acta |volume=322 |issue= 1-2 |pages= 67-75 |year= 2002 |pmid= 12104083 |doi= }}
*{{cite journal | author=Basu S, Schaefer TM, Ghosh M, ''et al.'' |title=Molecular cloning and sequencing of 25 different rhesus macaque chemokine cDNAs reveals evolutionary conservation among C, CC, CXC, AND CX3C families of chemokines. |journal=Cytokine |volume=18 |issue= 3 |pages= 140-8 |year= 2003 |pmid= 12126650 |doi= }}
*{{cite journal | author=D'Ambrosio D, Albanesi C, Lang R, ''et al.'' |title=Quantitative differences in chemokine receptor engagement generate diversity in integrin-dependent lymphocyte adhesion. |journal=J. Immunol. |volume=169 |issue= 5 |pages= 2303-12 |year= 2002 |pmid= 12193695 |doi= }}
*{{cite journal | author=Matsumoto N, Mukae H, Nakamura-Uchiyama F, ''et al.'' |title=Elevated levels of thymus and activation-regulated chemokine (TARC) in pleural effusion samples from patients infested with Paragonimus westermani. |journal=Clin. Exp. Immunol. |volume=130 |issue= 2 |pages= 314-8 |year= 2002 |pmid= 12390321 |doi= }}
*{{cite journal | author=Zheng X, Nakamura K, Tojo M, ''et al.'' |title=TGF-beta1-mediated regulation of thymus and activation-regulated chemokine (TARC/CCL17) synthesis and secretion by HaCaT cells co-stimulated with TNF-alpha and IFN-gamma. |journal=J. Dermatol. Sci. |volume=30 |issue= 2 |pages= 154-60 |year= 2003 |pmid= 12413771 |doi= }}
*{{cite journal | author=Kakinuma T, Nakamura K, Wakugawa M, ''et al.'' |title=IL-4, but not IL-13, modulates TARC (thymus and activation-regulated chemokine)/CCL17 and IP-10 (interferon-induced protein of 10kDA)/CXCL10 release by TNF-alpha and IFN-gamma in HaCaT cell line. |journal=Cytokine |volume=20 |issue= 1 |pages= 1-6 |year= 2003 |pmid= 12441140 |doi= }}
*{{cite journal | author=Uchida T, Suto H, Ra C, ''et al.'' |title=Preferential expression of T(h)2-type chemokine and its receptor in atopic dermatitis. |journal=Int. Immunol. |volume=14 |issue= 12 |pages= 1431-8 |year= 2003 |pmid= 12456591 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DCC... {November 17, 2007 12:27:52 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:28:16 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Deleted in colorectal carcinoma
| HGNCid = 2701
| Symbol = DCC
| AltSymbols =; CRC18; CRCR1
| OMIM = 120470
| ECnumber =
| Homologene = 21081
| MGIid = 94869
| Function = {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0030424 |text = axon}}
| Process = {{GNF_GO|id=GO:0001764 |text = neuron migration}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007409 |text = axonogenesis}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1630
| Hs_Ensembl = ENSG00000187323
| Hs_RefseqProtein = NP_005206
| Hs_RefseqmRNA = NM_005215
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 48121156
| Hs_GenLoc_end = 49311021
| Hs_Uniprot = P43146
| Mm_EntrezGene = 13176
| Mm_Ensembl = ENSMUSG00000060534
| Mm_RefseqmRNA = NM_007831
| Mm_RefseqProtein = NP_031857
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 71384359
| Mm_GenLoc_end = 72475815
| Mm_Uniprot = Q3TZP5
}}
}}
'''Deleted in colorectal carcinoma''', also known as '''DCC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DCC deleted in colorectal carcinoma| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1630| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Friess H, Berberat P, Schilling M, ''et al.'' |title=Pancreatic cancer: the potential clinical relevance of alterations in growth factors and their receptors. |journal=J. Mol. Med. |volume=74 |issue= 1 |pages= 35-42 |year= 1996 |pmid= 8834768 |doi= }}
*{{cite journal | author=Arakawa H |title=Netrin-1 and its receptors in tumorigenesis. |journal=Nat. Rev. Cancer |volume=4 |issue= 12 |pages= 978-87 |year= 2005 |pmid= 15573119 |doi= 10.1038/nrc1504 }}
*{{cite journal | author=Nigro JM, Cho KR, Fearon ER, ''et al.'' |title=Scrambled exons. |journal=Cell |volume=64 |issue= 3 |pages= 607-13 |year= 1991 |pmid= 1991322 |doi= }}
*{{cite journal | author=Fearon ER, Cho KR, Nigro JM, ''et al.'' |title=Identification of a chromosome 18q gene that is altered in colorectal cancers. |journal=Science |volume=247 |issue= 4938 |pages= 49-56 |year= 1990 |pmid= 2294591 |doi= }}
*{{cite journal | author=Fearon ER, Ekstrand BC, Hu G, ''et al.'' |title=Studies of the deleted in colorectal cancer gene in normal and neoplastic tissues. |journal=Cold Spring Harb. Symp. Quant. Biol. |volume=59 |issue= |pages= 637-43 |year= 1995 |pmid= 7587124 |doi= }}
*{{cite journal | author=Maesawa C, Tamura G, Suzuki Y, ''et al.'' |title=The sequential accumulation of genetic alterations characteristic of the colorectal adenoma-carcinoma sequence does not occur between gastric adenoma and adenocarcinoma. |journal=J. Pathol. |volume=176 |issue= 3 |pages= 249-58 |year= 1995 |pmid= 7674088 |doi= 10.1002/path.1711760307 }}
*{{cite journal | author=Hedrick L, Cho KR, Fearon ER, ''et al.'' |title=The DCC gene product in cellular differentiation and colorectal tumorigenesis. |journal=Genes Dev. |volume=8 |issue= 10 |pages= 1174-83 |year= 1994 |pmid= 7926722 |doi= }}
*{{cite journal | author=Reale MA, Hu G, Zafar AI, ''et al.'' |title=Expression and alternative splicing of the deleted in colorectal cancer (DCC) gene in normal and malignant tissues. |journal=Cancer Res. |volume=54 |issue= 16 |pages= 4493-501 |year= 1994 |pmid= 8044801 |doi= }}
*{{cite journal | author=Suzuki T, Ishioka C, Gamo M, ''et al.'' |title=[Genetic alterations of human colorectal cancer] |journal=Gan To Kagaku Ryoho |volume=21 |issue= 3 |pages= 343-50 |year= 1994 |pmid= 8109990 |doi= }}
*{{cite journal | author=Miyake S, Nagai K, Yoshino K, ''et al.'' |title=Point mutations and allelic deletion of tumor suppressor gene DCC in human esophageal squamous cell carcinomas and their relation to metastasis. |journal=Cancer Res. |volume=54 |issue= 11 |pages= 3007-10 |year= 1994 |pmid= 8187090 |doi= }}
*{{cite journal | author=Cho KR, Oliner JD, Simons JW, ''et al.'' |title=The DCC gene: structural analysis and mutations in colorectal carcinomas. |journal=Genomics |volume=19 |issue= 3 |pages= 525-31 |year= 1994 |pmid= 8188295 |doi= 10.1006/geno.1994.1102 }}
*{{cite journal | author=Keino-Masu K, Masu M, Hinck L, ''et al.'' |title=Deleted in Colorectal Cancer (DCC) encodes a netrin receptor. |journal=Cell |volume=87 |issue= 2 |pages= 175-85 |year= 1996 |pmid= 8861902 |doi= }}
*{{cite journal | author=Hu G, Zhang S, Vidal M, ''et al.'' |title=Mammalian homologs of seven in absentia regulate DCC via the ubiquitin-proteasome pathway. |journal=Genes Dev. |volume=11 |issue= 20 |pages= 2701-14 |year= 1997 |pmid= 9334332 |doi= }}
*{{cite journal | author=Mehlen P, Rabizadeh S, Snipas SJ, ''et al.'' |title=The DCC gene product induces apoptosis by a mechanism requiring receptor proteolysis. |journal=Nature |volume=395 |issue= 6704 |pages= 801-4 |year= 1998 |pmid= 9796814 |doi= 10.1038/27441 }}
*{{cite journal | author=Hu G, Fearon ER |title=Siah-1 N-terminal RING domain is required for proteolysis function, and C-terminal sequences regulate oligomerization and binding to target proteins. |journal=Mol. Cell. Biol. |volume=19 |issue= 1 |pages= 724-32 |year= 1999 |pmid= 9858595 |doi= }}
*{{cite journal | author=Meyerhardt JA, Caca K, Eckstrand BC, ''et al.'' |title=Netrin-1: interaction with deleted in colorectal cancer (DCC) and alterations in brain tumors and neuroblastomas. |journal=Cell Growth Differ. |volume=10 |issue= 1 |pages= 35-42 |year= 1999 |pmid= 9950216 |doi= }}
*{{cite journal | author=Hilgers W, Song JJ, Haye M, ''et al.'' |title=Homozygous deletions inactivate DCC, but not MADH4/DPC4/SMAD4, in a subset of pancreatic and biliary cancers. |journal=Genes Chromosomes Cancer |volume=27 |issue= 4 |pages= 353-7 |year= 2000 |pmid= 10719364 |doi= }}
*{{cite journal | author=Corset V, Nguyen-Ba-Charvet KT, Forcet C, ''et al.'' |title=Netrin-1-mediated axon outgrowth and cAMP production requires interaction with adenosine A2b receptor. |journal=Nature |volume=407 |issue= 6805 |pages= 747-50 |year= 2000 |pmid= 11048721 |doi= 10.1038/35037600 }}
*{{cite journal | author=Forcet C, Ye X, Granger L, ''et al.'' |title=The dependence receptor DCC (deleted in colorectal cancer) defines an alternative mechanism for caspase activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 6 |pages= 3416-21 |year= 2001 |pmid= 11248093 |doi= 10.1073/pnas.051378298 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DCX... {November 17, 2007 12:28:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:29:22 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DCX_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mjd.
| PDB = {{PDB2|1mjd}}, {{PDB2|2bqq}}
| Name = Doublecortex; lissencephaly, X-linked (doublecortin)
| HGNCid = 2714
| Symbol = DCX
| AltSymbols =; DBCN; DC; LISX; SCLH; XLIS
| OMIM = 300121
| ECnumber =
| Homologene = 7683
| MGIid = 1277171
| GeneAtlas_image1 = PBB_GE_DCX_204850_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DCX_204851_s_at_tn.png
| Function = {{GNF_GO|id=GO:0008017 |text = microtubule binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005875 |text = microtubule associated complex}}
| Process = {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007417 |text = central nervous system development}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1641
| Hs_Ensembl = ENSG00000077279
| Hs_RefseqProtein = NP_000546
| Hs_RefseqmRNA = NM_000555
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 110423663
| Hs_GenLoc_end = 110542259
| Hs_Uniprot = O43602
| Mm_EntrezGene = 13193
| Mm_Ensembl = ENSMUSG00000031285
| Mm_RefseqmRNA = NM_010025
| Mm_RefseqProtein = NP_034155
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 139102214
| Mm_GenLoc_end = 139179679
| Mm_Uniprot = Q3V349
}}
}}
'''Doublecortex; lissencephaly, X-linked (doublecortin)''', also known as '''DCX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DCX doublecortex; lissencephaly, X-linked (doublecortin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1641| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = In the developing cortex, cortical neurons must migrate over long distances to reach the site of their final differentiation. The protein encoded by this gene is a cytoplasmic protein which appears to direct neuronal migration by regulating the organization and stability of microtubules. The encoded protein contains two doublecortin domains, which bind microtubules. In addition, the encoded protein interacts with LIS1, the regulatory gamma subunit of platelet activating factor acetylhydrolase, and this interaction is important to proper microtubule function in the developing cortex. Mutations in this gene are a cause of X-linked lissencephaly. Multiple transcript variants encoding at least three different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: DCX doublecortex; lissencephaly, X-linked (doublecortin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1641| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=des Portes V, Pinard JM, Smadja D, ''et al.'' |title=Dominant X linked subcortical laminar heterotopia and lissencephaly syndrome (XSCLH/LIS): evidence for the occurrence of mutation in males and mapping of a potential locus in Xq22. |journal=J. Med. Genet. |volume=34 |issue= 3 |pages= 177-83 |year= 1997 |pmid= 9132485 |doi= }}
*{{cite journal | author=des Portes V, Pinard JM, Billuart P, ''et al.'' |title=A novel CNS gene required for neuronal migration and involved in X-linked subcortical laminar heterotopia and lissencephaly syndrome. |journal=Cell |volume=92 |issue= 1 |pages= 51-61 |year= 1998 |pmid= 9489699 |doi= }}
*{{cite journal | author=Gleeson JG, Allen KM, Fox JW, ''et al.'' |title=Doublecortin, a brain-specific gene mutated in human X-linked lissencephaly and double cortex syndrome, encodes a putative signaling protein. |journal=Cell |volume=92 |issue= 1 |pages= 63-72 |year= 1998 |pmid= 9489700 |doi= }}
*{{cite journal | author=des Portes V, Francis F, Pinard JM, ''et al.'' |title=doublecortin is the major gene causing X-linked subcortical laminar heterotopia (SCLH). |journal=Hum. Mol. Genet. |volume=7 |issue= 7 |pages= 1063-70 |year= 1999 |pmid= 9618162 |doi= }}
*{{cite journal | author=Sossey-Alaoui K, Hartung AJ, Guerrini R, ''et al.'' |title=Human doublecortin (DCX) and the homologous gene in mouse encode a putative Ca2+-dependent signaling protein which is mutated in human X-linked neuronal migration defects. |journal=Hum. Mol. Genet. |volume=7 |issue= 8 |pages= 1327-32 |year= 1998 |pmid= 9668176 |doi= }}
*{{cite journal | author=Pilz DT, Matsumoto N, Minnerath S, ''et al.'' |title=LIS1 and XLIS (DCX) mutations cause most classical lissencephaly, but different patterns of malformation. |journal=Hum. Mol. Genet. |volume=7 |issue= 13 |pages= 2029-37 |year= 1999 |pmid= 9817918 |doi= }}
*{{cite journal | author=Gleeson JG, Minnerath SR, Fox JW, ''et al.'' |title=Characterization of mutations in the gene doublecortin in patients with double cortex syndrome. |journal=Ann. Neurol. |volume=45 |issue= 2 |pages= 146-53 |year= 1999 |pmid= 9989615 |doi= }}
*{{cite journal | author=Kato M, Kimura T, Lin C, ''et al.'' |title=A novel mutation of the doublecortin gene in Japanese patients with X-linked lissencephaly and subcortical band heterotopia. |journal=Hum. Genet. |volume=104 |issue= 4 |pages= 341-4 |year= 1999 |pmid= 10369164 |doi= }}
*{{cite journal | author=Gleeson JG, Lin PT, Flanagan LA, Walsh CA |title=Doublecortin is a microtubule-associated protein and is expressed widely by migrating neurons. |journal=Neuron |volume=23 |issue= 2 |pages= 257-71 |year= 1999 |pmid= 10399933 |doi= }}
*{{cite journal | author=Pilz DT, Kuc J, Matsumoto N, ''et al.'' |title=Subcortical band heterotopia in rare affected males can be caused by missense mutations in DCX (XLIS) or LIS1. |journal=Hum. Mol. Genet. |volume=8 |issue= 9 |pages= 1757-60 |year= 2000 |pmid= 10441340 |doi= }}
*{{cite journal | author=Sakamoto M, Ono J, Okada S, ''et al.'' |title=Genetic alteration of the DCX gene in Japanese patients with subcortical laminar heterotopia or isolated lissencephaly sequence. |journal=J. Hum. Genet. |volume=45 |issue= 3 |pages= 167-70 |year= 2000 |pmid= 10807542 |doi= }}
*{{cite journal | author=Caspi M, Atlas R, Kantor A, ''et al.'' |title=Interaction between LIS1 and doublecortin, two lissencephaly gene products. |journal=Hum. Mol. Genet. |volume=9 |issue= 15 |pages= 2205-13 |year= 2001 |pmid= 11001923 |doi= }}
*{{cite journal | author=Matsumoto N, Leventer RJ, Kuc JA, ''et al.'' |title=Mutation analysis of the DCX gene and genotype/phenotype correlation in subcortical band heterotopia. |journal=Eur. J. Hum. Genet. |volume=9 |issue= 1 |pages= 5-12 |year= 2001 |pmid= 11175293 |doi= 10.1038/sj.ejhg.5200548 }}
*{{cite journal | author=Demelas L, Serra G, Conti M, ''et al.'' |title=Incomplete penetrance with normal MRI in a woman with germline mutation of the DCX gene. |journal=Neurology |volume=57 |issue= 2 |pages= 327-30 |year= 2001 |pmid= 11468322 |doi= }}
*{{cite journal | author=Friocourt G, Chafey P, Billuart P, ''et al.'' |title=Doublecortin interacts with mu subunits of clathrin adaptor complexes in the developing nervous system. |journal=Mol. Cell. Neurosci. |volume=18 |issue= 3 |pages= 307-19 |year= 2001 |pmid= 11591131 |doi= 10.1006/mcne.2001.1022 }}
*{{cite journal | author=Kato M, Kanai M, Soma O, ''et al.'' |title=Mutation of the doublecortin gene in male patients with double cortex syndrome: somatic mosaicism detected by hair root analysis. |journal=Ann. Neurol. |volume=50 |issue= 4 |pages= 547-51 |year= 2001 |pmid= 11601509 |doi= }}
*{{cite journal | author=des Portes V, Abaoub L, Joannard A, ''et al.'' |title=So-called 'cryptogenic' partial seizures resulting from a subtle cortical dysgenesis due to a doublecortin gene mutation. |journal=Seizure : the journal of the British Epilepsy Association |volume=11 |issue= 4 |pages= 273-7 |year= 2002 |pmid= 12027577 |doi= 10.1053/seiz.2001.0607 }}
*{{cite journal | author=Kizhatil K, Wu YX, Sen A, Bennett V |title=A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin. |journal=J. Neurosci. |volume=22 |issue= 18 |pages= 7948-58 |year= 2002 |pmid= 12223548 |doi= }}
*{{cite journal | author=D'Agostino MD, Bernasconi A, Das S, ''et al.'' |title=Subcortical band heterotopia (SBH) in males: clinical, imaging and genetic findings in comparison with females. |journal=Brain |volume=125 |issue= Pt 11 |pages= 2507-22 |year= 2002 |pmid= 12390976 |doi= }}
*{{cite journal | author=Meyer G, Perez-Garcia CG, Gleeson JG |title=Selective expression of doublecortin and LIS1 in developing human cortex suggests unique modes of neuronal movement. |journal=Cereb. Cortex |volume=12 |issue= 12 |pages= 1225-36 |year= 2003 |pmid= 12427674 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DES... {November 17, 2007 12:29:22 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:30:06 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Desmin
| HGNCid = 2770
| Symbol = DES
| AltSymbols =; CMD1I; CSM1; CSM2; FLJ12025; FLJ39719; FLJ41013; FLJ41793
| OMIM = 125660
| ECnumber =
| Homologene = 56469
| MGIid = 94885
| GeneAtlas_image1 = PBB_GE_DES_202222_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DES_214027_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005626 |text = insoluble fraction}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005882 |text = intermediate filament}} {{GNF_GO|id=GO:0030018 |text = Z disc}} {{GNF_GO|id=GO:0042383 |text = sarcolemma}} {{GNF_GO|id=GO:0043292 |text = contractile fiber}} {{GNF_GO|id=GO:0045202 |text = synapse}}
| Process = {{GNF_GO|id=GO:0006936 |text = muscle contraction}} {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0008016 |text = regulation of heart contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1674
| Hs_Ensembl = ENSG00000175084
| Hs_RefseqProtein = NP_001918
| Hs_RefseqmRNA = NM_001927
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 219991343
| Hs_GenLoc_end = 219999705
| Hs_Uniprot = P17661
| Mm_EntrezGene = 13346
| Mm_Ensembl = ENSMUSG00000026208
| Mm_RefseqmRNA = NM_010043
| Mm_RefseqProtein = NP_034173
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 75243492
| Mm_GenLoc_end = 75250864
| Mm_Uniprot = Q3V1K9
}}
}}
'''Desmin''', also known as '''DES''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DES desmin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1674| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a muscle-specific class III intermediate filament. Homopolymers of this protein form a stable intracytoplasmic filamentous network connecting myofibrils to each other and to the plasma membrane. Mutations in this gene are associated with desmin-related myopathy, a familial cardiac and skeletal myopathy (CSM), and with distal myopathies.<ref name="entrez">{{cite web | title = Entrez Gene: DES desmin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1674| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Snásel J, Pichová I |title=The cleavage of host cell proteins by HIV-1 protease. |journal=Folia Biol. (Praha) |volume=42 |issue= 5 |pages= 227-30 |year= 1997 |pmid= 8997639 |doi= }}
*{{cite journal | author=Garbuglia M, Verzini M, Sorci G, ''et al.'' |title=The calcium-modulated proteins, S100A1 and S100B, as potential regulators of the dynamics of type III intermediate filaments. |journal=Braz. J. Med. Biol. Res. |volume=32 |issue= 10 |pages= 1177-85 |year= 2000 |pmid= 10510252 |doi= }}
*{{cite journal | author=Li ZL, Paulin D |title=High level desmin expression depends on a muscle-specific enhancer. |journal=J. Biol. Chem. |volume=266 |issue= 10 |pages= 6562-70 |year= 1991 |pmid= 2007603 |doi= }}
*{{cite journal | author=Shoeman RL, Höner B, Stoller TJ, ''et al.'' |title=Human immunodeficiency virus type 1 protease cleaves the intermediate filament proteins vimentin, desmin, and glial fibrillary acidic protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 16 |pages= 6336-40 |year= 1990 |pmid= 2201025 |doi= }}
*{{cite journal | author=Viegas-Péquignot E, Li ZL, Dutrillaux B, ''et al.'' |title=Assignment of human desmin gene to band 2q35 by nonradioactive in situ hybridization. |journal=Hum. Genet. |volume=83 |issue= 1 |pages= 33-6 |year= 1989 |pmid= 2670738 |doi= }}
*{{cite journal | author=Li ZL, Lilienbaum A, Butler-Browne G, Paulin D |title=Human desmin-coding gene: complete nucleotide sequence, characterization and regulation of expression during myogenesis and development. |journal=Gene |volume=78 |issue= 2 |pages= 243-54 |year= 1989 |pmid= 2673923 |doi= }}
*{{cite journal | author=Langley RC, Cohen CM |title=Association of spectrin with desmin intermediate filaments. |journal=J. Cell. Biochem. |volume=30 |issue= 2 |pages= 101-9 |year= 1986 |pmid= 2939097 |doi= 10.1002/jcb.240300202 }}
*{{cite journal | author=Ariza A, Coll J, Fernández-Figueras MT, ''et al.'' |title=Desmin myopathy: a multisystem disorder involving skeletal, cardiac, and smooth muscle. |journal=Hum. Pathol. |volume=26 |issue= 9 |pages= 1032-7 |year= 1995 |pmid= 7672786 |doi= }}
*{{cite journal | author=Behr T, Fischer P, Müller-Felber W, ''et al.'' |title=Myofibrillogenesis in primary tissue cultures of adult human skeletal muscle: expression of desmin, titin, and nebulin. |journal=The Clinical investigator |volume=72 |issue= 2 |pages= 150-5 |year= 1994 |pmid= 8186663 |doi= }}
*{{cite journal | author=Shoeman RL, Sachse C, Höner B, ''et al.'' |title=Cleavage of human and mouse cytoskeletal and sarcomeric proteins by human immunodeficiency virus type 1 protease. Actin, desmin, myosin, and tropomyosin. |journal=Am. J. Pathol. |volume=142 |issue= 1 |pages= 221-30 |year= 1993 |pmid= 8424456 |doi= }}
*{{cite journal | author=Rogatsch H, Jezek D, Hittmair A, ''et al.'' |title=Expression of vimentin, cytokeratin, and desmin in Sertoli cells of human fetal, cryptorchid, and tumour-adjacent testicular tissue. |journal=Virchows Arch. |volume=427 |issue= 5 |pages= 497-502 |year= 1996 |pmid= 8624579 |doi= }}
*{{cite journal | author=Garbuglia M, Verzini M, Giambanco I, ''et al.'' |title=Effects of calcium-binding proteins (S-100a(o), S-100a, S-100b) on desmin assembly in vitro. |journal=FASEB J. |volume=10 |issue= 2 |pages= 317-24 |year= 1996 |pmid= 8641565 |doi= }}
*{{cite journal | author=Vicart P, Dupret JM, Hazan J, ''et al.'' |title=Human desmin gene: cDNA sequence, regional localization and exclusion of the locus in a familial desmin-related myopathy. |journal=Hum. Genet. |volume=98 |issue= 4 |pages= 422-9 |year= 1996 |pmid= 8792816 |doi= }}
*{{cite journal | author=Meng JJ, Bornslaeger EA, Green KJ, ''et al.'' |title=Two-hybrid analysis reveals fundamental differences in direct interactions between desmoplakin and cell type-specific intermediate filaments. |journal=J. Biol. Chem. |volume=272 |issue= 34 |pages= 21495-503 |year= 1997 |pmid= 9261168 |doi= }}
*{{cite journal | author=van der Flier A, Gaspar AC, Thorsteinsdóttir S, ''et al.'' |title=Spatial and temporal expression of the beta1D integrin during mouse development. |journal=Dev. Dyn. |volume=210 |issue= 4 |pages= 472-86 |year= 1998 |pmid= 9415431 |doi= 10.1002/(SICI)1097-0177(199712)210:4<472::AID-AJA10>3.0.CO;2-9 }}
*{{cite journal | author=Goldfarb LG, Park KY, Cervenáková L, ''et al.'' |title=Missense mutations in desmin associated with familial cardiac and skeletal myopathy. |journal=Nat. Genet. |volume=19 |issue= 4 |pages= 402-3 |year= 1998 |pmid= 9697706 |doi= 10.1038/1300 }}
*{{cite journal | author=Muñoz-Mármol AM, Strasser G, Isamat M, ''et al.'' |title=A dysfunctional desmin mutation in a patient with severe generalized myopathy. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 19 |pages= 11312-7 |year= 1998 |pmid= 9736733 |doi= }}
*{{cite journal | author=Li D, Tapscoft T, Gonzalez O, ''et al.'' |title=Desmin mutation responsible for idiopathic dilated cardiomyopathy. |journal=Circulation |volume=100 |issue= 5 |pages= 461-4 |year= 1999 |pmid= 10430757 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DHFR... {November 17, 2007 12:30:06 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:30:46 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DHFR_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1boz.
| PDB = {{PDB2|1boz}}, {{PDB2|1dhf}}, {{PDB2|1dlr}}, {{PDB2|1dls}}, {{PDB2|1drf}}, {{PDB2|1hfp}}, {{PDB2|1hfq}}, {{PDB2|1hfr}}, {{PDB2|1kms}}, {{PDB2|1kmv}}, {{PDB2|1mvs}}, {{PDB2|1mvt}}, {{PDB2|1ohj}}, {{PDB2|1ohk}}, {{PDB2|1pd8}}, {{PDB2|1pd9}}, {{PDB2|1pdb}}, {{PDB2|1s3u}}, {{PDB2|1s3v}}, {{PDB2|1s3w}}, {{PDB2|1u71}}, {{PDB2|1u72}}, {{PDB2|1yho}}, {{PDB2|2c2s}}, {{PDB2|2c2t}}, {{PDB2|2dhf}}
| Name = Dihydrofolate reductase
| HGNCid = 2861
| Symbol = DHFR
| AltSymbols =;
| OMIM = 126060
| ECnumber =
| Homologene = 56470
| MGIid = 94890
| Function = {{GNF_GO|id=GO:0004146 |text = dihydrofolate reductase activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0050661 |text = NADP binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0006545 |text = glycine biosynthetic process}} {{GNF_GO|id=GO:0006730 |text = one-carbon compound metabolic process}} {{GNF_GO|id=GO:0009165 |text = nucleotide biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1719
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000782
| Hs_RefseqmRNA = NM_000791
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 13361
| Mm_Ensembl = ENSMUSG00000021707
| Mm_RefseqmRNA = NM_010049
| Mm_RefseqProtein = NP_034179
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 93455536
| Mm_GenLoc_end = 93489806
| Mm_Uniprot = Q544T5
}}
}}
'''Dihydrofolate reductase''', also known as '''DHFR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DHFR dihydrofolate reductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1719| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Dihydrofolate reductase converts dihydrofolate into tetrahydrofolate, a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and certain amino acids. While the functional dihydrofolate reductase gene has been mapped to chromosome 5, multiple intronless processed pseudogenes or dihydrofolate reductase-like genes have been identified on separate chromosomes. Dihydrofolate reductase deficiency has been linked to megaloblastic anemia.<ref name="entrez">{{cite web | title = Entrez Gene: DHFR dihydrofolate reductase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1719| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Banerjee D, Mayer-Kuckuk P, Capiaux G, ''et al.'' |title=Novel aspects of resistance to drugs targeted to dihydrofolate reductase and thymidylate synthase. |journal=Biochim. Biophys. Acta |volume=1587 |issue= 2-3 |pages= 164-73 |year= 2002 |pmid= 12084458 |doi= }}
*{{cite journal | author=Stockman BJ, Nirmala NR, Wagner G, ''et al.'' |title=Sequence-specific 1H and 15N resonance assignments for human dihydrofolate reductase in solution. |journal=Biochemistry |volume=31 |issue= 1 |pages= 218-29 |year= 1992 |pmid= 1731871 |doi= }}
*{{cite journal | author=Beltzer JP, Spiess M |title=In vitro binding of the asialoglycoprotein receptor to the beta adaptin of plasma membrane coated vesicles. |journal=EMBO J. |volume=10 |issue= 12 |pages= 3735-42 |year= 1991 |pmid= 1935897 |doi= }}
*{{cite journal | author=Davies JF, Delcamp TJ, Prendergast NJ, ''et al.'' |title=Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate. |journal=Biochemistry |volume=29 |issue= 40 |pages= 9467-79 |year= 1991 |pmid= 2248959 |doi= }}
*{{cite journal | author=Will CL, Dolnick BJ |title=5-Fluorouracil inhibits dihydrofolate reductase precursor mRNA processing and/or nuclear mRNA stability in methotrexate-resistant KB cells. |journal=J. Biol. Chem. |volume=264 |issue= 35 |pages= 21413-21 |year= 1990 |pmid= 2592384 |doi= }}
*{{cite journal | author=Masters JN, Attardi G |title=Discrete human dihydrofolate reductase gene transcripts present in polysomal RNA map with their 5' ends several hundred nucleotides upstream of the main mRNA start site. |journal=Mol. Cell. Biol. |volume=5 |issue= 3 |pages= 493-500 |year= 1985 |pmid= 2859520 |doi= }}
*{{cite journal | author=Miszta H, Dabrowski Z, Lanotte M |title=In vitro patterns of enzymic tetrahydrofolate dehydrogenase (EC 1.5.1.3) expression in bone marrow stromal cells. |journal=Leukemia |volume=2 |issue= 11 |pages= 754-9 |year= 1988 |pmid= 3185016 |doi= }}
*{{cite journal | author=Oefner C, D'Arcy A, Winkler FK |title=Crystal structure of human dihydrofolate reductase complexed with folate. |journal=Eur. J. Biochem. |volume=174 |issue= 2 |pages= 377-85 |year= 1988 |pmid= 3383852 |doi= }}
*{{cite journal | author=Yang JK, Masters JN, Attardi G |title=Human dihydrofolate reductase gene organization. Extensive conservation of the G + C-rich 5' non-coding sequence and strong intron size divergence from homologous mammalian genes. |journal=J. Mol. Biol. |volume=176 |issue= 2 |pages= 169-87 |year= 1984 |pmid= 6235374 |doi= }}
*{{cite journal | author=Masters JN, Yang JK, Cellini A, Attardi G |title=A human dihydrofolate reductase pseudogene and its relationship to the multiple forms of specific messenger RNA. |journal=J. Mol. Biol. |volume=167 |issue= 1 |pages= 23-36 |year= 1983 |pmid= 6306253 |doi= }}
*{{cite journal | author=Chen MJ, Shimada T, Moulton AD, ''et al.'' |title=The functional human dihydrofolate reductase gene. |journal=J. Biol. Chem. |volume=259 |issue= 6 |pages= 3933-43 |year= 1984 |pmid= 6323448 |doi= }}
*{{cite journal | author=Funanage VL, Myoda TT, Moses PA, Cowell HR |title=Assignment of the human dihydrofolate reductase gene to the q11----q22 region of chromosome 5. |journal=Mol. Cell. Biol. |volume=4 |issue= 10 |pages= 2010-6 |year= 1985 |pmid= 6504041 |doi= }}
*{{cite journal | author=Masters JN, Attardi G |title=The nucleotide sequence of the cDNA coding for the human dihydrofolic acid reductase. |journal=Gene |volume=21 |issue= 1-2 |pages= 59-63 |year= 1983 |pmid= 6687716 |doi= }}
*{{cite journal | author=Morandi C, Masters JN, Mottes M, Attardi G |title=Multiple forms of human dihydrofolate reductase messenger RNA. Cloning and expression in Escherichia coli of their DNA coding sequence. |journal=J. Mol. Biol. |volume=156 |issue= 3 |pages= 583-607 |year= 1982 |pmid= 6750132 |doi= }}
*{{cite journal | author=Bonifaci N, Sitia R, Rubartelli A |title=Nuclear translocation of an exogenous fusion protein containing HIV Tat requires unfolding. |journal=AIDS |volume=9 |issue= 9 |pages= 995-1000 |year= 1996 |pmid= 8527095 |doi= }}
*{{cite journal | author=Mayhew M, da Silva AC, Martin J, ''et al.'' |title=Protein folding in the central cavity of the GroEL-GroES chaperonin complex. |journal=Nature |volume=379 |issue= 6564 |pages= 420-6 |year= 1996 |pmid= 8559246 |doi= 10.1038/379420a0 }}
*{{cite journal | author=Gross M, Robinson CV, Mayhew M, ''et al.'' |title=Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling. |journal=Protein Sci. |volume=5 |issue= 12 |pages= 2506-13 |year= 1997 |pmid= 8976559 |doi= }}
*{{cite journal | author=Schleiff E, Shore GC, Goping IS |title=Human mitochondrial import receptor, Tom20p. Use of glutathione to reveal specific interactions between Tom20-glutathione S-transferase and mitochondrial precursor proteins. |journal=FEBS Lett. |volume=404 |issue= 2-3 |pages= 314-8 |year= 1997 |pmid= 9119086 |doi= }}
*{{cite journal | author=Cody V, Galitsky N, Luft JR, ''et al.'' |title=Comparison of two independent crystal structures of human dihydrofolate reductase ternary complexes reduced with nicotinamide adenine dinucleotide phosphate and the very tight-binding inhibitor PT523. |journal=Biochemistry |volume=36 |issue= 45 |pages= 13897-903 |year= 1997 |pmid= 9374868 |doi= 10.1021/bi971711l }}
*{{cite journal | author=Vanguri VK, Wang S, Godyna S, ''et al.'' |title=Thrombospondin-1 binds to polyhistidine with high affinity and specificity. |journal=Biochem. J. |volume=347 |issue= Pt 2 |pages= 469-73 |year= 2001 |pmid= 10749676 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DST... {November 17, 2007 12:23:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:25:27 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DST_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2iak.
| PDB = {{PDB2|2iak}}
| Name = Dystonin
| HGNCid = 1090
| Symbol = DST
| AltSymbols =; BP240; BPA; BPAG1; CATX-15; D6S1101; DMH; FLJ46791; KIAA0465; KIAA1470; MACF2
| OMIM = 113810
| ECnumber =
| Homologene = 81841
| MGIid =
| GeneAtlas_image1 = PBB_GE_DST_212253_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_DST_212254_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_DST_215016_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0051015 |text = actin filament binding}}
| Component = {{GNF_GO|id=GO:0005604 |text = basement membrane}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005911 |text = intercellular junction}} {{GNF_GO|id=GO:0016023 |text = cytoplasmic membrane-bound vesicle}} {{GNF_GO|id=GO:0030056 |text = hemidesmosome}}
| Process = {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0008090 |text = retrograde axon cargo transport}} {{GNF_GO|id=GO:0030036 |text = actin cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0045104 |text = intermediate filament cytoskeleton organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 667
| Hs_Ensembl = ENSG00000151914
| Hs_RefseqProtein = NP_001714
| Hs_RefseqmRNA = NM_001723
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 56430744
| Hs_GenLoc_end = 56927363
| Hs_Uniprot = O94833
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Dystonin''', also known as '''DST''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DST dystonin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=667| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the plakin protein family of adhesion junction plaque proteins. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for this gene, but the full-length nature of some variants has not been defined. It has been known that some isoforms are expressed in neural and muscle tissue, anchoring neural intermediate filaments to the actin cytoskeleton, and some isoforms are expressed in epithelial tissue, anchoring keratin-containing intermediate filaments to hemidesmosomes. Consistent with the expression, mice defective for this gene show skin blistering and neurodegeneration.<ref name="entrez">{{cite web | title = Entrez Gene: DST dystonin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=667| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi= }}
*{{cite journal | author=Tanaka T, Parry DA, Klaus-Kovtun V, ''et al.'' |title=Comparison of molecularly cloned bullous pemphigoid antigen to desmoplakin I confirms that they define a new family of cell adhesion junction plaque proteins. |journal=J. Biol. Chem. |volume=266 |issue= 19 |pages= 12555-9 |year= 1991 |pmid= 1712022 |doi= }}
*{{cite journal | author=Sawamura D, Li K, Chu ML, Uitto J |title=Human bullous pemphigoid antigen (BPAG1). Amino acid sequences deduced from cloned cDNAs predict biologically important peptide segments and protein domains. |journal=J. Biol. Chem. |volume=266 |issue= 27 |pages= 17784-90 |year= 1991 |pmid= 1717441 |doi= }}
*{{cite journal | author=Sawamura D, Li KH, Nomura K, ''et al.'' |title=Bullous pemphigoid antigen: cDNA cloning, cellular expression, and evidence for polymorphism of the human gene. |journal=J. Invest. Dermatol. |volume=96 |issue= 6 |pages= 908-15 |year= 1991 |pmid= 2045679 |doi= }}
*{{cite journal | author=Owaribe K, Kartenbeck J, Stumpp S, ''et al.'' |title=The hemidesmosomal plaque. I. Characterization of a major constituent protein as a differentiation marker for certain forms of epithelia. |journal=Differentiation |volume=45 |issue= 3 |pages= 207-20 |year= 1991 |pmid= 2090522 |doi= }}
*{{cite journal | author=Sawamura D, Nomura K, Sugita Y, ''et al.'' |title=Bullous pemphigoid antigen (BPAG1): cDNA cloning and mapping of the gene to the short arm of human chromosome 6. |journal=Genomics |volume=8 |issue= 4 |pages= 722-6 |year= 1991 |pmid= 2276744 |doi= }}
*{{cite journal | author=Stanley JR, Tanaka T, Mueller S, ''et al.'' |title=Isolation of complementary DNA for bullous pemphigoid antigen by use of patients' autoantibodies. |journal=J. Clin. Invest. |volume=82 |issue= 6 |pages= 1864-70 |year= 1989 |pmid= 2461961 |doi= }}
*{{cite journal | author=Westgate GE, Weaver AC, Couchman JR |title=Bullous pemphigoid antigen localization suggests an intracellular association with hemidesmosomes. |journal=J. Invest. Dermatol. |volume=84 |issue= 3 |pages= 218-24 |year= 1985 |pmid= 2579167 |doi= }}
*{{cite journal | author=Mutasim DF, Morrison LH, Takahashi Y, ''et al.'' |title=Definition of bullous pemphigoid antibody binding to intracellular and extracellular antigen associated with hemidesmosomes. |journal=J. Invest. Dermatol. |volume=92 |issue= 2 |pages= 225-30 |year= 1989 |pmid= 2645368 |doi= }}
*{{cite journal | author=Mutasim DF, Takahashi Y, Labib RS, ''et al.'' |title=A pool of bullous pemphigoid antigen(s) is intracellular and associated with the basal cell cytoskeleton-hemidesmosome complex. |journal=J. Invest. Dermatol. |volume=84 |issue= 1 |pages= 47-53 |year= 1985 |pmid= 3880796 |doi= }}
*{{cite journal | author=Nomura K, Sugawara T, Sato T, ''et al.'' |title=Expression of laminin, type IV procollagen and 230 kDa bullous pemphigoid antigen genes by keratinocytes and fibroblasts in culture: application of the polymerase chain reaction for detection of small amounts of messenger RNA. |journal=Arch. Dermatol. Res. |volume=286 |issue= 7 |pages= 408-13 |year= 1995 |pmid= 7818282 |doi= }}
*{{cite journal | author=Brown A, Lemieux N, Rossant J, Kothary R |title=Human homolog of a mouse sequence from the dystonia musculorum locus is on chromosome 6p12. |journal=Mamm. Genome |volume=5 |issue= 7 |pages= 434-7 |year= 1994 |pmid= 7919656 |doi= }}
*{{cite journal | author=Hopkinson SB, Jones JC |title=Identification of a second protein product of the gene encoding a human epidermal autoantigen. |journal=Biochem. J. |volume=300 ( Pt 3) |issue= |pages= 851-7 |year= 1994 |pmid= 8010969 |doi= }}
*{{cite journal | author=Elgart GW, Stanley JR |title=Cloning of the 5' mRNA for the 230-kD bullous pemphigoid antigen by rapid amplification of cDNA ends. |journal=J. Invest. Dermatol. |volume=101 |issue= 2 |pages= 244-6 |year= 1993 |pmid= 8345227 |doi= }}
*{{cite journal | author=Tamai K, Sawamura D, Do HC, ''et al.'' |title=The human 230-kD bullous pemphigoid antigen gene (BPAG1). Exon-intron organization and identification of regulatory tissue specific elements in the promoter region. |journal=J. Clin. Invest. |volume=92 |issue= 2 |pages= 814-22 |year= 1993 |pmid= 8349819 |doi= }}
*{{cite journal | author=Brown A, Dalpé G, Mathieu M, Kothary R |title=Cloning and characterization of the neural isoforms of human dystonin. |journal=Genomics |volume=29 |issue= 3 |pages= 777-80 |year= 1996 |pmid= 8575775 |doi= 10.1006/geno.1995.9936 }}
*{{cite journal | author=Tang HY, Chaffotte AF, Thacher SM |title=Structural analysis of the predicted coiled-coil rod domain of the cytoplasmic bullous pemphigoid antigen (BPAG1). Empirical localization of the N-terminal globular domain-rod boundary. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9716-22 |year= 1996 |pmid= 8621649 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Hillier LD, Lennon G, Becker M, ''et al.'' |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807-28 |year= 1997 |pmid= 8889549 |doi= }}
*{{cite journal | author=Nagase T, Ishikawa K, Suyama M, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=5 |issue= 5 |pages= 277-86 |year= 1999 |pmid= 9872452 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HIST2H2BE... {November 17, 2007 12:39:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:40:00 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HIST2H2BE_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aoi.
| PDB = {{PDB2|1aoi}}, {{PDB2|1eqz}}, {{PDB2|1f66}}, {{PDB2|1hio}}, {{PDB2|1hq3}}, {{PDB2|1kx3}}, {{PDB2|1kx4}}, {{PDB2|1kx5}}, {{PDB2|1m18}}, {{PDB2|1m19}}, {{PDB2|1m1a}}, {{PDB2|1p34}}, {{PDB2|1p3a}}, {{PDB2|1p3b}}, {{PDB2|1p3f}}, {{PDB2|1p3g}}, {{PDB2|1p3i}}, {{PDB2|1p3k}}, {{PDB2|1p3l}}, {{PDB2|1p3m}}, {{PDB2|1p3o}}, {{PDB2|1p3p}}, {{PDB2|1s32}}, {{PDB2|1tzy}}, {{PDB2|1u35}}, {{PDB2|1zbb}}, {{PDB2|1zla}}, {{PDB2|2aro}}, {{PDB2|2cv5}}, {{PDB2|2f8n}}, {{PDB2|2fj7}}, {{PDB2|2hio}}, {{PDB2|2nzd}}
| Name = Histone cluster 2, H2be
| HGNCid = 4760
| Symbol = HIST2H2BE
| AltSymbols =; H2B.1; GL105; H2B; H2B/q; H2BFQ; MGC129733; MGC129734
| OMIM = 601831
| ECnumber =
| Homologene = 88682
| MGIid = 2448387
| GeneAtlas_image1 = PBB_GE_HIST2H2BE_202708_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}}
| Component = {{GNF_GO|id=GO:0000786 |text = nucleosome}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}}
| Process = {{GNF_GO|id=GO:0006334 |text = nucleosome assembly}} {{GNF_GO|id=GO:0007001 |text = chromosome organization and biogenesis (sensu Eukaryota)}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8349
| Hs_Ensembl = ENSG00000184678
| Hs_RefseqProtein = NP_003519
| Hs_RefseqmRNA = NM_003528
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 148122633
| Hs_GenLoc_end = 148124826
| Hs_Uniprot = Q16778
| Mm_EntrezGene = 319182
| Mm_Ensembl = ENSMUSG00000064168
| Mm_RefseqmRNA = NM_178197
| Mm_RefseqProtein = NP_835504
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 23550437
| Mm_GenLoc_end = 23550817
| Mm_Uniprot = Q64478
}}
}}
'''Histone cluster 2, H2be''', also known as '''HIST2H2BE''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H2BE histone cluster 2, H2be| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8349| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene encodes a member of the histone H2B family, and generates two transcripts through the use of the conserved stem-loop termination motif, and the polyA addition motif.<ref name="entrez">{{cite web | title = Entrez Gene: HIST2H2BE histone cluster 2, H2be| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8349| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Collart D, Romain PL, Huebner K, ''et al.'' |title=A human histone H2B.1 variant gene, located on chromosome 1, utilizes alternative 3' end processing. |journal=J. Cell. Biochem. |volume=50 |issue= 4 |pages= 374-85 |year= 1993 |pmid= 1469070 |doi= 10.1002/jcb.240500406 }}
*{{cite journal | author=Collart D, Ramsey-Ewing A, Bortell R, ''et al.'' |title=Isolation and characterization of a cDNA from a human histone H2B gene which is reciprocally expressed in relation to replication-dependent H2B histone genes during HL60 cell differentiation. |journal=Biochemistry |volume=30 |issue= 6 |pages= 1610-7 |year= 1991 |pmid= 1993178 |doi= }}
*{{cite journal | author=Jackson S, Brooks W, Jackson V |title=Dynamics of the interactions of histones H2A,H2B and H3,H4 with torsionally stressed DNA. |journal=Biochemistry |volume=33 |issue= 18 |pages= 5392-403 |year= 1994 |pmid= 8180162 |doi= }}
*{{cite journal | author=Frohm M, Gunne H, Bergman AC, ''et al.'' |title=Biochemical and antibacterial analysis of human wound and blister fluid. |journal=Eur. J. Biochem. |volume=237 |issue= 1 |pages= 86-92 |year= 1996 |pmid= 8620898 |doi= }}
*{{cite journal | author=Rodriguez P, Munroe D, Prawitt D, ''et al.'' |title=Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone. |journal=Genomics |volume=44 |issue= 3 |pages= 253-65 |year= 1997 |pmid= 9325046 |doi= 10.1006/geno.1997.4868 }}
*{{cite journal | author=El Kharroubi A, Piras G, Zensen R, Martin MA |title=Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2535-44 |year= 1998 |pmid= 9566873 |doi= }}
*{{cite journal | author=Zhang Y, Sun ZW, Iratni R, ''et al.'' |title=SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex. |journal=Mol. Cell |volume=1 |issue= 7 |pages= 1021-31 |year= 1998 |pmid= 9651585 |doi= }}
*{{cite journal | author=Lorain S, Quivy JP, Monier-Gavelle F, ''et al.'' |title=Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA. |journal=Mol. Cell. Biol. |volume=18 |issue= 9 |pages= 5546-56 |year= 1998 |pmid= 9710638 |doi= }}
*{{cite journal | author=Khan IU, Wallin R, Gupta RS, Kammer GM |title=Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T lymphocyte plasma membrane. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 18 |pages= 10425-30 |year= 1998 |pmid= 9724719 |doi= }}
*{{cite journal | author=Becker W, Weber Y, Wetzel K, ''et al.'' |title=Sequence characteristics, subcellular localization, and substrate specificity of DYRK-related kinases, a novel family of dual specificity protein kinases. |journal=J. Biol. Chem. |volume=273 |issue= 40 |pages= 25893-902 |year= 1998 |pmid= 9748265 |doi= }}
*{{cite journal | author=Allen MP, Zeng C, Schneider K, ''et al.'' |title=Growth arrest-specific gene 6 (Gas6)/adhesion related kinase (Ark) signaling promotes gonadotropin-releasing hormone neuronal survival via extracellular signal-regulated kinase (ERK) and Akt. |journal=Mol. Endocrinol. |volume=13 |issue= 2 |pages= 191-201 |year= 1999 |pmid= 9973250 |doi= }}
*{{cite journal | author=Piredda L, Farrace MG, Lo Bello M, ''et al.'' |title=Identification of 'tissue' transglutaminase binding proteins in neural cells committed to apoptosis. |journal=FASEB J. |volume=13 |issue= 2 |pages= 355-64 |year= 1999 |pmid= 9973324 |doi= }}
*{{cite journal | author=Carrier F, Georgel PT, Pourquier P, ''et al.'' |title=Gadd45, a p53-responsive stress protein, modifies DNA accessibility on damaged chromatin. |journal=Mol. Cell. Biol. |volume=19 |issue= 3 |pages= 1673-85 |year= 1999 |pmid= 10022855 |doi= }}
*{{cite journal | author=Kawasaki H, Schiltz L, Chiu R, ''et al.'' |title=ATF-2 has intrinsic histone acetyltransferase activity which is modulated by phosphorylation. |journal=Nature |volume=405 |issue= 6783 |pages= 195-200 |year= 2000 |pmid= 10821277 |doi= 10.1038/35012097 }}
*{{cite journal | author=Deng L, de la Fuente C, Fu P, ''et al.'' |title=Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. |journal=Virology |volume=277 |issue= 2 |pages= 278-95 |year= 2001 |pmid= 11080476 |doi= 10.1006/viro.2000.0593 }}
*{{cite journal | author=Baake M, Doenecke D, Albig W |title=Characterisation of nuclear localisation signals of the four human core histones. |journal=J. Cell. Biochem. |volume=81 |issue= 2 |pages= 333-46 |year= 2001 |pmid= 11241673 |doi= }}
*{{cite journal | author=Chadwick BP, Willard HF |title=A novel chromatin protein, distantly related to histone H2A, is largely excluded from the inactive X chromosome. |journal=J. Cell Biol. |volume=152 |issue= 2 |pages= 375-84 |year= 2001 |pmid= 11266453 |doi= }}
*{{cite journal | author=Freire J, Covelo G, Sarandeses C, ''et al.'' |title=Identification of nuclear-import and cell-cycle regulatory proteins that bind to prothymosin alpha. |journal=Biochem. Cell Biol. |volume=79 |issue= 2 |pages= 123-31 |year= 2001 |pmid= 11310559 |doi= }}
*{{cite journal | author=Nemergut ME, Mizzen CA, Stukenberg T, ''et al.'' |title=Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B. |journal=Science |volume=292 |issue= 5521 |pages= 1540-3 |year= 2001 |pmid= 11375490 |doi= 10.1126/science.292.5521.1540 }}
*{{cite journal | author=Deng L, Wang D, de la Fuente C, ''et al.'' |title=Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA. |journal=Virology |volume=289 |issue= 2 |pages= 312-26 |year= 2001 |pmid= 11689053 |doi= 10.1006/viro.2001.1129 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NCF1... {November 17, 2007 12:42:07 PM PST}
- SEARCH REDIRECT: Control Box Found: NCF1 {November 17, 2007 12:42:29 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:42:30 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:42:30 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:42:30 PM PST}
- UPDATED: Updated protein page: NCF1 {November 17, 2007 12:42:38 PM PST}
- INFO: Beginning work on PDCD6IP... {November 17, 2007 12:40:29 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:41:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PDCD6IP_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2oev.
| PDB = {{PDB2|2oev}}, {{PDB2|2oew}}, {{PDB2|2oex}}, {{PDB2|2ojq}}
| Name = Programmed cell death 6 interacting protein
| HGNCid = 8766
| Symbol = PDCD6IP
| AltSymbols =; AIP1; Alix; DRIP4; HP95; MGC17003
| OMIM = 608074
| ECnumber =
| Homologene = 22614
| MGIid = 1333753
| GeneAtlas_image1 = PBB_GE_PDCD6IP_217746_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0015031 |text = protein transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10015
| Hs_Ensembl = ENSG00000170248
| Hs_RefseqProtein = NP_037506
| Hs_RefseqmRNA = NM_013374
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 33814561
| Hs_GenLoc_end = 33886198
| Hs_Uniprot = Q8WUM4
| Mm_EntrezGene = 18571
| Mm_Ensembl = ENSMUSG00000032504
| Mm_RefseqmRNA = NM_011052
| Mm_RefseqProtein = NP_035182
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 113501953
| Mm_GenLoc_end = 113556927
| Mm_Uniprot = Q3TED2
}}
}}
'''Programmed cell death 6 interacting protein''', also known as '''PDCD6IP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PDCD6IP programmed cell death 6 interacting protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10015| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein thought to participate in programmed cell death. Studies using mouse cells have shown that overexpression of this protein can block apoptosis. In addition, the product of this gene binds to the product of the PDCD6 gene, a protein required for apoptosis, in a calcium-dependent manner. This gene product also binds to endophilins, proteins that regulate membrane shape during endocytosis. Overexpression of this gene product and endophilins results in cytoplasmic vacuolization which may be partly responsible for the protection against cell death.<ref name="entrez">{{cite web | title = Entrez Gene: PDCD6IP programmed cell death 6 interacting protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10015| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wood JD, Yuan J, Margolis RL, ''et al.'' |title=Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins. |journal=Mol. Cell. Neurosci. |volume=11 |issue= 3 |pages= 149-60 |year= 1998 |pmid= 9647693 |doi= 10.1006/mcne.1998.0677 }}
*{{cite journal | author=Vito P, Pellegrini L, Guiet C, D'Adamio L |title=Cloning of AIP1, a novel protein that associates with the apoptosis-linked gene ALG-2 in a Ca2+-dependent reaction. |journal=J. Biol. Chem. |volume=274 |issue= 3 |pages= 1533-40 |year= 1999 |pmid= 9880530 |doi= }}
*{{cite journal | author=Missotten M, Nichols A, Rieger K, Sadoul R |title=Alix, a novel mouse protein undergoing calcium-dependent interaction with the apoptosis-linked-gene 2 (ALG-2) protein. |journal=Cell Death Differ. |volume=6 |issue= 2 |pages= 124-9 |year= 1999 |pmid= 10200558 |doi= 10.1038/sj.cdd.4400456 }}
*{{cite journal | author=Nagase T, Kikuno R, Ishikawa KI, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=7 |issue= 1 |pages= 65-73 |year= 2000 |pmid= 10718198 |doi= }}
*{{cite journal | author=Wu Y, Pan S, Che S, ''et al.'' |title=Overexpression of Hp95 induces G1 phase arrest in confluent HeLa cells. |journal=Differentiation |volume=67 |issue= 4-5 |pages= 139-53 |year= 2002 |pmid= 11683497 |doi= }}
*{{cite journal | author=Satoh H, Shibata H, Nakano Y, ''et al.'' |title=ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-dependent manner. |journal=Biochem. Biophys. Res. Commun. |volume=291 |issue= 5 |pages= 1166-72 |year= 2002 |pmid= 11883939 |doi= 10.1006/bbrc.2002.6600 }}
*{{cite journal | author=Chatellard-Causse C, Blot B, Cristina N, ''et al.'' |title=Alix (ALG-2-interacting protein X), a protein involved in apoptosis, binds to endophilins and induces cytoplasmic vacuolization. |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 29108-15 |year= 2002 |pmid= 12034747 |doi= 10.1074/jbc.M204019200 }}
*{{cite journal | author=Wu Y, Pan S, Luo W, ''et al.'' |title=Hp95 promotes anoikis and inhibits tumorigenicity of HeLa cells. |journal=Oncogene |volume=21 |issue= 44 |pages= 6801-8 |year= 2002 |pmid= 12360406 |doi= 10.1038/sj.onc.1205849 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Vincent O, Rainbow L, Tilburn J, ''et al.'' |title=YPXL/I is a protein interaction motif recognized by aspergillus PalA and its human homologue, AIP1/Alix. |journal=Mol. Cell. Biol. |volume=23 |issue= 5 |pages= 1647-55 |year= 2003 |pmid= 12588984 |doi= }}
*{{cite journal | author=Schmidt MH, Chen B, Randazzo LM, Bogler O |title=SETA/CIN85/Ruk and its binding partner AIP1 associate with diverse cytoskeletal elements, including FAKs, and modulate cell adhesion. |journal=J. Cell. Sci. |volume=116 |issue= Pt 14 |pages= 2845-55 |year= 2004 |pmid= 12771190 |doi= 10.1242/jcs.00522 }}
*{{cite journal | author=Katoh K, Shibata H, Suzuki H, ''et al.'' |title=The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting. |journal=J. Biol. Chem. |volume=278 |issue= 40 |pages= 39104-13 |year= 2003 |pmid= 12860994 |doi= 10.1074/jbc.M301604200 }}
*{{cite journal | author=Leonard D, Ajuh P, Lamond AI, Legerski RJ |title=hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing. |journal=Biochem. Biophys. Res. Commun. |volume=308 |issue= 4 |pages= 793-801 |year= 2003 |pmid= 12927788 |doi= }}
*{{cite journal | author=Strack B, Calistri A, Craig S, ''et al.'' |title=AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. |journal=Cell |volume=114 |issue= 6 |pages= 689-99 |year= 2003 |pmid= 14505569 |doi= }}
*{{cite journal | author=von Schwedler UK, Stuchell M, Müller B, ''et al.'' |title=The protein network of HIV budding. |journal=Cell |volume=114 |issue= 6 |pages= 701-13 |year= 2003 |pmid= 14505570 |doi= }}
*{{cite journal | author=Martin-Serrano J, Yarovoy A, Perez-Caballero D, ''et al.'' |title=Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 21 |pages= 12414-9 |year= 2003 |pmid= 14519844 |doi= 10.1073/pnas.2133846100 }}
*{{cite journal | author=Peck JW, Bowden ET, Burbelo PD |title=Structure and function of human Vps20 and Snf7 proteins. |journal=Biochem. J. |volume=377 |issue= Pt 3 |pages= 693-700 |year= 2004 |pmid= 14583093 |doi= 10.1042/BJ20031347 }}
*{{cite journal | author=Katoh K, Shibata H, Hatta K, Maki M |title=CHMP4b is a major binding partner of the ALG-2-interacting protein Alix among the three CHMP4 isoforms. |journal=Arch. Biochem. Biophys. |volume=421 |issue= 1 |pages= 159-65 |year= 2004 |pmid= 14678797 |doi= }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Matsuo H, Chevallier J, Mayran N, ''et al.'' |title=Role of LBPA and Alix in multivesicular liposome formation and endosome organization. |journal=Science |volume=303 |issue= 5657 |pages= 531-4 |year= 2004 |pmid= 14739459 |doi= 10.1126/science.1092425 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRPH2... {November 17, 2007 12:32:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:33:06 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Peripherin 2 (retinal degeneration, slow)
| HGNCid = 9942
| Symbol = PRPH2
| AltSymbols =; PRPH; AOFMD; AVMD; RDS; RP7; TSPAN22; rd2
| OMIM = 179605
| ECnumber =
| Homologene = 273
| MGIid = 102791
| GeneAtlas_image1 = PBB_GE_PRPH2_206625_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5961
| Hs_Ensembl = ENSG00000112619
| Hs_RefseqProtein = NP_000313
| Hs_RefseqmRNA = NM_000322
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 42772318
| Hs_GenLoc_end = 42798290
| Hs_Uniprot = P23942
| Mm_EntrezGene = 19133
| Mm_Ensembl = ENSMUSG00000023978
| Mm_RefseqmRNA = NM_008938
| Mm_RefseqProtein = NP_032964
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 46373676
| Mm_GenLoc_end = 46388117
| Mm_Uniprot = Q3UWK3
}}
}}
'''Peripherin 2 (retinal degeneration, slow)''', also known as '''PRPH2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRPH2 peripherin 2 (retinal degeneration, slow)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5961| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility. This encoded protein is a cell surface glycoprotein found in the outer segment of both rod and cone photoreceptor cells. It may function as an adhesion molecule involved in stabilization and compaction of outer segment disks or in the maintenance of the curvature of the rim. This protein is essential for disk morphogenesis. Defects in this gene are associated with both central and peripheral retinal degenerations. Some of the various phenotypically different disorders are autosomal dominant retinitis pigmentosa, progressive macular degeneration, macular dystrophy and retinitis pigmentosa digenic.<ref name="entrez">{{cite web | title = Entrez Gene: PRPH2 peripherin 2 (retinal degeneration, slow)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5961| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Berditchevski F |title=Complexes of tetraspanins with integrins: more than meets the eye. |journal=J. Cell. Sci. |volume=114 |issue= Pt 23 |pages= 4143-51 |year= 2002 |pmid= 11739647 |doi= }}
*{{cite journal | author=Boesze-Battaglia K, Goldberg AF |title=Photoreceptor renewal: a role for peripherin/rds. |journal=Int. Rev. Cytol. |volume=217 |issue= |pages= 183-225 |year= 2002 |pmid= 12019563 |doi= }}
*{{cite journal | author=Farrar GJ, Kenna P, Jordan SA, ''et al.'' |title=Autosomal dominant retinitis pigmentosa: a novel mutation at the peripherin/RDS locus in the original 6p-linked pedigree. |journal=Genomics |volume=14 |issue= 3 |pages= 805-7 |year= 1992 |pmid= 1427912 |doi= }}
*{{cite journal | author=Jordan SA, Farrar GJ, Kumar-Singh R, ''et al.'' |title=Autosomal dominant retinitis pigmentosa (adRP; RP6): cosegregation of RP6 and the peripherin-RDS locus in a late-onset family of Irish origin. |journal=Am. J. Hum. Genet. |volume=50 |issue= 3 |pages= 634-9 |year= 1992 |pmid= 1539599 |doi= }}
*{{cite journal | author=Travis GH, Christerson L, Danielson PE, ''et al.'' |title=The human retinal degeneration slow (RDS) gene: chromosome assignment and structure of the mRNA. |journal=Genomics |volume=10 |issue= 3 |pages= 733-9 |year= 1991 |pmid= 1679750 |doi= }}
*{{cite journal | author=Kajiwara K, Hahn LB, Mukai S, ''et al.'' |title=Mutations in the human retinal degeneration slow gene in autosomal dominant retinitis pigmentosa. |journal=Nature |volume=354 |issue= 6353 |pages= 480-3 |year= 1992 |pmid= 1684223 |doi= 10.1038/354480a0 }}
*{{cite journal | author=Farrar GJ, Kenna P, Jordan SA, ''et al.'' |title=A three-base-pair deletion in the peripherin-RDS gene in one form of retinitis pigmentosa. |journal=Nature |volume=354 |issue= 6353 |pages= 478-80 |year= 1992 |pmid= 1749427 |doi= 10.1038/354478a0 }}
*{{cite journal | author=Davies K |title=Human genetics. Mapping the way forward. |journal=Nature |volume=353 |issue= 6347 |pages= 798-9 |year= 1991 |pmid= 1944554 |doi= 10.1038/353798a0 }}
*{{cite journal | author=Connell G, Bascom R, Molday L, ''et al.'' |title=Photoreceptor peripherin is the normal product of the gene responsible for retinal degeneration in the rds mouse. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 3 |pages= 723-6 |year= 1991 |pmid= 1992463 |doi= }}
*{{cite journal | author=Travis GH, Brennan MB, Danielson PE, ''et al.'' |title=Identification of a photoreceptor-specific mRNA encoded by the gene responsible for retinal degeneration slow (rds). |journal=Nature |volume=338 |issue= 6210 |pages= 70-3 |year= 1989 |pmid= 2918924 |doi= 10.1038/338070a0 }}
*{{cite journal | author=Reig C, Serra A, Gean E, ''et al.'' |title=A point mutation in the RDS-peripherin gene in a Spanish family with central areolar choroidal dystrophy. |journal=Ophthalmic Genet. |volume=16 |issue= 2 |pages= 39-44 |year= 1996 |pmid= 7493155 |doi= }}
*{{cite journal | author=Feist RM, White MF, Skalka H, Stone EM |title=Choroidal neovascularization in a patient with adult foveomacular dystrophy and a mutation in the retinal degeneration slow gene (Pro 210 Arg) |journal=Am. J. Ophthalmol. |volume=118 |issue= 2 |pages= 259-60 |year= 1994 |pmid= 7519821 |doi= }}
*{{cite journal | author=Gorin MB, Jackson KE, Ferrell RE, ''et al.'' |title=A peripherin/retinal degeneration slow mutation (Pro-210-Arg) associated with macular and peripheral retinal degeneration. |journal=Ophthalmology |volume=102 |issue= 2 |pages= 246-55 |year= 1995 |pmid= 7862413 |doi= }}
*{{cite journal | author=Grüning G, Millan JM, Meins M, ''et al.'' |title=Mutations in the human peripherin/RDS gene associated with autosomal dominant retinitis pigmentosa. |journal=Hum. Mutat. |volume=3 |issue= 3 |pages= 321-3 |year= 1994 |pmid= 8019570 |doi= 10.1002/humu.1380030326 }}
*{{cite journal | author=Kikawa E, Nakazawa M, Chida Y, ''et al.'' |title=A novel mutation (Asn244Lys) in the peripherin/RDS gene causing autosomal dominant retinitis pigmentosa associated with bull's-eye maculopathy detected by nonradioisotopic SSCP. |journal=Genomics |volume=20 |issue= 1 |pages= 137-9 |year= 1994 |pmid= 8020945 |doi= 10.1006/geno.1994.1142 }}
*{{cite journal | author=Farrar GJ, Kenna P, Jordan SA, ''et al.'' |title=Autosomal dominant retinitis pigmentosa: a novel mutation at the peripherin/RDS locus in the original 6p-linked pedigree. |journal=Genomics |volume=15 |issue= 2 |pages= 466 |year= 1993 |pmid= 8449524 |doi= }}
*{{cite journal | author=Nichols BE, Sheffield VC, Vandenburgh K, ''et al.'' |title=Butterfly-shaped pigment dystrophy of the fovea caused by a point mutation in codon 167 of the RDS gene. |journal=Nat. Genet. |volume=3 |issue= 3 |pages= 202-7 |year= 1993 |pmid= 8485574 |doi= 10.1038/ng0393-202 }}
*{{cite journal | author=Wells J, Wroblewski J, Keen J, ''et al.'' |title=Mutations in the human retinal degeneration slow (RDS) gene can cause either retinitis pigmentosa or macular dystrophy. |journal=Nat. Genet. |volume=3 |issue= 3 |pages= 213-8 |year= 1993 |pmid= 8485576 |doi= 10.1038/ng0393-213 }}
*{{cite journal | author=Keen TJ, Inglehearn CF |title=Mutations and polymorphisms in the human peripherin-RDS gene and their involvement in inherited retinal degeneration. |journal=Hum. Mutat. |volume=8 |issue= 4 |pages= 297-303 |year= 1997 |pmid= 8956033 |doi= 10.1002/(SICI)1098-1004(1996)8:4<297::AID-HUMU1>3.0.CO;2-5 }}
*{{cite journal | author=Felbor U, Schilling H, Weber BH |title=Adult vitelliform macular dystrophy is frequently associated with mutations in the peripherin/RDS gene. |journal=Hum. Mutat. |volume=10 |issue= 4 |pages= 301-9 |year= 1997 |pmid= 9338584 |doi= 10.1002/(SICI)1098-1004(1997)10:4<301::AID-HUMU6>3.0.CO;2-J }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSME3... {November 17, 2007 12:41:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:42:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Proteasome (prosome, macropain) activator subunit 3 (PA28 gamma; Ki)
| HGNCid = 9570
| Symbol = PSME3
| AltSymbols =; Ki; PA28-gamma; PA28G; REG-GAMMA
| OMIM = 605129
| ECnumber =
| Homologene = 2111
| MGIid = 1096366
| GeneAtlas_image1 = PBB_GE_PSME3_200988_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSME3_200987_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_PSME3_209852_x_at_tn.png
| Function = {{GNF_GO|id=GO:0008538 |text = proteasome activator activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0000502 |text = proteasome complex (sensu Eukaryota)}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0008537 |text = proteasome activator complex}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10197
| Hs_Ensembl = ENSG00000131467
| Hs_RefseqProtein = NP_005780
| Hs_RefseqmRNA = NM_005789
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 38238949
| Hs_GenLoc_end = 38249301
| Hs_Uniprot = P61289
| Mm_EntrezGene = 19192
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_011192
| Mm_RefseqProtein = NP_035322
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Proteasome (prosome, macropain) activator subunit 3 (PA28 gamma; Ki)''', also known as '''PSME3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSME3 proteasome (prosome, macropain) activator subunit 3 (PA28 gamma; Ki)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10197| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. The immunoproteasome contains an alternate regulator, referred to as the 11S regulator or PA28, that replaces the 19S regulator. Three subunits (alpha, beta and gamma) of the 11S regulator have been identified. This gene encodes the gamma subunit of the 11S regulator. Six gamma subunits combine to form a homohexameric ring. Two transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: PSME3 proteasome (prosome, macropain) activator subunit 3 (PA28 gamma; Ki)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10197| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue= |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
*{{cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi= }}
*{{cite journal | author=Nikaido T, Shimada K, Shibata M, ''et al.'' |title=Cloning and nucleotide sequence of cDNA for Ki antigen, a highly conserved nuclear protein detected with sera from patients with systemic lupus erythematosus. |journal=Clin. Exp. Immunol. |volume=79 |issue= 2 |pages= 209-14 |year= 1990 |pmid= 1968796 |doi= }}
*{{cite journal | author=Miki Y, Swensen J, Shattuck-Eidens D, ''et al.'' |title=A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1. |journal=Science |volume=266 |issue= 5182 |pages= 66-71 |year= 1994 |pmid= 7545954 |doi= }}
*{{cite journal | author=Harshman K, Bell R, Rosenthal J, ''et al.'' |title=Comparison of the positional cloning methods used to isolate the BRCA1 gene. |journal=Hum. Mol. Genet. |volume=4 |issue= 8 |pages= 1259-66 |year= 1995 |pmid= 7581362 |doi= }}
*{{cite journal | author=Jacob A, Kandpal G, Patanjali SR, Kandpal RP |title=Molecular cloning and expression pattern of genes from a 470 Kb region near BRCA1 locus on chromosome 17q21. |journal=Oncogene |volume=11 |issue= 5 |pages= 981-6 |year= 1995 |pmid= 7675458 |doi= }}
*{{cite journal | author=Albertsen HM, Smith SA, Mazoyer S, ''et al.'' |title=A physical map and candidate genes in the BRCA1 region on chromosome 17q12-21. |journal=Nat. Genet. |volume=7 |issue= 4 |pages= 472-9 |year= 1994 |pmid= 7951316 |doi= 10.1038/ng0894-472 }}
*{{cite journal | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi= }}
*{{cite journal | author=Kandil E, Kohda K, Ishibashi T, ''et al.'' |title=PA28 subunits of the mouse proteasome: primary structures and chromosomal localization of the genes. |journal=Immunogenetics |volume=46 |issue= 4 |pages= 337-44 |year= 1997 |pmid= 9218537 |doi= }}
*{{cite journal | author=McCusker D, Jones T, Sheer D, Trowsdale J |title=Genetic relationships of the genes encoding the human proteasome beta subunits and the proteasome PA28 complex. |journal=Genomics |volume=45 |issue= 2 |pages= 362-7 |year= 1998 |pmid= 9344661 |doi= 10.1006/geno.1997.4948 }}
*{{cite journal | author=Knowlton JR, Johnston SC, Whitby FG, ''et al.'' |title=Structure of the proteasome activator REGalpha (PA28alpha). |journal=Nature |volume=390 |issue= 6660 |pages= 639-43 |year= 1998 |pmid= 9403698 |doi= 10.1038/37670 }}
*{{cite journal | author=Kohda K, Ishibashi T, Shimbara N, ''et al.'' |title=Characterization of the mouse PA28 activator complex gene family: complete organizations of the three member genes and a physical map of the approximately 150-kb region containing the alpha- and beta-subunit genes. |journal=J. Immunol. |volume=160 |issue= 10 |pages= 4923-35 |year= 1998 |pmid= 9590240 |doi= }}
*{{cite journal | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi= }}
*{{cite journal | author=Wójcik C, Tanaka K, Paweletz N, ''et al.'' |title=Proteasome activator (PA28) subunits, alpha, beta and gamma (Ki antigen) in NT2 neuronal precursor cells and HeLa S3 cells. |journal=Eur. J. Cell Biol. |volume=77 |issue= 2 |pages= 151-60 |year= 1999 |pmid= 9840465 |doi= }}
*{{cite journal | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
*{{cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
*{{cite journal | author=Araya R, Takahashi R, Nomura Y |title=Yeast two-hybrid screening using constitutive-active caspase-7 as bait in the identification of PA28gamma as an effector caspase substrate. |journal=Cell Death Differ. |volume=9 |issue= 3 |pages= 322-8 |year= 2002 |pmid= 11859414 |doi= 10.1038/sj/cdd/4400949 }}
*{{cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
*{{cite journal | author=Huang X, Seifert U, Salzmann U, ''et al.'' |title=The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing. |journal=J. Mol. Biol. |volume=323 |issue= 4 |pages= 771-82 |year= 2002 |pmid= 12419264 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTPN13... {November 17, 2007 12:31:08 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:32:31 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PTPN13_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1d5g.
| PDB = {{PDB2|1d5g}}, {{PDB2|1gm1}}, {{PDB2|1ozi}}, {{PDB2|1q7x}}, {{PDB2|1vj6}}, {{PDB2|1wch}}, {{PDB2|3pdz}}
| Name = Protein tyrosine phosphatase, non-receptor type 13 (APO-1/CD95 (Fas)-associated phosphatase)
| HGNCid = 9646
| Symbol = PTPN13
| AltSymbols =; DKFZp686J1497; FAP-1; PNP1; PTP-BAS; PTP-BL; PTP1E; PTPL1; PTPLE
| OMIM = 600267
| ECnumber =
| Homologene = 7909
| MGIid = 103293
| GeneAtlas_image1 = PBB_GE_PTPN13_204201_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004726 |text = non-membrane spanning protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}}
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5783
| Hs_Ensembl = ENSG00000163629
| Hs_RefseqProtein = NP_006255
| Hs_RefseqmRNA = NM_006264
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 87734909
| Hs_GenLoc_end = 87955326
| Hs_Uniprot = Q12923
| Mm_EntrezGene = 19249
| Mm_Ensembl = ENSMUSG00000034573
| Mm_RefseqmRNA = NM_011204
| Mm_RefseqProtein = NP_035334
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 103665481
| Mm_GenLoc_end = 103838654
| Mm_Uniprot = Q6PG62
}}
}}
'''Protein tyrosine phosphatase, non-receptor type 13 (APO-1/CD95 (Fas)-associated phosphatase)''', also known as '''PTPN13''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPN13 protein tyrosine phosphatase, non-receptor type 13 (APO-1/CD95 (Fas)-associated phosphatase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5783| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP is a large protein that possesses a PTP domain at C-terminus, and multiple noncatalytic domains, which include a domain with similarity to band 4.1 superfamily of cytoskeletal-associated proteins, a region consisting of five PDZ domains, and a leucine zipper motif. This PTP was found to interact with, and dephosphorylate Fas receptor, as well as IkappaBalpha through the PDZ domains, which suggested its role in Fas mediated programmed cell death. This PTP was also shown to interact with GTPase-activating protein, and thus may function as a regulator of Rho signaling pathway. Four alternatively spliced transcript variants, which encode distinct proteins, have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: PTPN13 protein tyrosine phosphatase, non-receptor type 13 (APO-1/CD95 (Fas)-associated phosphatase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5783| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sato T, Irie S, Kitada S, Reed JC |title=FAP-1: a protein tyrosine phosphatase that associates with Fas. |journal=Science |volume=268 |issue= 5209 |pages= 411-5 |year= 1995 |pmid= 7536343 |doi= }}
*{{cite journal | author=Saras J, Claesson-Welsh L, Heldin CH, Gonez LJ |title=Cloning and characterization of PTPL1, a protein tyrosine phosphatase with similarities to cytoskeletal-associated proteins. |journal=J. Biol. Chem. |volume=269 |issue= 39 |pages= 24082-9 |year= 1994 |pmid= 7929060 |doi= }}
*{{cite journal | author=Banville D, Ahmad S, Stocco R, Shen SH |title=A novel protein-tyrosine phosphatase with homology to both the cytoskeletal proteins of the band 4.1 family and junction-associated guanylate kinases. |journal=J. Biol. Chem. |volume=269 |issue= 35 |pages= 22320-7 |year= 1994 |pmid= 8071359 |doi= }}
*{{cite journal | author=Maekawa K, Imagawa N, Nagamatsu M, Harada S |title=Molecular cloning of a novel protein-tyrosine phosphatase containing a membrane-binding domain and GLGF repeats. |journal=FEBS Lett. |volume=337 |issue= 2 |pages= 200-6 |year= 1994 |pmid= 8287977 |doi= }}
*{{cite journal | author=Inazawa J, Ariyama T, Abe T, ''et al.'' |title=PTPN13, a fas-associated protein tyrosine phosphatase, is located on the long arm of chromosome 4 at band q21.3. |journal=Genomics |volume=31 |issue= 2 |pages= 240-2 |year= 1997 |pmid= 8824809 |doi= 10.1006/geno.1996.0039 }}
*{{cite journal | author=Yanagisawa J, Takahashi M, Kanki H, ''et al.'' |title=The molecular interaction of Fas and FAP-1. A tripeptide blocker of human Fas interaction with FAP-1 promotes Fas-induced apoptosis. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8539-45 |year= 1997 |pmid= 9079683 |doi= }}
*{{cite journal | author=Saras J, Engström U, Góñez LJ, Heldin CH |title=Characterization of the interactions between PDZ domains of the protein-tyrosine phosphatase PTPL1 and the carboxyl-terminal tail of Fas. |journal=J. Biol. Chem. |volume=272 |issue= 34 |pages= 20979-81 |year= 1997 |pmid= 9261095 |doi= }}
*{{cite journal | author=Saras J, Franzén P, Aspenström P, ''et al.'' |title=A novel GTPase-activating protein for Rho interacts with a PDZ domain of the protein-tyrosine phosphatase PTPL1. |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24333-8 |year= 1997 |pmid= 9305890 |doi= }}
*{{cite journal | author=Ekiel I, Banville D, Shen SH, ''et al.'' |title=Main-chain signal assignment for the PDZ2 domain from human protein tyrosine phosphatase hPTP1E and its complex with a C-terminal peptide from the Fas receptor. |journal=J. Biomol. NMR |volume=12 |issue= 3 |pages= 455-6 |year= 1999 |pmid= 9835052 |doi= }}
*{{cite journal | author=Maekawa K, Imagawa N, Naito A, ''et al.'' |title=Association of protein-tyrosine phosphatase PTP-BAS with the transcription-factor-inhibitory protein IkappaBalpha through interaction between the PDZ1 domain and ankyrin repeats. |journal=Biochem. J. |volume=337 ( Pt 2) |issue= |pages= 179-84 |year= 1999 |pmid= 9882613 |doi= }}
*{{cite journal | author=Lin D, Gish GD, Songyang Z, Pawson T |title=The carboxyl terminus of B class ephrins constitutes a PDZ domain binding motif. |journal=J. Biol. Chem. |volume=274 |issue= 6 |pages= 3726-33 |year= 1999 |pmid= 9920925 |doi= }}
*{{cite journal | author=Murthy KK, Clark K, Fortin Y, ''et al.'' |title=ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E. |journal=J. Biol. Chem. |volume=274 |issue= 29 |pages= 20679-87 |year= 1999 |pmid= 10400701 |doi= }}
*{{cite journal | author=Cuppen E, van Ham M, Pepers B, ''et al.'' |title=Identification and molecular characterization of BP75, a novel bromodomain-containing protein. |journal=FEBS Lett. |volume=459 |issue= 3 |pages= 291-8 |year= 1999 |pmid= 10526152 |doi= }}
*{{cite journal | author=Irie S, Hachiya T, Rabizadeh S, ''et al.'' |title=Functional interaction of Fas-associated phosphatase-1 (FAP-1) with p75(NTR) and their effect on NF-kappaB activation. |journal=FEBS Lett. |volume=460 |issue= 2 |pages= 191-8 |year= 1999 |pmid= 10544233 |doi= }}
*{{cite journal | author=Lee SH, Shin MS, Park WS, ''et al.'' |title=Immunohistochemical localization of FAP-1, an inhibitor of Fas-mediated apoptosis, in normal and neoplastic human tissues. |journal=APMIS |volume=107 |issue= 12 |pages= 1101-8 |year= 2000 |pmid= 10660140 |doi= }}
*{{cite journal | author=Kozlov G, Gehring K, Ekiel I |title=Solution structure of the PDZ2 domain from human phosphatase hPTP1E and its interactions with C-terminal peptides from the Fas receptor. |journal=Biochemistry |volume=39 |issue= 10 |pages= 2572-80 |year= 2000 |pmid= 10704206 |doi= }}
*{{cite journal | author=Cuppen E, van Ham M, Wansink DG, ''et al.'' |title=The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL. |journal=Eur. J. Cell Biol. |volume=79 |issue= 4 |pages= 283-93 |year= 2000 |pmid= 10826496 |doi= }}
*{{cite journal | author=Erdmann KS, Kuhlmann J, Lessmann V, ''et al.'' |title=The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain. |journal=Oncogene |volume=19 |issue= 34 |pages= 3894-901 |year= 2000 |pmid= 10951583 |doi= 10.1038/sj.onc.1203725 }}
*{{cite journal | author=Nakai Y, Irie S, Sato TA |title=Identification of IkappaBalpha as a substrate of Fas-associated phosphatase-1. |journal=Eur. J. Biochem. |volume=267 |issue= 24 |pages= 7170-5 |year= 2001 |pmid= 11106428 |doi= }}
*{{cite journal | author=Gross C, Heumann R, Erdmann KS |title=The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif. |journal=FEBS Lett. |volume=496 |issue= 2-3 |pages= 101-4 |year= 2001 |pmid= 11356191 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PYY... {November 17, 2007 12:30:46 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:31:08 PM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PYY_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1qbf.
| PDB = {{PDB2|1qbf}}, {{PDB2|1ru5}}, {{PDB2|1ruu}}, {{PDB2|2dez}}, {{PDB2|2df0}}
| Name = Peptide YY
| HGNCid = 9748
| Symbol = PYY
| AltSymbols =; PYY1
| OMIM = 600781
| ECnumber =
| Homologene = 3066
| MGIid = 99924
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007586 |text = digestion}} {{GNF_GO|id=GO:0007631 |text = feeding behavior}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5697
| Hs_Ensembl = ENSG00000131096
| Hs_RefseqProtein = NP_004151
| Hs_RefseqmRNA = NM_004160
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 39385637
| Hs_GenLoc_end = 39437363
| Hs_Uniprot = P10082
| Mm_EntrezGene = 217212
| Mm_Ensembl = ENSMUSG00000017311
| Mm_RefseqmRNA = NM_145435
| Mm_RefseqProtein = NP_663410
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 101922932
| Mm_GenLoc_end = 101923442
| Mm_Uniprot = Q3V334
}}
}}
'''Peptide YY''', also known as '''PYY''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PYY peptide YY| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5697| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ekblad E, Sundler F |title=Distribution of pancreatic polypeptide and peptide YY. |journal=Peptides |volume=23 |issue= 2 |pages= 251-61 |year= 2002 |pmid= 11825640 |doi= }}
*{{cite journal | author=Sandström O, El-Salhy M |title=Ontogeny and the effect of aging on pancreatic polypeptide and peptide YY. |journal=Peptides |volume=23 |issue= 2 |pages= 263-7 |year= 2002 |pmid= 11825641 |doi= }}
*{{cite journal | author=Yang H |title=Central and peripheral regulation of gastric acid secretion by peptide YY. |journal=Peptides |volume=23 |issue= 2 |pages= 349-58 |year= 2002 |pmid= 11825649 |doi= }}
*{{cite journal | author=Naruse S, Kitagawa M, Ishiguro H, Hayakawa T |title=Feedback regulation of pancreatic secretion by peptide YY. |journal=Peptides |volume=23 |issue= 2 |pages= 359-65 |year= 2002 |pmid= 11825650 |doi= }}
*{{cite journal | author=Aponte GW |title=PYY-mediated fatty acid induced intestinal differentiation. |journal=Peptides |volume=23 |issue= 2 |pages= 367-76 |year= 2002 |pmid= 11825651 |doi= }}
*{{cite journal | author=Hagan MM |title=Peptide YY: a key mediator of orexigenic behavior. |journal=Peptides |volume=23 |issue= 2 |pages= 377-82 |year= 2002 |pmid= 11825652 |doi= }}
*{{cite journal | author=Mannon PJ |title=Peptide YY as a growth factor for intestinal epithelium. |journal=Peptides |volume=23 |issue= 2 |pages= 383-8 |year= 2002 |pmid= 11825653 |doi= }}
*{{cite journal | author=Tseng WW, Liu CD |title=Peptide YY and cancer: current findings and potential clinical applications. |journal=Peptides |volume=23 |issue= 2 |pages= 389-95 |year= 2002 |pmid= 11825654 |doi= }}
*{{cite journal | author=El-Salhy M, Suhr O, Danielsson A |title=Peptide YY in gastrointestinal disorders. |journal=Peptides |volume=23 |issue= 2 |pages= 397-402 |year= 2002 |pmid= 11825655 |doi= }}
*{{cite journal | author=Imamura M |title=Effects of surgical manipulation of the intestine on peptide YY and its physiology. |journal=Peptides |volume=23 |issue= 2 |pages= 403-7 |year= 2002 |pmid= 11825656 |doi= }}
*{{cite journal | author=Beglinger C, Degen L |title=Gastrointestinal satiety signals in humans--physiologic roles for GLP-1 and PYY? |journal=Physiol. Behav. |volume=89 |issue= 4 |pages= 460-4 |year= 2007 |pmid= 16828127 |doi= 10.1016/j.physbeh.2006.05.048 }}
*{{cite journal | author=Eberlein GA, Eysselein VE, Schaeffer M, ''et al.'' |title=A new molecular form of PYY: structural characterization of human PYY(3-36) and PYY(1-36). |journal=Peptides |volume=10 |issue= 4 |pages= 797-803 |year= 1989 |pmid= 2587421 |doi= }}
*{{cite journal | author=Facer P, Bishop AE, Cole GA, ''et al.'' |title=Developmental profile of chromogranin, hormonal peptides, and 5-hydroxytryptamine in gastrointestinal endocrine cells. |journal=Gastroenterology |volume=97 |issue= 1 |pages= 48-57 |year= 1989 |pmid= 2721879 |doi= }}
*{{cite journal | author=Tatemoto K, Nakano I, Makk G, ''et al.'' |title=Isolation and primary structure of human peptide YY. |journal=Biochem. Biophys. Res. Commun. |volume=157 |issue= 2 |pages= 713-7 |year= 1989 |pmid= 3202875 |doi= }}
*{{cite journal | author=Lukinius AI, Ericsson JL, Lundqvist MK, Wilander EM |title=Ultrastructural localization of serotonin and polypeptide YY (PYY) in endocrine cells of the human rectum. |journal=J. Histochem. Cytochem. |volume=34 |issue= 6 |pages= 719-26 |year= 1986 |pmid= 3517149 |doi= }}
*{{cite journal | author=Adrian TE, Ferri GL, Bacarese-Hamilton AJ, ''et al.'' |title=Human distribution and release of a putative new gut hormone, peptide YY. |journal=Gastroenterology |volume=89 |issue= 5 |pages= 1070-7 |year= 1985 |pmid= 3840109 |doi= }}
*{{cite journal | author=Lundell I, Blomqvist AG, Berglund MM, ''et al.'' |title=Cloning of a human receptor of the NPY receptor family with high affinity for pancreatic polypeptide and peptide YY. |journal=J. Biol. Chem. |volume=270 |issue= 49 |pages= 29123-8 |year= 1996 |pmid= 7493937 |doi= }}
*{{cite journal | author=Bard JA, Walker MW, Branchek TA, Weinshank RL |title=Cloning and functional expression of a human Y4 subtype receptor for pancreatic polypeptide, neuropeptide Y, and peptide YY. |journal=J. Biol. Chem. |volume=270 |issue= 45 |pages= 26762-5 |year= 1995 |pmid= 7592911 |doi= }}
*{{cite journal | author=Hort Y, Baker E, Sutherland GR, ''et al.'' |title=Gene duplication of the human peptide YY gene (PYY) generated the pancreatic polypeptide gene (PPY) on chromosome 17q21.1. |journal=Genomics |volume=26 |issue= 1 |pages= 77-83 |year= 1995 |pmid= 7782089 |doi= }}
*{{cite journal | author=Kohri K, Nata K, Yonekura H, ''et al.'' |title=Cloning and structural determination of human peptide YY cDNA and gene. |journal=Biochim. Biophys. Acta |volume=1173 |issue= 3 |pages= 345-9 |year= 1993 |pmid= 8318545 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RIPK1... {November 17, 2007 12:40:00 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:40:29 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Receptor (TNFRSF)-interacting serine-threonine kinase 1
| HGNCid = 10019
| Symbol = RIPK1
| AltSymbols =; RIP; FLJ39204
| OMIM = 603453
| ECnumber =
| Homologene = 2820
| MGIid = 108212
| GeneAtlas_image1 = PBB_GE_RIPK1_209941_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8737
| Hs_Ensembl = ENSG00000137275
| Hs_RefseqProtein = NP_003795
| Hs_RefseqmRNA = NM_003804
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 3009212
| Hs_GenLoc_end = 3060418
| Hs_Uniprot = Q13546
| Mm_EntrezGene = 19766
| Mm_Ensembl = ENSMUSG00000021408
| Mm_RefseqmRNA = NM_009068
| Mm_RefseqProtein = NP_033094
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 34010339
| Mm_GenLoc_end = 34042635
| Mm_Uniprot = Q60855
}}
}}
'''Receptor (TNFRSF)-interacting serine-threonine kinase 1''', also known as '''RIPK1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RIPK1 receptor (TNFRSF)-interacting serine-threonine kinase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8737| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Festjens N, Vanden Berghe T, Cornelis S, Vandenabeele P |title=RIP1, a kinase on the crossroads of a cell's decision to live or die. |journal=Cell Death Differ. |volume=14 |issue= 3 |pages= 400-10 |year= 2007 |pmid= 17301840 |doi= 10.1038/sj.cdd.4402085 }}
*{{cite journal | author=Stanger BZ, Leder P, Lee TH, ''et al.'' |title=RIP: a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. |journal=Cell |volume=81 |issue= 4 |pages= 513-23 |year= 1995 |pmid= 7538908 |doi= }}
*{{cite journal | author=Hsu H, Huang J, Shu HB, ''et al.'' |title=TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. |journal=Immunity |volume=4 |issue= 4 |pages= 387-96 |year= 1996 |pmid= 8612133 |doi= }}
*{{cite journal | author=Takeuchi M, Rothe M, Goeddel DV |title=Anatomy of TRAF2. Distinct domains for nuclear factor-kappaB activation and association with tumor necrosis factor signaling proteins. |journal=J. Biol. Chem. |volume=271 |issue= 33 |pages= 19935-42 |year= 1996 |pmid= 8702708 |doi= }}
*{{cite journal | author=Duan H, Dixit VM |title=RAIDD is a new 'death' adaptor molecule. |journal=Nature |volume=385 |issue= 6611 |pages= 86-9 |year= 1997 |pmid= 8985253 |doi= 10.1038/385086a0 }}
*{{cite journal | author=Ahmad M, Srinivasula SM, Wang L, ''et al.'' |title=CRADD, a novel human apoptotic adaptor molecule for caspase-2, and FasL/tumor necrosis factor receptor-interacting protein RIP. |journal=Cancer Res. |volume=57 |issue= 4 |pages= 615-9 |year= 1997 |pmid= 9044836 |doi= }}
*{{cite journal | author=Chaudhary PM, Eby M, Jasmin A, ''et al.'' |title=Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-kappaB pathway. |journal=Immunity |volume=7 |issue= 6 |pages= 821-30 |year= 1998 |pmid= 9430227 |doi= }}
*{{cite journal | author=Juo P, Kuo CJ, Yuan J, Blenis J |title=Essential requirement for caspase-8/FLICE in the initiation of the Fas-induced apoptotic cascade. |journal=Curr. Biol. |volume=8 |issue= 18 |pages= 1001-8 |year= 1998 |pmid= 9740801 |doi= }}
*{{cite journal | author=Li Y, Kang J, Friedman J, ''et al.'' |title=Identification of a cell protein (FIP-3) as a modulator of NF-kappaB activity and as a target of an adenovirus inhibitor of tumor necrosis factor alpha-induced apoptosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 3 |pages= 1042-7 |year= 1999 |pmid= 9927690 |doi= }}
*{{cite journal | author=Yu PW, Huang BC, Shen M, ''et al.'' |title=Identification of RIP3, a RIP-like kinase that activates apoptosis and NFkappaB. |journal=Curr. Biol. |volume=9 |issue= 10 |pages= 539-42 |year= 1999 |pmid= 10339433 |doi= }}
*{{cite journal | author=Sanz L, Sanchez P, Lallena MJ, ''et al.'' |title=The interaction of p62 with RIP links the atypical PKCs to NF-kappaB activation. |journal=EMBO J. |volume=18 |issue= 11 |pages= 3044-53 |year= 1999 |pmid= 10356400 |doi= 10.1093/emboj/18.11.3044 }}
*{{cite journal | author=Sun X, Lee J, Navas T, ''et al.'' |title=RIP3, a novel apoptosis-inducing kinase. |journal=J. Biol. Chem. |volume=274 |issue= 24 |pages= 16871-5 |year= 1999 |pmid= 10358032 |doi= }}
*{{cite journal | author=Izumi KM, Cahir McFarland ED, Ting AT, ''et al.'' |title=The Epstein-Barr virus oncoprotein latent membrane protein 1 engages the tumor necrosis factor receptor-associated proteins TRADD and receptor-interacting protein (RIP) but does not induce apoptosis or require RIP for NF-kappaB activation. |journal=Mol. Cell. Biol. |volume=19 |issue= 8 |pages= 5759-67 |year= 1999 |pmid= 10409763 |doi= }}
*{{cite journal | author=Lin Y, Devin A, Rodriguez Y, Liu ZG |title=Cleavage of the death domain kinase RIP by caspase-8 prompts TNF-induced apoptosis. |journal=Genes Dev. |volume=13 |issue= 19 |pages= 2514-26 |year= 1999 |pmid= 10521396 |doi= }}
*{{cite journal | author=Chaudhary PM, Jasmin A, Eby MT, Hood L |title=Modulation of the NF-kappa B pathway by virally encoded death effector domains-containing proteins. |journal=Oncogene |volume=18 |issue= 42 |pages= 5738-46 |year= 1999 |pmid= 10523854 |doi= 10.1038/sj.onc.1202976 }}
*{{cite journal | author=Lewis J, Devin A, Miller A, ''et al.'' |title=Disruption of hsp90 function results in degradation of the death domain kinase, receptor-interacting protein (RIP), and blockage of tumor necrosis factor-induced nuclear factor-kappaB activation. |journal=J. Biol. Chem. |volume=275 |issue= 14 |pages= 10519-26 |year= 2000 |pmid= 10744744 |doi= }}
*{{cite journal | author=Kataoka T, Budd RC, Holler N, ''et al.'' |title=The caspase-8 inhibitor FLIP promotes activation of NF-kappaB and Erk signaling pathways. |journal=Curr. Biol. |volume=10 |issue= 11 |pages= 640-8 |year= 2000 |pmid= 10837247 |doi= }}
*{{cite journal | author=Inohara N, Koseki T, Lin J, ''et al.'' |title=An induced proximity model for NF-kappa B activation in the Nod1/RICK and RIP signaling pathways. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 27823-31 |year= 2000 |pmid= 10880512 |doi= 10.1074/jbc.M003415200 }}
*{{cite journal | author=Chaudhary PM, Eby MT, Jasmin A, ''et al.'' |title=Activation of the NF-kappaB pathway by caspase 8 and its homologs. |journal=Oncogene |volume=19 |issue= 39 |pages= 4451-60 |year= 2000 |pmid= 11002417 |doi= 10.1038/sj.onc.1203812 }}
*{{cite journal | author=Kim JW, Choi EJ, Joe CO |title=Activation of death-inducing signaling complex (DISC) by pro-apoptotic C-terminal fragment of RIP. |journal=Oncogene |volume=19 |issue= 39 |pages= 4491-9 |year= 2000 |pmid= 11002422 |doi= 10.1038/sj.onc.1203796 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC22A5... {November 17, 2007 12:33:41 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:34:09 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Solute carrier family 22 (organic cation transporter), member 5
| HGNCid = 10969
| Symbol = SLC22A5
| AltSymbols =; CDSP; FLJ46769; OCTN2
| OMIM = 603377
| ECnumber =
| Homologene = 68295
| MGIid = 1329012
| GeneAtlas_image1 = PBB_GE_SLC22A5_205074_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0015075 |text = ion transmembrane transporter activity}} {{GNF_GO|id=GO:0015226 |text = carnitine transporter activity}} {{GNF_GO|id=GO:0015293 |text = symporter activity}} {{GNF_GO|id=GO:0031402 |text = sodium ion binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006814 |text = sodium ion transport}} {{GNF_GO|id=GO:0015879 |text = carnitine transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6584
| Hs_Ensembl = ENSG00000197375
| Hs_RefseqProtein = NP_003051
| Hs_RefseqmRNA = NM_003060
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 131733343
| Hs_GenLoc_end = 131759205
| Hs_Uniprot = O76082
| Mm_EntrezGene = 20520
| Mm_Ensembl = ENSMUSG00000018900
| Mm_RefseqmRNA = NM_011396
| Mm_RefseqProtein = NP_035526
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 53707951
| Mm_GenLoc_end = 53735083
| Mm_Uniprot = Q3USA0
}}
}}
'''Solute carrier family 22 (organic cation transporter), member 5''', also known as '''SLC22A5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC22A5 solute carrier family 22 (organic cation transporter), member 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6584| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Polyspecific organic cation transporters in the liver, kidney, intestine, and other organs are critical for elimination of many endogenous small organic cations as well as a wide array of drugs and environmental toxins. The encoded protein is a plasma integral membrane protein which functions both as an organic cation transporter and as a sodium-dependent high affinity carnitine transporter. The encoded protein is involved in the active cellular uptake of carnitine. Mutations in this gene are the cause of systemic primary carnitine deficiency (CDSP), an autosomal recessive disorder manifested early in life by hypoketotic hypoglycemia and acute metabolic decompensation, and later in life by skeletal myopathy or cardiomyopathy.<ref name="entrez">{{cite web | title = Entrez Gene: SLC22A5 solute carrier family 22 (organic cation transporter), member 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6584| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Silverberg MS |title=OCTNs: will the real IBD5 gene please stand up? |journal=World J. Gastroenterol. |volume=12 |issue= 23 |pages= 3678-81 |year= 2006 |pmid= 16773684 |doi= }}
*{{cite journal | author=Matsuishi T, Hirata K, Terasawa K, ''et al.'' |title=Successful carnitine treatment in two siblings having lipid storage myopathy with hypertrophic cardiomyopathy. |journal=Neuropediatrics |volume=16 |issue= 1 |pages= 6-12 |year= 1985 |pmid= 3974805 |doi= }}
*{{cite journal | author=Wu X, Prasad PD, Leibach FH, Ganapathy V |title=cDNA sequence, transport function, and genomic organization of human OCTN2, a new member of the organic cation transporter family. |journal=Biochem. Biophys. Res. Commun. |volume=246 |issue= 3 |pages= 589-95 |year= 1998 |pmid= 9618255 |doi= 10.1006/bbrc.1998.8669 }}
*{{cite journal | author=Shoji Y, Koizumi A, Kayo T, ''et al.'' |title=Evidence for linkage of human primary systemic carnitine deficiency with D5S436: a novel gene locus on chromosome 5q. |journal=Am. J. Hum. Genet. |volume=63 |issue= 1 |pages= 101-8 |year= 1998 |pmid= 9634512 |doi= }}
*{{cite journal | author=Tamai I, Ohashi R, Nezu J, ''et al.'' |title=Molecular and functional identification of sodium ion-dependent, high affinity human carnitine transporter OCTN2. |journal=J. Biol. Chem. |volume=273 |issue= 32 |pages= 20378-82 |year= 1998 |pmid= 9685390 |doi= }}
*{{cite journal | author=Nezu J, Tamai I, Oku A, ''et al.'' |title=Primary systemic carnitine deficiency is caused by mutations in a gene encoding sodium ion-dependent carnitine transporter. |journal=Nat. Genet. |volume=21 |issue= 1 |pages= 91-4 |year= 1999 |pmid= 9916797 |doi= 10.1038/5030 }}
*{{cite journal | author=Tang NL, Ganapathy V, Wu X, ''et al.'' |title=Mutations of OCTN2, an organic cation/carnitine transporter, lead to deficient cellular carnitine uptake in primary carnitine deficiency. |journal=Hum. Mol. Genet. |volume=8 |issue= 4 |pages= 655-60 |year= 1999 |pmid= 10072434 |doi= }}
*{{cite journal | author=Burwinkel B, Kreuder J, Schweitzer S, ''et al.'' |title=Carnitine transporter OCTN2 mutations in systemic primary carnitine deficiency: a novel Arg169Gln mutation and a recurrent Arg282ter mutation associated with an unconventional splicing abnormality. |journal=Biochem. Biophys. Res. Commun. |volume=261 |issue= 2 |pages= 484-7 |year= 1999 |pmid= 10425211 |doi= 10.1006/bbrc.1999.1060 }}
*{{cite journal | author=Wu X, Huang W, Prasad PD, ''et al.'' |title=Functional characteristics and tissue distribution pattern of organic cation transporter 2 (OCTN2), an organic cation/carnitine transporter. |journal=J. Pharmacol. Exp. Ther. |volume=290 |issue= 3 |pages= 1482-92 |year= 1999 |pmid= 10454528 |doi= }}
*{{cite journal | author=Vaz FM, Scholte HR, Ruiter J, ''et al.'' |title=Identification of two novel mutations in OCTN2 of three patients with systemic carnitine deficiency. |journal=Hum. Genet. |volume=105 |issue= 1-2 |pages= 157-61 |year= 1999 |pmid= 10480371 |doi= }}
*{{cite journal | author=Koizumi A, Nozaki J, Ohura T, ''et al.'' |title=Genetic epidemiology of the carnitine transporter OCTN2 gene in a Japanese population and phenotypic characterization in Japanese pedigrees with primary systemic carnitine deficiency. |journal=Hum. Mol. Genet. |volume=8 |issue= 12 |pages= 2247-54 |year= 1999 |pmid= 10545605 |doi= }}
*{{cite journal | author=Seth P, Wu X, Huang W, ''et al.'' |title=Mutations in novel organic cation transporter (OCTN2), an organic cation/carnitine transporter, with differential effects on the organic cation transport function and the carnitine transport function. |journal=J. Biol. Chem. |volume=274 |issue= 47 |pages= 33388-92 |year= 1999 |pmid= 10559218 |doi= }}
*{{cite journal | author=Mayatepek E, Nezu J, Tamai I, ''et al.'' |title=Two novel missense mutations of the OCTN2 gene (W283R and V446F) in a patient with primary systemic carnitine deficiency. |journal=Hum. Mutat. |volume=15 |issue= 1 |pages= 118 |year= 2000 |pmid= 10612840 |doi= 10.1002/(SICI)1098-1004(200001)15:1<118::AID-HUMU28>3.0.CO;2-8 }}
*{{cite journal | author=Wang Y, Kelly MA, Cowan TM, Longo N |title=A missense mutation in the OCTN2 gene associated with residual carnitine transport activity. |journal=Hum. Mutat. |volume=15 |issue= 3 |pages= 238-45 |year= 2000 |pmid= 10679939 |doi= 10.1002/(SICI)1098-1004(200003)15:3<238::AID-HUMU4>3.0.CO;2-3 }}
*{{cite journal | author=Ohashi R, Tamai I, Inano A, ''et al.'' |title=Studies on functional sites of organic cation/carnitine transporter OCTN2 (SLC22A5) using a Ser467Cys mutant protein. |journal=J. Pharmacol. Exp. Ther. |volume=302 |issue= 3 |pages= 1286-94 |year= 2002 |pmid= 12183691 |doi= 10.1124/jpet.102.036004 }}
*{{cite journal | author=Rahbeeni Z, Vaz FM, Al-Hussein K, ''et al.'' |title=Identification of two novel mutations in OCTN2 from two Saudi patients with systemic carnitine deficiency. |journal=J. Inherit. Metab. Dis. |volume=25 |issue= 5 |pages= 363-9 |year= 2003 |pmid= 12408185 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Elimrani I, Lahjouji K, Seidman E, ''et al.'' |title=Expression and localization of organic cation/carnitine transporter OCTN2 in Caco-2 cells. |journal=Am. J. Physiol. Gastrointest. Liver Physiol. |volume=284 |issue= 5 |pages= G863-71 |year= 2003 |pmid= 12684216 |doi= 10.1152/ajpgi.00220.2002 }}
*{{cite journal | author=Karlic H, Lohninger A, Laschan C, ''et al.'' |title=Downregulation of carnitine acyltransferases and organic cation transporter OCTN2 in mononuclear cells in healthy elderly and patients with myelodysplastic syndromes. |journal=J. Mol. Med. |volume=81 |issue= 7 |pages= 435-42 |year= 2004 |pmid= 12802501 |doi= 10.1007/s00109-003-0447-6 }}
*{{cite journal | author=Amat di San Filippo C, Wang Y, Longo N |title=Functional domains in the carnitine transporter OCTN2, defective in primary carnitine deficiency. |journal=J. Biol. Chem. |volume=278 |issue= 48 |pages= 47776-84 |year= 2004 |pmid= 14506273 |doi= 10.1074/jbc.M307911200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SMARCA2... {November 17, 2007 12:34:09 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:35:08 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SMARCA2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2dat.
| PDB = {{PDB2|2dat}}
| Name = SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2
| HGNCid = 11098
| Symbol = SMARCA2
| AltSymbols =; SWI2; BAF190; BRM; FLJ36757; MGC74511; SNF2; SNF2L2; SNF2LA; Sth1p; hBRM; hSNF2a
| OMIM = 600014
| ECnumber =
| Homologene = 2308
| MGIid = 99603
| GeneAtlas_image1 = PBB_GE_SMARCA2_206542_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SMARCA2_206544_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_SMARCA2_217707_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004386 |text = helicase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6595
| Hs_Ensembl = ENSG00000080503
| Hs_RefseqProtein = NP_003061
| Hs_RefseqmRNA = NM_003070
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 2005342
| Hs_GenLoc_end = 2183624
| Hs_Uniprot = P51531
| Mm_EntrezGene = 67155
| Mm_Ensembl = ENSMUSG00000024921
| Mm_RefseqmRNA = NM_011416
| Mm_RefseqProtein = NP_035546
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 26672257
| Mm_GenLoc_end = 26845418
| Mm_Uniprot =
}}
}}
'''SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2''', also known as '''SMARCA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SMARCA2 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6595| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the SWI/SNF family of proteins and is highly similar to the brahma protein of Drosophila. Members of this family have helicase and ATPase activities and are thought to regulate transcription of certain genes by altering the chromatin structure around those genes. The encoded protein is part of the large ATP-dependent chromatin remodeling complex SNF/SWI, which is required for transcriptional activation of genes normally repressed by chromatin. Two transcript variants encoding different isoforms have been found for this gene, which contains a trinucleotide repeat (CAG) length polymorphism.<ref name="entrez">{{cite web | title = Entrez Gene: SMARCA2 SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6595| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Aves SJ, Hindley J, Phear GA, Tongue N |title=A fission yeast gene mapping close to suc1 encodes a protein containing two bromodomains. |journal=Mol. Gen. Genet. |volume=248 |issue= 4 |pages= 491-8 |year= 1995 |pmid= 7565614 |doi= }}
*{{cite journal | author=Muchardt C, Yaniv M, Mattei MG |title=Assignment of HBRM, the human homolog of S. cerevisiae SNF2/SWI2 and Drosophila brm genes, to chromosome region 9p23-p24, by in situ hybridization. |journal=Mamm. Genome |volume=5 |issue= 4 |pages= 241-3 |year= 1994 |pmid= 8012116 |doi= }}
*{{cite journal | author=Chiba H, Muramatsu M, Nomoto A, Kato H |title=Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and Drosophila brahma are transcriptional coactivators cooperating with the estrogen receptor and the retinoic acid receptor. |journal=Nucleic Acids Res. |volume=22 |issue= 10 |pages= 1815-20 |year= 1994 |pmid= 8208605 |doi= }}
*{{cite journal | author=Muchardt C, Yaniv M |title=A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm genes potentiates transcriptional activation by the glucocorticoid receptor. |journal=EMBO J. |volume=12 |issue= 11 |pages= 4279-90 |year= 1993 |pmid= 8223438 |doi= }}
*{{cite journal | author=Muchardt C, Reyes JC, Bourachot B, ''et al.'' |title=The hbrm and BRG-1 proteins, components of the human SNF/SWI complex, are phosphorylated and excluded from the condensed chromosomes during mitosis. |journal=EMBO J. |volume=15 |issue= 13 |pages= 3394-402 |year= 1996 |pmid= 8670841 |doi= }}
*{{cite journal | author=Wang W, Xue Y, Zhou S, ''et al.'' |title=Diversity and specialization of mammalian SWI/SNF complexes. |journal=Genes Dev. |volume=10 |issue= 17 |pages= 2117-30 |year= 1996 |pmid= 8804307 |doi= }}
*{{cite journal | author=Wang W, Côté J, Xue Y, ''et al.'' |title=Purification and biochemical heterogeneity of the mammalian SWI-SNF complex. |journal=EMBO J. |volume=15 |issue= 19 |pages= 5370-82 |year= 1996 |pmid= 8895581 |doi= }}
*{{cite journal | author=Ichinose H, Garnier JM, Chambon P, Losson R |title=Ligand-dependent interaction between the estrogen receptor and the human homologues of SWI2/SNF2. |journal=Gene |volume=188 |issue= 1 |pages= 95-100 |year= 1997 |pmid= 9099865 |doi= }}
*{{cite journal | author=Cho H, Orphanides G, Sun X, ''et al.'' |title=A human RNA polymerase II complex containing factors that modify chromatin structure. |journal=Mol. Cell. Biol. |volume=18 |issue= 9 |pages= 5355-63 |year= 1998 |pmid= 9710619 |doi= }}
*{{cite journal | author=Thaete C, Brett D, Monaghan P, ''et al.'' |title=Functional domains of the SYT and SYT-SSX synovial sarcoma translocation proteins and co-localization with the SNF protein BRM in the nucleus. |journal=Hum. Mol. Genet. |volume=8 |issue= 4 |pages= 585-91 |year= 1999 |pmid= 10072425 |doi= }}
*{{cite journal | author=Phelan ML, Sif S, Narlikar GJ, Kingston RE |title=Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits. |journal=Mol. Cell |volume=3 |issue= 2 |pages= 247-53 |year= 1999 |pmid= 10078207 |doi= }}
*{{cite journal | author=Lee DW, Zhang K, Ning ZQ, ''et al.'' |title=Proliferation-associated SNF2-like gene (PASG): a SNF2 family member altered in leukemia. |journal=Cancer Res. |volume=60 |issue= 13 |pages= 3612-22 |year= 2000 |pmid= 10910076 |doi= }}
*{{cite journal | author=Phelan ML, Schnitzler GR, Kingston RE |title=Octamer transfer and creation of stably remodeled nucleosomes by human SWI-SNF and its isolated ATPases. |journal=Mol. Cell. Biol. |volume=20 |issue= 17 |pages= 6380-9 |year= 2000 |pmid= 10938115 |doi= }}
*{{cite journal | author=Xue Y, Canman JC, Lee CS, ''et al.'' |title=The human SWI/SNF-B chromatin-remodeling complex is related to yeast rsc and localizes at kinetochores of mitotic chromosomes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 24 |pages= 13015-20 |year= 2001 |pmid= 11078522 |doi= 10.1073/pnas.240208597 }}
*{{cite journal | author=Machida Y, Murai K, Miyake K, Iijima S |title=Expression of chromatin remodeling factors during neural differentiation. |journal=J. Biochem. |volume=129 |issue= 1 |pages= 43-9 |year= 2001 |pmid= 11134956 |doi= }}
*{{cite journal | author=de la Serna IL, Carlson KA, Imbalzano AN |title=Mammalian SWI/SNF complexes promote MyoD-mediated muscle differentiation. |journal=Nat. Genet. |volume=27 |issue= 2 |pages= 187-90 |year= 2001 |pmid= 11175787 |doi= 10.1038/84826 }}
*{{cite journal | author=Ruhf ML, Braun A, Papoulas O, ''et al.'' |title=The domino gene of Drosophila encodes novel members of the SWI2/SNF2 family of DNA-dependent ATPases, which contribute to the silencing of homeotic genes. |journal=Development |volume=128 |issue= 8 |pages= 1429-41 |year= 2001 |pmid= 11262242 |doi= }}
*{{cite journal | author=Strobeck MW, Reisman DN, Gunawardena RW, ''et al.'' |title=Compensation of BRG-1 function by Brm: insight into the role of the core SWI-SNF subunits in retinoblastoma tumor suppressor signaling. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 4782-9 |year= 2002 |pmid= 11719516 |doi= 10.1074/jbc.M109532200 }}
*{{cite journal | author=Kato H, Tjernberg A, Zhang W, ''et al.'' |title=SYT associates with human SNF/SWI complexes and the C-terminal region of its fusion partner SSX1 targets histones. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 5498-505 |year= 2002 |pmid= 11734557 |doi= 10.1074/jbc.M108702200 }}
*{{cite journal | author=Mizutani T, Ito T, Nishina M, ''et al.'' |title=Maintenance of integrated proviral gene expression requires Brm, a catalytic subunit of SWI/SNF complex. |journal=J. Biol. Chem. |volume=277 |issue= 18 |pages= 15859-64 |year= 2002 |pmid= 11850427 |doi= 10.1074/jbc.M112421200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SMPD1... {November 17, 2007 12:35:08 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:35:35 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Sphingomyelin phosphodiesterase 1, acid lysosomal (acid sphingomyelinase)
| HGNCid = 11120
| Symbol = SMPD1
| AltSymbols =; ASM; NPD
| OMIM = 607608
| ECnumber =
| Homologene = 457
| MGIid = 98325
| GeneAtlas_image1 = PBB_GE_SMPD1_209420_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SMPD1_216230_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0004767 |text = sphingomyelin phosphodiesterase activity}} {{GNF_GO|id=GO:0008907 |text = integrase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016798 |text = hydrolase activity, acting on glycosyl bonds}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0006685 |text = sphingomyelin catabolic process}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6609
| Hs_Ensembl = ENSG00000166311
| Hs_RefseqProtein = NP_000534
| Hs_RefseqmRNA = NM_000543
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 6368231
| Hs_GenLoc_end = 6372801
| Hs_Uniprot = P17405
| Mm_EntrezGene = 20597
| Mm_Ensembl = ENSMUSG00000037049
| Mm_RefseqmRNA = NM_011421
| Mm_RefseqProtein = NP_035551
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 105428213
| Mm_GenLoc_end = 105432204
| Mm_Uniprot = Q3UEE0
}}
}}
'''Sphingomyelin phosphodiesterase 1, acid lysosomal (acid sphingomyelinase)''', also known as '''SMPD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SMPD1 sphingomyelin phosphodiesterase 1, acid lysosomal (acid sphingomyelinase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6609| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Stoffel W |title=Functional analysis of acid and neutral sphingomyelinases in vitro and in vivo. |journal=Chem. Phys. Lipids |volume=102 |issue= 1-2 |pages= 107-21 |year= 2000 |pmid= 11001565 |doi= }}
*{{cite journal | author=Newrzella D, Stoffel W |title=Molecular cloning of the acid sphingomyelinase of the mouse and the organization and complete nucleotide sequence of the gene. |journal=Biol. Chem. Hoppe-Seyler |volume=373 |issue= 12 |pages= 1233-8 |year= 1993 |pmid= 1292508 |doi= }}
*{{cite journal | author=Takahashi T, Desnick RJ, Takada G, Schuchman EH |title=Identification of a missense mutation (S436R) in the acid sphingomyelinase gene from a Japanese patient with type B Niemann-Pick disease. |journal=Hum. Mutat. |volume=1 |issue= 1 |pages= 70-1 |year= 1993 |pmid= 1301192 |doi= 10.1002/humu.1380010111 }}
*{{cite journal | author=Levran O, Desnick RJ, Schuchman EH |title=Identification and expression of a common missense mutation (L302P) in the acid sphingomyelinase gene of Ashkenazi Jewish type A Niemann-Pick disease patients. |journal=Blood |volume=80 |issue= 8 |pages= 2081-7 |year= 1992 |pmid= 1391960 |doi= }}
*{{cite journal | author=Takahashi T, Suchi M, Desnick RJ, ''et al.'' |title=Identification and expression of five mutations in the human acid sphingomyelinase gene causing types A and B Niemann-Pick disease. Molecular evidence for genetic heterogeneity in the neuronopathic and non-neuronopathic forms. |journal=J. Biol. Chem. |volume=267 |issue= 18 |pages= 12552-8 |year= 1992 |pmid= 1618760 |doi= }}
*{{cite journal | author=Schuchman EH, Levran O, Suchi M, Desnick RJ |title=An MspI polymorphism in the human acid sphingomyelinase gene (SMPD1). |journal=Nucleic Acids Res. |volume=19 |issue= 11 |pages= 3160 |year= 1991 |pmid= 1711683 |doi= }}
*{{cite journal | author=Ferlinz K, Hurwitz R, Sandhoff K |title=Molecular basis of acid sphingomyelinase deficiency in a patient with Niemann-Pick disease type A. |journal=Biochem. Biophys. Res. Commun. |volume=179 |issue= 3 |pages= 1187-91 |year= 1991 |pmid= 1718266 |doi= }}
*{{cite journal | author=Schuchman EH, Levran O, Pereira LV, Desnick RJ |title=Structural organization and complete nucleotide sequence of the gene encoding human acid sphingomyelinase (SMPD1). |journal=Genomics |volume=12 |issue= 2 |pages= 197-205 |year= 1992 |pmid= 1740330 |doi= }}
*{{cite journal | author=Schuchman EH, Suchi M, Takahashi T, ''et al.'' |title=Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs. |journal=J. Biol. Chem. |volume=266 |issue= 13 |pages= 8531-9 |year= 1991 |pmid= 1840600 |doi= }}
*{{cite journal | author=Levran O, Desnick RJ, Schuchman EH |title=Niemann-Pick type B disease. Identification of a single codon deletion in the acid sphingomyelinase gene and genotype/phenotype correlations in type A and B patients. |journal=J. Clin. Invest. |volume=88 |issue= 3 |pages= 806-10 |year= 1991 |pmid= 1885770 |doi= }}
*{{cite journal | author=da Veiga Pereira L, Desnick RJ, Adler DA, ''et al.'' |title=Regional assignment of the human acid sphingomyelinase gene (SMPD1) by PCR analysis of somatic cell hybrids and in situ hybridization to 11p15.1----p15.4. |journal=Genomics |volume=9 |issue= 2 |pages= 229-34 |year= 1991 |pmid= 2004772 |doi= }}
*{{cite journal | author=Levran O, Desnick RJ, Schuchman EH |title=Niemann-Pick disease: a frequent missense mutation in the acid sphingomyelinase gene of Ashkenazi Jewish type A and B patients. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 9 |pages= 3748-52 |year= 1991 |pmid= 2023926 |doi= }}
*{{cite journal | author=Quintern LE, Schuchman EH, Levran O, ''et al.'' |title=Isolation of cDNA clones encoding human acid sphingomyelinase: occurrence of alternatively processed transcripts. |journal=EMBO J. |volume=8 |issue= 9 |pages= 2469-73 |year= 1989 |pmid= 2555181 |doi= }}
*{{cite journal | author=Horinouchi K, Erlich S, Perl DP, ''et al.'' |title=Acid sphingomyelinase deficient mice: a model of types A and B Niemann-Pick disease. |journal=Nat. Genet. |volume=10 |issue= 3 |pages= 288-93 |year= 1995 |pmid= 7670466 |doi= 10.1038/ng0795-288 }}
*{{cite journal | author=Sperl W, Bart G, Vanier MT, ''et al.'' |title=A family with visceral course of Niemann-Pick disease, macular halo syndrome and low sphingomyelin degradation rate. |journal=J. Inherit. Metab. Dis. |volume=17 |issue= 1 |pages= 93-103 |year= 1994 |pmid= 8051942 |doi= }}
*{{cite journal | author=Ida H, Rennert OM, Eto Y, Chan WY |title=Cloning of a human acid sphingomyelinase cDNA with a new mutation that renders the enzyme inactive. |journal=J. Biochem. |volume=114 |issue= 1 |pages= 15-20 |year= 1993 |pmid= 8407868 |doi= }}
*{{cite journal | author=Ida H, Rennert OM, Maekawa K, Eto Y |title=Identification of three novel mutations in the acid sphinogomyelinase gene of Japanese patients with Niemann-Pick disease type A and B. |journal=Hum. Mutat. |volume=7 |issue= 1 |pages= 65-7 |year= 1996 |pmid= 8664904 |doi= 10.1002/(SICI)1098-1004(1996)7:1<65::AID-HUMU10>3.0.CO;2-Q }}
*{{cite journal | author=Schuchman EH |title=Two new mutations in the acid sphingomyelinase gene causing type a Niemann-pick disease: N389T and R441X. |journal=Hum. Mutat. |volume=6 |issue= 4 |pages= 352-4 |year= 1996 |pmid= 8680412 |doi= 10.1002/humu.1380060412 }}
*{{cite journal | author=Takahashi T, Suchi M, Sato W, ''et al.'' |title=Identification and expression of a missense mutation (Y446C) in the acid sphingomyelinase gene from a Japanese patient with type A Niemann-Pick disease. |journal=Tohoku J. Exp. Med. |volume=177 |issue= 2 |pages= 117-23 |year= 1996 |pmid= 8693491 |doi= }}
*{{cite journal | author=Ferlinz K, Hurwitz R, Moczall H, ''et al.'' |title=Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site-directed mutagenesis. |journal=Eur. J. Biochem. |volume=243 |issue= 1-2 |pages= 511-7 |year= 1997 |pmid= 9030779 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SNRP70... {November 17, 2007 12:35:35 PM PST}
- SEARCH REDIRECT: Control Box Found: SNRP70 {November 17, 2007 12:36:06 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:36:09 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:36:09 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:36:09 PM PST}
- UPDATED: Updated protein page: SNRP70 {November 17, 2007 12:36:16 PM PST}
- INFO: Beginning work on TCF2... {November 17, 2007 12:36:16 PM PST}
- SEARCH REDIRECT: Control Box Found: TCF2 {November 17, 2007 12:37:32 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:37:33 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:37:33 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:37:33 PM PST}
- UPDATED: Updated protein page: TCF2 {November 17, 2007 12:37:41 PM PST}
- INFO: Beginning work on TCP1... {November 17, 2007 12:37:41 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 17, 2007 12:38:44 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = T-complex 1
| HGNCid = 11655
| Symbol = TCP1
| AltSymbols =; CCT-alpha; CCT1; CCTa; D6S230E; TCP-1-alpha
| OMIM = 186980
| ECnumber =
| Homologene = 5656
| MGIid = 98535
| GeneAtlas_image1 = PBB_GE_TCP1_222011_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_TCP1_208778_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_TCP1_222010_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}
| Component = {{GNF_GO|id=GO:0000242 |text = pericentriolar material}} {{GNF_GO|id=GO:0005720 |text = nuclear heterochromatin}} {{GNF_GO|id=GO:0005815 |text = microtubule organizing center}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005832 |text = chaperonin-containing T-complex}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0007021 |text = tubulin folding}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6950
| Hs_Ensembl = ENSG00000120438
| Hs_RefseqProtein = NP_001008897
| Hs_RefseqmRNA = NM_001008897
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 160119520
| Hs_GenLoc_end = 160130731
| Hs_Uniprot = P17987
| Mm_EntrezGene = 21454
| Mm_Ensembl = ENSMUSG00000068039
| Mm_RefseqmRNA = NM_013686
| Mm_RefseqProtein = NP_038714
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 12759413
| Mm_GenLoc_end = 12767488
| Mm_Uniprot = Q3TJ96
}}
}}
'''T-complex 1''', also known as '''TCP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TCP1 t-complex 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6950| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a molecular chaperone that is member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: TCP1 t-complex 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6950| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Horwich AL, Willison KR |title=Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1. |journal=Philos. Trans. R. Soc. Lond., B, Biol. Sci. |volume=339 |issue= 1289 |pages= 313-25; discussion 325-6 |year= 1993 |pmid= 8098536 |doi= 10.1098/rstb.1993.0030 }}
*{{cite journal | author=Burston SG, Clarke AR |title=Molecular chaperones: physical and mechanistic properties. |journal=Essays Biochem. |volume=29 |issue= |pages= 125-36 |year= 1997 |pmid= 9189717 |doi= }}
*{{cite journal | author=Blanché H, Wright LG, Vergnaud G, ''et al.'' |title=Genetic mapping of three human homologues of murine t-complex genes localizes TCP10 to 6q27, 15 cM distal to TCP1 and PLG. |journal=Genomics |volume=12 |issue= 4 |pages= 826-8 |year= 1992 |pmid= 1572657 |doi= }}
*{{cite journal | author=Dawson SJ, White LA |title=Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin. |journal=J. Infect. |volume=24 |issue= 3 |pages= 317-20 |year= 1992 |pmid= 1602151 |doi= }}
*{{cite journal | author=Yaffe MB, Farr GW, Miklos D, ''et al.'' |title=TCP1 complex is a molecular chaperone in tubulin biogenesis. |journal=Nature |volume=358 |issue= 6383 |pages= 245-8 |year= 1992 |pmid= 1630491 |doi= 10.1038/358245a0 }}
*{{cite journal | author=Lewis VA, Hynes GM, Zheng D, ''et al.'' |title=T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol. |journal=Nature |volume=358 |issue= 6383 |pages= 249-52 |year= 1992 |pmid= 1630492 |doi= 10.1038/358249a0 }}
*{{cite journal | author=Ursic D, Culbertson MR |title=The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. |journal=Mol. Cell. Biol. |volume=11 |issue= 5 |pages= 2629-40 |year= 1991 |pmid= 1901944 |doi= }}
*{{cite journal | author=Kirchhoff C, Willison K |title=Nucleotide and amino-acid sequence of human testis-derived TCP1. |journal=Nucleic Acids Res. |volume=18 |issue= 14 |pages= 4247 |year= 1990 |pmid= 2377466 |doi= }}
*{{cite journal | author=Fonatsch C, Gradl G, Ragoussis J, Ziegler A |title=Assignment of the TCP1 locus to the long arm of human chromosome 6 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=45 |issue= 2 |pages= 109-12 |year= 1987 |pmid= 3476253 |doi= }}
*{{cite journal | author=Willison K, Kelly A, Dudley K, ''et al.'' |title=The human homologue of the mouse t-complex gene, TCP1, is located on chromosome 6 but is not near the HLA region. |journal=EMBO J. |volume=6 |issue= 7 |pages= 1967-74 |year= 1987 |pmid= 3653076 |doi= }}
*{{cite journal | author=Roobol A, Holmes FE, Hayes NV, ''et al.'' |title=Cytoplasmic chaperonin complexes enter neurites developing in vitro and differ in subunit composition within single cells. |journal=J. Cell. Sci. |volume=108 ( Pt 4) |issue= |pages= 1477-88 |year= 1995 |pmid= 7615668 |doi= }}
*{{cite journal | author=Ashworth A |title=Two acetyl-CoA acetyltransferase genes located in the t-complex region of mouse chromosome 17 partially overlap the Tcp-1 and Tcp-1x genes. |journal=Genomics |volume=18 |issue= 2 |pages= 195-8 |year= 1994 |pmid= 7904580 |doi= 10.1006/geno.1993.1454 }}
*{{cite journal | author=Miklos D, Caplan S, Mertens D, ''et al.'' |title=Primary structure and function of a second essential member of the heterooligomeric TCP1 chaperonin complex of yeast, TCP1 beta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 7 |pages= 2743-7 |year= 1994 |pmid= 7908441 |doi= }}
*{{cite journal | author=Chen X, Sullivan DS, Huffaker TC |title=Two yeast genes with similarity to TCP-1 are required for microtubule and actin function in vivo. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 19 |pages= 9111-5 |year= 1994 |pmid= 7916460 |doi= }}
*{{cite journal | author=Kubota H, Hynes G, Carne A, ''et al.'' |title=Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin. |journal=Curr. Biol. |volume=4 |issue= 2 |pages= 89-99 |year= 1994 |pmid= 7953530 |doi= }}
*{{cite journal | author=Frydman J, Hartl FU |title=Principles of chaperone-assisted protein folding: differences between in vitro and in vivo mechanisms. |journal=Science |volume=272 |issue= 5267 |pages= 1497-502 |year= 1996 |pmid= 8633246 |doi= }}
*{{cite journal | author=Moudjou M, Bordes N, Paintrand M, Bornens M |title=gamma-Tubulin in mammalian cells: the centrosomal and the cytosolic forms. |journal=J. Cell. Sci. |volume=109 ( Pt 4) |issue= |pages= 875-87 |year= 1996 |pmid= 8718679 |doi= }}
*{{cite journal | author=Morrison K, Papapetrou C, Attwood J, ''et al.'' |title=Genetic mapping of the human homologue (T) of mouse T(Brachyury) and a search for allele association between human T and spina bifida. |journal=Hum. Mol. Genet. |volume=5 |issue= 5 |pages= 669-74 |year= 1997 |pmid= 8733136 |doi= }}
*{{cite journal | author=Masuno M, Fukao T, Song XQ, ''et al.'' |title=Assignment of the human cytosolic acetoacetyl-coenzyme A thiolase (ACAT2) gene to chromosome 6q25.3-q26. |journal=Genomics |volume=36 |issue= 1 |pages= 217-8 |year= 1997 |pmid= 8812443 |doi= 10.1006/geno.1996.0452 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TP53BP1... {November 17, 2007 12:38:44 PM PST}
- SEARCH REDIRECT: Control Box Found: TP53BP1 {November 17, 2007 12:39:15 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 17, 2007 12:39:16 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 17, 2007 12:39:16 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 17, 2007 12:39:16 PM PST}
- UPDATED: Updated protein page: TP53BP1 {November 17, 2007 12:39:25 PM PST}
end log.
