Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 19:27, 16 November 2007 (UTC)
[edit]Proteins without matches (10)
[edit]Proteins with a High Potential Match (7)
[edit]Redirected Proteins (8)
[edit]Manual Inspection (Page not found) (17)
[edit]
Protein Status Grid - Date: 19:27, 16 November 2007 (UTC)
[edit]Vebose Log - Date: 19:27, 16 November 2007 (UTC)
[edit]- INFO: Beginning work on ABCD1... {November 16, 2007 11:06:26 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:06:57 AM 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 = ATP-binding cassette, sub-family D (ALD), member 1
| HGNCid = 61
| Symbol = ABCD1
| AltSymbols =; ABC42; ALD; ALDP; AMN
| OMIM = 300371
| ECnumber =
| Homologene = 55426
| MGIid = 1349215
| 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:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0042626 |text = ATPase activity, coupled to transmembrane movement of substances}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005777 |text = peroxisome}} {{GNF_GO|id=GO:0005779 |text = integral to peroxisomal membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0007031 |text = peroxisome organization and biogenesis}} {{GNF_GO|id=GO:0015919 |text = peroxisomal membrane transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 215
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000024
| Hs_RefseqmRNA = NM_000033
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 11666
| Mm_Ensembl = ENSMUSG00000031378
| Mm_RefseqmRNA = XM_973209
| Mm_RefseqProtein = XP_978303
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 69969429
| Mm_GenLoc_end = 69991252
| Mm_Uniprot = P48410
}}
}}
'''ATP-binding cassette, sub-family D (ALD), member 1''', also known as '''ABCD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ABCD1 ATP-binding cassette, sub-family D (ALD), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=215| 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 superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the ALD subfamily, which is involved in peroxisomal import of fatty acids and/or fatty acyl-CoAs in the organelle. All known peroxisomal ABC transporters are half transporters which require a partner half transporter molecule to form a functional homodimeric or heterodimeric transporter. This peroxisomal membrane protein is likely involved in the peroxisomal transport or catabolism of very long chain fatty acids. Defects in this gene have been identified as the underlying cause of adrenoleukodystrophy, an X-chromosome recessively inherited demyelinating disorder of the nervous system.<ref name="entrez">{{cite web | title = Entrez Gene: ABCD1 ATP-binding cassette, sub-family D (ALD), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=215| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Aubourg P, Mosser J, Douar AM, ''et al.'' |title=Adrenoleukodystrophy gene: unexpected homology to a protein involved in peroxisome biogenesis. |journal=Biochimie |volume=75 |issue= 3-4 |pages= 293-302 |year= 1993 |pmid= 8507690 |doi= }}
*{{cite journal | author=Moser HW, Powers JM, Smith KD |title=Adrenoleukodystrophy: molecular genetics, pathology, and Lorenzo's oil. |journal=Brain Pathol. |volume=5 |issue= 3 |pages= 259-66 |year= 1996 |pmid= 8520725 |doi= }}
*{{cite journal | author=Dodd A, Rowland SA, Hawkes SL, ''et al.'' |title=Mutations in the adrenoleukodystrophy gene. |journal=Hum. Mutat. |volume=9 |issue= 6 |pages= 500-11 |year= 1997 |pmid= 9195223 |doi= 10.1002/(SICI)1098-1004(1997)9:6<500::AID-HUMU2>3.0.CO;2-5 }}
*{{cite journal | author=Kemp S, Pujol A, Waterham HR, ''et al.'' |title=ABCD1 mutations and the X-linked adrenoleukodystrophy mutation database: role in diagnosis and clinical correlations. |journal=Hum. Mutat. |volume=18 |issue= 6 |pages= 499-515 |year= 2002 |pmid= 11748843 |doi= 10.1002/humu.1227 }}
*{{cite journal | author=Lan F |title=Molecular diagnostics in China. |journal=Clin. Chem. Lab. Med. |volume=39 |issue= 12 |pages= 1190-4 |year= 2002 |pmid= 11798073 |doi= }}
*{{cite journal | author=Feil R, Aubourg P, Mosser J, ''et al.'' |title=Adrenoleukodystrophy: a complex chromosomal rearrangement in the Xq28 red/green-color-pigment gene region indicates two possible gene localizations. |journal=Am. J. Hum. Genet. |volume=49 |issue= 6 |pages= 1361-71 |year= 1992 |pmid= 1746561 |doi= }}
*{{cite journal | author=Moser HW, Moser AE, Singh I, O'Neill BP |title=Adrenoleukodystrophy: survey of 303 cases: biochemistry, diagnosis, and therapy. |journal=Ann. Neurol. |volume=16 |issue= 6 |pages= 628-41 |year= 1985 |pmid= 6524872 |doi= 10.1002/ana.410160603 }}
*{{cite journal | author=Migeon BR, Moser HW, Moser AB, ''et al.'' |title=Adrenoleukodystrophy: evidence for X linkage, inactivation, and selection favoring the mutant allele in heterozygous cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=78 |issue= 8 |pages= 5066-70 |year= 1982 |pmid= 6795626 |doi= }}
*{{cite journal | author=Kok F, Neumann S, Sarde CO, ''et al.'' |title=Mutational analysis of patients with X-linked adrenoleukodystrophy. |journal=Hum. Mutat. |volume=6 |issue= 2 |pages= 104-15 |year= 1995 |pmid= 7581394 |doi= 10.1002/humu.1380060203 }}
*{{cite journal | author=Watkins PA, Gould SJ, Smith MA, ''et al.'' |title=Altered expression of ALDP in X-linked adrenoleukodystrophy. |journal=Am. J. Hum. Genet. |volume=57 |issue= 2 |pages= 292-301 |year= 1995 |pmid= 7668254 |doi= }}
*{{cite journal | author=Braun A, Ambach H, Kammerer S, ''et al.'' |title=Mutations in the gene for X-linked adrenoleukodystrophy in patients with different clinical phenotypes. |journal=Am. J. Hum. Genet. |volume=56 |issue= 4 |pages= 854-61 |year= 1995 |pmid= 7717396 |doi= }}
*{{cite journal | author=Berger J, Molzer B, Faé I, Bernheimer H |title=X-linked adrenoleukodystrophy (ALD): a novel mutation of the ALD gene in 6 members of a family presenting with 5 different phenotypes. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 3 |pages= 1638-43 |year= 1995 |pmid= 7811247 |doi= 10.1006/bbrc.1994.2855 }}
*{{cite journal | author=Ligtenberg MJ, Kemp S, Sarde CO, ''et al.'' |title=Spectrum of mutations in the gene encoding the adrenoleukodystrophy protein. |journal=Am. J. Hum. Genet. |volume=56 |issue= 1 |pages= 44-50 |year= 1995 |pmid= 7825602 |doi= }}
*{{cite journal | author=Fuchs S, Sarde CO, Wedemann H, ''et al.'' |title=Missense mutations are frequent in the gene for X-chromosomal adrenoleukodystrophy (ALD). |journal=Hum. Mol. Genet. |volume=3 |issue= 10 |pages= 1903-5 |year= 1995 |pmid= 7849723 |doi= }}
*{{cite journal | author=Cartier N, Sarde CO, Douar AM, ''et al.'' |title=Abnormal messenger RNA expression and a missense mutation in patients with X-linked adrenoleukodystrophy. |journal=Hum. Mol. Genet. |volume=2 |issue= 11 |pages= 1949-51 |year= 1994 |pmid= 7904210 |doi= }}
*{{cite journal | author=Sarde CO, Mosser J, Kioschis P, ''et al.'' |title=Genomic organization of the adrenoleukodystrophy gene. |journal=Genomics |volume=22 |issue= 1 |pages= 13-20 |year= 1994 |pmid= 7959759 |doi= 10.1006/geno.1994.1339 }}
*{{cite journal | author=Kobayashi T, Yamada T, Yasutake T, ''et al.'' |title=Adrenoleukodystrophy gene encodes an 80 kDa membrane protein. |journal=Biochem. Biophys. Res. Commun. |volume=201 |issue= 2 |pages= 1029-34 |year= 1994 |pmid= 8002973 |doi= 10.1006/bbrc.1994.1805 }}
*{{cite journal | author=Mosser J, Lutz Y, Stoeckel ME, ''et al.'' |title=The gene responsible for adrenoleukodystrophy encodes a peroxisomal membrane protein. |journal=Hum. Mol. Genet. |volume=3 |issue= 2 |pages= 265-71 |year= 1994 |pmid= 8004093 |doi= }}
*{{cite journal | author=Fanen P, Guidoux S, Sarde CO, ''et al.'' |title=Identification of mutations in the putative ATP-binding domain of the adrenoleukodystrophy gene. |journal=J. Clin. Invest. |volume=94 |issue= 2 |pages= 516-20 |year= 1994 |pmid= 8040304 |doi= }}
*{{cite journal | author=Mosser J, Douar AM, Sarde CO, ''et al.'' |title=Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters. |journal=Nature |volume=361 |issue= 6414 |pages= 726-30 |year= 1993 |pmid= 8441467 |doi= 10.1038/361726a0 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BAG1... {November 16, 2007 11:06:57 AM PST}
- SEARCH REDIRECT: Control Box Found: BAG1 {November 16, 2007 11:07:22 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:07:23 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:07:23 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:07:23 AM PST}
- UPDATED: Updated protein page: BAG1 {November 16, 2007 11:07:28 AM PST}
- INFO: Beginning work on CDK6... {November 16, 2007 11:07:29 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:08:12 AM 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_CDK6_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1bi7.
| PDB = {{PDB2|1bi7}}, {{PDB2|1bi8}}, {{PDB2|1blx}}, {{PDB2|1g3n}}, {{PDB2|1jow}}, {{PDB2|1xo2}}, {{PDB2|2euf}}, {{PDB2|2f2c}}
| Name = Cyclin-dependent kinase 6
| HGNCid = 1777
| Symbol = CDK6
| AltSymbols =; MGC59692; PLSTIRE
| OMIM = 603368
| ECnumber =
| Homologene = 963
| MGIid = 1277162
| GeneAtlas_image1 = PBB_GE_CDK6_207143_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: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:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0000080 |text = G1 phase of mitotic cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0051301 |text = cell division}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1021
| Hs_Ensembl = ENSG00000105810
| Hs_RefseqProtein = NP_001250
| Hs_RefseqmRNA = NM_001259
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 92072175
| Hs_GenLoc_end = 92301148
| Hs_Uniprot = Q00534
| Mm_EntrezGene = 12571
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_009873
| Mm_RefseqProtein = NP_034003
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Cyclin-dependent kinase 6''', also known as '''CDK6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CDK6 cyclin-dependent kinase 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1021| 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 cyclin-dependent protein kinase (CDK) family. CDK family members are highly similar to the gene products of Saccharomyces cerevisiae cdc28, and Schizosaccharomyces pombe cdc2, and are known to be important regulators of cell cycle progression. This kinase is a catalytic subunit of the protein kinase complex that is important for cell cycle G1 phase progression and G1/S transition. The activity of this kinase first appears in mid-G1 phase, which is controlled by the regulatory subunits including D-type cyclins and members of INK4 family of CDK inhibitors. This kinase, as well as CDK4, has been shown to phosphorylate, and thus regulate the activity of, tumor suppressor protein Rb.<ref name="entrez">{{cite web | title = Entrez Gene: CDK6 cyclin-dependent kinase 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1021| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Meyerson M, Enders GH, Wu CL, ''et al.'' |title=A family of human cdc2-related protein kinases. |journal=EMBO J. |volume=11 |issue= 8 |pages= 2909-17 |year= 1992 |pmid= 1639063 |doi= }}
*{{cite journal | author=Adams MD, Kerlavage AR, Fleischmann RD, ''et al.'' |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3-174 |year= 1995 |pmid= 7566098 |doi= }}
*{{cite journal | author=Aprelikova O, Xiong Y, Liu ET |title=Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase. |journal=J. Biol. Chem. |volume=270 |issue= 31 |pages= 18195-7 |year= 1995 |pmid= 7629134 |doi= }}
*{{cite journal | author=Lucas JJ, Szepesi A, Modiano JF, ''et al.'' |title=Regulation of synthesis and activity of the PLSTIRE protein (cyclin-dependent kinase 6 (cdk6)), a major cyclin D-associated cdk4 homologue in normal human T lymphocytes. |journal=J. Immunol. |volume=154 |issue= 12 |pages= 6275-84 |year= 1995 |pmid= 7759865 |doi= }}
*{{cite journal | author=Bullrich F, MacLachlan TK, Sang N, ''et al.'' |title=Chromosomal mapping of members of the cdc2 family of protein kinases, cdk3, cdk6, PISSLRE, and PITALRE, and a cdk inhibitor, p27Kip1, to regions involved in human cancer. |journal=Cancer Res. |volume=55 |issue= 6 |pages= 1199-205 |year= 1995 |pmid= 7882308 |doi= }}
*{{cite journal | author=Guan KL, Jenkins CW, Li Y, ''et al.'' |title=Growth suppression by p18, a p16INK4/MTS1- and p14INK4B/MTS2-related CDK6 inhibitor, correlates with wild-type pRb function. |journal=Genes Dev. |volume=8 |issue= 24 |pages= 2939-52 |year= 1995 |pmid= 8001816 |doi= }}
*{{cite journal | author=Meyerson M, Harlow E |title=Identification of G1 kinase activity for cdk6, a novel cyclin D partner. |journal=Mol. Cell. Biol. |volume=14 |issue= 3 |pages= 2077-86 |year= 1994 |pmid= 8114739 |doi= }}
*{{cite journal | author=Fåhraeus R, Paramio JM, Ball KL, ''et al.'' |title=Inhibition of pRb phosphorylation and cell-cycle progression by a 20-residue peptide derived from p16CDKN2/INK4A. |journal=Curr. Biol. |volume=6 |issue= 1 |pages= 84-91 |year= 1996 |pmid= 8805225 |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=Lamphere L, Fiore F, Xu X, ''et al.'' |title=Interaction between Cdc37 and Cdk4 in human cells. |journal=Oncogene |volume=14 |issue= 16 |pages= 1999-2004 |year= 1997 |pmid= 9150368 |doi= 10.1038/sj.onc.1201036 }}
*{{cite journal | author=Nagasawa M, Melamed I, Kupfer A, ''et al.'' |title=Rapid nuclear translocation and increased activity of cyclin-dependent kinase 6 after T cell activation. |journal=J. Immunol. |volume=158 |issue= 11 |pages= 5146-54 |year= 1997 |pmid= 9164930 |doi= }}
*{{cite journal | author=Ezhevsky SA, Nagahara H, Vocero-Akbani AM, ''et al.'' |title=Hypo-phosphorylation of the retinoblastoma protein (pRb) by cyclin D:Cdk4/6 complexes results in active pRb. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 20 |pages= 10699-704 |year= 1997 |pmid= 9380698 |doi= }}
*{{cite journal | author=Fåhraeus R, Laín S, Ball KL, Lane DP |title=Characterization of the cyclin-dependent kinase inhibitory domain of the INK4 family as a model for a synthetic tumour suppressor molecule. |journal=Oncogene |volume=16 |issue= 5 |pages= 587-96 |year= 1998 |pmid= 9482104 |doi= 10.1038/sj.onc.1201580 }}
*{{cite journal | author=Gonzales AJ, Goldsworthy TL, Fox TR |title=Chemical transformation of mouse liver cells results in altered cyclin D-CDK protein complexes. |journal=Carcinogenesis |volume=19 |issue= 6 |pages= 1093-102 |year= 1998 |pmid= 9667749 |doi= }}
*{{cite journal | author=Russo AA, Tong L, Lee JO, ''et al.'' |title=Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a. |journal=Nature |volume=395 |issue= 6699 |pages= 237-43 |year= 1998 |pmid= 9751050 |doi= 10.1038/26155 }}
*{{cite journal | author=Brotherton DH, Dhanaraj V, Wick S, ''et al.'' |title=Crystal structure of the complex of the cyclin D-dependent kinase Cdk6 bound to the cell-cycle inhibitor p19INK4d. |journal=Nature |volume=395 |issue= 6699 |pages= 244-50 |year= 1998 |pmid= 9751051 |doi= 10.1038/26164 }}
*{{cite journal | author=Jiang W, Wells NJ, Hunter T |title=Multistep regulation of DNA replication by Cdk phosphorylation of HsCdc6. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 11 |pages= 6193-8 |year= 1999 |pmid= 10339564 |doi= }}
*{{cite journal | author=Yarbrough WG, Buckmire RA, Bessho M, Liu ET |title=Biologic and biochemical analyses of p16(INK4a) mutations from primary tumors. |journal=J. Natl. Cancer Inst. |volume=91 |issue= 18 |pages= 1569-74 |year= 1999 |pmid= 10491434 |doi= }}
*{{cite journal | author=Harbour JW, Luo RX, Dei Santi A, ''et al.'' |title=Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1. |journal=Cell |volume=98 |issue= 6 |pages= 859-69 |year= 1999 |pmid= 10499802 |doi= }}
*{{cite journal | author=Grossel MJ, Baker GL, Hinds PW |title=cdk6 can shorten G(1) phase dependent upon the N-terminal INK4 interaction domain. |journal=J. Biol. Chem. |volume=274 |issue= 42 |pages= 29960-7 |year= 1999 |pmid= 10514479 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CDKN2B... {November 16, 2007 11:08:12 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:08:48 AM 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 = Cyclin-dependent kinase inhibitor 2B (p15, inhibits CDK4)
| HGNCid = 1788
| Symbol = CDKN2B
| AltSymbols =; INK4B; MTS2; P15; TP15
| OMIM = 600431
| ECnumber =
| Homologene = 55859
| MGIid = 104737
| GeneAtlas_image1 = PBB_GE_CDKN2B_207530_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004861 |text = cyclin-dependent protein kinase inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000079 |text = regulation of cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1030
| Hs_Ensembl = ENSG00000147883
| Hs_RefseqProtein = NP_004927
| Hs_RefseqmRNA = NM_004936
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 21992902
| Hs_GenLoc_end = 21999312
| Hs_Uniprot = P42772
| Mm_EntrezGene = 12579
| Mm_Ensembl = ENSMUSG00000073802
| Mm_RefseqmRNA = XM_989888
| Mm_RefseqProtein = XP_994982
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 88777525
| Mm_GenLoc_end = 88782177
| Mm_Uniprot = O54846
}}
}}
'''Cyclin-dependent kinase inhibitor 2B (p15, inhibits CDK4)''', also known as '''CDKN2B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CDKN2B cyclin-dependent kinase inhibitor 2B (p15, inhibits CDK4)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1030| 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 lies adjacent to the tumor suppressor gene CDKN2A in a region that is frequently mutated and deleted in a wide variety of tumors. This gene encodes a cyclin-dependent kinase inhibitor, which forms a complex with CDK4 or CDK6, and prevents the activation of the CDK kinases, thus the encoded protein functions as a cell growth regulator that controls cell cycle G1 progression. The expression of this gene was found to be dramatically induced by TGF beta, which suggested its role in the TGF beta induced growth inhibition. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: CDKN2B cyclin-dependent kinase inhibitor 2B (p15, inhibits CDK4)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1030| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hall M, Bates S, Peters G |title=Evidence for different modes of action of cyclin-dependent kinase inhibitors: p15 and p16 bind to kinases, p21 and p27 bind to cyclins. |journal=Oncogene |volume=11 |issue= 8 |pages= 1581-8 |year= 1995 |pmid= 7478582 |doi= }}
*{{cite journal | author=Stone S, Dayananth P, Jiang P, ''et al.'' |title=Genomic structure, expression and mutational analysis of the P15 (MTS2) gene. |journal=Oncogene |volume=11 |issue= 5 |pages= 987-91 |year= 1995 |pmid= 7675459 |doi= }}
*{{cite journal | author=Okamoto A, Hussain SP, Hagiwara K, ''et al.'' |title=Mutations in the p16INK4/MTS1/CDKN2, p15INK4B/MTS2, and p18 genes in primary and metastatic lung cancer. |journal=Cancer Res. |volume=55 |issue= 7 |pages= 1448-51 |year= 1995 |pmid= 7882351 |doi= }}
*{{cite journal | author=Jen J, Harper JW, Bigner SH, ''et al.'' |title=Deletion of p16 and p15 genes in brain tumors. |journal=Cancer Res. |volume=54 |issue= 24 |pages= 6353-8 |year= 1995 |pmid= 7987828 |doi= }}
*{{cite journal | author=Guan KL, Jenkins CW, Li Y, ''et al.'' |title=Growth suppression by p18, a p16INK4/MTS1- and p14INK4B/MTS2-related CDK6 inhibitor, correlates with wild-type pRb function. |journal=Genes Dev. |volume=8 |issue= 24 |pages= 2939-52 |year= 1995 |pmid= 8001816 |doi= }}
*{{cite journal | author=Hannon GJ, Beach D |title=p15INK4B is a potential effector of TGF-beta-induced cell cycle arrest. |journal=Nature |volume=371 |issue= 6494 |pages= 257-61 |year= 1994 |pmid= 8078588 |doi= 10.1038/371257a0 }}
*{{cite journal | author=Kamb A, Gruis NA, Weaver-Feldhaus J, ''et al.'' |title=A cell cycle regulator potentially involved in genesis of many tumor types. |journal=Science |volume=264 |issue= 5157 |pages= 436-40 |year= 1994 |pmid= 8153634 |doi= }}
*{{cite journal | author=Reynisdóttir I, Massagué J |title=The subcellular locations of p15(Ink4b) and p27(Kip1) coordinate their inhibitory interactions with cdk4 and cdk2. |journal=Genes Dev. |volume=11 |issue= 4 |pages= 492-503 |year= 1997 |pmid= 9042862 |doi= }}
*{{cite journal | author=Sandhu C, Garbe J, Bhattacharya N, ''et al.'' |title=Transforming growth factor beta stabilizes p15INK4B protein, increases p15INK4B-cdk4 complexes, and inhibits cyclin D1-cdk4 association in human mammary epithelial cells. |journal=Mol. Cell. Biol. |volume=17 |issue= 5 |pages= 2458-67 |year= 1997 |pmid= 9111314 |doi= }}
*{{cite journal | author=Iavarone A, Massagué J |title=Repression of the CDK activator Cdc25A and cell-cycle arrest by cytokine TGF-beta in cells lacking the CDK inhibitor p15. |journal=Nature |volume=387 |issue= 6631 |pages= 417-22 |year= 1997 |pmid= 9163429 |doi= 10.1038/387417a0 }}
*{{cite journal | author=Tsubari M, Tiihonen E, Laiho M |title=Cloning and characterization of p10, an alternatively spliced form of p15 cyclin-dependent kinase inhibitor. |journal=Cancer Res. |volume=57 |issue= 14 |pages= 2966-73 |year= 1997 |pmid= 9230210 |doi= }}
*{{cite journal | author=Rich JN, Zhang M, Datto MB, ''et al.'' |title=Transforming growth factor-beta-mediated p15(INK4B) induction and growth inhibition in astrocytes is SMAD3-dependent and a pathway prominently altered in human glioma cell lines. |journal=J. Biol. Chem. |volume=274 |issue= 49 |pages= 35053-8 |year= 2000 |pmid= 10574984 |doi= }}
*{{cite journal | author=Yuan C, Selby TL, Li J, ''et al.'' |title=Tumor suppressor INK4: refinement of p16INK4A structure and determination of p15INK4B structure by comparative modeling and NMR data. |journal=Protein Sci. |volume=9 |issue= 6 |pages= 1120-8 |year= 2000 |pmid= 10892805 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Staller P, Peukert K, Kiermaier A, ''et al.'' |title=Repression of p15INK4b expression by Myc through association with Miz-1. |journal=Nat. Cell Biol. |volume=3 |issue= 4 |pages= 392-9 |year= 2001 |pmid= 11283613 |doi= 10.1038/35070076 }}
*{{cite journal | author=Orlow I, Cordon-Cardo C |title=Evaluation of alterations in the tumor suppressor genes INK4A and INK4B in human bladder tumors. |journal=Methods Mol. Biol. |volume=179 |issue= |pages= 43-59 |year= 2002 |pmid= 11692873 |doi= }}
*{{cite journal | author=Agiostratidou G, Derventzi A, Gonos ES |title=Over-expression of CDKIs p15INK4b, p16INK4a and p21CIP1/WAF1 genes mediate growth arrest in human osteosarcoma cell lines. |journal=In Vivo |volume=15 |issue= 5 |pages= 443-6 |year= 2002 |pmid= 11695244 |doi= }}
*{{cite journal | author=Simon M, Park TW, Köster G, ''et al.'' |title=Alterations of INK4a(p16-p14ARF)/INK4b(p15) expression and telomerase activation in meningioma progression. |journal=J. Neurooncol. |volume=55 |issue= 3 |pages= 149-58 |year= 2002 |pmid= 11859969 |doi= }}
*{{cite journal | author=Scarisbrick JJ, Woolford AJ, Calonje E, ''et al.'' |title=Frequent abnormalities of the p15 and p16 genes in mycosis fungoides and sezary syndrome. |journal=J. Invest. Dermatol. |volume=118 |issue= 3 |pages= 493-9 |year= 2002 |pmid= 11874489 |doi= 10.1046/j.0022-202x.2001.01682.x }}
*{{cite journal | author=Kudoh K, Ichikawa Y, Yoshida S, ''et al.'' |title=Inactivation of p16/CDKN2 and p15/MTS2 is associated with prognosis and response to chemotherapy in ovarian cancer. |journal=Int. J. Cancer |volume=99 |issue= 4 |pages= 579-82 |year= 2002 |pmid= 11992549 |doi= 10.1002/ijc.10331 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CTSK... {November 16, 2007 11:08:48 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:09:28 AM 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_CTSK_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1atk.
| PDB = {{PDB2|1atk}}, {{PDB2|1au0}}, {{PDB2|1au2}}, {{PDB2|1au3}}, {{PDB2|1au4}}, {{PDB2|1ayu}}, {{PDB2|1ayv}}, {{PDB2|1ayw}}, {{PDB2|1bgo}}, {{PDB2|1by8}}, {{PDB2|1mem}}, {{PDB2|1nl6}}, {{PDB2|1nlj}}, {{PDB2|1q6k}}, {{PDB2|1snk}}, {{PDB2|1tu6}}, {{PDB2|1u9v}}, {{PDB2|1u9w}}, {{PDB2|1u9x}}, {{PDB2|1vsn}}, {{PDB2|1yk7}}, {{PDB2|1yk8}}, {{PDB2|1yt7}}, {{PDB2|2ato}}, {{PDB2|2aux}}, {{PDB2|2auz}}, {{PDB2|2bdl}}, {{PDB2|2f7d}}, {{PDB2|2ftd}}, {{PDB2|7pck}}
| Name = Cathepsin K
| HGNCid = 2536
| Symbol = CTSK
| AltSymbols =; CTS02; CTSO; CTSO1; CTSO2; MGC23107; PKND; PYCD
| OMIM = 601105
| ECnumber =
| Homologene = 68053
| MGIid = 107823
| GeneAtlas_image1 = PBB_GE_CTSK_202450_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004216 |text = cathepsin K activity}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1513
| Hs_Ensembl = ENSG00000143387
| Hs_RefseqProtein = NP_000387
| Hs_RefseqmRNA = NM_000396
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 149035311
| Hs_GenLoc_end = 149047436
| Hs_Uniprot = P43235
| Mm_EntrezGene = 13038
| Mm_Ensembl = ENSMUSG00000028111
| Mm_RefseqmRNA = NM_007802
| Mm_RefseqProtein = NP_031828
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 95584660
| Mm_GenLoc_end = 95594766
| Mm_Uniprot = Q545T0
}}
}}
'''Cathepsin K''', also known as '''CTSK''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CTSK cathepsin K| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1513| 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 lysosomal cysteine proteinase involved in bone remodeling and resorption. This protein, which is a member of the peptidase C1 protein family, is predominantly expressed in osteoclasts. However, the encoded protein is also expressed in a significant fraction of human breast cancers, where it could contribute to tumor invasiveness. Mutations in this gene are the cause of pycnodysostosis, an autosomal recessive disease characterized by osteosclerosis and short stature. This gene may be subject to RNA editing.<ref name="entrez">{{cite web | title = Entrez Gene: CTSK cathepsin K| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1513| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Motyckova G, Fisher DE |title=Pycnodysostosis: role and regulation of cathepsin K in osteoclast function and human disease. |journal=Curr. Mol. Med. |volume=2 |issue= 5 |pages= 407-21 |year= 2003 |pmid= 12125807 |doi= }}
*{{cite journal | author=Troen BR |title=The regulation of cathepsin K gene expression. |journal=Ann. N. Y. Acad. Sci. |volume=1068 |issue= |pages= 165-72 |year= 2006 |pmid= 16831915 |doi= 10.1196/annals.1346.018 }}
*{{cite journal | author=Del Nery E, Chagas JR, Juliano MA, ''et al.'' |title=Evaluation of the extent of the binding site in human tissue kallikrein by synthetic substrates with sequences of human kininogen fragments. |journal=Biochem. J. |volume=312 ( Pt 1) |issue= |pages= 233-8 |year= 1996 |pmid= 7492318 |doi= }}
*{{cite journal | author=Brömme D, Okamoto K |title=Human cathepsin O2, a novel cysteine protease highly expressed in osteoclastomas and ovary molecular cloning, sequencing and tissue distribution. |journal=Biol. Chem. Hoppe-Seyler |volume=376 |issue= 6 |pages= 379-84 |year= 1995 |pmid= 7576232 |doi= }}
*{{cite journal | author=Gelb BD, Edelson JG, Desnick RJ |title=Linkage of pycnodysostosis to chromosome 1q21 by homozygosity mapping. |journal=Nat. Genet. |volume=10 |issue= 2 |pages= 235-7 |year= 1995 |pmid= 7663521 |doi= 10.1038/ng0695-235 }}
*{{cite journal | author=Polymeropoulos MH, Ortiz De Luna RI, Ide SE, ''et al.'' |title=The gene for pycnodysostosis maps to human chromosome 1cen-q21. |journal=Nat. Genet. |volume=10 |issue= 2 |pages= 238-9 |year= 1995 |pmid= 7663522 |doi= 10.1038/ng0695-238 }}
*{{cite journal | author=Shi GP, Chapman HA, Bhairi SM, ''et al.'' |title=Molecular cloning of human cathepsin O, a novel endoproteinase and homologue of rabbit OC2. |journal=FEBS Lett. |volume=357 |issue= 2 |pages= 129-34 |year= 1995 |pmid= 7805878 |doi= }}
*{{cite journal | author=Inaoka T, Bilbe G, Ishibashi O, ''et al.'' |title=Molecular cloning of human cDNA for cathepsin K: novel cysteine proteinase predominantly expressed in bone. |journal=Biochem. Biophys. Res. Commun. |volume=206 |issue= 1 |pages= 89-96 |year= 1995 |pmid= 7818555 |doi= 10.1006/bbrc.1995.1013 }}
*{{cite journal | author=Velasco G, Ferrando AA, Puente XS, ''et al.'' |title=Human cathepsin O. Molecular cloning from a breast carcinoma, production of the active enzyme in Escherichia coli, and expression analysis in human tissues. |journal=J. Biol. Chem. |volume=269 |issue= 43 |pages= 27136-42 |year= 1994 |pmid= 7929457 |doi= }}
*{{cite journal | author=Li YP, Alexander M, Wucherpfennig AL, ''et al.'' |title=Cloning and complete coding sequence of a novel human cathepsin expressed in giant cells of osteoclastomas. |journal=J. Bone Miner. Res. |volume=10 |issue= 8 |pages= 1197-202 |year= 1996 |pmid= 8585423 |doi= }}
*{{cite journal | author=Bossard MJ, Tomaszek TA, Thompson SK, ''et al.'' |title=Proteolytic activity of human osteoclast cathepsin K. Expression, purification, activation, and substrate identification. |journal=J. Biol. Chem. |volume=271 |issue= 21 |pages= 12517-24 |year= 1996 |pmid= 8647860 |doi= }}
*{{cite journal | author=Gelb BD, Shi GP, Chapman HA, Desnick RJ |title=Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency. |journal=Science |volume=273 |issue= 5279 |pages= 1236-8 |year= 1996 |pmid= 8703060 |doi= }}
*{{cite journal | author=Johnson MR, Polymeropoulos MH, Vos HL, ''et al.'' |title=A nonsense mutation in the cathepsin K gene observed in a family with pycnodysostosis. |journal=Genome Res. |volume=6 |issue= 11 |pages= 1050-5 |year= 1997 |pmid= 8938428 |doi= }}
*{{cite journal | author=Littlewood-Evans A, Kokubo T, Ishibashi O, ''et al.'' |title=Localization of cathepsin K in human osteoclasts by in situ hybridization and immunohistochemistry. |journal=Bone |volume=20 |issue= 2 |pages= 81-6 |year= 1997 |pmid= 9028530 |doi= }}
*{{cite journal | author=McGrath ME, Klaus JL, Barnes MG, Brömme D |title=Crystal structure of human cathepsin K complexed with a potent inhibitor. |journal=Nat. Struct. Biol. |volume=4 |issue= 2 |pages= 105-9 |year= 1997 |pmid= 9033587 |doi= }}
*{{cite journal | author=Rood JA, Van Horn S, Drake FH, ''et al.'' |title=Genomic organization and chromosome localization of the human cathepsin K gene (CTSK). |journal=Genomics |volume=41 |issue= 2 |pages= 169-76 |year= 1997 |pmid= 9143491 |doi= 10.1006/geno.1997.4614 }}
*{{cite journal | author=Gelb BD, Shi GP, Heller M, ''et al.'' |title=Structure and chromosomal assignment of the human cathepsin K gene. |journal=Genomics |volume=41 |issue= 2 |pages= 258-62 |year= 1997 |pmid= 9143502 |doi= 10.1006/geno.1997.4631 }}
*{{cite journal | author=Gomes RA, Juliano L, Chagas JR, Hial V |title=Characterization of kininogenase activity of an acidic proteinase isolated from human kidney. |journal=Can. J. Physiol. Pharmacol. |volume=75 |issue= 6 |pages= 757-61 |year= 1997 |pmid= 9276160 |doi= }}
*{{cite journal | author=Thompson SK, Halbert SM, Bossard MJ, ''et al.'' |title=Design of potent and selective human cathepsin K inhibitors that span the active site. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 26 |pages= 14249-54 |year= 1998 |pmid= 9405598 |doi= }}
*{{cite journal | author=Gelb BD, Willner JP, Dunn TM, ''et al.'' |title=Paternal uniparental disomy for chromosome 1 revealed by molecular analysis of a patient with pycnodysostosis. |journal=Am. J. Hum. Genet. |volume=62 |issue= 4 |pages= 848-54 |year= 1998 |pmid= 9529353 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DRD1... {November 16, 2007 11:09:28 AM PST}
- SEARCH REDIRECT: Control Box Found: DRD1 {November 16, 2007 11:09:53 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:09:55 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:09:55 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:09:55 AM PST}
- UPDATED: Updated protein page: DRD1 {November 16, 2007 11:10:01 AM PST}
- INFO: Beginning work on FANCC... {November 16, 2007 11:10:01 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:10:34 AM 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 = Fanconi anemia, complementation group C
| HGNCid = 3584
| Symbol = FANCC
| AltSymbols =; FA3; FAC; FACC; FLJ14675
| OMIM = 227645
| ECnumber =
| Homologene = 109
| MGIid = 95480
| GeneAtlas_image1 = PBB_GE_FANCC_205189_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006289 |text = nucleotide-excision repair}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0007281 |text = germ cell development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2176
| Hs_Ensembl = ENSG00000158169
| Hs_RefseqProtein = NP_000127
| Hs_RefseqmRNA = NM_000136
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 96901158
| Hs_GenLoc_end = 97119812
| Hs_Uniprot = Q00597
| Mm_EntrezGene = 14088
| Mm_Ensembl = ENSMUSG00000021461
| Mm_RefseqmRNA = NM_001042673
| Mm_RefseqProtein = NP_001036138
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 63313931
| Mm_GenLoc_end = 63440720
| Mm_Uniprot = P50652
}}
}}
'''Fanconi anemia, complementation group C''', also known as '''FANCC''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FANCC Fanconi anemia, complementation group C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2176| 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 delays the onset of apoptosis and promotes homologous recombination repair of damaged DNA. Mutations in this gene result in Fanconi anemia.<ref name="entrez">{{cite web | title = Entrez Gene: FANCC Fanconi anemia, complementation group C| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2176| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Strathdee CA, Duncan AM, Buchwald M |title=Evidence for at least four Fanconi anaemia genes including FACC on chromosome 9. |journal=Nat. Genet. |volume=1 |issue= 3 |pages= 196-8 |year= 1993 |pmid= 1303234 |doi= 10.1038/ng0692-196 }}
*{{cite journal | author=Strathdee CA, Gavish H, Shannon WR, Buchwald M |title=Cloning of cDNAs for Fanconi's anaemia by functional complementation. |journal=Nature |volume=356 |issue= 6372 |pages= 763-7 |year= 1992 |pmid= 1574115 |doi= 10.1038/356763a0 }}
*{{cite journal | author=Strathdee CA, Gavish H, Shannon WR, Buchwald M |title=Cloning of cDNAs for Fanconi's anaemia by functional complementation. |journal=Nature |volume=358 |issue= 6385 |pages= 434 |year= 1992 |pmid= 1641028 |doi= 10.1038/358434a0 }}
*{{cite journal | author=Verlander PC, Kaporis A, Liu Q, ''et al.'' |title=Carrier frequency of the IVS4 + 4 A-->T mutation of the Fanconi anemia gene FAC in the Ashkenazi Jewish population. |journal=Blood |volume=86 |issue= 11 |pages= 4034-8 |year= 1996 |pmid= 7492758 |doi= }}
*{{cite journal | author=Yamashita T, Barber DL, Zhu Y, ''et al.'' |title=The Fanconi anemia polypeptide FACC is localized to the cytoplasm. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6712-6 |year= 1994 |pmid= 7517562 |doi= }}
*{{cite journal | author=Segal GM, Magenis RE, Brown M, ''et al.'' |title=Repression of Fanconi anemia gene (FACC) expression inhibits growth of hematopoietic progenitor cells. |journal=J. Clin. Invest. |volume=94 |issue= 2 |pages= 846-52 |year= 1994 |pmid= 7518843 |doi= }}
*{{cite journal | author=Youssoufian H |title=Localization of Fanconi anemia C protein to the cytoplasm of mammalian cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 17 |pages= 7975-9 |year= 1994 |pmid= 8058745 |doi= }}
*{{cite journal | author=Whitney MA, Jakobs P, Kaback M, ''et al.'' |title=The Ashkenazi Jewish Fanconi anemia mutation: incidence among patients and carrier frequency in the at-risk population. |journal=Hum. Mutat. |volume=3 |issue= 4 |pages= 339-41 |year= 1994 |pmid= 8081385 |doi= 10.1002/humu.1380030402 }}
*{{cite journal | author=Murer-Orlando M, Llerena JC, Birjandi F, ''et al.'' |title=FACC gene mutations and early prenatal diagnosis of Fanconi's anaemia. |journal=Lancet |volume=342 |issue= 8872 |pages= 686 |year= 1993 |pmid= 8103176 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Verlander PC, Lin JD, Udono MU, ''et al.'' |title=Mutation analysis of the Fanconi anemia gene FACC. |journal=Am. J. Hum. Genet. |volume=54 |issue= 4 |pages= 595-601 |year= 1994 |pmid= 8128956 |doi= }}
*{{cite journal | author=Whitney MA, Saito H, Jakobs PM, ''et al.'' |title=A common mutation in the FACC gene causes Fanconi anaemia in Ashkenazi Jews. |journal=Nat. Genet. |volume=4 |issue= 2 |pages= 202-5 |year= 1993 |pmid= 8348157 |doi= 10.1038/ng0693-202 }}
*{{cite journal | author=Gibson RA, Buchwald M, Roberts RG, Mathew CG |title=Characterisation of the exon structure of the Fanconi anaemia group C gene by vectorette PCR. |journal=Hum. Mol. Genet. |volume=2 |issue= 1 |pages= 35-8 |year= 1993 |pmid= 8490620 |doi= }}
*{{cite journal | author=Gavish H, dos Santos CC, Buchwald M |title=A Leu554-to-Pro substitution completely abolishes the functional complementing activity of the Fanconi anemia (FACC) protein. |journal=Hum. Mol. Genet. |volume=2 |issue= 2 |pages= 123-6 |year= 1993 |pmid= 8499901 |doi= }}
*{{cite journal | author=Youssoufian H, Li Y, Martin ME, Buchwald M |title=Induction of Fanconi anemia cellular phenotype in human 293 cells by overexpression of a mutant FAC allele. |journal=J. Clin. Invest. |volume=97 |issue= 4 |pages= 957-62 |year= 1996 |pmid= 8613549 |doi= }}
*{{cite journal | author=Yamashita T, Wu N, Kupfer G, ''et al.'' |title=Clinical variability of Fanconi anemia (type C) results from expression of an amino terminal truncated Fanconi anemia complementation group C polypeptide with partial activity. |journal=Blood |volume=87 |issue= 10 |pages= 4424-32 |year= 1996 |pmid= 8639804 |doi= }}
*{{cite journal | author=Lo Ten Foe JR, Rooimans MA, Joenje H, Arwert F |title=Novel frameshift mutation (1806insA) in exon 14 of the Fanconi anemia C gene, FAC. |journal=Hum. Mutat. |volume=7 |issue= 3 |pages= 264-5 |year= 1996 |pmid= 8829660 |doi= 10.1002/(SICI)1098-1004(1996)7:3<264::AID-HUMU11>3.0.CO;2-0 }}
*{{cite journal | author=Gibson RA, Morgan NV, Goldstein LH, ''et al.'' |title=Novel mutations and polymorphisms in the Fanconi anemia group C gene. |journal=Hum. Mutat. |volume=8 |issue= 2 |pages= 140-8 |year= 1996 |pmid= 8844212 |doi= 10.1002/(SICI)1098-1004(1996)8:2<140::AID-HUMU6>3.0.CO;2-F }}
*{{cite journal | author=Kupfer GM, Yamashita T, Naf D, ''et al.'' |title=The Fanconi anemia polypeptide, FAC, binds to the cyclin-dependent kinase, cdc2. |journal=Blood |volume=90 |issue= 3 |pages= 1047-54 |year= 1997 |pmid= 9242535 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FOXO3A... {November 16, 2007 11:10:34 AM PST}
- SEARCH REDIRECT: Control Box Found: FOXO3A {November 16, 2007 11:11:16 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:11:20 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:11:20 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:11:20 AM PST}
- UPDATED: Updated protein page: FOXO3A {November 16, 2007 11:11:25 AM PST}
- INFO: Beginning work on GAA... {November 16, 2007 11:11:25 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:12:00 AM 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 = Glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II)
| HGNCid = 4065
| Symbol = GAA
| AltSymbols =; LYAG
| OMIM = 606800
| ECnumber =
| Homologene = 37268
| MGIid = 95609
| GeneAtlas_image1 = PBB_GE_GAA_202812_at_tn.png
| Function = {{GNF_GO|id=GO:0004553 |text = hydrolase activity, hydrolyzing O-glycosyl compounds}} {{GNF_GO|id=GO:0004558 |text = alpha-glucosidase activity}}
| Component = {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0005980 |text = glycogen catabolic process}} {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2548
| Hs_Ensembl = ENSG00000171298
| Hs_RefseqProtein = NP_000143
| Hs_RefseqmRNA = NM_000152
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 75689877
| Hs_GenLoc_end = 75708273
| Hs_Uniprot = P10253
| Mm_EntrezGene = 14387
| Mm_Ensembl = ENSMUSG00000025579
| Mm_RefseqmRNA = NM_008064
| Mm_RefseqProtein = NP_032090
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 119084118
| Mm_GenLoc_end = 119101544
| Mm_Uniprot = P70699
}}
}}
'''Glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II)''', also known as '''GAA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GAA glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2548| 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 acid alpha-glucosidase, which is essential for the degradation of glycogen to glucose in lysosomes. Different forms of acid alpha-glucosidase are obtained by proteolytic processing. Defects in this gene are the cause of glycogen storage disease II, also known as Pompe's disease, which is an autosomal recessive disorder with a broad clinical spectrum. Three transcript variants encoding the same protein have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: GAA glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2548| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Feizi T, Larkin M |title=AIDS and glycosylation. |journal=Glycobiology |volume=1 |issue= 1 |pages= 17-23 |year= 1992 |pmid= 2136376 |doi= }}
*{{cite journal | author=Reuser AJ, Kroos MA, Hermans MM, ''et al.'' |title=Glycogenosis type II (acid maltase deficiency). |journal=Muscle Nerve |volume=3 |issue= |pages= S61-9 |year= 1995 |pmid= 7603530 |doi= }}
*{{cite journal | author=Land A, Braakman I |title=Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum. |journal=Biochimie |volume=83 |issue= 8 |pages= 783-90 |year= 2001 |pmid= 11530211 |doi= }}
*{{cite journal | author=Zhong N, Martiniuk F, Tzall S, Hirschhorn R |title=Identification of a missense mutation in one allele of a patient with Pompe disease, and use of endonuclease digestion of PCR-amplified RNA to demonstrate lack of mRNA expression from the second allele. |journal=Am. J. Hum. Genet. |volume=49 |issue= 3 |pages= 635-45 |year= 1991 |pmid= 1652892 |doi= }}
*{{cite journal | author=Fenouillet E, Gluckman JC |title=Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein. |journal=J. Gen. Virol. |volume=72 ( Pt 8) |issue= |pages= 1919-26 |year= 1991 |pmid= 1678778 |doi= }}
*{{cite journal | author=Martiniuk F, Mehler M, Bodkin M, ''et al.'' |title=Identification of a missense mutation in an adult-onset patient with glycogenosis type II expressing only one allele. |journal=DNA Cell Biol. |volume=10 |issue= 9 |pages= 681-7 |year= 1992 |pmid= 1684505 |doi= }}
*{{cite journal | author=Ratner L, vander Heyden N, Dedera D |title=Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity. |journal=Virology |volume=181 |issue= 1 |pages= 180-92 |year= 1991 |pmid= 1704656 |doi= }}
*{{cite journal | author=Dedera DA, Gu RL, Ratner L |title=Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function. |journal=Virology |volume=187 |issue= 1 |pages= 377-82 |year= 1992 |pmid= 1736542 |doi= }}
*{{cite journal | author=Hermans MM, Kroos MA, van Beeumen J, ''et al.'' |title=Human lysosomal alpha-glucosidase. Characterization of the catalytic site. |journal=J. Biol. Chem. |volume=266 |issue= 21 |pages= 13507-12 |year= 1991 |pmid= 1856189 |doi= }}
*{{cite journal | author=Hermans MM, de Graaff E, Kroos MA, ''et al.'' |title=Identification of a point mutation in the human lysosomal alpha-glucosidase gene causing infantile glycogenosis type II. |journal=Biochem. Biophys. Res. Commun. |volume=179 |issue= 2 |pages= 919-26 |year= 1991 |pmid= 1898413 |doi= }}
*{{cite journal | author=Murphy CI, Lennick M, Lehar SM, ''et al.'' |title=Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding. |journal=Genet. Anal. Tech. Appl. |volume=7 |issue= 6 |pages= 160-71 |year= 1991 |pmid= 2076345 |doi= }}
*{{cite journal | author=Martiniuk F, Mehler M, Tzall S, ''et al.'' |title=Sequence of the cDNA and 5'-flanking region for human acid alpha-glucosidase, detection of an intron in the 5' untranslated leader sequence, definition of 18-bp polymorphisms, and differences with previous cDNA and amino acid sequences. |journal=DNA Cell Biol. |volume=9 |issue= 2 |pages= 85-94 |year= 1990 |pmid= 2111708 |doi= }}
*{{cite journal | author=Kalyanaraman VS, Rodriguez V, Veronese F, ''et al.'' |title=Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1. |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 3 |pages= 371-80 |year= 1990 |pmid= 2187500 |doi= }}
*{{cite journal | author=Martiniuk F, Bodkin M, Tzall S, Hirschhorn R |title=Identification of the base-pair substitution responsible for a human acid alpha glucosidase allele with lower "affinity" for glycogen (GAA 2) and transient gene expression in deficient cells. |journal=Am. J. Hum. Genet. |volume=47 |issue= 3 |pages= 440-5 |year= 1990 |pmid= 2203258 |doi= }}
*{{cite journal | author=Hoefsloot LH, Hoogeveen-Westerveld M, Reuser AJ, Oostra BA |title=Characterization of the human lysosomal alpha-glucosidase gene. |journal=Biochem. J. |volume=272 |issue= 2 |pages= 493-7 |year= 1991 |pmid= 2268276 |doi= }}
*{{cite journal | author=Shimizu H, Tsuchie H, Honma H, ''et al.'' |title=Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins. |journal=Jpn. J. Med. Sci. Biol. |volume=43 |issue= 3 |pages= 75-87 |year= 1991 |pmid= 2283726 |doi= }}
*{{cite journal | author=Leonard CK, Spellman MW, Riddle L, ''et al.'' |title=Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells. |journal=J. Biol. Chem. |volume=265 |issue= 18 |pages= 10373-82 |year= 1990 |pmid= 2355006 |doi= }}
*{{cite journal | author=Pal R, Hoke GM, Sarngadharan MG |title=Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3384-8 |year= 1989 |pmid= 2541446 |doi= }}
*{{cite journal | author=Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP |title=Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport. |journal=J. Virol. |volume=63 |issue= 6 |pages= 2452-6 |year= 1989 |pmid= 2542563 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HDAC4... {November 16, 2007 11:19:44 AM PST}
- SEARCH REDIRECT: Control Box Found: HDAC4 {November 16, 2007 11:20:17 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:20:18 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:20:18 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:20:18 AM PST}
- UPDATED: Updated protein page: HDAC4 {November 16, 2007 11:20:24 AM PST}
- INFO: Beginning work on PKD2... {November 16, 2007 11:12:00 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:12:30 AM 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 = Polycystic kidney disease 2 (autosomal dominant)
| HGNCid = 9009
| Symbol = PKD2
| AltSymbols =; PC2; APKD2; MGC138466; MGC138468; PKD4
| OMIM = 173910
| ECnumber =
| Homologene = 20104
| MGIid = 1099818
| Function = {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005247 |text = voltage-gated chloride channel activity}} {{GNF_GO|id=GO:0005248 |text = voltage-gated sodium channel activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0008092 |text = cytoskeletal protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005929 |text = cilium}} {{GNF_GO|id=GO:0005932 |text = basal body}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006812 |text = cation transport}} {{GNF_GO|id=GO:0006816 |text = calcium ion transport}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007259 |text = JAK-STAT cascade}} {{GNF_GO|id=GO:0007368 |text = determination of left/right symmetry}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0050974 |text = detection of mechanical stimulus during sensory perception}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5311
| Hs_Ensembl = ENSG00000118762
| Hs_RefseqProtein = NP_000288
| Hs_RefseqmRNA = NM_000297
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 89147844
| Hs_GenLoc_end = 89217952
| Hs_Uniprot = Q13563
| Mm_EntrezGene = 18764
| Mm_Ensembl = ENSMUSG00000034462
| Mm_RefseqmRNA = XM_984803
| Mm_RefseqProtein = XP_989897
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 104699752
| Mm_GenLoc_end = 104746120
| Mm_Uniprot = Q7TSI7
}}
}}
'''Polycystic kidney disease 2 (autosomal dominant)''', also known as '''PKD2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PKD2 polycystic kidney disease 2 (autosomal dominant)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5311| 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 polycystin protein family. The encoded protein contains multiple transmembrane domains, and cytoplasmic N- and C-termini. The protein may be an integral membrane protein involved in cell-cell/matrix interactions. The encoded protein may function in renal tubular development, morphology, and function, and may modulate intracellular calcium homoeostasis and other signal transduction pathways. This protein interacts with polycystin 1 to produce cation-permeable currents. Mutations in this gene have been associated with autosomal dominant polycystic kidney disease.<ref name="entrez">{{cite web | title = Entrez Gene: PKD2 polycystic kidney disease 2 (autosomal dominant)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5311| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Torres VE |title=New insights into polycystic kidney disease and its treatment. |journal=Curr. Opin. Nephrol. Hypertens. |volume=7 |issue= 2 |pages= 159-69 |year= 1998 |pmid= 9529618 |doi= }}
*{{cite journal | author=Deltas CC |title=Mutations of the human polycystic kidney disease 2 (PKD2) gene. |journal=Hum. Mutat. |volume=18 |issue= 1 |pages= 13-24 |year= 2001 |pmid= 11438989 |doi= 10.1002/humu.1145 }}
*{{cite journal | author=Boletta A, Germino GG |title=Role of polycystins in renal tubulogenesis. |journal=Trends Cell Biol. |volume=13 |issue= 9 |pages= 484-92 |year= 2004 |pmid= 12946628 |doi= }}
*{{cite journal | author=Cantiello HF |title=Regulation of calcium signaling by polycystin-2. |journal=Am. J. Physiol. Renal Physiol. |volume=286 |issue= 6 |pages= F1012-29 |year= 2004 |pmid= 15130895 |doi= 10.1152/ajprenal.00181.2003 }}
*{{cite journal | author=Everson GT, Taylor MR, Doctor RB |title=Polycystic disease of the liver. |journal=Hepatology |volume=40 |issue= 4 |pages= 774-82 |year= 2004 |pmid= 15382167 |doi= 10.1002/hep.20431 }}
*{{cite journal | author=Witzgall R |title=TRPP2 channel regulation. |journal=Handb Exp Pharmacol |volume= |issue= 179 |pages= 363-75 |year= 2007 |pmid= 17217069 |doi= 10.1007/978-3-540-34891-7_22 }}
*{{cite journal | author=Köttgen M |title=TRPP2 and autosomal dominant polycystic kidney disease. |journal=Biochim. Biophys. Acta |volume=1772 |issue= 8 |pages= 836-50 |year= 2007 |pmid= 17292589 |doi= 10.1016/j.bbadis.2007.01.003 }}
*{{cite journal | author=Peters DJ, Spruit L, Saris JJ, ''et al.'' |title=Chromosome 4 localization of a second gene for autosomal dominant polycystic kidney disease. |journal=Nat. Genet. |volume=5 |issue= 4 |pages= 359-62 |year= 1994 |pmid= 8298643 |doi= 10.1038/ng1293-359 }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Mochizuki T, Wu G, Hayashi T, ''et al.'' |title=PKD2, a gene for polycystic kidney disease that encodes an integral membrane protein. |journal=Science |volume=272 |issue= 5266 |pages= 1339-42 |year= 1996 |pmid= 8650545 |doi= }}
*{{cite journal | author=Schneider MC, Rodriguez AM, Nomura H, ''et al.'' |title=A gene similar to PKD1 maps to chromosome 4q22: a candidate gene for PKD2. |journal=Genomics |volume=38 |issue= 1 |pages= 1-4 |year= 1997 |pmid= 8954772 |doi= 10.1006/geno.1996.0584 }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Qian F, Germino FJ, Cai Y, ''et al.'' |title=PKD1 interacts with PKD2 through a probable coiled-coil domain. |journal=Nat. Genet. |volume=16 |issue= 2 |pages= 179-83 |year= 1997 |pmid= 9171830 |doi= 10.1038/ng0697-179 }}
*{{cite journal | author=Xenophontos S, Constantinides R, Hayashi T, ''et al.'' |title=A translation frameshift mutation induced by a cytosine insertion in the polycystic kidney disease 2 gene (PDK2). |journal=Hum. Mol. Genet. |volume=6 |issue= 6 |pages= 949-52 |year= 1997 |pmid= 9175744 |doi= }}
*{{cite journal | author=Tsiokas L, Kim E, Arnould T, ''et al.'' |title=Homo- and heterodimeric interactions between the gene products of PKD1 and PKD2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 13 |pages= 6965-70 |year= 1997 |pmid= 9192675 |doi= }}
*{{cite journal | author=Hayashi T, Mochizuki T, Reynolds DM, ''et al.'' |title=Characterization of the exon structure of the polycystic kidney disease 2 gene (PKD2). |journal=Genomics |volume=44 |issue= 1 |pages= 131-6 |year= 1997 |pmid= 9286709 |doi= 10.1006/geno.1997.4851 }}
*{{cite journal | author=Veldhuisen B, Saris JJ, de Haij S, ''et al.'' |title=A spectrum of mutations in the second gene for autosomal dominant polycystic kidney disease (PKD2). |journal=Am. J. Hum. Genet. |volume=61 |issue= 3 |pages= 547-55 |year= 1997 |pmid= 9326320 |doi= }}
*{{cite journal | author=Viribay M, Hayashi T, Tellería D, ''et al.'' |title=Novel stop and frameshifting mutations in the autosomal dominant polycystic kidney disease 2 (PKD2) gene. |journal=Hum. Genet. |volume=101 |issue= 2 |pages= 229-34 |year= 1998 |pmid= 9402976 |doi= }}
*{{cite journal | author=Pei Y, Wang K, Kasenda M, ''et al.'' |title=A novel frameshift mutation induced by an adenosine insertion in the polycystic kidney disease 2 (PKD2) gene. |journal=Kidney Int. |volume=53 |issue= 5 |pages= 1127-32 |year= 1998 |pmid= 9573526 |doi= 10.1046/j.1523-1755.1998.00890.x }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRF1... {November 16, 2007 11:12:30 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:13:11 AM 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 =
| image_source =
| PDB =
| Name = Perforin 1 (pore forming protein)
| HGNCid = 9360
| Symbol = PRF1
| AltSymbols =; FLH2; HPLH2; MGC65093; P1; PFP
| OMIM = 170280
| ECnumber =
| Homologene = 3698
| MGIid = 97551
| GeneAtlas_image1 = PBB_GE_PRF1_214617_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0016023 |text = cytoplasmic membrane-bound vesicle}}
| Process = {{GNF_GO|id=GO:0006926 |text = virus-infected cell apoptosis}} {{GNF_GO|id=GO:0006927 |text = transformed cell apoptosis}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0009405 |text = pathogenesis}} {{GNF_GO|id=GO:0019835 |text = cytolysis}} {{GNF_GO|id=GO:0019836 |text = hemolysis by symbiont of host red blood cells}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5551
| Hs_Ensembl = ENSG00000180644
| Hs_RefseqProtein = NP_005032
| Hs_RefseqmRNA = NM_005041
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 72027110
| Hs_GenLoc_end = 72032521
| Hs_Uniprot = P14222
| Mm_EntrezGene = 18646
| Mm_Ensembl = ENSMUSG00000037202
| Mm_RefseqmRNA = NM_011073
| Mm_RefseqProtein = NP_035203
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 60693191
| Mm_GenLoc_end = 60699667
| Mm_Uniprot = P10820
}}
}}
'''Perforin 1 (pore forming protein)''', also known as '''PRF1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRF1 perforin 1 (pore forming protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5551| 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 has structural and functional similarities to complement component 9 (C9). Like C9, this protein creates transmembrane tubules and is capable of lysing non-specifically a variety of target cells. This protein is one of the main cytolytic proteins of cytolytic granules, and it is known to be a key effector molecule for T-cell- and natural killer-cell-mediated cytolysis. Defects in this gene cause familial hemophagocytic lymphohistiocytosis type 2 (HPLH2), a rare and lethal autosomal recessive disorder of early childhood. Alternative splicing results in multiple transcript variants encoding the same protein.<ref name="entrez">{{cite web | title = Entrez Gene: PRF1 perforin 1 (pore forming protein)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5551| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Trapani JA |title=Target cell apoptosis induced by cytotoxic T cells and natural killer cells involves synergy between the pore-forming protein, perforin, and the serine protease, granzyme B. |journal=Australian and New Zealand journal of medicine |volume=25 |issue= 6 |pages= 793-9 |year= 1996 |pmid= 8770355 |doi= }}
*{{cite journal | author=Fink TM, Zimmer M, Weitz S, ''et al.'' |title=Human perforin (PRF1) maps to 10q22, a region that is syntenic with mouse chromosome 10. |journal=Genomics |volume=13 |issue= 4 |pages= 1300-2 |year= 1992 |pmid= 1505959 |doi= }}
*{{cite journal | author=Peitsch MC, Amiguet P, Guy R, ''et al.'' |title=Localization and molecular modelling of the membrane-inserted domain of the ninth component of human complement and perforin. |journal=Mol. Immunol. |volume=27 |issue= 7 |pages= 589-602 |year= 1990 |pmid= 2395434 |doi= }}
*{{cite journal | author=Young JD, Hengartner H, Podack ER, Cohn ZA |title=Purification and characterization of a cytolytic pore-forming protein from granules of cloned lymphocytes with natural killer activity. |journal=Cell |volume=44 |issue= 6 |pages= 849-59 |year= 1986 |pmid= 2420467 |doi= }}
*{{cite journal | author=Young JD, Cohn ZA, Podack ER |title=The ninth component of complement and the pore-forming protein (perforin 1) from cytotoxic T cells: structural, immunological, and functional similarities. |journal=Science |volume=233 |issue= 4760 |pages= 184-90 |year= 1986 |pmid= 2425429 |doi= }}
*{{cite journal | author=Lichtenheld MG, Podack ER |title=Structure of the human perforin gene. A simple gene organization with interesting potential regulatory sequences. |journal=J. Immunol. |volume=143 |issue= 12 |pages= 4267-74 |year= 1990 |pmid= 2480391 |doi= }}
*{{cite journal | author=Shinkai Y, Yoshida MC, Maeda K, ''et al.'' |title=Molecular cloning and chromosomal assignment of a human perforin (PFP) gene. |journal=Immunogenetics |volume=30 |issue= 6 |pages= 452-7 |year= 1990 |pmid= 2592021 |doi= }}
*{{cite journal | author=Shinkai Y, Takio K, Okumura K |title=Homology of perforin to the ninth component of complement (C9). |journal=Nature |volume=334 |issue= 6182 |pages= 525-7 |year= 1988 |pmid= 3261391 |doi= 10.1038/334525a0 }}
*{{cite journal | author=Lichtenheld MG, Olsen KJ, Lu P, ''et al.'' |title=Structure and function of human perforin. |journal=Nature |volume=335 |issue= 6189 |pages= 448-51 |year= 1988 |pmid= 3419519 |doi= 10.1038/335448a0 }}
*{{cite journal | author=Goebel WS, Schloemer RH, Brahmi Z |title=Target cell-induced perforin mRNA turnover in NK3.3 cells is mediated by multiple elements within the mRNA coding region. |journal=Mol. Immunol. |volume=33 |issue= 4-5 |pages= 341-9 |year= 1996 |pmid= 8676885 |doi= }}
*{{cite journal | author=Nöske K, Bilzer T, Planz O, Stitz L |title=Virus-specific CD4+ T cells eliminate borna disease virus from the brain via induction of cytotoxic CD8+ T cells. |journal=J. Virol. |volume=72 |issue= 5 |pages= 4387-95 |year= 1998 |pmid= 9557729 |doi= }}
*{{cite journal | author=Andrin C, Pinkoski MJ, Burns K, ''et al.'' |title=Interaction between a Ca2+-binding protein calreticulin and perforin, a component of the cytotoxic T-cell granules. |journal=Biochemistry |volume=37 |issue= 29 |pages= 10386-94 |year= 1998 |pmid= 9671507 |doi= 10.1021/bi980595z }}
*{{cite journal | author=Yu CR, Ortaldo JR, Curiel RE, ''et al.'' |title=Role of a STAT binding site in the regulation of the human perforin promoter. |journal=J. Immunol. |volume=162 |issue= 5 |pages= 2785-90 |year= 1999 |pmid= 10072525 |doi= }}
*{{cite journal | author=Stepp SE, Dufourcq-Lagelouse R, Le Deist F, ''et al.'' |title=Perforin gene defects in familial hemophagocytic lymphohistiocytosis. |journal=Science |volume=286 |issue= 5446 |pages= 1957-9 |year= 1999 |pmid= 10583959 |doi= }}
*{{cite journal | author=Takahashi T, Nieda M, Koezuka Y, ''et al.'' |title=Analysis of human V alpha 24+ CD4+ NKT cells activated by alpha-glycosylceramide-pulsed monocyte-derived dendritic cells. |journal=J. Immunol. |volume=164 |issue= 9 |pages= 4458-64 |year= 2000 |pmid= 10779745 |doi= }}
*{{cite journal | author=Badovinac VP, Tvinnereim AR, Harty JT |title=Regulation of antigen-specific CD8+ T cell homeostasis by perforin and interferon-gamma. |journal=Science |volume=290 |issue= 5495 |pages= 1354-8 |year= 2000 |pmid= 11082062 |doi= }}
*{{cite journal | author=Göransdotter Ericson K, Fadeel B, Nilsson-Ardnor S, ''et al.'' |title=Spectrum of perforin gene mutations in familial hemophagocytic lymphohistiocytosis. |journal=Am. J. Hum. Genet. |volume=68 |issue= 3 |pages= 590-7 |year= 2001 |pmid= 11179007 |doi= }}
*{{cite journal | author=Clementi R, zur Stadt U, Savoldi G, ''et al.'' |title=Six novel mutations in the PRF1 gene in children with haemophagocytic lymphohistiocytosis. |journal=J. Med. Genet. |volume=38 |issue= 9 |pages= 643-6 |year= 2002 |pmid= 11565555 |doi= }}
*{{cite journal | author=Ambach A, Bonnekoh B, Gollnick H |title=Perforin granule release from cytotoxic lymphocytes ex vivo is inhibited by ciclosporin but not by methotrexate. |journal=Skin Pharmacol. Appl. Skin Physiol. |volume=14 |issue= 5 |pages= 249-60 |year= 2001 |pmid= 11586066 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMC5... {November 16, 2007 11:13:11 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:13:43 AM 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) 26S subunit, ATPase, 5
| HGNCid = 9552
| Symbol = PSMC5
| AltSymbols =; p45; S8; SUG1; TBP10; TRIP1; p45/SUG
| OMIM = 601681
| ECnumber =
| Homologene = 2098
| MGIid = 105047
| GeneAtlas_image1 = PBB_GE_PSMC5_209503_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003712 |text = transcription cofactor activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0031531 |text = thyrotropin-releasing hormone receptor binding}}
| Component = {{GNF_GO|id=GO:0000502 |text = proteasome complex (sensu Eukaryota)}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} {{GNF_GO|id=GO:0030163 |text = protein catabolic process}} {{GNF_GO|id=GO:0043069 |text = negative regulation of programmed cell death}} {{GNF_GO|id=GO:0043161 |text = proteasomal ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0043193 |text = positive regulation of gene-specific transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5705
| Hs_Ensembl = ENSG00000087191
| Hs_RefseqProtein = NP_002796
| Hs_RefseqmRNA = NM_002805
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 59258519
| Hs_GenLoc_end = 59263098
| Hs_Uniprot = P62195
| Mm_EntrezGene = 19184
| Mm_Ensembl = ENSMUSG00000020708
| Mm_RefseqmRNA = NM_008950
| Mm_RefseqProtein = NP_032976
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 106072244
| Mm_GenLoc_end = 106079207
| Mm_Uniprot = Q99KR1
}}
}}
'''Proteasome (prosome, macropain) 26S subunit, ATPase, 5''', also known as '''PSMC5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMC5 proteasome (prosome, macropain) 26S subunit, ATPase, 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5705| 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. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. In addition to participation in proteasome functions, this subunit may participate in transcriptional regulation since it has been shown to interact with the thyroid hormone receptor and retinoid X receptor-alpha.<ref name="entrez">{{cite web | title = Entrez Gene: PSMC5 proteasome (prosome, macropain) 26S subunit, ATPase, 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5705| 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=Nelbock P, Dillon PJ, Perkins A, Rosen CA |title=A cDNA for a protein that interacts with the human immunodeficiency virus Tat transactivator. |journal=Science |volume=248 |issue= 4963 |pages= 1650-3 |year= 1990 |pmid= 2194290 |doi= }}
*{{cite journal | author=Akiyama K, Yokota K, Kagawa S, ''et al.'' |title=cDNA cloning of a new putative ATPase subunit p45 of the human 26S proteasome, a homolog of yeast transcriptional factor Sug1p. |journal=FEBS Lett. |volume=363 |issue= 1-2 |pages= 151-6 |year= 1995 |pmid= 7729537 |doi= }}
*{{cite journal | author=Lee JW, Choi HS, Gyuris J, ''et al.'' |title=Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. |journal=Mol. Endocrinol. |volume=9 |issue= 2 |pages= 243-54 |year= 1995 |pmid= 7776974 |doi= }}
*{{cite journal | author=Lee JW, Ryan F, Swaffield JC, ''et al.'' |title=Interaction of thyroid-hormone receptor with a conserved transcriptional mediator. |journal=Nature |volume=374 |issue= 6517 |pages= 91-4 |year= 1995 |pmid= 7870181 |doi= 10.1038/374091a0 }}
*{{cite journal | author=Shaw DR, Ennis HL |title=Molecular cloning and developmental regulation of Dictyostelium discoideum homologues of the human and yeast HIV1 Tat-binding protein. |journal=Biochem. Biophys. Res. Commun. |volume=193 |issue= 3 |pages= 1291-6 |year= 1993 |pmid= 8323548 |doi= 10.1006/bbrc.1993.1765 }}
*{{cite journal | author=Ohana B, Moore PA, Ruben SM, ''et al.'' |title=The type 1 human immunodeficiency virus Tat binding protein is a transcriptional activator belonging to an additional family of evolutionarily conserved genes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 1 |pages= 138-42 |year= 1993 |pmid= 8419915 |doi= }}
*{{cite journal | author=Dubiel W, Ferrell K, Rechsteiner M |title=Peptide sequencing identifies MSS1, a modulator of HIV Tat-mediated transactivation, as subunit 7 of the 26 S protease. |journal=FEBS Lett. |volume=323 |issue= 3 |pages= 276-8 |year= 1993 |pmid= 8500623 |doi= }}
*{{cite journal | author=vom Baur E, Zechel C, Heery D, ''et al.'' |title=Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1. |journal=EMBO J. |volume=15 |issue= 1 |pages= 110-24 |year= 1996 |pmid= 8598193 |doi= }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Wang W, Chevray PM, Nathans D |title=Mammalian Sug1 and c-Fos in the nuclear 26S proteasome. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 16 |pages= 8236-40 |year= 1996 |pmid= 8710853 |doi= }}
*{{cite journal | author=Hoyle J, Tan KH, Fisher EM |title=Localization of genes encoding two human one-domain members of the AAA family: PSMC5 (the thyroid hormone receptor-interacting protein, TRIP1) and PSMC3 (the Tat-binding protein, TBP1). |journal=Hum. Genet. |volume=99 |issue= 2 |pages= 285-8 |year= 1997 |pmid= 9048938 |doi= }}
*{{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=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Weeda G, Rossignol M, Fraser RA, ''et al.'' |title=The XPB subunit of repair/transcription factor TFIIH directly interacts with SUG1, a subunit of the 26S proteasome and putative transcription factor. |journal=Nucleic Acids Res. |volume=25 |issue= 12 |pages= 2274-83 |year= 1997 |pmid= 9173976 |doi= }}
*{{cite journal | author=Chen Y, Sharp ZD, Lee WH |title=HEC binds to the seventh regulatory subunit of the 26 S proteasome and modulates the proteolysis of mitotic cyclins. |journal=J. Biol. Chem. |volume=272 |issue= 38 |pages= 24081-7 |year= 1997 |pmid= 9295362 |doi= }}
*{{cite journal | author=Tipler CP, Hutchon SP, Hendil K, ''et al.'' |title=Purification and characterization of 26S proteasomes from human and mouse spermatozoa. |journal=Mol. Hum. Reprod. |volume=3 |issue= 12 |pages= 1053-60 |year= 1998 |pmid= 9464850 |doi= }}
*{{cite journal | author=Tanahashi N, Suzuki M, Fujiwara T, ''et al.'' |title=Chromosomal localization and immunological analysis of a family of human 26S proteasomal ATPases. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 1 |pages= 229-32 |year= 1998 |pmid= 9473509 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTHR1... {November 16, 2007 11:13:43 AM PST}
- SEARCH REDIRECT: Control Box Found: PTHR1 {November 16, 2007 11:14:09 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:14:11 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:14:11 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:14:11 AM PST}
- UPDATED: Updated protein page: PTHR1 {November 16, 2007 11:14:17 AM PST}
- INFO: Beginning work on PTMA... {November 16, 2007 11:14:17 AM PST}
- SEARCH REDIRECT: Control Box Found: PTMA {November 16, 2007 11:14:42 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:14:44 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:14:44 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:14:44 AM PST}
- UPDATED: Updated protein page: PTMA {November 16, 2007 11:14:49 AM PST}
- INFO: Beginning work on PTN... {November 16, 2007 11:14:49 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:15:22 AM 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 = Pleiotrophin (heparin binding growth factor 8, neurite growth-promoting factor 1)
| HGNCid = 9630
| Symbol = PTN
| AltSymbols =; HARP; HBGF8; HBNF; NEGF1
| OMIM = 162095
| ECnumber =
| Homologene = 2117
| MGIid = 97804
| GeneAtlas_image1 = PBB_GE_PTN_209465_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_PTN_209466_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_PTN_211737_x_at_tn.png
| Function = {{GNF_GO|id=GO:0004864 |text = protein phosphatase inhibitor activity}} {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0007185 |text = transmembrane receptor protein tyrosine phosphatase signaling pathway}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007612 |text = learning}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0030282 |text = bone mineralization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5764
| Hs_Ensembl = ENSG00000105894
| Hs_RefseqProtein = NP_002816
| Hs_RefseqmRNA = NM_002825
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 136562637
| Hs_GenLoc_end = 136679086
| Hs_Uniprot = P21246
| Mm_EntrezGene = 19242
| Mm_Ensembl = ENSMUSG00000029838
| Mm_RefseqmRNA = NM_008973
| Mm_RefseqProtein = NP_032999
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 36645087
| Mm_GenLoc_end = 36741513
| Mm_Uniprot = Q3TSS2
}}
}}
'''Pleiotrophin (heparin binding growth factor 8, neurite growth-promoting factor 1)''', also known as '''PTN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTN pleiotrophin (heparin binding growth factor 8, neurite growth-promoting factor 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5764| 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=Milner PG, Shah D, Veile R, ''et al.'' |title=Cloning, nucleotide sequence, and chromosome localization of the human pleiotrophin gene. |journal=Biochemistry |volume=31 |issue= 48 |pages= 12023-8 |year= 1993 |pmid= 1457401 |doi= }}
*{{cite journal | author=Li YS, Hoffman RM, Le Beau MM, ''et al.'' |title=Characterization of the human pleiotrophin gene. Promoter region and chromosomal localization. |journal=J. Biol. Chem. |volume=267 |issue= 36 |pages= 26011-6 |year= 1993 |pmid= 1464612 |doi= }}
*{{cite journal | author=Tezuka K, Takeshita S, Hakeda Y, ''et al.'' |title=Isolation of mouse and human cDNA clones encoding a protein expressed specifically in osteoblasts and brain tissues. |journal=Biochem. Biophys. Res. Commun. |volume=173 |issue= 1 |pages= 246-51 |year= 1991 |pmid= 1701634 |doi= }}
*{{cite journal | author=Wellstein A, Fang WJ, Khatri A, ''et al.'' |title=A heparin-binding growth factor secreted from breast cancer cells homologous to a developmentally regulated cytokine. |journal=J. Biol. Chem. |volume=267 |issue= 4 |pages= 2582-7 |year= 1992 |pmid= 1733956 |doi= }}
*{{cite journal | author=Kretschmer PJ, Fairhurst JL, Decker MM, ''et al.'' |title=Cloning, characterization and developmental regulation of two members of a novel human gene family of neurite outgrowth-promoting proteins. |journal=Growth Factors |volume=5 |issue= 2 |pages= 99-114 |year= 1992 |pmid= 1768439 |doi= }}
*{{cite journal | author=Li YS, Milner PG, Chauhan AK, ''et al.'' |title=Cloning and expression of a developmentally regulated protein that induces mitogenic and neurite outgrowth activity. |journal=Science |volume=250 |issue= 4988 |pages= 1690-4 |year= 1991 |pmid= 2270483 |doi= }}
*{{cite journal | author=Huber D, Gautschi-Sova P, Böhlen P |title=Amino-terminal sequences of a novel heparin-binding protein from human, bovine, rat, and chick brain: high interspecies homology. |journal=Neurochem. Res. |volume=15 |issue= 4 |pages= 435-9 |year= 1990 |pmid= 2388713 |doi= }}
*{{cite journal | author=Asundi VK, Carey DJ |title=Self-association of N-syndecan (syndecan-3) core protein is mediated by a novel structural motif in the transmembrane domain and ectodomain flanking region. |journal=J. Biol. Chem. |volume=270 |issue= 44 |pages= 26404-10 |year= 1995 |pmid= 7592855 |doi= }}
*{{cite journal | author=Raulo E, Chernousov MA, Carey DJ, ''et al.'' |title=Isolation of a neuronal cell surface receptor of heparin binding growth-associated molecule (HB-GAM). Identification as N-syndecan (syndecan-3). |journal=J. Biol. Chem. |volume=269 |issue= 17 |pages= 12999-3004 |year= 1994 |pmid= 8175719 |doi= }}
*{{cite journal | author=Fabri L, Maruta H, Muramatsu H, ''et al.'' |title=Structural characterisation of native and recombinant forms of the neurotrophic cytokine MK. |journal=J. Chromatogr. |volume=646 |issue= 1 |pages= 213-25 |year= 1993 |pmid= 8408430 |doi= }}
*{{cite journal | author=Kretschmer PJ, Fairhurst JL, Hulmes JD, ''et al.'' |title=Genomic organization of the human HBNF gene and characterization of an HBNF variant protein as a splice mutant. |journal=Biochem. Biophys. Res. Commun. |volume=192 |issue= 2 |pages= 420-9 |year= 1993 |pmid= 8484754 |doi= 10.1006/bbrc.1993.1432 }}
*{{cite journal | author=Hulmes JD, Seddon AP, Decker MM, Böhlen P |title=Comparison of the disulfide bond arrangements of human recombinant and bovine brain heparin binding neurite-promoting factors. |journal=Biochem. Biophys. Res. Commun. |volume=192 |issue= 2 |pages= 738-46 |year= 1993 |pmid= 8484780 |doi= 10.1006/bbrc.1993.1476 }}
*{{cite journal | author=Kinnunen T, Raulo E, Nolo R, ''et al.'' |title=Neurite outgrowth in brain neurons induced by heparin-binding growth-associated molecule (HB-GAM) depends on the specific interaction of HB-GAM with heparan sulfate at the cell surface. |journal=J. Biol. Chem. |volume=271 |issue= 4 |pages= 2243-8 |year= 1996 |pmid= 8567685 |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=Masuda H, Tsujimura A, Yoshioka M, ''et al.'' |title=Bone mass loss due to estrogen deficiency is compensated in transgenic mice overexpressing human osteoblast stimulating factor-1. |journal=Biochem. Biophys. Res. Commun. |volume=238 |issue= 2 |pages= 528-33 |year= 1997 |pmid= 9299545 |doi= 10.1006/bbrc.1997.7188 }}
*{{cite journal | author=Milev P, Chiba A, Häring M, ''et al.'' |title=High affinity binding and overlapping localization of neurocan and phosphacan/protein-tyrosine phosphatase-zeta/beta with tenascin-R, amphoterin, and the heparin-binding growth-associated molecule. |journal=J. Biol. Chem. |volume=273 |issue= 12 |pages= 6998-7005 |year= 1998 |pmid= 9507007 |doi= }}
*{{cite journal | author=Fages C, Kaksonen M, Kinnunen T, ''et al.'' |title=Regulation of mRNA localization by transmembrane signalling: local interaction of HB-GAM (heparin-binding growth-associated molecule) with the cell surface localizes beta-actin mRNA. |journal=J. Cell. Sci. |volume=111 ( Pt 20) |issue= |pages= 3073-80 |year= 1998 |pmid= 9739080 |doi= }}
*{{cite journal | author=Zhang N, Zhong R, Deuel TF |title=Domain structure of pleiotrophin required for transformation. |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 12959-62 |year= 1999 |pmid= 10224041 |doi= }}
*{{cite journal | author=Bernard-Pierrot I, Héroult M, Lemaître G, ''et al.'' |title=Glycosaminoglycans promote HARP/PTN dimerization. |journal=Biochem. Biophys. Res. Commun. |volume=266 |issue= 2 |pages= 437-42 |year= 2000 |pmid= 10600521 |doi= 10.1006/bbrc.1999.1835 }}
*{{cite journal | author=Meng K, Rodriguez-Peña A, Dimitrov T, ''et al.'' |title=Pleiotrophin signals increased tyrosine phosphorylation of beta beta-catenin through inactivation of the intrinsic catalytic activity of the receptor-type protein tyrosine phosphatase beta/zeta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 6 |pages= 2603-8 |year= 2000 |pmid= 10706604 |doi= 10.1073/pnas.020487997 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAD50... {November 16, 2007 11:20:24 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:20:59 AM 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 = RAD50 homolog (S. cerevisiae)
| HGNCid = 9816
| Symbol = RAD50
| AltSymbols =; RAD50-2; hRad50
| OMIM = 604040
| ECnumber =
| Homologene = 38092
| MGIid = 109292
| GeneAtlas_image1 = PBB_GE_RAD50_208393_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RAD50_209349_at_tn.png
| Function = {{GNF_GO|id=GO:0000014 |text = single-stranded DNA specific endodeoxyribonuclease activity}} {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004518 |text = nuclease activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008408 |text = 3'-5' exonuclease activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0030674 |text = protein binding, bridging}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0000781 |text = chromosome, telomeric region}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}} {{GNF_GO|id=GO:0030870 |text = Mre11 complex}}
| Process = {{GNF_GO|id=GO:0000019 |text = regulation of mitotic recombination}} {{GNF_GO|id=GO:0006302 |text = double-strand break repair}} {{GNF_GO|id=GO:0007004 |text = telomere maintenance via telomerase}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007126 |text = meiosis}} {{GNF_GO|id=GO:0007131 |text = meiotic recombination}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 10111
| Hs_Ensembl = ENSG00000113522
| Hs_RefseqProtein = NP_005723
| Hs_RefseqmRNA = NM_005732
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 131920529
| Hs_GenLoc_end = 132007651
| Hs_Uniprot = Q92878
| Mm_EntrezGene = 19360
| Mm_Ensembl = ENSMUSG00000020380
| Mm_RefseqmRNA = NM_009012
| Mm_RefseqProtein = NP_033038
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 53492942
| Mm_GenLoc_end = 53550742
| Mm_Uniprot = Q3UNL2
}}
}}
'''RAD50 homolog (S. cerevisiae)''', also known as '''RAD50''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAD50 RAD50 homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10111| 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 highly similar to Saccharomyces cerevisiae Rad50, a protein involved in DNA double-strand break repair. This protein forms a complex with MRE11 and NBS1. The protein complex binds to DNA and displays numerous enzymatic activities that are required for nonhomologous joining of DNA ends. This protein, cooperating with its partners, is important for DNA double-strand break repair, cell cycle checkpoint activation, telomere maintenance, and meiotic recombination. Knockout studies of the mouse homolog suggest this gene is essential for cell growth and viability. Two alternatively spliced transcript variants of this gene, which encode distinct proteins, have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: RAD50 RAD50 homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10111| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Stracker TH, Theunissen JW, Morales M, Petrini JH |title=The Mre11 complex and the metabolism of chromosome breaks: the importance of communicating and holding things together. |journal=DNA Repair (Amst.) |volume=3 |issue= 8-9 |pages= 845-54 |year= 2005 |pmid= 15279769 |doi= 10.1016/j.dnarep.2004.03.014 }}
*{{cite journal | author=Dolganov GM, Maser RS, Novikov A, ''et al.'' |title=Human Rad50 is physically associated with human Mre11: identification of a conserved multiprotein complex implicated in recombinational DNA repair. |journal=Mol. Cell. Biol. |volume=16 |issue= 9 |pages= 4832-41 |year= 1996 |pmid= 8756642 |doi= }}
*{{cite journal | author=Maser RS, Monsen KJ, Nelms BE, Petrini JH |title=hMre11 and hRad50 nuclear foci are induced during the normal cellular response to DNA double-strand breaks. |journal=Mol. Cell. Biol. |volume=17 |issue= 10 |pages= 6087-96 |year= 1997 |pmid= 9315668 |doi= }}
*{{cite journal | author=Carney JP, Maser RS, Olivares H, ''et al.'' |title=The hMre11/hRad50 protein complex and Nijmegen breakage syndrome: linkage of double-strand break repair to the cellular DNA damage response. |journal=Cell |volume=93 |issue= 3 |pages= 477-86 |year= 1998 |pmid= 9590181 |doi= }}
*{{cite journal | author=Paull TT, Gellert M |title=The 3' to 5' exonuclease activity of Mre 11 facilitates repair of DNA double-strand breaks. |journal=Mol. Cell |volume=1 |issue= 7 |pages= 969-79 |year= 1998 |pmid= 9651580 |doi= }}
*{{cite journal | author=Trujillo KM, Yuan SS, Lee EY, Sung P |title=Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95. |journal=J. Biol. Chem. |volume=273 |issue= 34 |pages= 21447-50 |year= 1998 |pmid= 9705271 |doi= }}
*{{cite journal | author=Paull TT, Gellert M |title=Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex. |journal=Genes Dev. |volume=13 |issue= 10 |pages= 1276-88 |year= 1999 |pmid= 10346816 |doi= }}
*{{cite journal | author=Kim KK, Shin BA, Seo KH, ''et al.'' |title=Molecular cloning and characterization of splice variants of human RAD50 gene. |journal=Gene |volume=235 |issue= 1-2 |pages= 59-67 |year= 1999 |pmid= 10415333 |doi= }}
*{{cite journal | author=Zhong Q, Chen CF, Li S, ''et al.'' |title=Association of BRCA1 with the hRad50-hMre11-p95 complex and the DNA damage response. |journal=Science |volume=285 |issue= 5428 |pages= 747-50 |year= 1999 |pmid= 10426999 |doi= }}
*{{cite journal | author=Wang Y, Cortez D, Yazdi P, ''et al.'' |title=BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures. |journal=Genes Dev. |volume=14 |issue= 8 |pages= 927-39 |year= 2000 |pmid= 10783165 |doi= }}
*{{cite journal | author=Gatei M, Young D, Cerosaletti KM, ''et al.'' |title=ATM-dependent phosphorylation of nibrin in response to radiation exposure. |journal=Nat. Genet. |volume=25 |issue= 1 |pages= 115-9 |year= 2000 |pmid= 10802669 |doi= 10.1038/75508 }}
*{{cite journal | author=Zhao S, Weng YC, Yuan SS, ''et al.'' |title=Functional link between ataxia-telangiectasia and Nijmegen breakage syndrome gene products. |journal=Nature |volume=405 |issue= 6785 |pages= 473-7 |year= 2000 |pmid= 10839544 |doi= 10.1038/35013083 }}
*{{cite journal | author=Zhu XD, Küster B, Mann M, ''et al.'' |title=Cell-cycle-regulated association of RAD50/MRE11/NBS1 with TRF2 and human telomeres. |journal=Nat. Genet. |volume=25 |issue= 3 |pages= 347-52 |year= 2000 |pmid= 10888888 |doi= 10.1038/77139 }}
*{{cite journal | author=Paull TT, Rogakou EP, Yamazaki V, ''et al.'' |title=A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage. |journal=Curr. Biol. |volume=10 |issue= 15 |pages= 886-95 |year= 2001 |pmid= 10959836 |doi= }}
*{{cite journal | author=Xiao J, Liu CC, Chen PL, Lee WH |title=RINT-1, a novel Rad50-interacting protein, participates in radiation-induced G(2)/M checkpoint control. |journal=J. Biol. Chem. |volume=276 |issue= 9 |pages= 6105-11 |year= 2001 |pmid= 11096100 |doi= 10.1074/jbc.M008893200 }}
*{{cite journal | author=Desai-Mehta A, Cerosaletti KM, Concannon P |title=Distinct functional domains of nibrin mediate Mre11 binding, focus formation, and nuclear localization. |journal=Mol. Cell. Biol. |volume=21 |issue= 6 |pages= 2184-91 |year= 2001 |pmid= 11238951 |doi= 10.1128/MCB.21.6.2184-2191.2001 }}
*{{cite journal | author=Buscemi G, Savio C, Zannini L, ''et al.'' |title=Chk2 activation dependence on Nbs1 after DNA damage. |journal=Mol. Cell. Biol. |volume=21 |issue= 15 |pages= 5214-22 |year= 2001 |pmid= 11438675 |doi= 10.1128/MCB.21.15.5214-5222.2001 }}
*{{cite journal | author=Chiba N, Parvin JD |title=Redistribution of BRCA1 among four different protein complexes following replication blockage. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 38549-54 |year= 2001 |pmid= 11504724 |doi= 10.1074/jbc.M105227200 }}
*{{cite journal | author=Grenon M, Gilbert C, Lowndes NF |title=Checkpoint activation in response to double-strand breaks requires the Mre11/Rad50/Xrs2 complex. |journal=Nat. Cell Biol. |volume=3 |issue= 9 |pages= 844-7 |year= 2001 |pmid= 11533665 |doi= 10.1038/ncb0901-844 }}
*{{cite journal | author=de Jager M, van Noort J, van Gent DC, ''et al.'' |title=Human Rad50/Mre11 is a flexible complex that can tether DNA ends. |journal=Mol. Cell |volume=8 |issue= 5 |pages= 1129-35 |year= 2002 |pmid= 11741547 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RBBP4... {November 16, 2007 11:15:22 AM PST}
- SEARCH REDIRECT: Control Box Found: RBBP4 {November 16, 2007 11:15:43 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:15:46 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:15:46 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:15:46 AM PST}
- UPDATED: Updated protein page: RBBP4 {November 16, 2007 11:15:51 AM PST}
- INFO: Beginning work on SCNN1B... {November 16, 2007 11:15:51 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:16:20 AM 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 = Sodium channel, nonvoltage-gated 1, beta (Liddle syndrome)
| HGNCid = 10600
| Symbol = SCNN1B
| AltSymbols =; ENaCb; ENaCbeta; SCNEB
| OMIM = 600760
| ECnumber =
| Homologene = 284
| MGIid = 104696
| GeneAtlas_image1 = PBB_GE_SCNN1B_205464_at_tn.png
| Function = {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015280 |text = amiloride-sensitive sodium channel activity}} {{GNF_GO|id=GO:0031402 |text = sodium ion binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006814 |text = sodium ion transport}} {{GNF_GO|id=GO:0007588 |text = excretion}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6338
| Hs_Ensembl = ENSG00000168447
| Hs_RefseqProtein = NP_000327
| Hs_RefseqmRNA = NM_000336
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 23221133
| Hs_GenLoc_end = 23300120
| Hs_Uniprot = P51168
| Mm_EntrezGene = 20277
| Mm_Ensembl = ENSMUSG00000030873
| Mm_RefseqmRNA = NM_011325
| Mm_RefseqProtein = NP_035455
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 121656228
| Mm_GenLoc_end = 121709876
| Mm_Uniprot = Q3TP51
}}
}}
'''Sodium channel, nonvoltage-gated 1, beta (Liddle syndrome)''', also known as '''SCNN1B''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SCNN1B sodium channel, nonvoltage-gated 1, beta (Liddle syndrome)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6338| 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=Alvarez de la Rosa D, Canessa CM, Fyfe GK, Zhang P |title=Structure and regulation of amiloride-sensitive sodium channels. |journal=Annu. Rev. Physiol. |volume=62 |issue= |pages= 573-94 |year= 2000 |pmid= 10845103 |doi= 10.1146/annurev.physiol.62.1.573 }}
*{{cite journal | author=Rossier BC, Pradervand S, Schild L, Hummler E |title=Epithelial sodium channel and the control of sodium balance: interaction between genetic and environmental factors. |journal=Annu. Rev. Physiol. |volume=64 |issue= |pages= 877-97 |year= 2002 |pmid= 11826291 |doi= 10.1146/annurev.physiol.64.082101.143243 }}
*{{cite journal | author=Peters KW, Qi J, Johnson JP, ''et al.'' |title=Role of snare proteins in CFTR and ENaC trafficking. |journal=Pflugers Arch. |volume=443 Suppl 1 |issue= |pages= S65-9 |year= 2002 |pmid= 11845306 |doi= 10.1007/s004240100647 }}
*{{cite journal | author=Edelheit O, Hanukoglu I, Gizewska M, ''et al.'' |title=Novel mutations in epithelial sodium channel (ENaC) subunit genes and phenotypic expression of multisystem pseudohypoaldosteronism. |journal=Clin. Endocrinol. (Oxf) |volume=62 |issue= 5 |pages= 547-53 |year= 2005 |pmid= 15853823 |doi= 10.1111/j.1365-2265.2005.02255.x }}
*{{cite journal | author=Voilley N, Bassilana F, Mignon C, ''et al.'' |title=Cloning, chromosomal localization, and physical linkage of the beta and gamma subunits (SCNN1B and SCNN1G) of the human epithelial amiloride-sensitive sodium channel. |journal=Genomics |volume=28 |issue= 3 |pages= 560-5 |year= 1996 |pmid= 7490094 |doi= 10.1006/geno.1995.1188 }}
*{{cite journal | author=Waldmann R, Champigny G, Bassilana F, ''et al.'' |title=Molecular cloning and functional expression of a novel amiloride-sensitive Na+ channel. |journal=J. Biol. Chem. |volume=270 |issue= 46 |pages= 27411-4 |year= 1996 |pmid= 7499195 |doi= }}
*{{cite journal | author=Hansson JH, Nelson-Williams C, Suzuki H, ''et al.'' |title=Hypertension caused by a truncated epithelial sodium channel gamma subunit: genetic heterogeneity of Liddle syndrome. |journal=Nat. Genet. |volume=11 |issue= 1 |pages= 76-82 |year= 1995 |pmid= 7550319 |doi= 10.1038/ng0995-76 }}
*{{cite journal | author=McDonald FJ, Price MP, Snyder PM, Welsh MJ |title=Cloning and expression of the beta- and gamma-subunits of the human epithelial sodium channel. |journal=Am. J. Physiol. |volume=268 |issue= 5 Pt 1 |pages= C1157-63 |year= 1995 |pmid= 7762608 |doi= }}
*{{cite journal | author=Shimkets RA, Warnock DG, Bositis CM, ''et al.'' |title=Liddle's syndrome: heritable human hypertension caused by mutations in the beta subunit of the epithelial sodium channel. |journal=Cell |volume=79 |issue= 3 |pages= 407-14 |year= 1994 |pmid= 7954808 |doi= }}
*{{cite journal | author=Snyder PM, Price MP, McDonald FJ, ''et al.'' |title=Mechanism by which Liddle's syndrome mutations increase activity of a human epithelial Na+ channel. |journal=Cell |volume=83 |issue= 6 |pages= 969-78 |year= 1996 |pmid= 8521520 |doi= }}
*{{cite journal | author=Hansson JH, Schild L, Lu Y, ''et al.'' |title=A de novo missense mutation of the beta subunit of the epithelial sodium channel causes hypertension and Liddle syndrome, identifying a proline-rich segment critical for regulation of channel activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 25 |pages= 11495-9 |year= 1996 |pmid= 8524790 |doi= }}
*{{cite journal | author=Chang SS, Grunder S, Hanukoglu A, ''et al.'' |title=Mutations in subunits of the epithelial sodium channel cause salt wasting with hyperkalaemic acidosis, pseudohypoaldosteronism type 1. |journal=Nat. Genet. |volume=12 |issue= 3 |pages= 248-53 |year= 1996 |pmid= 8589714 |doi= 10.1038/ng0396-248 }}
*{{cite journal | author=Tamura H, Schild L, Enomoto N, ''et al.'' |title=Liddle disease caused by a missense mutation of beta subunit of the epithelial sodium channel gene. |journal=J. Clin. Invest. |volume=97 |issue= 7 |pages= 1780-4 |year= 1996 |pmid= 8601645 |doi= }}
*{{cite journal | author=Firsov D, Schild L, Gautschi I, ''et al.'' |title=Cell surface expression of the epithelial Na channel and a mutant causing Liddle syndrome: a quantitative approach. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 26 |pages= 15370-5 |year= 1997 |pmid= 8986818 |doi= }}
*{{cite journal | author=Gründer S, Firsov D, Chang SS, ''et al.'' |title=A mutation causing pseudohypoaldosteronism type 1 identifies a conserved glycine that is involved in the gating of the epithelial sodium channel. |journal=EMBO J. |volume=16 |issue= 5 |pages= 899-907 |year= 1997 |pmid= 9118951 |doi= 10.1093/emboj/16.5.899 }}
*{{cite journal | author=Pirozzi G, McConnell SJ, Uveges AJ, ''et al.'' |title=Identification of novel human WW domain-containing proteins by cloning of ligand targets. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 14611-6 |year= 1997 |pmid= 9169421 |doi= }}
*{{cite journal | author=Inoue J, Iwaoka T, Tokunaga H, ''et al.'' |title=A family with Liddle's syndrome caused by a new missense mutation in the beta subunit of the epithelial sodium channel. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 6 |pages= 2210-3 |year= 1998 |pmid= 9626162 |doi= }}
*{{cite journal | author=Persu A, Barbry P, Bassilana F, ''et al.'' |title=Genetic analysis of the beta subunit of the epithelial Na+ channel in essential hypertension. |journal=Hypertension |volume=32 |issue= 1 |pages= 129-37 |year= 1998 |pmid= 9674649 |doi= }}
*{{cite journal | author=Uehara Y, Sasaguri M, Kinoshita A, ''et al.'' |title=Genetic analysis of the epithelial sodium channel in Liddle's syndrome. |journal=J. Hypertens. |volume=16 |issue= 8 |pages= 1131-5 |year= 1998 |pmid= 9794716 |doi= }}
*{{cite journal | author=Saxena A, Hanukoglu I, Strautnieks SS, ''et al.'' |title=Gene structure of the human amiloride-sensitive epithelial sodium channel beta subunit. |journal=Biochem. Biophys. Res. Commun. |volume=252 |issue= 1 |pages= 208-13 |year= 1998 |pmid= 9813171 |doi= 10.1006/bbrc.1998.9625 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SFTPB... {November 16, 2007 11:16:20 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:16:53 AM 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 = Surfactant, pulmonary-associated protein B
| HGNCid = 10801
| Symbol = SFTPB
| AltSymbols =; PSP-B; SFTB3; SFTP3; SP-B
| OMIM = 178640
| ECnumber =
| Homologene = 456
| MGIid = 109516
| GeneAtlas_image1 = PBB_GE_SFTPB_213936_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_SFTPB_214354_x_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005764 |text = lysosome}}
| Process = {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006665 |text = sphingolipid metabolic process}} {{GNF_GO|id=GO:0007585 |text = respiratory gaseous exchange}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0050828 |text = regulation of liquid surface tension}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6439
| Hs_Ensembl = ENSG00000168878
| Hs_RefseqProtein = NP_000533
| Hs_RefseqmRNA = NM_000542
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 85737954
| Hs_GenLoc_end = 85748823
| Hs_Uniprot = P07988
| Mm_EntrezGene = 20388
| Mm_Ensembl = ENSMUSG00000056370
| Mm_RefseqmRNA = XM_974249
| Mm_RefseqProtein = XP_979343
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 72234134
| Mm_GenLoc_end = 72242441
| Mm_Uniprot = Q2M2M2
}}
}}
'''Surfactant, pulmonary-associated protein B''', also known as '''SFTPB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SFTPB surfactant, pulmonary-associated protein B| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6439| 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=Pérez-Gil J |title=Lipid-protein interactions of hydrophobic proteins SP-B and SP-C in lung surfactant assembly and dynamics. |journal=Pediatric pathology & molecular medicine |volume=20 |issue= 6 |pages= 445-69 |year= 2002 |pmid= 11699574 |doi= }}
*{{cite journal | author=Johansson J, Curstedt T, Robertson B |title=Artificial surfactants based on analogues of SP-B and SP-C. |journal=Pediatric pathology & molecular medicine |volume=20 |issue= 6 |pages= 501-18 |year= 2002 |pmid= 11699576 |doi= }}
*{{cite journal | author=Nogee LM |title=Alterations in SP-B and SP-C expression in neonatal lung disease. |journal=Annu. Rev. Physiol. |volume=66 |issue= |pages= 601-23 |year= 2004 |pmid= 14977415 |doi= 10.1146/annurev.physiol.66.032102.134711 }}
*{{cite journal | author=Moore KJ, D'Amore-Bruno MA, Korfhagen TR, ''et al.'' |title=Chromosomal localization of three pulmonary surfactant protein genes in the mouse. |journal=Genomics |volume=12 |issue= 2 |pages= 388-93 |year= 1992 |pmid= 1346779 |doi= }}
*{{cite journal | author=Voorhout WF, Veenendaal T, Haagsman HP, ''et al.'' |title=Intracellular processing of pulmonary surfactant protein B in an endosomal/lysosomal compartment. |journal=Am. J. Physiol. |volume=263 |issue= 4 Pt 1 |pages= L479-86 |year= 1992 |pmid= 1415726 |doi= }}
*{{cite journal | author=Johansson J, Jörnvall H, Curstedt T |title=Human surfactant polypeptide SP-B. Disulfide bridges, C-terminal end, and peptide analysis of the airway form. |journal=FEBS Lett. |volume=301 |issue= 2 |pages= 165-7 |year= 1992 |pmid= 1568474 |doi= }}
*{{cite journal | author=Yu SH, Possmayer F |title=Effect of pulmonary surfactant protein B (SP-B) and calcium on phospholipid adsorption and squeeze-out of phosphatidylglycerol from binary phospholipid monolayers containing dipalmitoylphosphatidylcholine. |journal=Biochim. Biophys. Acta |volume=1126 |issue= 1 |pages= 26-34 |year= 1992 |pmid= 1606172 |doi= }}
*{{cite journal | author=Weaver TE, Whitsett JA |title=Processing of hydrophobic pulmonary surfactant protein B in rat type II cells. |journal=Am. J. Physiol. |volume=257 |issue= 2 Pt 1 |pages= L100-8 |year= 1989 |pmid= 2475034 |doi= }}
*{{cite journal | author=Pilot-Matias TJ, Kister SE, Fox JL, ''et al.'' |title=Structure and organization of the gene encoding human pulmonary surfactant proteolipid SP-B. |journal=DNA |volume=8 |issue= 2 |pages= 75-86 |year= 1989 |pmid= 2924687 |doi= }}
*{{cite journal | author=Glasser SW, Korfhagen TR, Weaver T, ''et al.'' |title=cDNA and deduced amino acid sequence of human pulmonary surfactant-associated proteolipid SPL(Phe). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 12 |pages= 4007-11 |year= 1987 |pmid= 3035561 |doi= }}
*{{cite journal | author=Revak SD, Merritt TA, Degryse E, ''et al.'' |title=Use of human surfactant low molecular weight apoproteins in the reconstitution of surfactant biologic activity. |journal=J. Clin. Invest. |volume=81 |issue= 3 |pages= 826-33 |year= 1988 |pmid= 3343343 |doi= }}
*{{cite journal | author=Jacobs KA, Phelps DS, Steinbrink R, ''et al.'' |title=Isolation of a cDNA clone encoding a high molecular weight precursor to a 6-kDa pulmonary surfactant-associated protein. |journal=J. Biol. Chem. |volume=262 |issue= 20 |pages= 9808-11 |year= 1987 |pmid= 3597440 |doi= }}
*{{cite journal | author=Vamvakopoulos NC, Modi WS, Floros J |title=Mapping the human pulmonary surfactant-associated protein B gene (SFTP3) to chromosome 2p12-->p11.2. |journal=Cytogenet. Cell Genet. |volume=68 |issue= 1-2 |pages= 8-10 |year= 1994 |pmid= 7956367 |doi= }}
*{{cite journal | author=Nogee LM, Garnier G, Dietz HC, ''et al.'' |title=A mutation in the surfactant protein B gene responsible for fatal neonatal respiratory disease in multiple kindreds. |journal=J. Clin. Invest. |volume=93 |issue= 4 |pages= 1860-3 |year= 1994 |pmid= 8163685 |doi= }}
*{{cite journal | author=Stuhrmann M, Bohnhorst B, Peters U, ''et al.'' |title=Prenatal diagnosis of congenital alveolar proteinosis (surfactant protein B deficiency). |journal=Prenat. Diagn. |volume=18 |issue= 9 |pages= 953-5 |year= 1999 |pmid= 9793979 |doi= }}
*{{cite journal | author=Wallot M, Wagenvoort C, deMello D, ''et al.'' |title=Congenital alveolar proteinosis caused by a novel mutation of the surfactant protein B gene and misalignment of lung vessels in consanguineous kindred infants. |journal=Eur. J. Pediatr. |volume=158 |issue= 6 |pages= 513-8 |year= 1999 |pmid= 10378403 |doi= }}
*{{cite journal | author=Tredano M, van Elburg RM, Kaspers AG, ''et al.'' |title=Compound SFTPB 1549C-->GAA (121ins2) and 457delC heterozygosity in severe congenital lung disease and surfactant protein B (SP-B) deficiency. |journal=Hum. Mutat. |volume=14 |issue= 6 |pages= 502-9 |year= 2000 |pmid= 10571948 |doi= 10.1002/(SICI)1098-1004(199912)14:6<502::AID-HUMU9>3.0.CO;2-C }}
*{{cite journal | author=Korimilli A, Gonzales LW, Guttentag SH |title=Intracellular localization of processing events in human surfactant protein B biosynthesis. |journal=J. Biol. Chem. |volume=275 |issue= 12 |pages= 8672-9 |year= 2000 |pmid= 10722708 |doi= }}
*{{cite journal | author=Gordon LM, Lee KY, Lipp MM, ''et al.'' |title=Conformational mapping of the N-terminal segment of surfactant protein B in lipid using 13C-enhanced Fourier transform infrared spectroscopy. |journal=J. Pept. Res. |volume=55 |issue= 4 |pages= 330-47 |year= 2000 |pmid= 10798379 |doi= }}
*{{cite journal | author=Lin Z, Pearson C, Chinchilli V, ''et al.'' |title=Polymorphisms of human SP-A, SP-B, and SP-D genes: association of SP-B Thr131Ile with ARDS. |journal=Clin. Genet. |volume=58 |issue= 3 |pages= 181-91 |year= 2001 |pmid= 11076040 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SHBG... {November 16, 2007 11:16:53 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:17:21 AM 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 = PBB_Protein_SHBG_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1d2s.
| PDB = {{PDB2|1d2s}}, {{PDB2|1f5f}}, {{PDB2|1kdk}}, {{PDB2|1kdm}}, {{PDB2|1lhn}}, {{PDB2|1lho}}, {{PDB2|1lhu}}, {{PDB2|1lhv}}, {{PDB2|1lhw}}
| Name = Sex hormone-binding globulin
| HGNCid = 10839
| Symbol = SHBG
| AltSymbols =; ABP; MGC126834; MGC138391
| OMIM = 182205
| ECnumber =
| Homologene = 813
| MGIid = 98295
| GeneAtlas_image1 = PBB_GE_SHBG_215689_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005497 |text = androgen binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0009914 |text = hormone transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6462
| Hs_Ensembl = ENSG00000129214
| Hs_RefseqProtein = NP_001031
| Hs_RefseqmRNA = NM_001040
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 7472099
| Hs_GenLoc_end = 7477426
| Hs_Uniprot = P04278
| Mm_EntrezGene = 20415
| Mm_Ensembl = ENSMUSG00000005202
| Mm_RefseqmRNA = XM_001006589
| Mm_RefseqProtein = XP_001006589
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 69431028
| Mm_GenLoc_end = 69434100
| Mm_Uniprot = Q5F214
}}
}}
'''Sex hormone-binding globulin''', also known as '''SHBG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SHBG sex hormone-binding globulin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6462| 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=Hammond GL, Bocchinfuso WP |title=Sex hormone-binding globulin: gene organization and structure/function analyses. |journal=Horm. Res. |volume=45 |issue= 3-5 |pages= 197-201 |year= 1996 |pmid= 8964583 |doi= }}
*{{cite journal | author=Rosner W, Hryb DJ, Khan MS, ''et al.'' |title=Sex hormone-binding globulin mediates steroid hormone signal transduction at the plasma membrane. |journal=J. Steroid Biochem. Mol. Biol. |volume=69 |issue= 1-6 |pages= 481-5 |year= 1999 |pmid= 10419028 |doi= }}
*{{cite journal | author=Power SG, Bocchinfuso WP, Pallesen M, ''et al.'' |title=Molecular analyses of a human sex hormone-binding globulin variant: evidence for an additional carbohydrate chain. |journal=J. Clin. Endocrinol. Metab. |volume=75 |issue= 4 |pages= 1066-70 |year= 1992 |pmid= 1400872 |doi= }}
*{{cite journal | author=Bérubé D, Séralini GE, Gagné R, Hammond GL |title=Localization of the human sex hormone-binding globulin gene (SHBG) to the short arm of chromosome 17 (17p12----p13). |journal=Cytogenet. Cell Genet. |volume=54 |issue= 1-2 |pages= 65-7 |year= 1991 |pmid= 2249477 |doi= }}
*{{cite journal | author=Gershagen S, Lundwall A, Fernlund P |title=Characterization of the human sex hormone binding globulin (SHBG) gene and demonstration of two transcripts in both liver and testis. |journal=Nucleic Acids Res. |volume=17 |issue= 22 |pages= 9245-58 |year= 1990 |pmid= 2587256 |doi= }}
*{{cite journal | author=Hammond GL, Underhill DA, Rykse HM, Smith CL |title=The human sex hormone-binding globulin gene contains exons for androgen-binding protein and two other testicular messenger RNAs. |journal=Mol. Endocrinol. |volume=3 |issue= 11 |pages= 1869-76 |year= 1990 |pmid= 2608061 |doi= }}
*{{cite journal | author=Que BG, Petra PH |title=Characterization of a cDNA coding for sex steroid-binding protein of human plasma. |journal=FEBS Lett. |volume=219 |issue= 2 |pages= 405-9 |year= 1987 |pmid= 2956125 |doi= }}
*{{cite journal | author=Gershagen S, Fernlund P, Lundwall A |title=A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S. |journal=FEBS Lett. |volume=220 |issue= 1 |pages= 129-35 |year= 1987 |pmid= 2956126 |doi= }}
*{{cite journal | author=Walsh KA, Titani K, Takio K, ''et al.'' |title=Amino acid sequence of the sex steroid binding protein of human blood plasma. |journal=Biochemistry |volume=25 |issue= 23 |pages= 7584-90 |year= 1987 |pmid= 3542030 |doi= }}
*{{cite journal | author=Hammond GL, Underhill DA, Smith CL, ''et al.'' |title=The cDNA-deduced primary structure of human sex hormone-binding globulin and location of its steroid-binding domain. |journal=FEBS Lett. |volume=215 |issue= 1 |pages= 100-4 |year= 1987 |pmid= 3569533 |doi= }}
*{{cite journal | author=Hammond GL, Robinson PA, Sugino H, ''et al.'' |title=Physicochemical characteristics of human sex hormone binding globulin: evidence for two identical subunits. |journal=J. Steroid Biochem. |volume=24 |issue= 4 |pages= 815-24 |year= 1986 |pmid= 3702459 |doi= }}
*{{cite journal | author=Hardy DO, Cariño C, Catterall JF, Larrea F |title=Molecular characterization of a genetic variant of the steroid hormone-binding globulin gene in heterozygous subjects. |journal=J. Clin. Endocrinol. Metab. |volume=80 |issue= 4 |pages= 1253-6 |year= 1995 |pmid= 7714097 |doi= }}
*{{cite journal | author=Cargill M, Altshuler D, Ireland J, ''et al.'' |title=Characterization of single-nucleotide polymorphisms in coding regions of human genes. |journal=Nat. Genet. |volume=22 |issue= 3 |pages= 231-8 |year= 1999 |pmid= 10391209 |doi= 10.1038/10290 }}
*{{cite journal | author=Grishkovskaya I, Avvakumov GV, Sklenar G, ''et al.'' |title=Crystal structure of human sex hormone-binding globulin: steroid transport by a laminin G-like domain. |journal=EMBO J. |volume=19 |issue= 4 |pages= 504-12 |year= 2000 |pmid= 10675319 |doi= 10.1093/emboj/19.4.504 }}
*{{cite journal | author=Hogeveen KN, Talikka M, Hammond GL |title=Human sex hormone-binding globulin promoter activity is influenced by a (TAAAA)n repeat element within an Alu sequence. |journal=J. Biol. Chem. |volume=276 |issue= 39 |pages= 36383-90 |year= 2001 |pmid= 11473114 |doi= 10.1074/jbc.M104681200 }}
*{{cite journal | author=Hryb DJ, Nakhla AM, Kahn SM, ''et al.'' |title=Sex hormone-binding globulin in the human prostate is locally synthesized and may act as an autocrine/paracrine effector. |journal=J. Biol. Chem. |volume=277 |issue= 29 |pages= 26618-22 |year= 2002 |pmid= 12015315 |doi= 10.1074/jbc.M202495200 }}
*{{cite journal | author=Raineri M, Catalano MG, Hammond GL, ''et al.'' |title=O-Glycosylation of human sex hormone-binding globulin is essential for inhibition of estradiol-induced MCF-7 breast cancer cell proliferation. |journal=Mol. Cell. Endocrinol. |volume=189 |issue= 1-2 |pages= 135-43 |year= 2002 |pmid= 12039072 |doi= }}
*{{cite journal | author=Grishkovskaya I, Avvakumov GV, Hammond GL, Muller YA |title=Resolution of a disordered region at the entrance of the human sex hormone-binding globulin steroid-binding site. |journal=J. Mol. Biol. |volume=318 |issue= 3 |pages= 621-6 |year= 2002 |pmid= 12054810 |doi= 10.1016/S0022-2836(02)00169-9 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TERF1... {November 16, 2007 11:17:21 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:17:54 AM 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_TERF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ba5.
| PDB = {{PDB2|1ba5}}, {{PDB2|1h6o}}, {{PDB2|1ity}}, {{PDB2|1iv6}}, {{PDB2|1w0t}}
| Name = Telomeric repeat binding factor (NIMA-interacting) 1
| HGNCid = 11728
| Symbol = TERF1
| AltSymbols =; TRF; FLJ41416; PIN2; TRBF1; TRF1; hTRF1-AS; t-TRF1
| OMIM = 600951
| ECnumber =
| Homologene = 7570
| MGIid = 109634
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003691 |text = double-stranded telomeric DNA binding}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0000781 |text = chromosome, telomeric region}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}}
| Process = {{GNF_GO|id=GO:0007004 |text = telomere maintenance via telomerase}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007067 |text = mitosis}} {{GNF_GO|id=GO:0045449 |text = regulation of transcription}} {{GNF_GO|id=GO:0051301 |text = cell division}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7013
| Hs_Ensembl =
| Hs_RefseqProtein = NP_003209
| Hs_RefseqmRNA = NM_003218
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 21749
| Mm_Ensembl = ENSMUSG00000025925
| Mm_RefseqmRNA = NM_009352
| Mm_RefseqProtein = NP_033378
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 15790872
| Mm_GenLoc_end = 15828645
| Mm_Uniprot = Q7TSK8
}}
}}
'''Telomeric repeat binding factor (NIMA-interacting) 1''', also known as '''TERF1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TERF1 telomeric repeat binding factor (NIMA-interacting) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7013| 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 telomere specific protein which is a component of the telomere nucleoprotein complex. This protein is present at telomeres throughout the cell cycle and functions as an inhibitor of telomerase, acting in cis to limit the elongation of individual chromosome ends. The protein structure contains a C-terminal Myb motif, a dimerization domain near its N-terminus and an acidic N-terminus. Two transcripts of this gene are alternatively spliced products.<ref name="entrez">{{cite web | title = Entrez Gene: TERF1 telomeric repeat binding factor (NIMA-interacting) 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7013| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Zhong Z, Shiue L, Kaplan S, de Lange T |title=A mammalian factor that binds telomeric TTAGGG repeats in vitro. |journal=Mol. Cell. Biol. |volume=12 |issue= 11 |pages= 4834-43 |year= 1992 |pmid= 1406665 |doi= }}
*{{cite journal | author=Chong L, van Steensel B, Broccoli D, ''et al.'' |title=A human telomeric protein. |journal=Science |volume=270 |issue= 5242 |pages= 1663-7 |year= 1996 |pmid= 7502076 |doi= }}
*{{cite journal | author=Lu KP, Hanes SD, Hunter T |title=A human peptidyl-prolyl isomerase essential for regulation of mitosis. |journal=Nature |volume=380 |issue= 6574 |pages= 544-7 |year= 1996 |pmid= 8606777 |doi= 10.1038/380544a0 }}
*{{cite journal | author=Bilaud T, Koering CE, Binet-Brasselet E, ''et al.'' |title=The telobox, a Myb-related telomeric DNA binding motif found in proteins from yeast, plants and human. |journal=Nucleic Acids Res. |volume=24 |issue= 7 |pages= 1294-303 |year= 1996 |pmid= 8614633 |doi= }}
*{{cite journal | author=Broccoli D, Chong L, Oelmann S, ''et al.'' |title=Comparison of the human and mouse genes encoding the telomeric protein, TRF1: chromosomal localization, expression and conserved protein domains. |journal=Hum. Mol. Genet. |volume=6 |issue= 1 |pages= 69-76 |year= 1997 |pmid= 9002672 |doi= }}
*{{cite journal | author=Bianchi A, Smith S, Chong L, ''et al.'' |title=TRF1 is a dimer and bends telomeric DNA. |journal=EMBO J. |volume=16 |issue= 7 |pages= 1785-94 |year= 1997 |pmid= 9130722 |doi= 10.1093/emboj/16.7.1785 }}
*{{cite journal | author=Broccoli D, Smogorzewska A, Chong L, de Lange T |title=Human telomeres contain two distinct Myb-related proteins, TRF1 and TRF2. |journal=Nat. Genet. |volume=17 |issue= 2 |pages= 231-5 |year= 1997 |pmid= 9326950 |doi= 10.1038/ng1097-231 }}
*{{cite journal | author=Shen M, Haggblom C, Vogt M, ''et al.'' |title=Characterization and cell cycle regulation of the related human telomeric proteins Pin2 and TRF1 suggest a role in mitosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 25 |pages= 13618-23 |year= 1998 |pmid= 9391075 |doi= }}
*{{cite journal | author=Nosaka K, Kawahara M, Masuda M, ''et al.'' |title=Association of nucleoside diphosphate kinase nm23-H2 with human telomeres. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 2 |pages= 342-8 |year= 1998 |pmid= 9480811 |doi= 10.1006/bbrc.1997.8097 }}
*{{cite journal | author=Nishikawa T, Nagadoi A, Yoshimura S, ''et al.'' |title=Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. |journal=Structure |volume=6 |issue= 8 |pages= 1057-65 |year= 1998 |pmid= 9739097 |doi= }}
*{{cite journal | author=Smith S, Giriat I, Schmitt A, de Lange T |title=Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. |journal=Science |volume=282 |issue= 5393 |pages= 1484-7 |year= 1998 |pmid= 9822378 |doi= }}
*{{cite journal | author=Kim SH, Kaminker P, Campisi J |title=TIN2, a new regulator of telomere length in human cells. |journal=Nat. Genet. |volume=23 |issue= 4 |pages= 405-12 |year= 1999 |pmid= 10581025 |doi= 10.1038/70508 }}
*{{cite journal | author=Smogorzewska A, van Steensel B, Bianchi A, ''et al.'' |title=Control of human telomere length by TRF1 and TRF2. |journal=Mol. Cell. Biol. |volume=20 |issue= 5 |pages= 1659-68 |year= 2000 |pmid= 10669743 |doi= }}
*{{cite journal | author=Wu G, Lee WH, Chen PL |title=NBS1 and TRF1 colocalize at promyelocytic leukemia bodies during late S/G2 phases in immortalized telomerase-negative cells. Implication of NBS1 in alternative lengthening of telomeres. |journal=J. Biol. Chem. |volume=275 |issue= 39 |pages= 30618-22 |year= 2000 |pmid= 10913111 |doi= 10.1074/jbc.C000390200 }}
*{{cite journal | author=Chi NW, Lodish HF |title=Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles. |journal=J. Biol. Chem. |volume=275 |issue= 49 |pages= 38437-44 |year= 2001 |pmid= 10988299 |doi= 10.1074/jbc.M007635200 }}
*{{cite journal | author=Kishi S, Wulf G, Nakamura M, Lu KP |title=Telomeric protein Pin2/TRF1 induces mitotic entry and apoptosis in cells with short telomeres and is down-regulated in human breast tumors. |journal=Oncogene |volume=20 |issue= 12 |pages= 1497-508 |year= 2001 |pmid= 11313893 |doi= 10.1038/sj.onc.1204229 }}
*{{cite journal | author=Kishi S, Zhou XZ, Ziv Y, ''et al.'' |title=Telomeric protein Pin2/TRF1 as an important ATM target in response to double strand DNA breaks. |journal=J. Biol. Chem. |volume=276 |issue= 31 |pages= 29282-91 |year= 2001 |pmid= 11375976 |doi= 10.1074/jbc.M011534200 }}
*{{cite journal | author=Fairall L, Chapman L, Moss H, ''et al.'' |title=Structure of the TRFH dimerization domain of the human telomeric proteins TRF1 and TRF2. |journal=Mol. Cell |volume=8 |issue= 2 |pages= 351-61 |year= 2001 |pmid= 11545737 |doi= }}
*{{cite journal | author=Zhou XZ, Lu KP |title=The Pin2/TRF1-interacting protein PinX1 is a potent telomerase inhibitor. |journal=Cell |volume=107 |issue= 3 |pages= 347-59 |year= 2001 |pmid= 11701125 |doi= }}
*{{cite journal | author=Nishikawa T, Okamura H, Nagadoi A, ''et al.'' |title=Solution structure of a telomeric DNA complex of human TRF1. |journal=Structure |volume=9 |issue= 12 |pages= 1237-51 |year= 2002 |pmid= 11738049 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TFF1... {November 16, 2007 11:17:54 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:18:35 AM 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_TFF1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hi7.
| PDB = {{PDB2|1hi7}}, {{PDB2|1ps2}}
| Name = Trefoil factor 1
| HGNCid = 11755
| Symbol = TFF1
| AltSymbols =; BCEI; D21S21; HP1.A; HPS2; pNR-2; pS2
| OMIM = 113710
| ECnumber =
| Homologene = 2426
| MGIid = 88135
| GeneAtlas_image1 = PBB_GE_TFF1_205009_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component =
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006952 |text = defense response}} {{GNF_GO|id=GO:0007586 |text = digestion}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7031
| Hs_Ensembl = ENSG00000160182
| Hs_RefseqProtein = NP_003216
| Hs_RefseqmRNA = NM_003225
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 42655462
| Hs_GenLoc_end = 42659713
| Hs_Uniprot = P04155
| Mm_EntrezGene = 21784
| Mm_Ensembl = ENSMUSG00000024032
| Mm_RefseqmRNA = NM_009362
| Mm_RefseqProtein = NP_033388
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 30872609
| Mm_GenLoc_end = 30892065
| Mm_Uniprot = Q149Y8
}}
}}
'''Trefoil factor 1''', also known as '''TFF1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TFF1 trefoil factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7031| 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 = Members of the trefoil family are characterized by having at least one copy of the trefoil motif, a 40-amino acid domain that contains three conserved disulfides. They are stable secretory proteins expressed in gastrointestinal mucosa. Their functions are not defined, but they may protect the mucosa from insults, stabilize the mucus layer, and affect healing of the epithelium. This gene, which is expressed in the gastric mucosa, has also been studied because of its expression in human tumors. This gene and two other related trefoil family member genes are found in a cluster on chromosome 21.<ref name="entrez">{{cite web | title = Entrez Gene: TFF1 trefoil factor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7031| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Langer G, Jagla W, Behrens-Baumann W, ''et al.'' |title=Ocular TFF-peptides: new mucus-associated secretory products of conjunctival goblet cells. |journal=Adv. Exp. Med. Biol. |volume=506 |issue= Pt A |pages= 313-6 |year= 2003 |pmid= 12613926 |doi= }}
*{{cite journal | author=Piggott NH, Henry JA, May FE, Westley BR |title=Antipeptide antibodies against the pNR-2 oestrogen-regulated protein of human breast cancer cells and detection of pNR-2 expression in normal tissues by immunohistochemistry. |journal=J. Pathol. |volume=163 |issue= 2 |pages= 95-104 |year= 1991 |pmid= 1707960 |doi= 10.1002/path.1711630204 }}
*{{cite journal | author=Mori K, Fujii R, Kida N, ''et al.'' |title=Complete primary structure of the human estrogen-responsive gene (pS2) product. |journal=J. Biochem. |volume=107 |issue= 1 |pages= 73-6 |year= 1990 |pmid= 2185238 |doi= }}
*{{cite journal | author=Tomasetto C, Rio MC, Gautier C, ''et al.'' |title=hSP, the domain-duplicated homolog of pS2 protein, is co-expressed with pS2 in stomach but not in breast carcinoma. |journal=EMBO J. |volume=9 |issue= 2 |pages= 407-14 |year= 1990 |pmid= 2303034 |doi= }}
*{{cite journal | author=Takahashi H, Kida N, Fujii R, ''et al.'' |title=Expression of the pS2 gene in human gastric cancer cells derived from poorly differentiated adenocarcinoma. |journal=FEBS Lett. |volume=261 |issue= 2 |pages= 283-6 |year= 1990 |pmid= 2311759 |doi= }}
*{{cite journal | author=Rio MC, Bellocq JP, Daniel JY, ''et al.'' |title=Breast cancer-associated pS2 protein: synthesis and secretion by normal stomach mucosa. |journal=Science |volume=241 |issue= 4866 |pages= 705-8 |year= 1988 |pmid= 3041593 |doi= }}
*{{cite journal | author=Rio MC, Lepage P, Diemunsch P, ''et al.'' |title=[Primary structure of human protein pS2] |journal=C. R. Acad. Sci. III, Sci. Vie |volume=307 |issue= 19 |pages= 825-31 |year= 1989 |pmid= 3146413 |doi= }}
*{{cite journal | author=Mori K, Fujii R, Kida N, ''et al.'' |title=Identification of a polypeptide secreted by human breast cancer cells (MCF-7) as the human estrogen-responsive gene (pS2) product. |journal=Biochem. Biophys. Res. Commun. |volume=155 |issue= 1 |pages= 366-72 |year= 1988 |pmid= 3261981 |doi= }}
*{{cite journal | author=Jeltsch JM, Roberts M, Schatz C, ''et al.'' |title=Structure of the human oestrogen-responsive gene pS2. |journal=Nucleic Acids Res. |volume=15 |issue= 4 |pages= 1401-14 |year= 1987 |pmid= 3822834 |doi= }}
*{{cite journal | author=Prud'homme JF, Fridlansky F, Le Cunff M, ''et al.'' |title=Cloning of a gene expressed in human breast cancer and regulated by estrogen in MCF-7 cells. |journal=DNA |volume=4 |issue= 1 |pages= 11-21 |year= 1985 |pmid= 3838275 |doi= }}
*{{cite journal | author=Jakowlew SB, Breathnach R, Jeltsch JM, ''et al.'' |title=Sequence of the pS2 mRNA induced by estrogen in the human breast cancer cell line MCF-7. |journal=Nucleic Acids Res. |volume=12 |issue= 6 |pages= 2861-78 |year= 1984 |pmid= 6324130 |doi= }}
*{{cite journal | author=Hanby AM, Poulsom R, Singh S, ''et al.'' |title=Spasmolytic polypeptide is a major antral peptide: distribution of the trefoil peptides human spasmolytic polypeptide and pS2 in the stomach. |journal=Gastroenterology |volume=105 |issue= 4 |pages= 1110-6 |year= 1993 |pmid= 8405856 |doi= }}
*{{cite journal | author=Polshakov VI, Frenkiel TA, Westley B, ''et al.'' |title=NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure. |journal=Eur. J. Biochem. |volume=233 |issue= 3 |pages= 847-55 |year= 1996 |pmid= 8521850 |doi= }}
*{{cite journal | author=Gött P, Beck S, Machado JC, ''et al.'' |title=Human trefoil peptides: genomic structure in 21q22.3 and coordinated expression. |journal=Eur. J. Hum. Genet. |volume=4 |issue= 6 |pages= 308-15 |year= 1997 |pmid= 9043862 |doi= }}
*{{cite journal | author=Seib T, Blin N, Hilgert K, ''et al.'' |title=The three human trefoil genes TFF1, TFF2, and TFF3 are located within a region of 55 kb on chromosome 21q22.3. |journal=Genomics |volume=40 |issue= 1 |pages= 200-2 |year= 1997 |pmid= 9070946 |doi= 10.1006/geno.1996.4511 }}
*{{cite journal | author=Polshakov VI, Williams MA, Gargaro AR, ''et al.'' |title=High-resolution solution structure of human pNR-2/pS2: a single trefoil motif protein. |journal=J. Mol. Biol. |volume=267 |issue= 2 |pages= 418-32 |year= 1997 |pmid= 9096235 |doi= 10.1006/jmbi.1997.0896 }}
*{{cite journal | author=Chadwick MP, Westley BR, May FE |title=Homodimerization and hetero-oligomerization of the single-domain trefoil protein pNR-2/pS2 through cysteine 58. |journal=Biochem. J. |volume=327 ( Pt 1) |issue= |pages= 117-23 |year= 1997 |pmid= 9355742 |doi= }}
*{{cite journal | author=Chen H, Lin RJ, Xie W, ''et al.'' |title=Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase. |journal=Cell |volume=98 |issue= 5 |pages= 675-86 |year= 1999 |pmid= 10490106 |doi= }}
*{{cite journal | author=Newton JL, Allen A, Westley BR, May FE |title=The human trefoil peptide, TFF1, is present in different molecular forms that are intimately associated with mucus in normal stomach. |journal=Gut |volume=46 |issue= 3 |pages= 312-20 |year= 2000 |pmid= 10673290 |doi= }}
*{{cite journal | author=Hattori M, Fujiyama A, Taylor TD, ''et al.'' |title=The DNA sequence of human chromosome 21. |journal=Nature |volume=405 |issue= 6784 |pages= 311-9 |year= 2000 |pmid= 10830953 |doi= 10.1038/35012518 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TGFB3... {November 16, 2007 11:18:35 AM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 16, 2007 11:19:00 AM 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_TGFB3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ktz.
| PDB = {{PDB2|1ktz}}, {{PDB2|1tgj}}, {{PDB2|1tgk}}
| Name = Transforming growth factor, beta 3
| HGNCid = 11769
| Symbol = TGFB3
| AltSymbols =; ARVD; FLJ16571; TGF-beta3
| OMIM = 190230
| ECnumber =
| Homologene = 2433
| MGIid = 98727
| GeneAtlas_image1 = PBB_GE_TGFB3_209747_at_tn.png
| Function = {{GNF_GO|id=GO:0005160 |text = transforming growth factor beta receptor binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component =
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0001701 |text = in utero embryonic development}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0009790 |text = embryonic development}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0016049 |text = cell growth}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7043
| Hs_Ensembl = ENSG00000119699
| Hs_RefseqProtein = NP_003230
| Hs_RefseqmRNA = NM_003239
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 75494195
| Hs_GenLoc_end = 75517242
| Hs_Uniprot = P10600
| Mm_EntrezGene = 21809
| Mm_Ensembl = ENSMUSG00000021253
| Mm_RefseqmRNA = XM_994378
| Mm_RefseqProtein = XP_999472
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 86945904
| Mm_GenLoc_end = 86968101
| Mm_Uniprot = Q3TRQ9
}}
}}
'''Transforming growth factor, beta 3''', also known as '''TGFB3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TGFB3 transforming growth factor, beta 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7043| 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=Kalluri R, Neilson EG |title=Epithelial-mesenchymal transition and its implications for fibrosis. |journal=J. Clin. Invest. |volume=112 |issue= 12 |pages= 1776-84 |year= 2004 |pmid= 14679171 |doi= 10.1172/JCI200320530 }}
*{{cite journal | author=Arrick BA, Lee AL, Grendell RL, Derynck R |title=Inhibition of translation of transforming growth factor-beta 3 mRNA by its 5' untranslated region. |journal=Mol. Cell. Biol. |volume=11 |issue= 9 |pages= 4306-13 |year= 1991 |pmid= 1875922 |doi= }}
*{{cite journal | author=ten Dijke P, Hansen P, Iwata KK, ''et al.'' |title=Identification of another member of the transforming growth factor type beta gene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 13 |pages= 4715-9 |year= 1988 |pmid= 3164476 |doi= }}
*{{cite journal | author=Derynck R, Lindquist PB, Lee A, ''et al.'' |title=A new type of transforming growth factor-beta, TGF-beta 3. |journal=EMBO J. |volume=7 |issue= 12 |pages= 3737-43 |year= 1989 |pmid= 3208746 |doi= }}
*{{cite journal | author=Barton DE, Foellmer BE, Du J, ''et al.'' |title=Chromosomal mapping of genes for transforming growth factors beta 2 and beta 3 in man and mouse: dispersion of TGF-beta gene family. |journal=Oncogene Res. |volume=3 |issue= 4 |pages= 323-31 |year= 1989 |pmid= 3226728 |doi= }}
*{{cite journal | author=Kaartinen V, Voncken JW, Shuler C, ''et al.'' |title=Abnormal lung development and cleft palate in mice lacking TGF-beta 3 indicates defects of epithelial-mesenchymal interaction. |journal=Nat. Genet. |volume=11 |issue= 4 |pages= 415-21 |year= 1996 |pmid= 7493022 |doi= 10.1038/ng1295-415 }}
*{{cite journal | author=Nishida K, Sotozono C, Adachi W, ''et al.'' |title=Transforming growth factor-beta 1, -beta 2 and -beta 3 mRNA expression in human cornea. |journal=Curr. Eye Res. |volume=14 |issue= 3 |pages= 235-41 |year= 1995 |pmid= 7796607 |doi= }}
*{{cite journal | author=Lin HY, Moustakas A, Knaus P, ''et al.'' |title=The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands. |journal=J. Biol. Chem. |volume=270 |issue= 6 |pages= 2747-54 |year= 1995 |pmid= 7852346 |doi= }}
*{{cite journal | author=Rampazzo A, Nava A, Danieli GA, ''et al.'' |title=The gene for arrhythmogenic right ventricular cardiomyopathy maps to chromosome 14q23-q24. |journal=Hum. Mol. Genet. |volume=3 |issue= 6 |pages= 959-62 |year= 1994 |pmid= 7951245 |doi= }}
*{{cite journal | author=Zhao Y, Chegini N, Flanders KC |title=Human fallopian tube expresses transforming growth factor (TGF beta) isoforms, TGF beta type I-III receptor messenger ribonucleic acid and protein, and contains [125I]TGF beta-binding sites. |journal=J. Clin. Endocrinol. Metab. |volume=79 |issue= 4 |pages= 1177-84 |year= 1994 |pmid= 7962292 |doi= }}
*{{cite journal | author=Hildebrand A, Romarís M, Rasmussen LM, ''et al.'' |title=Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta. |journal=Biochem. J. |volume=302 ( Pt 2) |issue= |pages= 527-34 |year= 1994 |pmid= 8093006 |doi= }}
*{{cite journal | author=López-Casillas F, Payne HM, Andres JL, Massagué J |title=Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites. |journal=J. Cell Biol. |volume=124 |issue= 4 |pages= 557-68 |year= 1994 |pmid= 8106553 |doi= }}
*{{cite journal | author=Mittl PR, Priestle JP, Cox DA, ''et al.'' |title=The crystal structure of TGF-beta 3 and comparison to TGF-beta 2: implications for receptor binding. |journal=Protein Sci. |volume=5 |issue= 7 |pages= 1261-71 |year= 1997 |pmid= 8819159 |doi= }}
*{{cite journal | author=Ambros RA, Kallakury BV, Malfetano JH, Mihm MC |title=Cytokine, cell adhesion receptor, and tumor suppressor gene expression in vulvar squamous carcinoma: correlation with prominent fibromyxoid stromal response. |journal=Int. J. Gynecol. Pathol. |volume=15 |issue= 4 |pages= 320-5 |year= 1997 |pmid= 8886879 |doi= }}
*{{cite journal | author=Djonov V, Ball RK, Graf S, ''et al.'' |title=Transforming growth factor-beta 3 is expressed in nondividing basal epithelial cells in normal human prostate and benign prostatic hyperplasia, and is no longer detectable in prostate carcinoma. |journal=Prostate |volume=31 |issue= 2 |pages= 103-9 |year= 1997 |pmid= 9140123 |doi= }}
*{{cite journal | author=Jin L, Qian X, Kulig E, ''et al.'' |title=Transforming growth factor-beta, transforming growth factor-beta receptor II, and p27Kip1 expression in nontumorous and neoplastic human pituitaries. |journal=Am. J. Pathol. |volume=151 |issue= 2 |pages= 509-19 |year= 1997 |pmid= 9250163 |doi= }}
*{{cite journal | author=Lidral AC, Romitti PA, Basart AM, ''et al.'' |title=Association of MSX1 and TGFB3 with nonsyndromic clefting in humans. |journal=Am. J. Hum. Genet. |volume=63 |issue= 2 |pages= 557-68 |year= 1998 |pmid= 9683588 |doi= }}
*{{cite journal | author=Barbara NP, Wrana JL, Letarte M |title=Endoglin is an accessory protein that interacts with the signaling receptor complex of multiple members of the transforming growth factor-beta superfamily. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 584-94 |year= 1999 |pmid= 9872992 |doi= }}
*{{cite journal | author=Lux A, Attisano L, Marchuk DA |title=Assignment of transforming growth factor beta1 and beta3 and a third new ligand to the type I receptor ALK-1. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 9984-92 |year= 1999 |pmid= 10187774 |doi= }}
*{{cite journal | author=Mori T, Kawara S, Shinozaki M, ''et al.'' |title=Role and interaction of connective tissue growth factor with transforming growth factor-beta in persistent fibrosis: A mouse fibrosis model. |journal=J. Cell. Physiol. |volume=181 |issue= 1 |pages= 153-9 |year= 1999 |pmid= 10457363 |doi= 10.1002/(SICI)1097-4652(199910)181:1<153::AID-JCP16>3.0.CO;2-K }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TRAF1... {November 16, 2007 11:19:00 AM PST}
- SEARCH REDIRECT: Control Box Found: TRAF1 {November 16, 2007 11:19:36 AM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 16, 2007 11:19:38 AM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 16, 2007 11:19:38 AM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 16, 2007 11:19:38 AM PST}
- UPDATED: Updated protein page: TRAF1 {November 16, 2007 11:19:44 AM PST}
end log.
