Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 07:44, 19 November 2007 (UTC)[edit]
Proteins without matches (11)[edit]
Proteins with a High Potential Match (3)[edit]
Redirected Proteins (11)[edit]
Manual Inspection (Page not found) (14)[edit]
Updated (11)[edit]
Protein Status Grid - Date: 07:44, 19 November 2007 (UTC)[edit]
Vebose Log - Date: 07:44, 19 November 2007 (UTC)[edit]
- INFO: Beginning work on ADAM12... {November 18, 2007 11:31:35 PM PST}
- SEARCH REDIRECT: Control Box Found: ADAM12 {November 18, 2007 11:32:51 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:32:54 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:32:54 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:32:54 PM PST}
- UPDATED: Updated protein page: ADAM12 {November 18, 2007 11:33:01 PM PST}
- INFO: Beginning work on ADAM15... {November 18, 2007 11:34:59 PM PST}
- SEARCH REDIRECT: Control Box Found: ADAM15 {November 18, 2007 11:35:21 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:35:24 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:35:24 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:35:24 PM PST}
- UPDATED: Updated protein page: ADAM15 {November 18, 2007 11:35:29 PM PST}
- INFO: Beginning work on AP1M1... {November 18, 2007 11:35:29 PM PST}
- SEARCH REDIRECT: Control Box Found: AP1M1 {November 18, 2007 11:36:05 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:36:06 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:36:06 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:36:06 PM PST}
- UPDATED: Updated protein page: AP1M1 {November 18, 2007 11:36:12 PM PST}
- INFO: Beginning work on BNIP3... {November 18, 2007 11:21:14 PM PST}
- SEARCH REDIRECT: Control Box Found: BNIP3 {November 18, 2007 11:21:35 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:21:37 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:21:37 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:21:37 PM PST}
- UPDATED: Updated protein page: BNIP3 {November 18, 2007 11:21:43 PM PST}
- INFO: Beginning work on CCL22... {November 18, 2007 11:25:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:25:31 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Chemokine (C-C motif) ligand 22
| HGNCid = 10621
| Symbol = CCL22
| AltSymbols =; MDC; A-152E5.1; ABCD-1; DC/B-CK; MGC34554; SCYA22; STCP-1
| OMIM = 602957
| ECnumber =
| Homologene = 7529
| MGIid = 1306779
| GeneAtlas_image1 = PBB_GE_CCL22_207861_at_tn.png
| Function = {{GNF_GO|id=GO:0008009 |text = chemokine activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0009615 |text = response to virus}} {{GNF_GO|id=GO:0019735 |text = antimicrobial humoral response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6367
| Hs_Ensembl = ENSG00000102962
| Hs_RefseqProtein = NP_002981
| Hs_RefseqmRNA = NM_002990
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 55950219
| Hs_GenLoc_end = 55957600
| Hs_Uniprot = O00626
| Mm_EntrezGene = 20299
| Mm_Ensembl = ENSMUSG00000031779
| Mm_RefseqmRNA = NM_009137
| Mm_RefseqProtein = NP_033163
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 97634719
| Mm_GenLoc_end = 97640698
| Mm_Uniprot = Q546S6
}}
}}
'''Chemokine (C-C motif) ligand 22''', also known as '''CCL22''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CCL22 chemokine (C-C motif) ligand 22| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6367| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The CC cytokines are proteins characterized by two adjacent cysteines. The cytokine encoded by this gene displays chemotactic activity for monocytes, dendritic cells, natural killer cells and for chronically activated T lymphocytes. It also displays a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. The product of this gene binds to chemokine receptor CCR4. This chemokine may play a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology.<ref name="entrez">{{cite web | title = Entrez Gene: CCL22 chemokine (C-C motif) ligand 22| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6367| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Robertson MJ |title=Role of chemokines in the biology of natural killer cells. |journal=J. Leukoc. Biol. |volume=71 |issue= 2 |pages= 173-83 |year= 2002 |pmid= 11818437 |doi= }}
*{{cite journal | author=Gear AR, Camerini D |title=Platelet chemokines and chemokine receptors: linking hemostasis, inflammation, and host defense. |journal=Microcirculation (New York, N.Y. : 1994) |volume=10 |issue= 3-4 |pages= 335-50 |year= 2003 |pmid= 12851650 |doi= 10.1038/sj.mn.7800198 }}
*{{cite journal | author=Godiska R, Chantry D, Raport CJ, ''et al.'' |title=Human macrophage-derived chemokine (MDC), a novel chemoattractant for monocytes, monocyte-derived dendritic cells, and natural killer cells. |journal=J. Exp. Med. |volume=185 |issue= 9 |pages= 1595-604 |year= 1997 |pmid= 9151897 |doi= }}
*{{cite journal | author=Chang M, McNinch J, Elias C, ''et al.'' |title=Molecular cloning and functional characterization of a novel CC chemokine, stimulated T cell chemotactic protein (STCP-1) that specifically acts on activated T lymphocytes. |journal=J. Biol. Chem. |volume=272 |issue= 40 |pages= 25229-37 |year= 1997 |pmid= 9312138 |doi= }}
*{{cite journal | author=Pal R, Garzino-Demo A, Markham PD, ''et al.'' |title=Inhibition of HIV-1 infection by the beta-chemokine MDC. |journal=Science |volume=278 |issue= 5338 |pages= 695-8 |year= 1997 |pmid= 9381181 |doi= }}
*{{cite journal | author=Imai T, Chantry D, Raport CJ, ''et al.'' |title=Macrophage-derived chemokine is a functional ligand for the CC chemokine receptor 4. |journal=J. Biol. Chem. |volume=273 |issue= 3 |pages= 1764-8 |year= 1998 |pmid= 9430724 |doi= }}
*{{cite journal | author=Nomiyama H, Imai T, Kusuda J, ''et al.'' |title=Human chemokines fractalkine (SCYD1), MDC (SCYA22) and TARC (SCYA17) are clustered on chromosome 16q13. |journal=Cytogenet. Cell Genet. |volume=81 |issue= 1 |pages= 10-1 |year= 1998 |pmid= 9691168 |doi= }}
*{{cite journal | author=Struyf S, Proost P, Sozzani S, ''et al.'' |title=Enhanced anti-HIV-1 activity and altered chemotactic potency of NH2-terminally processed macrophage-derived chemokine (MDC) imply an additional MDC receptor. |journal=J. Immunol. |volume=161 |issue= 6 |pages= 2672-5 |year= 1998 |pmid= 9743322 |doi= }}
*{{cite journal | author=Meucci O, Fatatis A, Simen AA, ''et al.'' |title=Chemokines regulate hippocampal neuronal signaling and gp120 neurotoxicity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 24 |pages= 14500-5 |year= 1998 |pmid= 9826729 |doi= }}
*{{cite journal | author=Proost P, Struyf S, Schols D, ''et al.'' |title=Truncation of macrophage-derived chemokine by CD26/ dipeptidyl-peptidase IV beyond its predicted cleavage site affects chemotactic activity and CC chemokine receptor 4 interaction. |journal=J. Biol. Chem. |volume=274 |issue= 7 |pages= 3988-93 |year= 1999 |pmid= 9933589 |doi= }}
*{{cite journal | author=Loftus BJ, Kim UJ, Sneddon VP, ''et al.'' |title=Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q. |journal=Genomics |volume=60 |issue= 3 |pages= 295-308 |year= 1999 |pmid= 10493829 |doi= 10.1006/geno.1999.5927 }}
*{{cite journal | author=Annunziato F, Romagnani P, Cosmi L, ''et al.'' |title=Macrophage-derived chemokine and EBI1-ligand chemokine attract human thymocytes in different stage of development and are produced by distinct subsets of medullary epithelial cells: possible implications for negative selection. |journal=J. Immunol. |volume=165 |issue= 1 |pages= 238-46 |year= 2000 |pmid= 10861057 |doi= }}
*{{cite journal | author=Vulcano M, Albanesi C, Stoppacciaro A, ''et al.'' |title=Dendritic cells as a major source of macrophage-derived chemokine/CCL22 in vitro and in vivo. |journal=Eur. J. Immunol. |volume=31 |issue= 3 |pages= 812-22 |year= 2001 |pmid= 11241286 |doi= }}
*{{cite journal | author=Berin MC, Dwinell MB, Eckmann L, Kagnoff MF |title=Production of MDC/CCL22 by human intestinal epithelial cells. |journal=Am. J. Physiol. Gastrointest. Liver Physiol. |volume=280 |issue= 6 |pages= G1217-26 |year= 2001 |pmid= 11352815 |doi= }}
*{{cite journal | author=Lambeir AM, Proost P, Durinx C, ''et al.'' |title=Kinetic investigation of chemokine truncation by CD26/dipeptidyl peptidase IV reveals a striking selectivity within the chemokine family. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 29839-45 |year= 2001 |pmid= 11390394 |doi= 10.1074/jbc.M103106200 }}
*{{cite journal | author=Wakahara S, Fujii Y, Nakao T, ''et al.'' |title=Gene expression profiles for Fc epsilon RI, cytokines and chemokines upon Fc epsilon RI activation in human cultured mast cells derived from peripheral blood. |journal=Cytokine |volume=16 |issue= 4 |pages= 143-52 |year= 2002 |pmid= 11792124 |doi= 10.1006/cyto.2001.0958 }}
*{{cite journal | author=Ghia P, Strola G, Granziero L, ''et al.'' |title=Chronic lymphocytic leukemia B cells are endowed with the capacity to attract CD4+, CD40L+ T cells by producing CCL22. |journal=Eur. J. Immunol. |volume=32 |issue= 5 |pages= 1403-13 |year= 2002 |pmid= 11981828 |doi= 10.1002/1521-4141(200205)32:5<1403::AID-IMMU1403>3.0.CO;2-Y }}
*{{cite journal | author=D'Ambrosio D, Albanesi C, Lang R, ''et al.'' |title=Quantitative differences in chemokine receptor engagement generate diversity in integrin-dependent lymphocyte adhesion. |journal=J. Immunol. |volume=169 |issue= 5 |pages= 2303-12 |year= 2002 |pmid= 12193695 |doi= }}
*{{cite journal | author=Campbell JD, Stinson MJ, Simons FE, HayGlass KT |title=Systemic chemokine and chemokine receptor responses are divergent in allergic versus non-allergic humans. |journal=Int. Immunol. |volume=14 |issue= 11 |pages= 1255-62 |year= 2003 |pmid= 12407016 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD83... {November 18, 2007 11:36:12 PM PST}
- SEARCH REDIRECT: Control Box Found: CD83 {November 18, 2007 11:36:39 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:36:42 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:36:42 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:36:42 PM PST}
- UPDATED: Updated protein page: CD83 {November 18, 2007 11:36:51 PM PST}
- INFO: Beginning work on CUL4A... {November 18, 2007 11:33:55 PM PST}
- SEARCH REDIRECT: Control Box Found: CUL4A {November 18, 2007 11:34:15 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:34:16 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:34:16 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:34:16 PM PST}
- UPDATED: Updated protein page: CUL4A {November 18, 2007 11:34:22 PM PST}
- INFO: Beginning work on IKBKE... {November 18, 2007 11:36:51 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:37:27 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| 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 = Inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase epsilon
| HGNCid = 14552
| Symbol = IKBKE
| AltSymbols =; IKK-i; IKKE; IKKI; KIAA0151; MGC125294; MGC125295; MGC125297
| OMIM = 605048
| ECnumber =
| Homologene = 23168
| MGIid = 1929612
| GeneAtlas_image1 = PBB_GE_IKBKE_214398_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_IKBKE_204549_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004704 |text = NF-kappaB-inducing kinase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008384 |text = IkappaB kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9641
| Hs_Ensembl = ENSG00000143466
| Hs_RefseqProtein = NP_054721
| Hs_RefseqmRNA = NM_014002
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 204710414
| Hs_GenLoc_end = 204736846
| Hs_Uniprot = Q14164
| Mm_EntrezGene = 56489
| Mm_Ensembl = ENSMUSG00000042349
| Mm_RefseqmRNA = NM_019777
| Mm_RefseqProtein = NP_062751
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 133082148
| Mm_GenLoc_end = 133107109
| Mm_Uniprot = Q5DU46
}}
}}
'''Inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase epsilon''', also known as '''IKBKE''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IKBKE inhibitor of kappa light polypeptide gene enhancer in B-cells, kinase epsilon| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9641| 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=Mercurio AM |title=Invasive skin carcinoma--Ras and alpha6beta4 integrin lead the way. |journal=Cancer Cell |volume=3 |issue= 3 |pages= 201-2 |year= 2003 |pmid= 12676577 |doi= }}
*{{cite journal | author=Nagase T, Seki N, Tanaka A, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1. |journal=DNA Res. |volume=2 |issue= 4 |pages= 167-74, 199-210 |year= 1996 |pmid= 8590280 |doi= }}
*{{cite journal | author=Shimada T, Kawai T, Takeda K, ''et al.'' |title=IKK-i, a novel lipopolysaccharide-inducible kinase that is related to IkappaB kinases. |journal=Int. Immunol. |volume=11 |issue= 8 |pages= 1357-62 |year= 1999 |pmid= 10421793 |doi= }}
*{{cite journal | author=Nomura F, Kawai T, Nakanishi K, Akira S |title=NF-kappaB activation through IKK-i-dependent I-TRAF/TANK phosphorylation. |journal=Genes Cells |volume=5 |issue= 3 |pages= 191-202 |year= 2000 |pmid= 10759890 |doi= }}
*{{cite journal | author=Peters RT, Liao SM, Maniatis T |title=IKKepsilon is part of a novel PMA-inducible IkappaB kinase complex. |journal=Mol. Cell |volume=5 |issue= 3 |pages= 513-22 |year= 2000 |pmid= 10882136 |doi= }}
*{{cite journal | author=Miller BS, Zandi E |title=Complete reconstitution of human IkappaB kinase (IKK) complex in yeast. Assessment of its stoichiometry and the role of IKKgamma on the complex activity in the absence of stimulation. |journal=J. Biol. Chem. |volume=276 |issue= 39 |pages= 36320-6 |year= 2001 |pmid= 11470787 |doi= 10.1074/jbc.M104051200 }}
*{{cite journal | author=Kishore N, Huynh QK, Mathialagan S, ''et al.'' |title=IKK-i and TBK-1 are enzymatically distinct from the homologous enzyme IKK-2: comparative analysis of recombinant human IKK-i, TBK-1, and IKK-2. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 13840-7 |year= 2002 |pmid= 11839743 |doi= 10.1074/jbc.M110474200 }}
*{{cite journal | author=Aupperle KR, Yamanishi Y, Bennett BL, ''et al.'' |title=Expression and regulation of inducible IkappaB kinase (IKK-i) in human fibroblast-like synoviocytes. |journal=Cell. Immunol. |volume=214 |issue= 1 |pages= 54-9 |year= 2002 |pmid= 11902829 |doi= 10.1006/cimm.2002.1885 }}
*{{cite journal | author=Bossis G, Salinas S, Cartier C, ''et al.'' |title=NF-kappaB activation upon interaction of HIV-1 envelope glycoproteins with cell surface CD4 involves IkappaB kinases. |journal=FEBS Lett. |volume=516 |issue= 1-3 |pages= 257-64 |year= 2002 |pmid= 11959143 |doi= }}
*{{cite journal | author=Chariot A, Leonardi A, Muller J, ''et al.'' |title=Association of the adaptor TANK with the I kappa B kinase (IKK) regulator NEMO connects IKK complexes with IKK epsilon and TBK1 kinases. |journal=J. Biol. Chem. |volume=277 |issue= 40 |pages= 37029-36 |year= 2002 |pmid= 12133833 |doi= 10.1074/jbc.M205069200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Fitzgerald KA, McWhirter SM, Faia KL, ''et al.'' |title=IKKepsilon and TBK1 are essential components of the IRF3 signaling pathway. |journal=Nat. Immunol. |volume=4 |issue= 5 |pages= 491-6 |year= 2003 |pmid= 12692549 |doi= 10.1038/ni921 }}
*{{cite journal | author=Kravchenko VV, Mathison JC, Schwamborn K, ''et al.'' |title=IKKi/IKKepsilon plays a key role in integrating signals induced by pro-inflammatory stimuli. |journal=J. Biol. Chem. |volume=278 |issue= 29 |pages= 26612-9 |year= 2003 |pmid= 12736252 |doi= 10.1074/jbc.M303001200 }}
*{{cite journal | author=Matsuda A, Suzuki Y, Honda G, ''et al.'' |title=Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. |journal=Oncogene |volume=22 |issue= 21 |pages= 3307-18 |year= 2003 |pmid= 12761501 |doi= 10.1038/sj.onc.1206406 }}
*{{cite journal | author=Fujita F, Taniguchi Y, Kato T, ''et al.'' |title=Identification of NAP1, a regulatory subunit of IkappaB kinase-related kinases that potentiates NF-kappaB signaling. |journal=Mol. Cell. Biol. |volume=23 |issue= 21 |pages= 7780-93 |year= 2003 |pmid= 14560022 |doi= }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Bouwmeester T, Bauch A, Ruffner H, ''et al.'' |title=A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway. |journal=Nat. Cell Biol. |volume=6 |issue= 2 |pages= 97-105 |year= 2004 |pmid= 14743216 |doi= 10.1038/ncb1086 }}
*{{cite journal | author=tenOever BR, Sharma S, Zou W, ''et al.'' |title=Activation of TBK1 and IKKvarepsilon kinases by vesicular stomatitis virus infection and the role of viral ribonucleoprotein in the development of interferon antiviral immunity. |journal=J. Virol. |volume=78 |issue= 19 |pages= 10636-49 |year= 2004 |pmid= 15367631 |doi= 10.1128/JVI.78.19.10636-10649.2004 }}
*{{cite journal | author=Buss H, Dörrie A, Schmitz ML, ''et al.'' |title=Constitutive and interleukin-1-inducible phosphorylation of p65 NF-{kappa}B at serine 536 is mediated by multiple protein kinases including I{kappa}B kinase (IKK)-{alpha}, IKK{beta}, IKK{epsilon}, TRAF family member-associated (TANK)-binding kinase 1 (TBK1), and an unknown kinase and couples p65 to TATA-binding protein-associated factor II31-mediated interleukin-8 transcription. |journal=J. Biol. Chem. |volume=279 |issue= 53 |pages= 55633-43 |year= 2005 |pmid= 15489227 |doi= 10.1074/jbc.M409825200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRDX2... {November 18, 2007 11:28:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:29:26 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PRDX2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1qmv.
| PDB = {{PDB2|1qmv}}
| Name = Peroxiredoxin 2
| HGNCid = 9353
| Symbol = PRDX2
| AltSymbols =; PRP; MGC4104; NKEFB; PRXII; TDPX1; TSA
| OMIM = 600538
| ECnumber =
| Homologene = 21182
| MGIid = 109486
| GeneAtlas_image1 = PBB_GE_PRDX2_39729_at_tn.png
| Function = {{GNF_GO|id=GO:0008379 |text = thioredoxin peroxidase activity}} {{GNF_GO|id=GO:0016209 |text = antioxidant activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0051920 |text = peroxiredoxin activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7001
| Hs_Ensembl = ENSG00000167815
| Hs_RefseqProtein = NP_859427
| Hs_RefseqmRNA = NM_181737
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 12768635
| Hs_GenLoc_end = 12773694
| Hs_Uniprot = P32119
| Mm_EntrezGene = 21672
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_011563
| Mm_RefseqProtein = NP_035693
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Peroxiredoxin 2''', also known as '''PRDX2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRDX2 peroxiredoxin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7001| 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 peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells. This protein may have a proliferative effect and play a role in cancer development or progression. The crystal structure of this protein has been resolved to 2.7 angstroms. Transcript variants encoding distinct isoforms have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: PRDX2 peroxiredoxin 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7001| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Rasmussen HH, van Damme J, Puype M, ''et al.'' |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960-9 |year= 1993 |pmid= 1286667 |doi= }}
*{{cite journal | author=Pahl P, Berger R, Hart I, ''et al.'' |title=Localization of TDPX1, a human homologue of the yeast thioredoxin-dependent peroxide reductase gene (TPX), to chromosome 13q12. |journal=Genomics |volume=26 |issue= 3 |pages= 602-6 |year= 1995 |pmid= 7607688 |doi= }}
*{{cite journal | author=Shau H, Butterfield LH, Chiu R, Kim A |title=Cloning and sequence analysis of candidate human natural killer-enhancing factor genes. |journal=Immunogenetics |volume=40 |issue= 2 |pages= 129-34 |year= 1994 |pmid= 8026862 |doi= }}
*{{cite journal | author=Chae HZ, Robison K, Poole LB, ''et al.'' |title=Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 15 |pages= 7017-21 |year= 1994 |pmid= 8041738 |doi= }}
*{{cite journal | author=Lim YS, Cha MK, Yun CH, ''et al.'' |title=Purification and characterization of thiol-specific antioxidant protein from human red blood cell: a new type of antioxidant protein. |journal=Biochem. Biophys. Res. Commun. |volume=199 |issue= 1 |pages= 199-206 |year= 1994 |pmid= 8123012 |doi= }}
*{{cite journal | author=Lim YS, Cha MK, Kim HK, Kim IH |title=The thiol-specific antioxidant protein from human brain: gene cloning and analysis of conserved cysteine regions. |journal=Gene |volume=140 |issue= 2 |pages= 279-84 |year= 1994 |pmid= 8144038 |doi= }}
*{{cite journal | author=Golaz O, Hughes GJ, Frutiger S, ''et al.'' |title=Plasma and red blood cell protein maps: update 1993. |journal=Electrophoresis |volume=14 |issue= 11 |pages= 1223-31 |year= 1994 |pmid= 8313871 |doi= }}
*{{cite journal | author=Cha MK, Kim IH |title=Glutathione-linked thiol peroxidase activity of human serum albumin: a possible antioxidant role of serum albumin in blood plasma. |journal=Biochem. Biophys. Res. Commun. |volume=222 |issue= 2 |pages= 619-25 |year= 1996 |pmid= 8670254 |doi= 10.1006/bbrc.1996.0793 }}
*{{cite journal | author=Ji H, Reid GE, Moritz RL, ''et al.'' |title=A two-dimensional gel database of human colon carcinoma proteins. |journal=Electrophoresis |volume=18 |issue= 3-4 |pages= 605-13 |year= 1997 |pmid= 9150948 |doi= 10.1002/elps.1150180344 }}
*{{cite journal | author=Wang ZM, Liu C, Dziarski R |title=Chemokines are the main proinflammatory mediators in human monocytes activated by Staphylococcus aureus, peptidoglycan, and endotoxin. |journal=J. Biol. Chem. |volume=275 |issue= 27 |pages= 20260-7 |year= 2000 |pmid= 10751418 |doi= 10.1074/jbc.M909168199 }}
*{{cite journal | author=Cha MK, Yun CH, Kim IH |title=Interaction of human thiol-specific antioxidant protein 1 with erythrocyte plasma membrane. |journal=Biochemistry |volume=39 |issue= 23 |pages= 6944-50 |year= 2000 |pmid= 10841776 |doi= }}
*{{cite journal | author=Schröder E, Littlechild JA, Lebedev AA, ''et al.'' |title=Crystal structure of decameric 2-Cys peroxiredoxin from human erythrocytes at 1.7 A resolution. |journal=Structure |volume=8 |issue= 6 |pages= 605-15 |year= 2000 |pmid= 10873855 |doi= }}
*{{cite journal | author=Harris JR, Schröder E, Isupov MN, ''et al.'' |title=Comparison of the decameric structure of peroxiredoxin-II by transmission electron microscopy and X-ray crystallography. |journal=Biochim. Biophys. Acta |volume=1547 |issue= 2 |pages= 221-34 |year= 2001 |pmid= 11410278 |doi= }}
*{{cite journal | author=Noh DY, Ahn SJ, Lee RA, ''et al.'' |title=Overexpression of peroxiredoxin in human breast cancer. |journal=Anticancer Res. |volume=21 |issue= 3B |pages= 2085-90 |year= 2001 |pmid= 11497302 |doi= }}
*{{cite journal | author=Kim SH, Fountoulakis M, Cairns N, Lubec G |title=Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down syndrome. |journal=J. Neural Transm. Suppl. |volume= |issue= 61 |pages= 223-35 |year= 2002 |pmid= 11771746 |doi= }}
*{{cite journal | author=Rabilloud T, Heller M, Gasnier F, ''et al.'' |title=Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19396-401 |year= 2002 |pmid= 11904290 |doi= 10.1074/jbc.M106585200 }}
*{{cite journal | author=Anahory T, Dechaud H, Bennes R, ''et al.'' |title=Identification of new proteins in follicular fluid of mature human follicles. |journal=Electrophoresis |volume=23 |issue= 7-8 |pages= 1197-202 |year= 2002 |pmid= 11981869 |doi= 10.1002/1522-2683(200204)23:7/8<1197::AID-ELPS1197>3.0.CO;2-2 }}
*{{cite journal | author=Shen C, Nathan C |title=Nonredundant antioxidant defense by multiple two-cysteine peroxiredoxins in human prostate cancer cells. |journal=Mol. Med. |volume=8 |issue= 2 |pages= 95-102 |year= 2002 |pmid= 12080185 |doi= }}
*{{cite journal | author=Geiben-Lynn R, Kursar M, Brown NV, ''et al.'' |title=HIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin family. |journal=J. Biol. Chem. |volume=278 |issue= 3 |pages= 1569-74 |year= 2003 |pmid= 12421812 |doi= 10.1074/jbc.M209964200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RDX... {November 18, 2007 11:21:43 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:22:06 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RDX_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gc6.
| PDB = {{PDB2|1gc6}}, {{PDB2|1gc7}}, {{PDB2|1j19}}, {{PDB2|2d10}}, {{PDB2|2d11}}, {{PDB2|2d2q}}, {{PDB2|2yvc}}
| Name = Radixin
| HGNCid = 9944
| Symbol = RDX
| AltSymbols =;
| OMIM = 179410
| ECnumber =
| Homologene = 37707
| MGIid = 97887
| GeneAtlas_image1 = PBB_GE_RDX_204969_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RDX_212397_at_tn.png
| GeneAtlas_image3 = PBB_GE_RDX_212398_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005902 |text = microvillus}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}}
| Process = {{GNF_GO|id=GO:0007016 |text = cytoskeletal anchoring}} {{GNF_GO|id=GO:0030033 |text = microvillus biogenesis}} {{GNF_GO|id=GO:0045176 |text = apical protein localization}} {{GNF_GO|id=GO:0051016 |text = barbed-end actin filament capping}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5962
| Hs_Ensembl = ENSG00000137710
| Hs_RefseqProtein = NP_002897
| Hs_RefseqmRNA = NM_002906
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 109605378
| Hs_GenLoc_end = 109672647
| Hs_Uniprot = P35241
| Mm_EntrezGene = 19684
| Mm_Ensembl = ENSMUSG00000032050
| Mm_RefseqmRNA = NM_009041
| Mm_RefseqProtein = NP_033067
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 51799393
| Mm_GenLoc_end = 51841094
| Mm_Uniprot = Q3TH46
}}
}}
'''Radixin''', also known as '''RDX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RDX radixin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5962| 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 = Radixin is a cytoskeletal protein that may be important in linking actin to the plasma membrane. It is highly similar in sequence to both ezrin and moesin. The radixin gene has been localized by fluorescence in situ hybridization to 11q23. A truncated version representing a pseudogene (RDXP2) was assigned to Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was mapped to 11p by Southern and PCR analyses.<ref name="entrez">{{cite web | title = Entrez Gene: RDX radixin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5962| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Hoeflich KP, Ikura M |title=Radixin: cytoskeletal adopter and signaling protein. |journal=Int. J. Biochem. Cell Biol. |volume=36 |issue= 11 |pages= 2131-6 |year= 2005 |pmid= 15313460 |doi= 10.1016/j.biocel.2003.11.018 }}
*{{cite journal | author=Matarrese P, Malorni W |title=Human immunodeficiency virus (HIV)-1 proteins and cytoskeleton: partners in viral life and host cell death. |journal=Cell Death Differ. |volume=12 Suppl 1 |issue= |pages= 932-41 |year= 2006 |pmid= 15818415 |doi= 10.1038/sj.cdd.4401582 }}
*{{cite journal | author=Sato N, Funayama N, Nagafuchi A, ''et al.'' |title=A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites. |journal=J. Cell. Sci. |volume=103 ( Pt 1) |issue= |pages= 131-43 |year= 1992 |pmid= 1429901 |doi= }}
*{{cite journal | author=Wilgenbus KK, Milatovich A, Francke U, Furthmayr H |title=Molecular cloning, cDNA sequence, and chromosomal assignment of the human radixin gene and two dispersed pseudogenes. |journal=Genomics |volume=16 |issue= 1 |pages= 199-206 |year= 1993 |pmid= 8486357 |doi= 10.1006/geno.1993.1159 }}
*{{cite journal | author=Hirao M, Sato N, Kondo T, ''et al.'' |title=Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. |journal=J. Cell Biol. |volume=135 |issue= 1 |pages= 37-51 |year= 1996 |pmid= 8858161 |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=Stemmer-Rachamimov AO, Gonzalez-Agosti C, Xu L, ''et al.'' |title=Expression of NF2-encoded merlin and related ERM family proteins in the human central nervous system. |journal=J. Neuropathol. Exp. Neurol. |volume=56 |issue= 6 |pages= 735-42 |year= 1997 |pmid= 9184664 |doi= }}
*{{cite journal | author=Takahashi K, Sasaki T, Mammoto A, ''et al.'' |title=Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein. |journal=J. Biol. Chem. |volume=272 |issue= 37 |pages= 23371-5 |year= 1997 |pmid= 9287351 |doi= }}
*{{cite journal | author=Kondo T, Takeuchi K, Doi Y, ''et al.'' |title=ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis. |journal=J. Cell Biol. |volume=139 |issue= 3 |pages= 749-58 |year= 1997 |pmid= 9348291 |doi= }}
*{{cite journal | author=Murthy A, Gonzalez-Agosti C, Cordero E, ''et al.'' |title=NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins. |journal=J. Biol. Chem. |volume=273 |issue= 3 |pages= 1273-6 |year= 1998 |pmid= 9430655 |doi= }}
*{{cite journal | author=Matsui T, Maeda M, Doi Y, ''et al.'' |title=Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. |journal=J. Cell Biol. |volume=140 |issue= 3 |pages= 647-57 |year= 1998 |pmid= 9456324 |doi= }}
*{{cite journal | author=Yonemura S, Hirao M, Doi Y, ''et al.'' |title=Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. |journal=J. Cell Biol. |volume=140 |issue= 4 |pages= 885-95 |year= 1998 |pmid= 9472040 |doi= }}
*{{cite journal | author=Bhartur SG, Goldenring JR |title=Mapping of ezrin dimerization using yeast two-hybrid screening. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 3 |pages= 874-7 |year= 1998 |pmid= 9501018 |doi= 10.1006/bbrc.1998.8196 }}
*{{cite journal | author=Takahashi K, Sasaki T, Mammoto A, ''et al.'' |title=Interaction of radixin with Rho small G protein GDP/GTP exchange protein Dbl. |journal=Oncogene |volume=16 |issue= 25 |pages= 3279-84 |year= 1998 |pmid= 9681826 |doi= 10.1038/sj.onc.1201874 }}
*{{cite journal | author=Lamb RF, Roy C, Diefenbach TJ, ''et al.'' |title=The TSC1 tumour suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase Rho. |journal=Nat. Cell Biol. |volume=2 |issue= 5 |pages= 281-7 |year= 2000 |pmid= 10806479 |doi= 10.1038/35010550 }}
*{{cite journal | author=Vaiskunaite R, Adarichev V, Furthmayr H, ''et al.'' |title=Conformational activation of radixin by G13 protein alpha subunit. |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26206-12 |year= 2000 |pmid= 10816569 |doi= 10.1074/jbc.M001863200 }}
*{{cite journal | author=Hamada K, Shimizu T, Matsui T, ''et al.'' |title=Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of the adhesion protein ICAM-2. |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=57 |issue= Pt 6 |pages= 891-2 |year= 2001 |pmid= 11375520 |doi= }}
*{{cite journal | author=Kikuchi S, Hata M, Fukumoto K, ''et al.'' |title=Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes. |journal=Nat. Genet. |volume=31 |issue= 3 |pages= 320-5 |year= 2002 |pmid= 12068294 |doi= 10.1038/ng905 }}
*{{cite journal | author=Dickson TC, Mintz CD, Benson DL, Salton SR |title=Functional binding interaction identified between the axonal CAM L1 and members of the ERM family. |journal=J. Cell Biol. |volume=157 |issue= 7 |pages= 1105-12 |year= 2002 |pmid= 12070130 |doi= 10.1083/jcb.200111076 }}
*{{cite journal | author=Haddad LA, Smith N, Bowser M, ''et al.'' |title=The TSC1 tumor suppressor hamartin interacts with neurofilament-L and possibly functions as a novel integrator of the neuronal cytoskeleton. |journal=J. Biol. Chem. |volume=277 |issue= 46 |pages= 44180-6 |year= 2003 |pmid= 12226091 |doi= 10.1074/jbc.M207211200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RFC1... {November 18, 2007 11:22:06 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:22:42 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Replication factor C (activator 1) 1, 145kDa
| HGNCid = 9969
| Symbol = RFC1
| AltSymbols =; A1; MGC51786; MHCBFB; PO-GA; RECC1; RFC; RFC140
| OMIM = 102579
| ECnumber =
| Homologene = 2187
| MGIid = 97891
| GeneAtlas_image1 = PBB_GE_RFC1_208021_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RFC1_209085_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008047 |text = enzyme activator activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0017111 |text = nucleoside-triphosphatase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005663 |text = DNA replication factor C complex}}
| Process = {{GNF_GO|id=GO:0006261 |text = DNA-dependent DNA replication}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007004 |text = telomere maintenance via telomerase}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5981
| Hs_Ensembl = ENSG00000035928
| Hs_RefseqProtein = NP_002904
| Hs_RefseqmRNA = NM_002913
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 38965471
| Hs_GenLoc_end = 39044390
| Hs_Uniprot = P35251
| Mm_EntrezGene = 19687
| Mm_Ensembl = ENSMUSG00000029191
| Mm_RefseqmRNA = NM_011258
| Mm_RefseqProtein = NP_035388
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 65542198
| Mm_GenLoc_end = 65598665
| Mm_Uniprot = Q3UJT6
}}
}}
'''Replication factor C (activator 1) 1, 145kDa''', also known as '''RFC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RFC1 replication factor C (activator 1) 1, 145kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5981| 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 the large subunit of replication factor C, which is a five subunit DNA polymerase accessory protein. Replication factor C is a DNA-dependent ATPase that is required for eukaryotic DNA replication and repair. The protein acts as an activator of DNA polymerases, binds to the 3' end of primers, and promotes coordinated synthesis of both strands. It also may have a role in telomere stability.<ref name="entrez">{{cite web | title = Entrez Gene: RFC1 replication factor C (activator 1) 1, 145kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5981| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lu Y, Riegel AT |title=The human DNA-binding protein, PO-GA, is homologous to the large subunit of mouse replication factor C: regulation by alternate 3' processing of mRNA. |journal=Gene |volume=145 |issue= 2 |pages= 261-5 |year= 1994 |pmid= 7914507 |doi= }}
*{{cite journal | author=Luckow B, Bunz F, Stillman B, ''et al.'' |title=Cloning, expression, and chromosomal localization of the 140-kilodalton subunit of replication factor C from mice and humans. |journal=Mol. Cell. Biol. |volume=14 |issue= 3 |pages= 1626-34 |year= 1994 |pmid= 8114700 |doi= }}
*{{cite journal | author=Bunz F, Kobayashi R, Stillman B |title=cDNAs encoding the large subunit of human replication factor C. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 23 |pages= 11014-8 |year= 1994 |pmid= 8248204 |doi= }}
*{{cite journal | author=Lu Y, Zeft AS, Riegel AT |title=Cloning and expression of a novel human DNA binding protein, PO-GA. |journal=Biochem. Biophys. Res. Commun. |volume=193 |issue= 2 |pages= 779-86 |year= 1993 |pmid= 8512577 |doi= 10.1006/bbrc.1993.1693 }}
*{{cite journal | author=Uhlmann F, Cai J, Flores-Rozas H, ''et al.'' |title=In vitro reconstitution of human replication factor C from its five subunits. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6521-6 |year= 1996 |pmid= 8692848 |doi= }}
*{{cite journal | author=Fotedar R, Mossi R, Fitzgerald P, ''et al.'' |title=A conserved domain of the large subunit of replication factor C binds PCNA and acts like a dominant negative inhibitor of DNA replication in mammalian cells. |journal=EMBO J. |volume=15 |issue= 16 |pages= 4423-33 |year= 1996 |pmid= 8861969 |doi= }}
*{{cite journal | author=Uchiumi F, Ohta T, Tanuma S |title=Replication factor C recognizes 5'-phosphate ends of telomeres. |journal=Biochem. Biophys. Res. Commun. |volume=229 |issue= 1 |pages= 310-5 |year= 1997 |pmid= 8954124 |doi= }}
*{{cite journal | author=Mossi R, Jónsson ZO, Allen BL, ''et al.'' |title=Replication factor C interacts with the C-terminal side of proliferating cell nuclear antigen. |journal=J. Biol. Chem. |volume=272 |issue= 3 |pages= 1769-76 |year= 1997 |pmid= 8999859 |doi= }}
*{{cite journal | author=Cujec TP, Cho H, Maldonado E, ''et al.'' |title=The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 1817-23 |year= 1997 |pmid= 9121429 |doi= }}
*{{cite journal | author=Ubeda M, Habener JF |title=The large subunit of the DNA replication complex C (DSEB/RF-C140) cleaved and inactivated by caspase-3 (CPP32/YAMA) during Fas-induced apoptosis. |journal=J. Biol. Chem. |volume=272 |issue= 31 |pages= 19562-8 |year= 1997 |pmid= 9235961 |doi= }}
*{{cite journal | author=Rhéaume E, Cohen LY, Uhlmann F, ''et al.'' |title=The large subunit of replication factor C is a substrate for caspase-3 in vitro and is cleaved by a caspase-3-like protease during Fas-mediated apoptosis. |journal=EMBO J. |volume=16 |issue= 21 |pages= 6346-54 |year= 1998 |pmid= 9351817 |doi= 10.1093/emboj/16.21.6346 }}
*{{cite journal | author=Ellison V, Stillman B |title=Reconstitution of recombinant human replication factor C (RFC) and identification of an RFC subcomplex possessing DNA-dependent ATPase activity. |journal=J. Biol. Chem. |volume=273 |issue= 10 |pages= 5979-87 |year= 1998 |pmid= 9488738 |doi= }}
*{{cite journal | author=Coll JM, Hickey RJ, Cronkey EA, ''et al.'' |title=Mapping specific protein-protein interactions within the core component of the breast cell DNA synthesome. |journal=Oncol. Res. |volume=9 |issue= 11-12 |pages= 629-39 |year= 1998 |pmid= 9563011 |doi= }}
*{{cite journal | author=Allen BL, Uhlmann F, Gaur LK, ''et al.'' |title=DNA recognition properties of the N-terminal DNA binding domain within the large subunit of replication factor C. |journal=Nucleic Acids Res. |volume=26 |issue= 17 |pages= 3877-82 |year= 1998 |pmid= 9705493 |doi= }}
*{{cite journal | author=van der Kuip H, Carius B, Haque SJ, ''et al.'' |title=The DNA-binding subunit p140 of replication factor C is upregulated in cycling cells and associates with G1 phase cell cycle regulatory proteins. |journal=J. Mol. Med. |volume=77 |issue= 4 |pages= 386-92 |year= 1999 |pmid= 10353443 |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=Yazdi PT, Wang Y, Zhao S, ''et al.'' |title=SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-phase checkpoint. |journal=Genes Dev. |volume=16 |issue= 5 |pages= 571-82 |year= 2002 |pmid= 11877377 |doi= 10.1101/gad.970702 }}
*{{cite journal | author=Anderson LA, Perkins ND |title=The large subunit of replication factor C interacts with the histone deacetylase, HDAC1. |journal=J. Biol. Chem. |volume=277 |issue= 33 |pages= 29550-4 |year= 2002 |pmid= 12045192 |doi= 10.1074/jbc.M200513200 }}
*{{cite journal | author=Ohta S, Shiomi Y, Sugimoto K, ''et al.'' |title=A proteomics approach to identify proliferating cell nuclear antigen (PCNA)-binding proteins in human cell lysates. Identification of the human CHL12/RFCs2-5 complex as a novel PCNA-binding protein. |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 40362-7 |year= 2002 |pmid= 12171929 |doi= 10.1074/jbc.M206194200 }}
*{{cite journal | author=Maruyama T, Farina A, Dey A, ''et al.'' |title=A Mammalian bromodomain protein, brd4, interacts with replication factor C and inhibits progression to S phase. |journal=Mol. Cell. Biol. |volume=22 |issue= 18 |pages= 6509-20 |year= 2002 |pmid= 12192049 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RNASE2... {November 18, 2007 11:22:42 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:23:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RNASE2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gqv.
| PDB = {{PDB2|1gqv}}, {{PDB2|1hi2}}, {{PDB2|1hi3}}, {{PDB2|1hi4}}, {{PDB2|1hi5}}, {{PDB2|1k2a}}, {{PDB2|2bex}}, {{PDB2|2bzz}}, {{PDB2|2c01}}, {{PDB2|2c02}}, {{PDB2|2c05}}
| Name = Ribonuclease, RNase A family, 2 (liver, eosinophil-derived neurotoxin)
| HGNCid = 10045
| Symbol = RNASE2
| AltSymbols =; EDN; RNS2
| OMIM = 131410
| ECnumber =
| Homologene = 68284
| MGIid = 1858238
| GeneAtlas_image1 = PBB_GE_RNASE2_206111_at_tn.png
| Function = {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0004519 |text = endonuclease activity}} {{GNF_GO|id=GO:0004522 |text = pancreatic ribonuclease activity}} {{GNF_GO|id=GO:0004540 |text = ribonuclease activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042613 |text = MHC class II protein complex}}
| Process = {{GNF_GO|id=GO:0002504 |text = antigen processing and presentation of peptide or polysaccharide antigen via MHC class II}} {{GNF_GO|id=GO:0006401 |text = RNA catabolic process}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6036
| Hs_Ensembl = ENSG00000169385
| Hs_RefseqProtein = NP_002925
| Hs_RefseqmRNA = NM_002934
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 20493470
| Hs_GenLoc_end = 20494434
| Hs_Uniprot = P10153
| Mm_EntrezGene = 53877
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_001017422
| Mm_RefseqProtein = NP_001017422
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Ribonuclease, RNase A family, 2 (liver, eosinophil-derived neurotoxin)''', also known as '''RNASE2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RNASE2 ribonuclease, RNase A family, 2 (liver, eosinophil-derived neurotoxin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6036| 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=Rosenberg HF, Domachowske JB |title=Eosinophils, ribonucleases and host defense: solving the puzzle. |journal=Immunol. Res. |volume=20 |issue= 3 |pages= 261-74 |year= 2000 |pmid= 10741866 |doi= }}
*{{cite journal | author=Abu-Ghazaleh RI, Dunnette SL, Loegering DA, ''et al.'' |title=Eosinophil granule proteins in peripheral blood granulocytes. |journal=J. Leukoc. Biol. |volume=52 |issue= 6 |pages= 611-8 |year= 1993 |pmid= 1464733 |doi= }}
*{{cite journal | author=Mastrianni DM, Eddy RL, Rosenberg HF, ''et al.'' |title=Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14. |journal=Genomics |volume=13 |issue= 1 |pages= 240-2 |year= 1992 |pmid= 1577491 |doi= }}
*{{cite journal | author=Sakakibara R, Hashida K, Kitahara T, Ishiguro M |title=Characterization of a unique nonsecretory ribonuclease from urine of pregnant women. |journal=J. Biochem. |volume=111 |issue= 3 |pages= 325-30 |year= 1992 |pmid= 1587793 |doi= }}
*{{cite journal | author=Hamann KJ, Ten RM, Loegering DA, ''et al.'' |title=Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes: evidence for intronless coding sequences in the ribonuclease gene superfamily. |journal=Genomics |volume=7 |issue= 4 |pages= 535-46 |year= 1990 |pmid= 2387583 |doi= }}
*{{cite journal | author=Hamann KJ, Barker RL, Loegering DA, ''et al.'' |title=Sequence of human eosinophil-derived neurotoxin cDNA: identity of deduced amino acid sequence with human nonsecretory ribonucleases. |journal=Gene |volume=83 |issue= 1 |pages= 161-7 |year= 1990 |pmid= 2591744 |doi= }}
*{{cite journal | author=Rosenberg HF, Tenen DG, Ackerman SJ |title=Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 12 |pages= 4460-4 |year= 1989 |pmid= 2734298 |doi= }}
*{{cite journal | author=Barker RL, Loegering DA, Ten RM, ''et al.'' |title=Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases. |journal=J. Immunol. |volume=143 |issue= 3 |pages= 952-5 |year= 1989 |pmid= 2745977 |doi= }}
*{{cite journal | author=Beintema JJ, Hofsteenge J, Iwama M, ''et al.'' |title=Amino acid sequence of the nonsecretory ribonuclease of human urine. |journal=Biochemistry |volume=27 |issue= 12 |pages= 4530-8 |year= 1988 |pmid= 3166997 |doi= }}
*{{cite journal | author=Sorrentino S, Tucker GK, Glitz DG |title=Purification and characterization of a ribonuclease from human liver. |journal=J. Biol. Chem. |volume=263 |issue= 31 |pages= 16125-31 |year= 1988 |pmid= 3182786 |doi= }}
*{{cite journal | author=Gleich GJ, Loegering DA, Bell MP, ''et al.'' |title=Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 10 |pages= 3146-50 |year= 1986 |pmid= 3458170 |doi= }}
*{{cite journal | author=Niwata Y, Ohgi K, Sanda A, ''et al.'' |title=Purification and properties of bovine kidney ribonucleases. |journal=J. Biochem. |volume=97 |issue= 3 |pages= 923-34 |year= 1985 |pmid= 3926759 |doi= }}
*{{cite journal | author=de Beer T, Vliegenthart JF, Löffler A, Hofsteenge J |title=The hexopyranosyl residue that is C-glycosidically linked to the side chain of tryptophan-7 in human RNase Us is alpha-mannopyranose. |journal=Biochemistry |volume=34 |issue= 37 |pages= 11785-9 |year= 1995 |pmid= 7547911 |doi= }}
*{{cite journal | author=Hofsteenge J, Müller DR, de Beer T, ''et al.'' |title=New type of linkage between a carbohydrate and a protein: C-glycosylation of a specific tryptophan residue in human RNase Us. |journal=Biochemistry |volume=33 |issue= 46 |pages= 13524-30 |year= 1994 |pmid= 7947762 |doi= }}
*{{cite journal | author=Kardana A, Bagshawe KD, Coles B, ''et al.'' |title=Characterisation of UGP and its relationship with beta-core fragment. |journal=Br. J. Cancer |volume=67 |issue= 4 |pages= 686-92 |year= 1993 |pmid= 8471426 |doi= }}
*{{cite journal | author=Mosimann SC, Newton DL, Youle RJ, James MN |title=X-ray crystallographic structure of recombinant eosinophil-derived neurotoxin at 1.83 A resolution. |journal=J. Mol. Biol. |volume=260 |issue= 4 |pages= 540-52 |year= 1996 |pmid= 8759319 |doi= 10.1006/jmbi.1996.0420 }}
*{{cite journal | author=Krieg J, Hartmann S, Vicentini A, ''et al.'' |title=Recognition signal for C-mannosylation of Trp-7 in RNase 2 consists of sequence Trp-x-x-Trp. |journal=Mol. Biol. Cell |volume=9 |issue= 2 |pages= 301-9 |year= 1998 |pmid= 9450956 |doi= }}
*{{cite journal | author=Sur S, Glitz DG, Kita H, ''et al.'' |title=Localization of eosinophil-derived neurotoxin and eosinophil cationic protein in neutrophilic leukocytes. |journal=J. Leukoc. Biol. |volume=63 |issue= 6 |pages= 715-22 |year= 1998 |pmid= 9620664 |doi= }}
*{{cite journal | author=Zhang J, Rosenberg HF |title=Sequence variation at two eosinophil-associated ribonuclease loci in humans. |journal=Genetics |volume=156 |issue= 4 |pages= 1949-58 |year= 2001 |pmid= 11102386 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RRM1... {November 18, 2007 11:23:07 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:23:35 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Ribonucleotide reductase M1 polypeptide
| HGNCid = 10451
| Symbol = RRM1
| AltSymbols =; R1; RIR1; RR1
| OMIM = 180410
| ECnumber =
| Homologene = 806
| MGIid = 98180
| GeneAtlas_image1 = PBB_GE_RRM1_201477_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RRM1_201476_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004748 |text = ribonucleoside-diphosphate reductase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}}
| Component = {{GNF_GO|id=GO:0005971 |text = ribonucleoside-diphosphate reductase complex}}
| Process = {{GNF_GO|id=GO:0006260 |text = DNA replication}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6240
| Hs_Ensembl = ENSG00000167325
| Hs_RefseqProtein = NP_001024
| Hs_RefseqmRNA = NM_001033
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 4072587
| Hs_GenLoc_end = 4116681
| Hs_Uniprot = P23921
| Mm_EntrezGene = 20133
| Mm_Ensembl = ENSMUSG00000030978
| Mm_RefseqmRNA = NM_009103
| Mm_RefseqProtein = NP_033129
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 102315638
| Mm_GenLoc_end = 102342746
| Mm_Uniprot = Q05DU8
}}
}}
'''Ribonucleotide reductase M1 polypeptide''', also known as '''RRM1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RRM1 ribonucleotide reductase M1 polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6240| 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 one of two non-identical subunits which constitute ribonucleoside-diphosphate reductase, an enzyme essential for the production of deoxyribonucleotides prior to DNA synthesis in S phase of dividing cells. It is one of several genes located in the imprinted gene domain of 11p15.5, an important tumor-suppressor gene region. Alterations in this region have been associated with the Beckwith-Wiedemann syndrome, Wilms tumor, rhabdomyosarcoma, adrenocrotical carcinoma, and lung, ovarian, and breast cancer. This gene may play a role in malignancies and disease that involve this region. This gene is oriented in a head-to-tail configuration with the stromal interaction molecule 1 gene (STIM1), with the 3' end of STIM1 situated 1.6 kb from the 5' end of this gene.<ref name="entrez">{{cite web | title = Entrez Gene: RRM1 ribonucleotide reductase M1 polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6240| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pavloff N, Rivard D, Masson S, ''et al.'' |title=Sequence analysis of the large and small subunits of human ribonucleotide reductase. |journal=DNA Seq. |volume=2 |issue= 4 |pages= 227-34 |year= 1992 |pmid= 1627826 |doi= }}
*{{cite journal | author=Byrne J, Smith P |title=Human polymorphic probe pE1.8 detects SacI polymorphism in the ribonucleotide reductase M1 subunit gene. |journal=Hum. Genet. |volume=87 |issue= 3 |pages= 376 |year= 1991 |pmid= 1677928 |doi= }}
*{{cite journal | author=Parker NJ, Begley CG, Fox RM |title=Human M1 subunit of ribonucleotide reductase: cDNA sequence and expression in stimulated lymphocytes. |journal=Nucleic Acids Res. |volume=19 |issue= 13 |pages= 3741 |year= 1991 |pmid= 1840662 |doi= }}
*{{cite journal | author=Mann GJ, Musgrove EA, Fox RM, Thelander L |title=Ribonucleotide reductase M1 subunit in cellular proliferation, quiescence, and differentiation. |journal=Cancer Res. |volume=48 |issue= 18 |pages= 5151-6 |year= 1988 |pmid= 3044582 |doi= }}
*{{cite journal | author=Brissenden JE, Caras I, Thelander L, Francke U |title=The structural gene for the M1 subunit of ribonucleotide reductase maps to chromosome 11, band p15, in human and to chromosome 7 in mouse. |journal=Exp. Cell Res. |volume=174 |issue= 1 |pages= 302-8 |year= 1988 |pmid= 3275546 |doi= }}
*{{cite journal | author=Engström Y, Francke U |title=Assignment of the structural gene for subunit M1 of human ribonucleotide reductase to the short arm of chromosome 11. |journal=Exp. Cell Res. |volume=158 |issue= 2 |pages= 477-83 |year= 1985 |pmid= 3891388 |doi= }}
*{{cite journal | author=Parker NJ, Begley CG, Fox RM |title=Human gene for the large subunit of ribonucleotide reductase (RRM1): functional analysis of the promoter. |journal=Genomics |volume=27 |issue= 2 |pages= 280-5 |year= 1995 |pmid= 7557993 |doi= 10.1006/geno.1995.1043 }}
*{{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=Parker NJ, Begley CG, Fox RM |title=Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking region of the gene. |journal=Genomics |volume=19 |issue= 1 |pages= 91-6 |year= 1994 |pmid= 8188248 |doi= 10.1006/geno.1994.1017 }}
*{{cite journal | author=Byrne JA, Smith PJ |title=The 11p15.5 ribonucleotide reductase M1 subunit locus is not imprinted in Wilms' tumour and hepatoblastoma. |journal=Hum. Genet. |volume=91 |issue= 3 |pages= 275-7 |year= 1993 |pmid= 8386696 |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= }}
*{{cite journal | author=Bepler G, O'briant KC, Kim YC, ''et al.'' |title=A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region. |journal=Genomics |volume=55 |issue= 2 |pages= 164-75 |year= 1999 |pmid= 9933563 |doi= 10.1006/geno.1998.5659 }}
*{{cite journal | author=Pitterle DM, Kim YC, Jolicoeur EM, ''et al.'' |title=Lung cancer and the human gene for ribonucleotide reductase subunit M1 (RRM1). |journal=Mamm. Genome |volume=10 |issue= 9 |pages= 916-22 |year= 1999 |pmid= 10441745 |doi= }}
*{{cite journal | author=Guittet O, Håkansson P, Voevodskaya N, ''et al.'' |title=Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells. |journal=J. Biol. Chem. |volume=276 |issue= 44 |pages= 40647-51 |year= 2001 |pmid= 11517226 |doi= 10.1074/jbc.M106088200 }}
*{{cite journal | author=Kashlan OB, Scott CP, Lear JD, Cooperman BS |title=A comprehensive model for the allosteric regulation of mammalian ribonucleotide reductase. Functional consequences of ATP- and dATP-induced oligomerization of the large subunit. |journal=Biochemistry |volume=41 |issue= 2 |pages= 462-74 |year= 2002 |pmid= 11781084 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Kashlan OB, Cooperman BS |title=Comprehensive model for allosteric regulation of mammalian ribonucleotide reductase: refinements and consequences. |journal=Biochemistry |volume=42 |issue= 6 |pages= 1696-706 |year= 2003 |pmid= 12578384 |doi= 10.1021/bi020634d }}
*{{cite journal | author=Xue L, Zhou B, Liu X, ''et al.'' |title=Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits. |journal=Cancer Res. |volume=63 |issue= 5 |pages= 980-6 |year= 2003 |pmid= 12615712 |doi= }}
*{{cite journal | author=Gautam A, Li ZR, Bepler G |title=RRM1-induced metastasis suppression through PTEN-regulated pathways. |journal=Oncogene |volume=22 |issue= 14 |pages= 2135-42 |year= 2003 |pmid= 12687015 |doi= 10.1038/sj.onc.1206232 }}
*{{cite journal | author=Rosell R, Scagliotti G, Danenberg KD, ''et al.'' |title=Transcripts in pretreatment biopsies from a three-arm randomized trial in metastatic non-small-cell lung cancer. |journal=Oncogene |volume=22 |issue= 23 |pages= 3548-53 |year= 2003 |pmid= 12789263 |doi= 10.1038/sj.onc.1206419 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RUVBL1... {November 18, 2007 11:34:22 PM PST}
- SEARCH REDIRECT: Control Box Found: RUVBL1 {November 18, 2007 11:34:52 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:34:53 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:34:53 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:34:53 PM PST}
- UPDATED: Updated protein page: RUVBL1 {November 18, 2007 11:34:59 PM PST}
- INFO: Beginning work on S100A2... {November 18, 2007 11:23:35 PM PST}
- SEARCH REDIRECT: Control Box Found: S100A2 {November 18, 2007 11:24:13 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:24:16 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:24:16 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:24:16 PM PST}
- UPDATED: Updated protein page: S100A2 {November 18, 2007 11:24:22 PM PST}
- INFO: Beginning work on SCP2... {November 18, 2007 11:24:22 PM PST}
- SEARCH REDIRECT: Control Box Found: SCP2 {November 18, 2007 11:24:53 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:24:55 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:24:55 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:24:55 PM PST}
- UPDATED: Updated protein page: SCP2 {November 18, 2007 11:25:01 PM PST}
- INFO: Beginning work on SEMG1... {November 18, 2007 11:25:31 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:25:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Semenogelin I
| HGNCid = 10742
| Symbol = SEMG1
| AltSymbols =; MGC14719; SEMG; SGI
| OMIM = 182140
| ECnumber =
| Homologene =
| MGIid =
| GeneAtlas_image1 = PBB_GE_SEMG1_206442_at_tn.png
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0030141 |text = secretory granule}}
| Process = {{GNF_GO|id=GO:0007320 |text = insemination}} {{GNF_GO|id=GO:0019953 |text = sexual reproduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6406
| Hs_Ensembl = ENSG00000124233
| Hs_RefseqProtein = NP_002998
| Hs_RefseqmRNA = NM_003007
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 43269052
| Hs_GenLoc_end = 43271827
| Hs_Uniprot = P04279
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Semenogelin I''', also known as '''SEMG1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SEMG1 semenogelin I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6406| 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 the predominant protein in semen. The encoded secreted protein is involved in the formation of a gel matrix that encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes this protein into smaller peptides, with each possibly having a separate function. The proteolysis process breaks down the gel matrix and allows the spermatozoa to move more freely. Two transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: SEMG1 semenogelin I| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6406| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Robert M, Gagnon C |title=Semenogelin I: a coagulum forming, multifunctional seminal vesicle protein. |journal=Cell. Mol. Life Sci. |volume=55 |issue= 6-7 |pages= 944-60 |year= 1999 |pmid= 10412373 |doi= }}
*{{cite journal | author=Ulvsbäck M, Lazure C, Lilja H, ''et al.'' |title=Gene structure of semenogelin I and II. The predominant proteins in human semen are encoded by two homologous genes on chromosome 20. |journal=J. Biol. Chem. |volume=267 |issue= 25 |pages= 18080-4 |year= 1992 |pmid= 1517240 |doi= }}
*{{cite journal | author=Schneider K, Kausler W, Tripier D, ''et al.'' |title=[Isolation and structure determination of two peptides occurring in human seminal plasma] |journal=Biol. Chem. Hoppe-Seyler |volume=370 |issue= 4 |pages= 353-6 |year= 1989 |pmid= 2757795 |doi= }}
*{{cite journal | author=Lilja H, Abrahamsson PA, Lundwall A |title=Semenogelin, the predominant protein in human semen. Primary structure and identification of closely related proteins in the male accessory sex glands and on the spermatozoa. |journal=J. Biol. Chem. |volume=264 |issue= 3 |pages= 1894-900 |year= 1989 |pmid= 2912989 |doi= }}
*{{cite journal | author=Li CH, Hammonds RG, Ramasharma K, Chung D |title=Human seminal alpha inhibins: isolation, characterization, and structure. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 12 |pages= 4041-4 |year= 1985 |pmid= 3889920 |doi= }}
*{{cite journal | author=Lilja H, Jeppsson JO |title=Amino acid sequence of the predominant basic protein in human seminal plasma. |journal=FEBS Lett. |volume=182 |issue= 1 |pages= 181-4 |year= 1985 |pmid= 3972122 |doi= }}
*{{cite journal | author=Ramasharma K, Sairam MR, Seidah NG, ''et al.'' |title=Isolation, structure, and synthesis of a human seminal plasma peptide with inhibin-like activity. |journal=Science |volume=223 |issue= 4641 |pages= 1199-202 |year= 1984 |pmid= 6422553 |doi= }}
*{{cite journal | author=Lilja H, Laurell CB, Jeppsson JO |title=Characterization of the predominant basic protein in human seminal plasma, one cleavage product of the major seminal vesicle protein. |journal=Scand. J. Clin. Lab. Invest. |volume=44 |issue= 5 |pages= 439-46 |year= 1984 |pmid= 6484484 |doi= }}
*{{cite journal | author=Seidah NG, Ramasharma K, Sairam MR, Chrétien M |title=Partial amino acid sequence of a human seminal plasma peptide with inhibin-like activity. |journal=FEBS Lett. |volume=167 |issue= 1 |pages= 98-102 |year= 1984 |pmid= 6698208 |doi= }}
*{{cite journal | author=Khan Z, Smyth DG |title=Isolation and identification of N-terminally extended forms of 5-oxoprolylglutamylprolinamide (Glp-Glu-Pro-NH2), a thyrotropin-releasing-hormone (TRH)-like peptide present in human semen. |journal=Eur. J. Biochem. |volume=212 |issue= 1 |pages= 35-40 |year= 1993 |pmid= 8444163 |doi= }}
*{{cite journal | author=Lundwall A |title=The structure of the semenogelin gene locus--nucleotide sequence of the intergenic and the flanking DNA. |journal=Eur. J. Biochem. |volume=235 |issue= 3 |pages= 466-70 |year= 1996 |pmid= 8654389 |doi= }}
*{{cite journal | author=Malm J, Hellman J, Magnusson H, ''et al.'' |title=Isolation and characterization of the major gel proteins in human semen, semenogelin I and semenogelin II. |journal=Eur. J. Biochem. |volume=238 |issue= 1 |pages= 48-53 |year= 1996 |pmid= 8665951 |doi= }}
*{{cite journal | author=Bjartell A, Malm J, Moller C, ''et al.'' |title=Distribution and tissue expression of semenogelin I and II in man as demonstrated by in situ hybridization and immunocytochemistry. |journal=J. Androl. |volume=17 |issue= 1 |pages= 17-26 |year= 1997 |pmid= 8833737 |doi= }}
*{{cite journal | author=Robert M, Gibbs BF, Jacobson E, Gagnon C |title=Characterization of prostate-specific antigen proteolytic activity on its major physiological substrate, the sperm motility inhibitor precursor/semenogelin I. |journal=Biochemistry |volume=36 |issue= 13 |pages= 3811-9 |year= 1997 |pmid= 9092810 |doi= 10.1021/bi9626158 }}
*{{cite journal | author=Peter A, Lilja H, Lundwall A, Malm J |title=Semenogelin I and semenogelin II, the major gel-forming proteins in human semen, are substrates for transglutaminase. |journal=Eur. J. Biochem. |volume=252 |issue= 2 |pages= 216-21 |year= 1998 |pmid= 9523691 |doi= }}
*{{cite journal | author=Lövgren J, Airas K, Lilja H |title=Enzymatic action of human glandular kallikrein 2 (hK2). Substrate specificity and regulation by Zn2+ and extracellular protease inhibitors. |journal=Eur. J. Biochem. |volume=262 |issue= 3 |pages= 781-9 |year= 1999 |pmid= 10411640 |doi= }}
*{{cite journal | author=Malm J, Hellman J, Hogg P, Lilja H |title=Enzymatic action of prostate-specific antigen (PSA or hK3): substrate specificity and regulation by Zn(2+), a tight-binding inhibitor. |journal=Prostate |volume=45 |issue= 2 |pages= 132-9 |year= 2000 |pmid= 11027412 |doi= }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal | author=Brillard-Bourdet M, Réhault S, Juliano L, ''et al.'' |title=Amidolytic activity of prostatic acid phosphatase on human semenogelins and semenogelin-derived synthetic substrates. |journal=Eur. J. Biochem. |volume=269 |issue= 1 |pages= 390-5 |year= 2002 |pmid= 11784334 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SFTPA2... {November 18, 2007 11:25:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:26:39 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Surfactant, pulmonary-associated protein A2
| HGNCid = 10799
| Symbol = SFTPA2
| AltSymbols =; SP-A1; COLEC5; SP-2A; SP-2A beta; SP-A1 beta; SP-A2; SPAII
| OMIM = 178642
| ECnumber =
| Homologene = 3946
| MGIid = 109518
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0007585 |text = respiratory gaseous exchange}} {{GNF_GO|id=GO:0050828 |text = regulation of liquid surface tension}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6436
| Hs_Ensembl =
| Hs_RefseqProtein = NP_008857
| Hs_RefseqmRNA = NM_006926
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 20387
| Mm_Ensembl = ENSMUSG00000021789
| Mm_RefseqmRNA = NM_023134
| Mm_RefseqProtein = NP_075623
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 40040501
| Mm_GenLoc_end = 40045165
| Mm_Uniprot = Q9CQI1
}}
}}
'''Surfactant, pulmonary-associated protein A2''', also known as '''SFTPA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SFTPA2 surfactant, pulmonary-associated protein A2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6436| 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=Floros J, Hoover RR |title=Genetics of the hydrophilic surfactant proteins A and D. |journal=Biochim. Biophys. Acta |volume=1408 |issue= 2-3 |pages= 312-22 |year= 1999 |pmid= 9813381 |doi= }}
*{{cite journal | author=Katyal SL, Singh G, Locker J |title=Characterization of a second human pulmonary surfactant-associated protein SP-A gene. |journal=Am. J. Respir. Cell Mol. Biol. |volume=6 |issue= 4 |pages= 446-52 |year= 1992 |pmid= 1372511 |doi= }}
*{{cite journal | author=Voss T, Melchers K, Scheirle G, Schäfer KP |title=Structural comparison of recombinant pulmonary surfactant protein SP-A derived from two human coding sequences: implications for the chain composition of natural human SP-A. |journal=Am. J. Respir. Cell Mol. Biol. |volume=4 |issue= 1 |pages= 88-94 |year= 1991 |pmid= 1986781 |doi= }}
*{{cite journal | author=Haagsman HP, White RT, Schilling J, ''et al.'' |title=Studies of the structure of lung surfactant protein SP-A. |journal=Am. J. Physiol. |volume=257 |issue= 6 Pt 1 |pages= L421-9 |year= 1990 |pmid= 2610270 |doi= }}
*{{cite journal | author=White RT, Damm D, Miller J, ''et al.'' |title=Isolation and characterization of the human pulmonary surfactant apoprotein gene. |journal=Nature |volume=317 |issue= 6035 |pages= 361-3 |year= 1985 |pmid= 2995821 |doi= }}
*{{cite journal | author=Floros J, Steinbrink R, Jacobs K, ''et al.'' |title=Isolation and characterization of cDNA clones for the 35-kDa pulmonary surfactant-associated protein. |journal=J. Biol. Chem. |volume=261 |issue= 19 |pages= 9029-33 |year= 1986 |pmid= 3755136 |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=McCormick SM, Boggaram V, Mendelson CR |title=Characterization of mRNA transcripts and organization of human SP-A1 and SP-A2 genes. |journal=Am. J. Physiol. |volume=266 |issue= 4 Pt 1 |pages= L354-66 |year= 1994 |pmid= 8179012 |doi= }}
*{{cite journal | author=Kölble K, Lu J, Mole SE, ''et al.'' |title=Assignment of the human pulmonary surfactant protein D gene (SFTP4) to 10q22-q23 close to the surfactant protein A gene cluster. |journal=Genomics |volume=17 |issue= 2 |pages= 294-8 |year= 1993 |pmid= 8406480 |doi= 10.1006/geno.1993.1324 }}
*{{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= }}
*{{cite journal | author=Stuart GR, Lynch NJ, Day AJ, ''et al.'' |title=The C1q and collectin binding site within C1q receptor (cell surface calreticulin). |journal=Immunopharmacology |volume=38 |issue= 1-2 |pages= 73-80 |year= 1998 |pmid= 9476117 |doi= }}
*{{cite journal | author=Karinch AM, Deiter G, Ballard PL, Floros J |title=Regulation of expression of human SP-A1 and SP-A2 genes in fetal lung explant culture. |journal=Biochim. Biophys. Acta |volume=1398 |issue= 2 |pages= 192-202 |year= 1998 |pmid= 9689918 |doi= }}
*{{cite journal | author=Saitoh H, Okayama H, Shimura S, ''et al.'' |title=Surfactant protein A2 gene expression by human airway submucosal gland cells. |journal=Am. J. Respir. Cell Mol. Biol. |volume=19 |issue= 2 |pages= 202-9 |year= 1998 |pmid= 9698591 |doi= }}
*{{cite journal | author=Goss KL, Kumar AR, Snyder JM |title=SP-A2 gene expression in human fetal lung airways. |journal=Am. J. Respir. Cell Mol. Biol. |volume=19 |issue= 4 |pages= 613-21 |year= 1998 |pmid= 9761758 |doi= }}
*{{cite journal | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |doi= }}
*{{cite journal | author=Wang G, Phelps DS, Umstead TM, Floros J |title=Human SP-A protein variants derived from one or both genes stimulate TNF-alpha production in the THP-1 cell line. |journal=Am. J. Physiol. Lung Cell Mol. Physiol. |volume=278 |issue= 5 |pages= L946-54 |year= 2000 |pmid= 10781424 |doi= }}
*{{cite journal | author=Berg T, Leth-Larsen R, Holmskov U, Højrup P |title=Structural characterisation of human proteinosis surfactant protein A. |journal=Biochim. Biophys. Acta |volume=1543 |issue= 1 |pages= 159-73 |year= 2001 |pmid= 11087951 |doi= }}
*{{cite journal | author=Lin Z, deMello D, Phelps DS, ''et al.'' |title=Both human SP-A1 and Sp-A2 genes are expressed in small and large intestine. |journal=Pediatric pathology & molecular medicine |volume=20 |issue= 5 |pages= 367-86 |year= 2002 |pmid= 11552738 |doi= }}
*{{cite journal | author=Madan T, Saxena S, Murthy KJ, ''et al.'' |title=Association of polymorphisms in the collagen region of human SP-A1 and SP-A2 genes with pulmonary tuberculosis in Indian population. |journal=Clin. Chem. Lab. Med. |volume=40 |issue= 10 |pages= 1002-8 |year= 2003 |pmid= 12476938 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC15A1... {November 18, 2007 11:27:11 PM PST}
- SEARCH REDIRECT: Control Box Found: SLC15A1 {November 18, 2007 11:27:41 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:27:44 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:27:44 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:27:44 PM PST}
- UPDATED: Updated protein page: SLC15A1 {November 18, 2007 11:27:49 PM PST}
- INFO: Beginning work on SLC16A1... {November 18, 2007 11:27:49 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:28:30 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Solute carrier family 16, member 1 (monocarboxylic acid transporter 1)
| HGNCid = 10922
| Symbol = SLC16A1
| AltSymbols =; MCT1; FLJ36745; MCT; MGC44475
| OMIM = 600682
| ECnumber =
| Homologene = 20662
| MGIid = 106013
| GeneAtlas_image1 = PBB_GE_SLC16A1_202236_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SLC16A1_202234_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_SLC16A1_202235_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0015130 |text = mevalonate transmembrane transporter activity}} {{GNF_GO|id=GO:0015293 |text = symporter activity}} {{GNF_GO|id=GO:0015355 |text = secondary active monocarboxylate transmembrane transporter activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{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:0015711 |text = organic anion transport}} {{GNF_GO|id=GO:0015728 |text = mevalonate transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6566
| Hs_Ensembl = ENSG00000155380
| Hs_RefseqProtein = NP_003042
| Hs_RefseqmRNA = NM_003051
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 113255992
| Hs_GenLoc_end = 113300498
| Hs_Uniprot = P53985
| Mm_EntrezGene = 20501
| Mm_Ensembl = ENSMUSG00000032902
| Mm_RefseqmRNA = NM_009196
| Mm_RefseqProtein = NP_033222
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 104767729
| Mm_GenLoc_end = 104787523
| Mm_Uniprot = Q3TIU1
}}
}}
'''Solute carrier family 16, member 1 (monocarboxylic acid transporter 1)''', also known as '''SLC16A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC16A1 solute carrier family 16, member 1 (monocarboxylic acid transporter 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6566| 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=Bonen A |title=The expression of lactate transporters (MCT1 and MCT4) in heart and muscle. |journal=Eur. J. Appl. Physiol. |volume=86 |issue= 1 |pages= 6-11 |year= 2002 |pmid= 11820324 |doi= }}
*{{cite journal | author=Halestrap AP, Meredith D |title=The SLC16 gene family-from monocarboxylate transporters (MCTs) to aromatic amino acid transporters and beyond. |journal=Pflugers Arch. |volume=447 |issue= 5 |pages= 619-28 |year= 2004 |pmid= 12739169 |doi= 10.1007/s00424-003-1067-2 }}
*{{cite journal | author=Kim CM, Goldstein JL, Brown MS |title=cDNA cloning of MEV, a mutant protein that facilitates cellular uptake of mevalonate, and identification of the point mutation responsible for its gain of function. |journal=J. Biol. Chem. |volume=267 |issue= 32 |pages= 23113-21 |year= 1992 |pmid= 1429658 |doi= }}
*{{cite journal | author=Garcia CK, Li X, Luna J, Francke U |title=cDNA cloning of the human monocarboxylate transporter 1 and chromosomal localization of the SLC16A1 locus to 1p13.2-p12. |journal=Genomics |volume=23 |issue= 2 |pages= 500-3 |year= 1995 |pmid= 7835905 |doi= 10.1006/geno.1994.1532 }}
*{{cite journal | author=Garcia CK, Goldstein JL, Pathak RK, ''et al.'' |title=Molecular characterization of a membrane transporter for lactate, pyruvate, and other monocarboxylates: implications for the Cori cycle. |journal=Cell |volume=76 |issue= 5 |pages= 865-73 |year= 1994 |pmid= 8124722 |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=Ritzhaupt A, Wood IS, Ellis A, ''et al.'' |title=Identification and characterization of a monocarboxylate transporter (MCT1) in pig and human colon: its potential to transport L-lactate as well as butyrate. |journal=J. Physiol. (Lond.) |volume=513 ( Pt 3) |issue= |pages= 719-32 |year= 1999 |pmid= 9824713 |doi= }}
*{{cite journal | author=Rahman B, Schneider HP, Bröer A, ''et al.'' |title=Helix 8 and helix 10 are involved in substrate recognition in the rat monocarboxylate transporter MCT1. |journal=Biochemistry |volume=38 |issue= 35 |pages= 11577-84 |year= 1999 |pmid= 10471310 |doi= 10.1021/bi990973f }}
*{{cite journal | author=Brooks GA, Brown MA, Butz CE, ''et al.'' |title=Cardiac and skeletal muscle mitochondria have a monocarboxylate transporter MCT1. |journal=J. Appl. Physiol. |volume=87 |issue= 5 |pages= 1713-8 |year= 1999 |pmid= 10562613 |doi= }}
*{{cite journal | author=Merezhinskaya N, Fishbein WN, Davis JI, Foellmer JW |title=Mutations in MCT1 cDNA in patients with symptomatic deficiency in lactate transport. |journal=Muscle Nerve |volume=23 |issue= 1 |pages= 90-7 |year= 2000 |pmid= 10590411 |doi= }}
*{{cite journal | author=Kirk P, Wilson MC, Heddle C, ''et al.'' |title=CD147 is tightly associated with lactate transporters MCT1 and MCT4 and facilitates their cell surface expression. |journal=EMBO J. |volume=19 |issue= 15 |pages= 3896-904 |year= 2000 |pmid= 10921872 |doi= 10.1093/emboj/19.15.3896 }}
*{{cite journal | author=Cuff MA, Lambert DW, Shirazi-Beechey SP |title=Substrate-induced regulation of the human colonic monocarboxylate transporter, MCT1. |journal=J. Physiol. (Lond.) |volume=539 |issue= Pt 2 |pages= 361-71 |year= 2002 |pmid= 11882670 |doi= }}
*{{cite journal | author=Cuff MA, Shirazi-Beechey SP |title=The human monocarboxylate transporter, MCT1: genomic organization and promoter analysis. |journal=Biochem. Biophys. Res. Commun. |volume=292 |issue= 4 |pages= 1048-56 |year= 2002 |pmid= 11944921 |doi= 10.1006/bbrc.2002.6763 }}
*{{cite journal | author=Lambert DW, Wood IS, Ellis A, Shirazi-Beechey SP |title=Molecular changes in the expression of human colonic nutrient transporters during the transition from normality to malignancy. |journal=Br. J. Cancer |volume=86 |issue= 8 |pages= 1262-9 |year= 2002 |pmid= 11953883 |doi= 10.1038/sj.bjc.6600264 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Zhang GZ, Huang GJ, Li WL, ''et al.'' |title=[Effect of co-inhibition of MCT1 gene and NHE1 gene on proliferation and growth of human lung adenocarcinoma cells] |journal=Ai Zheng |volume=21 |issue= 7 |pages= 719-23 |year= 2002 |pmid= 12479094 |doi= }}
*{{cite journal | author=Philp NJ, Wang D, Yoon H, Hjelmeland LM |title=Polarized expression of monocarboxylate transporters in human retinal pigment epithelium and ARPE-19 cells. |journal=Invest. Ophthalmol. Vis. Sci. |volume=44 |issue= 4 |pages= 1716-21 |year= 2003 |pmid= 12657613 |doi= }}
*{{cite journal | author=Asada K, Miyamoto K, Fukutomi T, ''et al.'' |title=Reduced expression of GNA11 and silencing of MCT1 in human breast cancers. |journal=Oncology |volume=64 |issue= 4 |pages= 380-8 |year= 2003 |pmid= 12759536 |doi= 10.1159/000070297 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC1A3... {November 18, 2007 11:26:39 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:27:11 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Solute carrier family 1 (glial high affinity glutamate transporter), member 3
| HGNCid = 10941
| Symbol = SLC1A3
| AltSymbols =; EA6; EAAT1; FLJ25094; GLAST; GLAST1
| OMIM = 600111
| ECnumber =
| Homologene = 20882
| MGIid = 99917
| GeneAtlas_image1 = PBB_GE_SLC1A3_202800_at_tn.png
| Function = {{GNF_GO|id=GO:0005313 |text = L-glutamate transmembrane transporter activity}} {{GNF_GO|id=GO:0015293 |text = symporter activity}} {{GNF_GO|id=GO:0017153 |text = sodium:dicarboxylate symporter activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042995 |text = cell projection}} {{GNF_GO|id=GO:0043025 |text = cell soma}}
| Process = {{GNF_GO|id=GO:0001504 |text = neurotransmitter uptake}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006835 |text = dicarboxylic acid transport}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0015813 |text = glutamate transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6507
| Hs_Ensembl = ENSG00000079215
| Hs_RefseqProtein = NP_004163
| Hs_RefseqmRNA = NM_004172
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 36642446
| Hs_GenLoc_end = 36724193
| Hs_Uniprot = P43003
| Mm_EntrezGene = 20512
| Mm_Ensembl = ENSMUSG00000005360
| Mm_RefseqmRNA = NM_148938
| Mm_RefseqProtein = NP_683740
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 8581335
| Mm_GenLoc_end = 8657945
| Mm_Uniprot = Q543U3
}}
}}
'''Solute carrier family 1 (glial high affinity glutamate transporter), member 3''', also known as '''SLC1A3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC1A3 solute carrier family 1 (glial high affinity glutamate transporter), member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6507| 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 = Glutamate and aspartate are excitatory neurotransmitters that have been implicated in a number of pathologic states of the nervous system. Accumulation of extracellular excitatory amino acids can be cytotoxic and may also lower the seizure threshold in epilepsy. EAAT1 (SLC1A3) is a member of a family of high-affinity sodium-dependent transporter molecules that regulate neurotransmitter concentrations at the excitatory glutamatergic synapses of the mammalian central nervous system (Kirschner et al., 1994).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: SLC1A3 solute carrier family 1 (glial high affinity glutamate transporter), member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6507| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Arriza JL, Fairman WA, Wadiche JI, ''et al.'' |title=Functional comparisons of three glutamate transporter subtypes cloned from human motor cortex. |journal=J. Neurosci. |volume=14 |issue= 9 |pages= 5559-69 |year= 1994 |pmid= 7521911 |doi= }}
*{{cite journal | author=Nomura N, Nagase T, Miyajima N, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. |journal=DNA Res. |volume=1 |issue= 5 |pages= 223-9 |year= 1995 |pmid= 7584044 |doi= }}
*{{cite journal | author=Takai S, Yamada K, Kawakami H, ''et al.'' |title=Localization of the gene (SLC1A3) encoding human glutamate transporter (GluT-1) to 5p13 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=69 |issue= 3-4 |pages= 209-10 |year= 1995 |pmid= 7698014 |doi= }}
*{{cite journal | author=Shashidharan P, Huntley GW, Meyer T, ''et al.'' |title=Neuron-specific human glutamate transporter: molecular cloning, characterization and expression in human brain. |journal=Brain Res. |volume=662 |issue= 1-2 |pages= 245-50 |year= 1995 |pmid= 7859077 |doi= }}
*{{cite journal | author=Kirschner MA, Arriza JL, Copeland NG, ''et al.'' |title=The mouse and human excitatory amino acid transporter gene (EAAT1) maps to mouse chromosome 15 and a region of syntenic homology on human chromosome 5. |journal=Genomics |volume=22 |issue= 3 |pages= 631-3 |year= 1995 |pmid= 8001975 |doi= 10.1006/geno.1994.1437 }}
*{{cite journal | author=Kawakami H, Tanaka K, Nakayama T, ''et al.'' |title=Cloning and expression of a human glutamate transporter. |journal=Biochem. Biophys. Res. Commun. |volume=199 |issue= 1 |pages= 171-6 |year= 1994 |pmid= 8123008 |doi= 10.1006/bbrc.1994.1210 }}
*{{cite journal | author=Shashidharan P, Plaitakis A |title=Cloning and characterization of a glutamate transporter cDNA from human cerebellum. |journal=Biochim. Biophys. Acta |volume=1216 |issue= 1 |pages= 161-4 |year= 1993 |pmid= 8218410 |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=Stoffel W, Sasse J, Düker M, ''et al.'' |title=Human high affinity, Na(+)-dependent L-glutamate/L-aspartate transporter GLAST-1 (EAAT-1): gene structure and localization to chromosome 5p11-p12. |journal=FEBS Lett. |volume=386 |issue= 2-3 |pages= 189-93 |year= 1996 |pmid= 8647279 |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=Dunlop J, Lou Z, McIlvain HB |title=Properties of excitatory amino acid transport in the human U373 astrocytoma cell line. |journal=Brain Res. |volume=839 |issue= 2 |pages= 235-42 |year= 1999 |pmid= 10519046 |doi= }}
*{{cite journal | author=Koch HP, Kavanaugh MP, Esslinger CS, ''et al.'' |title=Differentiation of substrate and nonsubstrate inhibitors of the high-affinity, sodium-dependent glutamate transporters. |journal=Mol. Pharmacol. |volume=56 |issue= 6 |pages= 1095-104 |year= 1999 |pmid= 10570036 |doi= }}
*{{cite journal | author=Ye ZC, Rothstein JD, Sontheimer H |title=Compromised glutamate transport in human glioma cells: reduction-mislocalization of sodium-dependent glutamate transporters and enhanced activity of cystine-glutamate exchange. |journal=J. Neurosci. |volume=19 |issue= 24 |pages= 10767-77 |year= 2000 |pmid= 10594060 |doi= }}
*{{cite journal | author=Szymocha R, Akaoka H, Dutuit M, ''et al.'' |title=Human T-cell lymphotropic virus type 1-infected T lymphocytes impair catabolism and uptake of glutamate by astrocytes via Tax-1 and tumor necrosis factor alpha. |journal=J. Virol. |volume=74 |issue= 14 |pages= 6433-41 |year= 2000 |pmid= 10864655 |doi= }}
*{{cite journal | author=Mordrelle A, Jullian E, Costa C, ''et al.'' |title=EAAT1 is involved in transport of L-glutamate during differentiation of the Caco-2 cell line. |journal=Am. J. Physiol. Gastrointest. Liver Physiol. |volume=279 |issue= 2 |pages= G366-73 |year= 2000 |pmid= 10915646 |doi= }}
*{{cite journal | author=Seal RP, Shigeri Y, Eliasof S, ''et al.'' |title=Sulfhydryl modification of V449C in the glutamate transporter EAAT1 abolishes substrate transport but not the substrate-gated anion conductance. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 26 |pages= 15324-9 |year= 2002 |pmid= 11752470 |doi= 10.1073/pnas.011400198 }}
*{{cite journal | author=Palmada M, Kinne-Saffran E, Centelles JJ, Kinne RK |title=Benzodiazepines differently modulate EAAT1/GLAST and EAAT2/GLT1 glutamate transporters expressed in CHO cells. |journal=Neurochem. Int. |volume=40 |issue= 4 |pages= 321-6 |year= 2002 |pmid= 11792462 |doi= }}
*{{cite journal | author=Scott HL, Pow DV, Tannenberg AE, Dodd PR |title=Aberrant expression of the glutamate transporter excitatory amino acid transporter 1 (EAAT1) in Alzheimer's disease. |journal=J. Neurosci. |volume=22 |issue= 3 |pages= RC206 |year= 2002 |pmid= 11826152 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Vallat-Decouvelaere AV, Chrétien F, Gras G, ''et al.'' |title=Expression of excitatory amino acid transporter-1 in brain macrophages and microglia of HIV-infected patients. A neuroprotective role for activated microglia? |journal=J. Neuropathol. Exp. Neurol. |volume=62 |issue= 5 |pages= 475-85 |year= 2003 |pmid= 12769187 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SMC1A... {November 18, 2007 11:33:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:33:55 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Structural maintenance of chromosomes 1A
| HGNCid = 11111
| Symbol = SMC1A
| AltSymbols =; DKFZp686L19178; DXS423E; KIAA0178; MGC138332; SB1.8; SMC1; SMC1L1; SMC1alpha; SMCB
| OMIM = 300040
| ECnumber =
| Homologene = 4597
| MGIid = 1344345
| GeneAtlas_image1 = PBB_GE_SMC1A_201589_at_tn.png
| GeneAtlas_image2 = PBB_GE_SMC1A_217555_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003682 |text = chromatin binding}} {{GNF_GO|id=GO:0003777 |text = microtubule motor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0000776 |text = kinetochore}} {{GNF_GO|id=GO:0000794 |text = condensed nuclear chromosome}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}} {{GNF_GO|id=GO:0008280 |text = cohesin core heterodimer}}
| Process = {{GNF_GO|id=GO:0000075 |text = cell cycle checkpoint}} {{GNF_GO|id=GO:0006259 |text = DNA metabolic process}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007052 |text = mitotic spindle organization and biogenesis}} {{GNF_GO|id=GO:0007059 |text = chromosome segregation}} {{GNF_GO|id=GO:0007064 |text = mitotic sister chromatid cohesion}} {{GNF_GO|id=GO:0007126 |text = meiosis}} {{GNF_GO|id=GO:0009314 |text = response to radiation}} {{GNF_GO|id=GO:0042770 |text = DNA damage response, signal transduction}} {{GNF_GO|id=GO:0051276 |text = chromosome organization and biogenesis}} {{GNF_GO|id=GO:0051301 |text = cell division}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8243
| Hs_Ensembl = ENSG00000072501
| Hs_RefseqProtein = NP_006297
| Hs_RefseqmRNA = NM_006306
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 53417795
| Hs_GenLoc_end = 53466343
| Hs_Uniprot = Q14683
| Mm_EntrezGene = 24061
| Mm_Ensembl = ENSMUSG00000041133
| Mm_RefseqmRNA = NM_019710
| Mm_RefseqProtein = NP_062684
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 147357144
| Mm_GenLoc_end = 147402683
| Mm_Uniprot = A0JLM6
}}
}}
'''Structural maintenance of chromosomes 1A''', also known as '''SMC1A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SMC1A structural maintenance of chromosomes 1A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8243| 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 = Proper cohesion of sister chromatids is a prerequisite for the correct segregation of chromosomes during cell division. The cohesin multiprotein complex is required for sister chromatid cohesion. This complex is composed partly of two structural maintenance of chromosomes (SMC) proteins, SMC3 and either SMC1L2 or the protein encoded by this gene. Most of the cohesin complexes dissociate from the chromosomes before mitosis, although those complexes at the kinetochore remain. Therefore, the encoded protein is thought to be an important part of functional kinetochores. In addition, this protein interacts with BRCA1 and is phosphorylated by ATM, indicating a potential role for this protein in DNA repair. This gene, which belongs to the SMC gene family, is located in an area of the X-chromosome that escapes X inactivation.<ref name="entrez">{{cite web | title = Entrez Gene: SMC1A structural maintenance of chromosomes 1A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8243| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Nakajima D, Okazaki N, Yamakawa H, ''et al.'' |title=Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. |journal=DNA Res. |volume=9 |issue= 3 |pages= 99-106 |year= 2003 |pmid= 12168954 |doi= }}
*{{cite journal | author=Rocques PJ, Clark J, Ball S, ''et al.'' |title=The human SB1.8 gene (DXS423E) encodes a putative chromosome segregation protein conserved in lower eukaryotes and prokaryotes. |journal=Hum. Mol. Genet. |volume=4 |issue= 2 |pages= 243-9 |year= 1995 |pmid= 7757074 |doi= }}
*{{cite journal | author=Brown CJ, Miller AP, Carrel L, ''et al.'' |title=The DXS423E gene in Xp11.21 escapes X chromosome inactivation. |journal=Hum. Mol. Genet. |volume=4 |issue= 2 |pages= 251-5 |year= 1995 |pmid= 7757075 |doi= }}
*{{cite journal | author=Matoba R, Okubo K, Hori N, ''et al.'' |title=The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression. |journal=Gene |volume=146 |issue= 2 |pages= 199-207 |year= 1994 |pmid= 8076819 |doi= }}
*{{cite journal | author=Nagase T, Seki N, Ishikawa K, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1. |journal=DNA Res. |volume=3 |issue= 1 |pages= 17-24 |year= 1996 |pmid= 8724849 |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=Schmiesing JA, Ball AR, Gregson HC, ''et al.'' |title=Identification of two distinct human SMC protein complexes involved in mitotic chromosome dynamics. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 22 |pages= 12906-11 |year= 1998 |pmid= 9789013 |doi= }}
*{{cite journal | author=Zheng L, Chen Y, Lee WH |title=Hec1p, an evolutionarily conserved coiled-coil protein, modulates chromosome segregation through interaction with SMC proteins. |journal=Mol. Cell. Biol. |volume=19 |issue= 8 |pages= 5417-28 |year= 1999 |pmid= 10409732 |doi= }}
*{{cite journal | author=Losada A, Yokochi T, Kobayashi R, Hirano T |title=Identification and characterization of SA/Scc3p subunits in the Xenopus and human cohesin complexes. |journal=J. Cell Biol. |volume=150 |issue= 3 |pages= 405-16 |year= 2000 |pmid= 10931856 |doi= }}
*{{cite journal | author=Sumara I, Vorlaufer E, Gieffers C, ''et al.'' |title=Characterization of vertebrate cohesin complexes and their regulation in prophase. |journal=J. Cell Biol. |volume=151 |issue= 4 |pages= 749-62 |year= 2000 |pmid= 11076961 |doi= }}
*{{cite journal | author=Revenkova E, Eijpe M, Heyting C, ''et al.'' |title=Novel meiosis-specific isoform of mammalian SMC1. |journal=Mol. Cell. Biol. |volume=21 |issue= 20 |pages= 6984-98 |year= 2001 |pmid= 11564881 |doi= 10.1128/MCB.21.20.6984-6998.2001 }}
*{{cite journal | author=Gregson HC, Schmiesing JA, Kim JS, ''et al.'' |title=A potential role for human cohesin in mitotic spindle aster assembly. |journal=J. Biol. Chem. |volume=276 |issue= 50 |pages= 47575-82 |year= 2002 |pmid= 11590136 |doi= 10.1074/jbc.M103364200 }}
*{{cite journal | author=Andersen JS, Lyon CE, Fox AH, ''et al.'' |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1-11 |year= 2002 |pmid= 11790298 |doi= }}
*{{cite journal | author=Kim ST, Xu B, Kastan MB |title=Involvement of the cohesin protein, Smc1, in Atm-dependent and independent responses to DNA damage. |journal=Genes Dev. |volume=16 |issue= 5 |pages= 560-70 |year= 2002 |pmid= 11877376 |doi= 10.1101/gad.970602 }}
*{{cite journal | author=Yazdi PT, Wang Y, Zhao S, ''et al.'' |title=SMC1 is a downstream effector in the ATM/NBS1 branch of the human S-phase checkpoint. |journal=Genes Dev. |volume=16 |issue= 5 |pages= 571-82 |year= 2002 |pmid= 11877377 |doi= 10.1101/gad.970702 }}
*{{cite journal | author=Gregson HC, Van Hooser AA, Ball AR, ''et al.'' |title=Localization of human SMC1 protein at kinetochores. |journal=Chromosome Res. |volume=10 |issue= 4 |pages= 267-77 |year= 2003 |pmid= 12199140 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Stewart GS, Wang B, Bignell CR, ''et al.'' |title=MDC1 is a mediator of the mammalian DNA damage checkpoint. |journal=Nature |volume=421 |issue= 6926 |pages= 961-6 |year= 2003 |pmid= 12607005 |doi= 10.1038/nature01446 }}
*{{cite journal | author=Wang Y, Qin J |title=MSH2 and ATR form a signaling module and regulate two branches of the damage response to DNA methylation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 26 |pages= 15387-92 |year= 2004 |pmid= 14657349 |doi= 10.1073/pnas.2536810100 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SSRP1... {November 18, 2007 11:28:30 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:28:57 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Structure specific recognition protein 1
| HGNCid = 11327
| Symbol = SSRP1
| AltSymbols =; FACT; FACT80; T160
| OMIM = 604328
| ECnumber =
| Homologene = 2370
| MGIid = 107912
| GeneAtlas_image1 = PBB_GE_SSRP1_200957_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SSRP1_200956_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0000785 |text = chromatin}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}}
| Process = {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6749
| Hs_Ensembl = ENSG00000149136
| Hs_RefseqProtein = NP_003137
| Hs_RefseqmRNA = NM_003146
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 56850036
| Hs_GenLoc_end = 56859927
| Hs_Uniprot = Q08945
| Mm_EntrezGene = 20833
| Mm_Ensembl = ENSMUSG00000027067
| Mm_RefseqmRNA = NM_182990
| Mm_RefseqProtein = NP_892035
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 84838111
| Mm_GenLoc_end = 84847948
| Mm_Uniprot = Q05DR5
}}
}}
'''Structure specific recognition protein 1''', also known as '''SSRP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SSRP1 structure specific recognition protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6749| 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 subunit of a heterodimer that, along with SUPT16H, forms chromatin transcriptional elongation factor FACT. FACT interacts specifically with histones H2A/H2B to effect nucleosome disassembly and transcription elongation. FACT and cisplatin-damaged DNA may be crucial to the anticancer mechanism of cisplatin. This encoded protein contains a high mobility group box which most likely constitutes the structure recognition element for cisplatin-modified DNA. This protein also functions as a co-activator of the transcriptional activator p63.<ref name="entrez">{{cite web | title = Entrez Gene: SSRP1 structure specific recognition protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6749| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bruhn SL, Pil PM, Essigmann JM, ''et al.'' |title=Isolation and characterization of human cDNA clones encoding a high mobility group box protein that recognizes structural distortions to DNA caused by binding of the anticancer agent cisplatin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 6 |pages= 2307-11 |year= 1992 |pmid= 1372440 |doi= }}
*{{cite journal | author=Toney JH, Donahue BA, Kellett PJ, ''et al.'' |title=Isolation of cDNAs encoding a human protein that binds selectively to DNA modified by the anticancer drug cis-diamminedichloroplatinum(II) |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 21 |pages= 8328-32 |year= 1989 |pmid= 2530581 |doi= }}
*{{cite journal | author=Nagulapalli S, Pongubala JM, Atchison ML |title=Multiple proteins physically interact with PU.1. Transcriptional synergy with NF-IL6 beta (C/EBP delta, CRP3). |journal=J. Immunol. |volume=155 |issue= 9 |pages= 4330-8 |year= 1995 |pmid= 7594592 |doi= }}
*{{cite journal | author=Orphanides G, LeRoy G, Chang CH, ''et al.'' |title=FACT, a factor that facilitates transcript elongation through nucleosomes. |journal=Cell |volume=92 |issue= 1 |pages= 105-16 |year= 1998 |pmid= 9489704 |doi= }}
*{{cite journal | author=Dyer MA, Hayes PJ, Baron MH |title=The HMG domain protein SSRP1/PREIIBF is involved in activation of the human embryonic beta-like globin gene. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2617-28 |year= 1998 |pmid= 9566881 |doi= }}
*{{cite journal | author=LeRoy G, Orphanides G, Lane WS, Reinberg D |title=Requirement of RSF and FACT for transcription of chromatin templates in vitro. |journal=Science |volume=282 |issue= 5395 |pages= 1900-4 |year= 1998 |pmid= 9836642 |doi= }}
*{{cite journal | author=Kelley DE, Stokes DG, Perry RP |title=CHD1 interacts with SSRP1 and depends on both its chromodomain and its ATPase/helicase-like domain for proper association with chromatin. |journal=Chromosoma |volume=108 |issue= 1 |pages= 10-25 |year= 1999 |pmid= 10199952 |doi= }}
*{{cite journal | author=Spencer JA, Baron MH, Olson EN |title=Cooperative transcriptional activation by serum response factor and the high mobility group protein SSRP1. |journal=J. Biol. Chem. |volume=274 |issue= 22 |pages= 15686-93 |year= 1999 |pmid= 10336466 |doi= }}
*{{cite journal | author=Orphanides G, Wu WH, Lane WS, ''et al.'' |title=The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins. |journal=Nature |volume=400 |issue= 6741 |pages= 284-8 |year= 1999 |pmid= 10421373 |doi= 10.1038/22350 }}
*{{cite journal | author=Wada T, Orphanides G, Hasegawa J, ''et al.'' |title=FACT relieves DSIF/NELF-mediated inhibition of transcriptional elongation and reveals functional differences between P-TEFb and TFIIH. |journal=Mol. Cell |volume=5 |issue= 6 |pages= 1067-72 |year= 2000 |pmid= 10912001 |doi= }}
*{{cite journal | author=Keller DM, Zeng X, Wang Y, ''et al.'' |title=A DNA damage-induced p53 serine 392 kinase complex contains CK2, hSpt16, and SSRP1. |journal=Mol. Cell |volume=7 |issue= 2 |pages= 283-92 |year= 2001 |pmid= 11239457 |doi= }}
*{{cite journal | author=Yarnell AT, Oh S, Reinberg D, Lippard SJ |title=Interaction of FACT, SSRP1, and the high mobility group (HMG) domain of SSRP1 with DNA damaged by the anticancer drug cisplatin. |journal=J. Biol. Chem. |volume=276 |issue= 28 |pages= 25736-41 |year= 2001 |pmid= 11344167 |doi= 10.1074/jbc.M101208200 }}
*{{cite journal | author=Santoro P, De Andrea M, Migliaretti G, ''et al.'' |title=High prevalence of autoantibodies against the nuclear high mobility group (HMG) protein SSRP1 in sera from patients with systemic lupus erythematosus, but not other rheumatic diseases. |journal=J. Rheumatol. |volume=29 |issue= 1 |pages= 90-3 |year= 2002 |pmid= 11824977 |doi= }}
*{{cite journal | author=Roig J, Mikhailov A, Belham C, Avruch J |title=Nercc1, a mammalian NIMA-family kinase, binds the Ran GTPase and regulates mitotic progression. |journal=Genes Dev. |volume=16 |issue= 13 |pages= 1640-58 |year= 2002 |pmid= 12101123 |doi= 10.1101/gad.972202 }}
*{{cite journal | author=Zeng SX, Dai MS, Keller DM, Lu H |title=SSRP1 functions as a co-activator of the transcriptional activator p63. |journal=EMBO J. |volume=21 |issue= 20 |pages= 5487-97 |year= 2002 |pmid= 12374749 |doi= }}
*{{cite journal | author=Keller DM, Lu H |title=p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 50206-13 |year= 2003 |pmid= 12393879 |doi= 10.1074/jbc.M209820200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Belotserkovskaya R, Oh S, Bondarenko VA, ''et al.'' |title=FACT facilitates transcription-dependent nucleosome alteration. |journal=Science |volume=301 |issue= 5636 |pages= 1090-3 |year= 2003 |pmid= 12934006 |doi= 10.1126/science.1085703 }}
*{{cite journal | author=Li J, Hawkins IC, Harvey CD, ''et al.'' |title=Regulation of alternative splicing by SRrp86 and its interacting proteins. |journal=Mol. Cell. Biol. |volume=23 |issue= 21 |pages= 7437-47 |year= 2003 |pmid= 14559993 |doi= }}
*{{cite journal | author=Tan BC, Lee SC |title=Nek9, a novel FACT-associated protein, modulates interphase progression. |journal=J. Biol. Chem. |volume=279 |issue= 10 |pages= 9321-30 |year= 2004 |pmid= 14660563 |doi= 10.1074/jbc.M311477200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TNNC1... {November 18, 2007 11:29:26 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 11:31:06 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TNNC1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aj4.
| PDB = {{PDB2|1aj4}}, {{PDB2|1ap4}}, {{PDB2|1dtl}}, {{PDB2|1fi5}}, {{PDB2|1ih0}}, {{PDB2|1j1d}}, {{PDB2|1j1e}}, {{PDB2|1la0}}, {{PDB2|1lxf}}, {{PDB2|1mxl}}, {{PDB2|1ozs}}, {{PDB2|1r2u}}, {{PDB2|1r6p}}, {{PDB2|1sbj}}, {{PDB2|1scv}}, {{PDB2|1spy}}, {{PDB2|1wrk}}, {{PDB2|1wrl}}, {{PDB2|2ctn}}, {{PDB2|3ctn}}
| Name = Troponin C type 1 (slow)
| HGNCid = 11943
| Symbol = TNNC1
| AltSymbols =; TNC; TNNC
| OMIM = 191040
| ECnumber =
| Homologene = 55728
| MGIid = 98779
| GeneAtlas_image1 = PBB_GE_TNNC1_209904_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006937 |text = regulation of muscle contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7134
| Hs_Ensembl = ENSG00000114854
| Hs_RefseqProtein = NP_003271
| Hs_RefseqmRNA = NM_003280
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 52460158
| Hs_GenLoc_end = 52463098
| Hs_Uniprot = P63316
| Mm_EntrezGene = 21924
| Mm_Ensembl = ENSMUSG00000021909
| Mm_RefseqmRNA = NM_009393
| Mm_RefseqProtein = NP_033419
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 30037321
| Mm_GenLoc_end = 30040720
| Mm_Uniprot = P19123
}}
}}
'''Troponin C type 1 (slow)''', also known as '''TNNC1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TNNC1 troponin C type 1 (slow)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7134| 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=Gomes AV, Potter JD |title=Cellular and molecular aspects of familial hypertrophic cardiomyopathy caused by mutations in the cardiac troponin I gene. |journal=Mol. Cell. Biochem. |volume=263 |issue= 1-2 |pages= 99-114 |year= 2005 |pmid= 15524171 |doi= }}
*{{cite journal | author=Tomasselli AG, Hui JO, Adams L, ''et al.'' |title=Actin, troponin C, Alzheimer amyloid precursor protein and pro-interleukin 1 beta as substrates of the protease from human immunodeficiency virus. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14548-53 |year= 1991 |pmid= 1907279 |doi= }}
*{{cite journal | author=Schreier T, Kedes L, Gahlmann R |title=Cloning, structural analysis, and expression of the human slow twitch skeletal muscle/cardiac troponin C gene. |journal=J. Biol. Chem. |volume=265 |issue= 34 |pages= 21247-53 |year= 1991 |pmid= 2250022 |doi= }}
*{{cite journal | author=Gahlmann R, Wade R, Gunning P, Kedes L |title=Differential expression of slow and fast skeletal muscle troponin C. Slow skeletal muscle troponin C is expressed in human fibroblasts. |journal=J. Mol. Biol. |volume=201 |issue= 2 |pages= 379-91 |year= 1988 |pmid= 3166492 |doi= }}
*{{cite journal | author=Roher A, Lieska N, Spitz W |title=The amino acid sequence of human cardiac troponin-C. |journal=Muscle Nerve |volume=9 |issue= 1 |pages= 73-7 |year= 1986 |pmid= 3951483 |doi= 10.1002/mus.880090112 }}
*{{cite journal | author=Grand RJ, Levine BA, Perry SV |title=Proton-magnetic-resonance studies on the interaction of rabbit skeletal-muscle troponin I with troponin C and actin. |journal=Biochem. J. |volume=203 |issue= 1 |pages= 61-8 |year= 1982 |pmid= 7103951 |doi= }}
*{{cite journal | author=Thierfelder L, Watkins H, MacRae C, ''et al.'' |title=Alpha-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: a disease of the sarcomere. |journal=Cell |volume=77 |issue= 5 |pages= 701-12 |year= 1994 |pmid= 8205619 |doi= }}
*{{cite journal | author=Jha PK, Leavis PC, Sarkar S |title=Interaction of deletion mutants of troponins I and T: COOH-terminal truncation of troponin T abolishes troponin I binding and reduces Ca2+ sensitivity of the reconstituted regulatory system. |journal=Biochemistry |volume=35 |issue= 51 |pages= 16573-80 |year= 1997 |pmid= 8987992 |doi= 10.1021/bi9622433 }}
*{{cite journal | author=Song WJ, Van Keuren ML, Drabkin HA, ''et al.'' |title=Assignment of the human slow twitch skeletal muscle/cardiac troponin C gene (TNNC1) to human chromosome 3p21.3-->3p14.3 using somatic cell hybrids. |journal=Cytogenet. Cell Genet. |volume=75 |issue= 1 |pages= 36-7 |year= 1997 |pmid= 8995486 |doi= }}
*{{cite journal | author=Takeda S, Kobayashi T, Taniguchi H, ''et al.'' |title=Structural and functional domains of the troponin complex revealed by limited digestion. |journal=Eur. J. Biochem. |volume=246 |issue= 3 |pages= 611-7 |year= 1997 |pmid= 9219516 |doi= }}
*{{cite journal | author=Spyracopoulos L, Li MX, Sia SK, ''et al.'' |title=Calcium-induced structural transition in the regulatory domain of human cardiac troponin C. |journal=Biochemistry |volume=36 |issue= 40 |pages= 12138-46 |year= 1997 |pmid= 9315850 |doi= 10.1021/bi971223d }}
*{{cite journal | author=Keane NE, Quirk PG, Gao Y, ''et al.'' |title=The ordered phosphorylation of cardiac troponin I by the cAMP-dependent protein kinase--structural consequences and functional implications. |journal=Eur. J. Biochem. |volume=248 |issue= 2 |pages= 329-37 |year= 1997 |pmid= 9346285 |doi= }}
*{{cite journal | author=Stefancsik R, Jha PK, Sarkar S |title=Identification and mutagenesis of a highly conserved domain in troponin T responsible for troponin I binding: potential role for coiled coil interaction. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 3 |pages= 957-62 |year= 1998 |pmid= 9448267 |doi= }}
*{{cite journal | author=Vassylyev DG, Takeda S, Wakatsuki S, ''et al.'' |title=Crystal structure of troponin C in complex with troponin I fragment at 2.3-A resolution. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 9 |pages= 4847-52 |year= 1998 |pmid= 9560191 |doi= }}
*{{cite journal | author=Redwood C, Lohmann K, Bing W, ''et al.'' |title=Investigation of a truncated cardiac troponin T that causes familial hypertrophic cardiomyopathy: Ca(2+) regulatory properties of reconstituted thin filaments depend on the ratio of mutant to wild-type protein. |journal=Circ. Res. |volume=86 |issue= 11 |pages= 1146-52 |year= 2000 |pmid= 10850966 |doi= }}
*{{cite journal | author=Hoffmann B, Schmidt-Traub H, Perrot A, ''et al.'' |title=First mutation in cardiac troponin C, L29Q, in a patient with hypertrophic cardiomyopathy. |journal=Hum. Mutat. |volume=17 |issue= 6 |pages= 524 |year= 2001 |pmid= 11385718 |doi= 10.1002/humu.1143 }}
*{{cite journal | author=Schmidtmann A, Lohmann K, Jaquet K |title=The interaction of the bisphosphorylated N-terminal arm of cardiac troponin I-A 31P-NMR study. |journal=FEBS Lett. |volume=513 |issue= 2-3 |pages= 289-93 |year= 2002 |pmid= 11904166 |doi= }}
*{{cite journal | author=Lindhout DA, Li MX, Schieve D, Sykes BD |title=Effects of T142 phosphorylation and mutation R145G on the interaction of the inhibitory region of human cardiac troponin I with the C-domain of human cardiac troponin C. |journal=Biochemistry |volume=41 |issue= 23 |pages= 7267-74 |year= 2002 |pmid= 12044157 |doi= }}
*{{cite journal | author=Wang X, Li MX, Sykes BD |title=Structure of the regulatory N-domain of human cardiac troponin C in complex with human cardiac troponin I147-163 and bepridil. |journal=J. Biol. Chem. |volume=277 |issue= 34 |pages= 31124-33 |year= 2002 |pmid= 12060657 |doi= 10.1074/jbc.M203896200 }}
*{{cite journal | author=Li MX, Saude EJ, Wang X, ''et al.'' |title=Kinetic studies of calcium and cardiac troponin I peptide binding to human cardiac troponin C using NMR spectroscopy. |journal=Eur. Biophys. J. |volume=31 |issue= 4 |pages= 245-56 |year= 2003 |pmid= 12122471 |doi= 10.1007/s00249-002-0227-1 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on USH2A... {November 18, 2007 11:31:06 PM PST}
- REDIRECT: Protein Redirected to: USH2A {November 18, 2007 11:31:27 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 11:31:29 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 11:31:29 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 11:31:29 PM PST}
- UPDATED: Updated protein page: USH2A {November 18, 2007 11:31:35 PM PST}
end log.
