Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 06:24, 19 November 2007 (UTC)
[edit]Proteins without matches (6)
[edit]Proteins with a High Potential Match (8)
[edit]Redirected Proteins (11)
[edit]Manual Inspection (Page not found) (14)
[edit]
Protein Status Grid - Date: 06:24, 19 November 2007 (UTC)
[edit]Vebose Log - Date: 06:24, 19 November 2007 (UTC)
[edit]- INFO: Beginning work on ADIPOR1... {November 18, 2007 10:16:24 PM PST}
- SEARCH REDIRECT: Control Box Found: ADIPOR1 {November 18, 2007 10:17:06 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:17:08 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:17:08 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:17:08 PM PST}
- UPDATED: Updated protein page: ADIPOR1 {November 18, 2007 10:17:16 PM PST}
- INFO: Beginning work on CD99... {November 18, 2007 9:59:59 PM PST}
- SEARCH REDIRECT: Control Box Found: CD99 {November 18, 2007 10:00:30 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:00:32 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:00:32 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:00:32 PM PST}
- UPDATED: Updated protein page: CD99 {November 18, 2007 10:00:41 PM PST}
- INFO: Beginning work on IL21... {November 18, 2007 10:17:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:17:35 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Interleukin 21
| HGNCid = 6005
| Symbol = IL21
| AltSymbols =; IL-21; Za11
| OMIM = 605384
| ECnumber =
| Homologene = 11032
| MGIid = 1890474
| GeneAtlas_image1 = PBB_GE_IL21_221271_at_tn.png
| Function = {{GNF_GO|id=GO:0005134 |text = interleukin-2 receptor binding}}
| Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0042102 |text = positive regulation of T cell proliferation}} {{GNF_GO|id=GO:0045078 |text = positive regulation of interferon-gamma biosynthetic process}} {{GNF_GO|id=GO:0048469 |text = cell maturation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 59067
| Hs_Ensembl = ENSG00000138684
| Hs_RefseqProtein = NP_068575
| Hs_RefseqmRNA = NM_021803
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 123753221
| Hs_GenLoc_end = 123761662
| Hs_Uniprot = Q9HBE4
| Mm_EntrezGene = 60505
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_021782
| Mm_RefseqProtein = NP_068554
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Interleukin 21''', also known as '''IL21''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL21 interleukin 21| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=59067| 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=Sivakumar PV, Foster DC, Clegg CH |title=Interleukin-21 is a T-helper cytokine that regulates humoral immunity and cell-mediated anti-tumour responses. |journal=Immunology |volume=112 |issue= 2 |pages= 177-82 |year= 2004 |pmid= 15147560 |doi= 10.1111/j.1365-2567.2004.01886.x }}
*{{cite journal | author=Leonard WJ, Spolski R |title=Interleukin-21: a modulator of lymphoid proliferation, apoptosis and differentiation. |journal=Nat. Rev. Immunol. |volume=5 |issue= 9 |pages= 688-98 |year= 2005 |pmid= 16138102 |doi= 10.1038/nri1688 }}
*{{cite journal | author=Brandt K, Singh PB, Bulfone-Paus S, Rückert R |title=Interleukin-21: a new modulator of immunity, infection, and cancer. |journal=Cytokine Growth Factor Rev. |volume=18 |issue= 3-4 |pages= 223-32 |year= 2007 |pmid= 17509926 |doi= 10.1016/j.cytogfr.2007.04.003 }}
*{{cite journal | author=Flores I, Casaseca T, Martinez-A C, ''et al.'' |title=Phosphatidic acid generation through interleukin 2 (IL-2)-induced alpha-diacylglycerol kinase activation is an essential step in IL-2-mediated lymphocyte proliferation. |journal=J. Biol. Chem. |volume=271 |issue= 17 |pages= 10334-40 |year= 1996 |pmid= 8626603 |doi= }}
*{{cite journal | author=Parrish-Novak J, Dillon SR, Nelson A, ''et al.'' |title=Interleukin 21 and its receptor are involved in NK cell expansion and regulation of lymphocyte function. |journal=Nature |volume=408 |issue= 6808 |pages= 57-63 |year= 2000 |pmid= 11081504 |doi= 10.1038/35040504 }}
*{{cite journal | author=Vosshenrich CA, Di Santo JP |title=Cytokines: IL-21 joins the gamma(c)-dependent network? |journal=Curr. Biol. |volume=11 |issue= 5 |pages= R175-7 |year= 2001 |pmid= 11267886 |doi= }}
*{{cite journal | author=Asao H, Okuyama C, Kumaki S, ''et al.'' |title=Cutting edge: the common gamma-chain is an indispensable subunit of the IL-21 receptor complex. |journal=J. Immunol. |volume=167 |issue= 1 |pages= 1-5 |year= 2001 |pmid= 11418623 |doi= }}
*{{cite journal | author=Strengell M, Sareneva T, Foster D, ''et al.'' |title=IL-21 up-regulates the expression of genes associated with innate immunity and Th1 response. |journal=J. Immunol. |volume=169 |issue= 7 |pages= 3600-5 |year= 2002 |pmid= 12244150 |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=Zhang JL, Foster D, Sebald W |title=Human IL-21 and IL-4 bind to partially overlapping epitopes of common gamma-chain. |journal=Biochem. Biophys. Res. Commun. |volume=300 |issue= 2 |pages= 291-6 |year= 2003 |pmid= 12504082 |doi= }}
*{{cite journal | author=Strengell M, Matikainen S, Sirén J, ''et al.'' |title=IL-21 in synergy with IL-15 or IL-18 enhances IFN-gamma production in human NK and T cells. |journal=J. Immunol. |volume=170 |issue= 11 |pages= 5464-9 |year= 2003 |pmid= 12759422 |doi= }}
*{{cite journal | author=Brandt K, Bulfone-Paus S, Foster DC, Rückert R |title=Interleukin-21 inhibits dendritic cell activation and maturation. |journal=Blood |volume=102 |issue= 12 |pages= 4090-8 |year= 2004 |pmid= 12893770 |doi= 10.1182/blood-2003-03-0669 }}
*{{cite journal | author=Sivori S, Cantoni C, Parolini S, ''et al.'' |title=IL-21 induces both rapid maturation of human CD34+ cell precursors towards NK cells and acquisition of surface killer Ig-like receptors. |journal=Eur. J. Immunol. |volume=33 |issue= 12 |pages= 3439-47 |year= 2004 |pmid= 14635054 |doi= 10.1002/eji.200324533 }}
*{{cite journal | author=Pène J, Gauchat JF, Lécart S, ''et al.'' |title=Cutting edge: IL-21 is a switch factor for the production of IgG1 and IgG3 by human B cells. |journal=J. Immunol. |volume=172 |issue= 9 |pages= 5154-7 |year= 2004 |pmid= 15100251 |doi= }}
*{{cite journal | author=Strengell M, Julkunen I, Matikainen S |title=IFN-alpha regulates IL-21 and IL-21R expression in human NK and T cells. |journal=J. Leukoc. Biol. |volume=76 |issue= 2 |pages= 416-22 |year= 2004 |pmid= 15178704 |doi= 10.1189/jlb.1003488 }}
*{{cite journal | author=Zhang SQ, Chen B, Luo X, Xu CZ |title=[Cloning and expression of human interleukin-21 cDNA in E.coli] |journal=Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi |volume=20 |issue= 4 |pages= 406-9 |year= 2005 |pmid= 15207081 |doi= }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal | author=Ozaki K, Spolski R, Ettinger R, ''et al.'' |title=Regulation of B cell differentiation and plasma cell generation by IL-21, a novel inducer of Blimp-1 and Bcl-6. |journal=J. Immunol. |volume=173 |issue= 9 |pages= 5361-71 |year= 2004 |pmid= 15494482 |doi= }}
*{{cite journal | author=Mehta DS, Wurster AL, Weinmann AS, Grusby MJ |title=NFATc2 and T-bet contribute to T-helper-cell-subset-specific regulation of IL-21 expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=102 |issue= 6 |pages= 2016-21 |year= 2005 |pmid= 15684054 |doi= 10.1073/pnas.0409512102 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LIG4... {November 18, 2007 9:56:13 PM PST}
- SEARCH REDIRECT: Control Box Found: LIG4 {November 18, 2007 9:56:58 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:57:00 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:57:00 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:57:00 PM PST}
- UPDATED: Updated protein page: LIG4 {November 18, 2007 9:57:06 PM PST}
- INFO: Beginning work on LNPEP... {November 18, 2007 9:57:06 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:57:38 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 = Leucyl/cystinyl aminopeptidase
| HGNCid = 6656
| Symbol = LNPEP
| AltSymbols =; PLAP; CAP; IRAP; P-LAP
| OMIM = 151300
| ECnumber =
| Homologene = 21148
| MGIid = 2387123
| Function = {{GNF_GO|id=GO:0004177 |text = aminopeptidase activity}} {{GNF_GO|id=GO:0004179 |text = membrane alanyl aminopeptidase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007565 |text = female pregnancy}} {{GNF_GO|id=GO:0030163 |text = protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4012
| Hs_Ensembl = ENSG00000113441
| Hs_RefseqProtein = NP_005566
| Hs_RefseqmRNA = NM_005575
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 96296924
| Hs_GenLoc_end = 96398975
| Hs_Uniprot = Q9UIQ6
| Mm_EntrezGene = 240028
| Mm_Ensembl = ENSMUSG00000023845
| Mm_RefseqmRNA = NM_172827
| Mm_RefseqProtein = NP_766415
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 17232341
| Mm_GenLoc_end = 17329107
| Mm_Uniprot =
}}
}}
'''Leucyl/cystinyl aminopeptidase''', also known as '''LNPEP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LNPEP leucyl/cystinyl aminopeptidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4012| 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 zinc-dependent aminopeptidase that cleaves vasopressin, oxytocin, lys-bradykinin, met-enkephalin, dynorphin A and other peptide hormones. The protein can be secreted in maternal serum, reside in intracellular vesicles with the insulin-responsive glucose transporter GLUT4, or form a type II integral membrane glycoprotein. The protein catalyzes the final step in the conversion of angiotensinogen to angiotensin IV (AT4) and is also a receptor for AT4. Alternative splicing results in multiple transcript variants encoding different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: LNPEP leucyl/cystinyl aminopeptidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4012| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Albiston AL, Mustafa T, McDowall SG, ''et al.'' |title=AT4 receptor is insulin-regulated membrane aminopeptidase: potential mechanisms of memory enhancement. |journal=Trends Endocrinol. Metab. |volume=14 |issue= 2 |pages= 72-7 |year= 2003 |pmid= 12591177 |doi= }}
*{{cite journal | author=Keller SR |title=The insulin-regulated aminopeptidase: a companion and regulator of GLUT4. |journal=Front. Biosci. |volume=8 |issue= |pages= s410-20 |year= 2004 |pmid= 12700100 |doi= }}
*{{cite journal | author=Keller SR |title=Role of the insulin-regulated aminopeptidase IRAP in insulin action and diabetes. |journal=Biol. Pharm. Bull. |volume=27 |issue= 6 |pages= 761-4 |year= 2005 |pmid= 15187412 |doi= }}
*{{cite journal | author=Nomura S, Ito T, Yamamoto E, ''et al.'' |title=Gene regulation and physiological function of placental leucine aminopeptidase/oxytocinase during pregnancy. |journal=Biochim. Biophys. Acta |volume=1751 |issue= 1 |pages= 19-25 |year= 2005 |pmid= 15894523 |doi= 10.1016/j.bbapap.2005.04.006 }}
*{{cite journal | author=Tsujimoto M, Hattori A |title=The oxytocinase subfamily of M1 aminopeptidases. |journal=Biochim. Biophys. Acta |volume=1751 |issue= 1 |pages= 9-18 |year= 2005 |pmid= 16054015 |doi= 10.1016/j.bbapap.2004.09.011 }}
*{{cite journal | author=Mizutani S, Shibata K, Kikkawa F, ''et al.'' |title=Essential role of placental leucine aminopeptidase in gynecologic malignancy. |journal=Expert Opin. Ther. Targets |volume=11 |issue= 4 |pages= 453-61 |year= 2007 |pmid= 17373876 |doi= 10.1517/14728222.11.4.453 }}
*{{cite journal | author=Tsujimoto M, Mizutani S, Adachi H, ''et al.'' |title=Identification of human placental leucine aminopeptidase as oxytocinase. |journal=Arch. Biochem. Biophys. |volume=292 |issue= 2 |pages= 388-92 |year= 1992 |pmid= 1731608 |doi= }}
*{{cite journal | author=Mizutani S, Akiyama H, Kurauchi O, ''et al.'' |title=In vitro degradation of angiotensin II (A-II) by human placental subcellular fractions, pregnancy sera and purified placental aminopeptidases. |journal=Acta Endocrinol. |volume=110 |issue= 1 |pages= 135-9 |year= 1985 |pmid= 3898693 |doi= }}
*{{cite journal | author=Beckman L, Björling G, Christodoulou C |title=Pregnancy enzymes and placental polymorphism. II. Leucine aminopeptidase. |journal=Acta genetica et statistica medica |volume=16 |issue= 2 |pages= 122-31 |year= 1966 |pmid= 5953194 |doi= }}
*{{cite journal | author=Rogi T, Tsujimoto M, Nakazato H, ''et al.'' |title=Human placental leucine aminopeptidase/oxytocinase. A new member of type II membrane-spanning zinc metallopeptidase family. |journal=J. Biol. Chem. |volume=271 |issue= 1 |pages= 56-61 |year= 1996 |pmid= 8550619 |doi= }}
*{{cite journal | author=Itoh C, Watanabe M, Nagamatsu A, ''et al.'' |title=Two molecular species of oxytocinase (L-cystine aminopeptidase) in human placenta: purification and characterization. |journal=Biol. Pharm. Bull. |volume=20 |issue= 1 |pages= 20-4 |year= 1997 |pmid= 9013800 |doi= }}
*{{cite journal | author=Laustsen PG, Rasmussen TE, Petersen K, ''et al.'' |title=The complete amino acid sequence of human placental oxytocinase. |journal=Biochim. Biophys. Acta |volume=1352 |issue= 1 |pages= 1-7 |year= 1997 |pmid= 9177475 |doi= }}
*{{cite journal | author=Nagasaka T, Nomura S, Okamura M, ''et al.'' |title=Immunohistochemical localization of placental leucine aminopeptidase/oxytocinase in normal human placental, fetal and adult tissues. |journal=Reprod. Fertil. Dev. |volume=9 |issue= 8 |pages= 747-53 |year= 1998 |pmid= 9733056 |doi= }}
*{{cite journal | author=Horio J, Nomura S, Okada M, ''et al.'' |title=Structural organization of the 5'-end and chromosomal assignment of human placental leucine aminopeptidase/insulin-regulated membrane aminopeptidase gene. |journal=Biochem. Biophys. Res. Commun. |volume=262 |issue= 1 |pages= 269-74 |year= 1999 |pmid= 10448104 |doi= 10.1006/bbrc.1999.1184 }}
*{{cite journal | author=Rasmussen TE, Pedraza-Díaz S, Hardré R, ''et al.'' |title=Structure of the human oxytocinase/insulin-regulated aminopeptidase gene and localization to chromosome 5q21. |journal=Eur. J. Biochem. |volume=267 |issue= 8 |pages= 2297-306 |year= 2000 |pmid= 10759854 |doi= }}
*{{cite journal | author=Nakanishi Y, Nomura S, Okada M, ''et al.'' |title=Immunoaffinity purification and characterization of native placental leucine aminopeptidase/oxytocinase from human placenta. |journal=Placenta |volume=21 |issue= 7 |pages= 628-34 |year= 2001 |pmid= 10985965 |doi= 10.1053/plac.2000.0564 }}
*{{cite journal | author=Chi NW, Lodish HF |title=Tankyrase is a golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles. |journal=J. Biol. Chem. |volume=275 |issue= 49 |pages= 38437-44 |year= 2001 |pmid= 10988299 |doi= 10.1074/jbc.M007635200 }}
*{{cite journal | author=Matsumoto H, Nagasaka T, Hattori A, ''et al.'' |title=Expression of placental leucine aminopeptidase/oxytocinase in neuronal cells and its action on neuronal peptides. |journal=Eur. J. Biochem. |volume=268 |issue= 11 |pages= 3259-66 |year= 2001 |pmid= 11389728 |doi= }}
*{{cite journal | author=Iwase A, Nomura S, Mizutani S |title=Characterization of a secretase activity for placental leucine aminopeptidase. |journal=Arch. Biochem. Biophys. |volume=393 |issue= 1 |pages= 163-9 |year= 2001 |pmid= 11516173 |doi= 10.1006/abbi.2001.2489 }}
*{{cite journal | author=Ito T, Nomura S, Okada M, ''et al.'' |title=Transcriptional regulation of human placental leucine aminopeptidase/oxytocinase gene. |journal=Mol. Hum. Reprod. |volume=7 |issue= 9 |pages= 887-94 |year= 2001 |pmid= 11517297 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LTBR... {November 18, 2007 9:57:38 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:58:24 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Lymphotoxin beta receptor (TNFR superfamily, member 3)
| HGNCid = 6718
| Symbol = LTBR
| AltSymbols =; CD18; D12S370; LT-BETA-R; TNF-R-III; TNFCR; TNFR-RP; TNFR2-RP; TNFRSF3
| OMIM = 600979
| ECnumber =
| Homologene = 1753
| MGIid = 104875
| GeneAtlas_image1 = PBB_GE_LTBR_203005_at_tn.png
| Function = {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4055
| Hs_Ensembl = ENSG00000111321
| Hs_RefseqProtein = NP_002333
| Hs_RefseqmRNA = NM_002342
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 6363595
| Hs_GenLoc_end = 6370994
| Hs_Uniprot = P36941
| Mm_EntrezGene = 17000
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_982227
| Mm_RefseqProtein = XP_987321
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Lymphotoxin beta receptor (TNFR superfamily, member 3)''', also known as '''LTBR''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LTBR lymphotoxin beta receptor (TNFR superfamily, member 3)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4055| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the tumor necrosis factor (TNF) family of receptors. It is expressed on the surface of most cell types, including cells of epithelial and myeloid lineages, but not on T and B lymphocytes. The protein specifically binds the lymphotoxin membrane form (a complex of lymphotoxin-alpha and lymphtoxin-beta). The encoded protein and its ligand play a role in the development and organization of lymphoid tissue and tranformed cells. Activation of the encoded protein can trigger apoptosis.<ref name="entrez">{{cite web | title = Entrez Gene: LTBR lymphotoxin beta receptor (TNFR superfamily, member 3)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4055| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Elewaut D, Ware CF |title=The unconventional role of LT alpha beta in T cell differentiation. |journal=Trends Immunol. |volume=28 |issue= 4 |pages= 169-75 |year= 2007 |pmid= 17336158 |doi= 10.1016/j.it.2007.02.005 }}
*{{cite journal | author=Browning JL, Ngam-ek A, Lawton P, ''et al.'' |title=Lymphotoxin beta, a novel member of the TNF family that forms a heteromeric complex with lymphotoxin on the cell surface. |journal=Cell |volume=72 |issue= 6 |pages= 847-56 |year= 1993 |pmid= 7916655 |doi= }}
*{{cite journal | author=Crowe PD, VanArsdale TL, Walter BN, ''et al.'' |title=A lymphotoxin-beta-specific receptor. |journal=Science |volume=264 |issue= 5159 |pages= 707-10 |year= 1994 |pmid= 8171323 |doi= }}
*{{cite journal | author=Baens M, Chaffanet M, Cassiman JJ, ''et al.'' |title=Construction and evaluation of a hncDNA library of human 12p transcribed sequences derived from a somatic cell hybrid. |journal=Genomics |volume=16 |issue= 1 |pages= 214-8 |year= 1993 |pmid= 8486360 |doi= 10.1006/geno.1993.1161 }}
*{{cite journal | author=Baens M, Aerssens J, van Zand K, ''et al.'' |title=Isolation and regional assignment of human chromosome 12p cDNAs. |journal=Genomics |volume=29 |issue= 1 |pages= 44-52 |year= 1996 |pmid= 8530100 |doi= 10.1006/geno.1995.1213 }}
*{{cite journal | author=Wang X, Bornslaeger EA, Haub O, ''et al.'' |title=A candidate gene for the amnionless gastrulation stage mouse mutation encodes a TRAF-related protein. |journal=Dev. Biol. |volume=177 |issue= 1 |pages= 274-90 |year= 1996 |pmid= 8660894 |doi= 10.1006/dbio.1996.0162 }}
*{{cite journal | author=Nakano H, Oshima H, Chung W, ''et al.'' |title=TRAF5, an activator of NF-kappaB and putative signal transducer for the lymphotoxin-beta receptor. |journal=J. Biol. Chem. |volume=271 |issue= 25 |pages= 14661-4 |year= 1996 |pmid= 8663299 |doi= }}
*{{cite journal | author=Matsumoto M, Hsieh TY, Zhu N, ''et al.'' |title=Hepatitis C virus core protein interacts with the cytoplasmic tail of lymphotoxin-beta receptor. |journal=J. Virol. |volume=71 |issue= 2 |pages= 1301-9 |year= 1997 |pmid= 8995654 |doi= }}
*{{cite journal | author=VanArsdale TL, VanArsdale SL, Force WR, ''et al.'' |title=Lymphotoxin-beta receptor signaling complex: role of tumor necrosis factor receptor-associated factor 3 recruitment in cell death and activation of nuclear factor kappaB. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 6 |pages= 2460-5 |year= 1997 |pmid= 9122217 |doi= }}
*{{cite journal | author=Wu MY, Hsu TL, Lin WW, ''et al.'' |title=Serine/threonine kinase activity associated with the cytoplasmic domain of the lymphotoxin-beta receptor in HepG2 cells. |journal=J. Biol. Chem. |volume=272 |issue= 27 |pages= 17154-9 |year= 1997 |pmid= 9202035 |doi= }}
*{{cite journal | author=Chen CM, You LR, Hwang LH, Lee YH |title=Direct interaction of hepatitis C virus core protein with the cellular lymphotoxin-beta receptor modulates the signal pathway of the lymphotoxin-beta receptor. |journal=J. Virol. |volume=71 |issue= 12 |pages= 9417-26 |year= 1997 |pmid= 9371602 |doi= }}
*{{cite journal | author=Mizushima S, Fujita M, Ishida T, ''et al.'' |title=Cloning and characterization of a cDNA encoding the human homolog of tumor necrosis factor receptor-associated factor 5 (TRAF5). |journal=Gene |volume=207 |issue= 2 |pages= 135-40 |year= 1998 |pmid= 9511754 |doi= }}
*{{cite journal | author=Krajewska M, Krajewski S, Zapata JM, ''et al.'' |title=TRAF-4 expression in epithelial progenitor cells. Analysis in normal adult, fetal, and tumor tissues. |journal=Am. J. Pathol. |volume=152 |issue= 6 |pages= 1549-61 |year= 1998 |pmid= 9626059 |doi= }}
*{{cite journal | author=Boussaud V, Soler P, Moreau J, ''et al.'' |title=Expression of three members of the TNF-R family of receptors (4-1BB, lymphotoxin-beta receptor, and Fas) in human lung. |journal=Eur. Respir. J. |volume=12 |issue= 4 |pages= 926-31 |year= 1999 |pmid= 9817170 |doi= }}
*{{cite journal | author=Murphy M, Walter BN, Pike-Nobile L, ''et al.'' |title=Expression of the lymphotoxin beta receptor on follicular stromal cells in human lymphoid tissues. |journal=Cell Death Differ. |volume=5 |issue= 6 |pages= 497-505 |year= 1999 |pmid= 10200501 |doi= 10.1038/sj.cdd.4400374 }}
*{{cite journal | author=Wu MY, Wang PY, Han SH, Hsieh SL |title=The cytoplasmic domain of the lymphotoxin-beta receptor mediates cell death in HeLa cells. |journal=J. Biol. Chem. |volume=274 |issue= 17 |pages= 11868-73 |year= 1999 |pmid= 10207006 |doi= }}
*{{cite journal | author=Yu KY, Kwon B, Ni J, ''et al.'' |title=A newly identified member of tumor necrosis factor receptor superfamily (TR6) suppresses LIGHT-mediated apoptosis. |journal=J. Biol. Chem. |volume=274 |issue= 20 |pages= 13733-6 |year= 1999 |pmid= 10318773 |doi= }}
*{{cite journal | author=Rooney IA, Butrovich KD, Glass AA, ''et al.'' |title=The lymphotoxin-beta receptor is necessary and sufficient for LIGHT-mediated apoptosis of tumor cells. |journal=J. Biol. Chem. |volume=275 |issue= 19 |pages= 14307-15 |year= 2000 |pmid= 10799510 |doi= }}
*{{cite journal | author=Langeggen H, Berge KE, Johnson E, Hetland G |title=Human umbilical vein endothelial cells express complement receptor 1 (CD35) and complement receptor 4 (CD11c/CD18) in vitro. |journal=Inflammation |volume=26 |issue= 3 |pages= 103-10 |year= 2003 |pmid= 12083416 |doi= }}
*{{cite journal | author=Chang YH, Hsieh SL, Chen MC, Lin WW |title=Lymphotoxin beta receptor induces interleukin 8 gene expression via NF-kappaB and AP-1 activation. |journal=Exp. Cell Res. |volume=278 |issue= 2 |pages= 166-74 |year= 2002 |pmid= 12169272 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LTC4S... {November 18, 2007 9:58:24 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:58:46 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Leukotriene C4 synthase
| HGNCid = 6719
| Symbol = LTC4S
| AltSymbols =; MGC33147
| OMIM = 246530
| ECnumber =
| Homologene = 7406
| MGIid = 107498
| Function = {{GNF_GO|id=GO:0004364 |text = glutathione transferase activity}} {{GNF_GO|id=GO:0004464 |text = leukotriene-C4 synthase activity}} {{GNF_GO|id=GO:0008047 |text = enzyme activator activity}} {{GNF_GO|id=GO:0016829 |text = lyase activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0019370 |text = leukotriene biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4056
| Hs_Ensembl =
| Hs_RefseqProtein = NP_665874
| Hs_RefseqmRNA = NM_145867
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 17001
| Mm_Ensembl = ENSMUSG00000020377
| Mm_RefseqmRNA = NM_008521
| Mm_RefseqProtein = NP_032547
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 50079885
| Mm_GenLoc_end = 50081955
| Mm_Uniprot = Q5SVR7
}}
}}
'''Leukotriene C4 synthase''', also known as '''LTC4S''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LTC4S leukotriene C4 synthase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4056| 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 MAPEG (Membrane Associated Proteins in Eicosanoid and Glutathione metabolism) family includes a number of human proteins, several of which are involved the production of leukotrienes. This gene encodes an enzyme that catalyzes the first step in the biosynthesis of cysteinyl leukotrienes, potent biological compounds derived from arachidonic acid. Leukotrienes have been implicated as mediators of anaphylaxis and inflammatory conditions such as human bronchial asthma. This protein localizes to the nuclear envelope and adjacent endoplasmic reticulum.<ref name="entrez">{{cite web | title = Entrez Gene: LTC4S leukotriene C4 synthase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4056| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Penrose JF |title=LTC4 synthase. Enzymology, biochemistry, and molecular characterization. |journal=Clinical reviews in allergy & immunology |volume=17 |issue= 1-2 |pages= 133-52 |year= 1999 |pmid= 10436863 |doi= }}
*{{cite journal | author=Penrose JF, Austen KF |title=The biochemical, molecular, and genomic aspects of leukotriene C4 synthase. |journal=Proc. Assoc. Am. Physicians |volume=111 |issue= 6 |pages= 537-46 |year= 2000 |pmid= 10591082 |doi= }}
*{{cite journal | author=Jakobsson PJ, Morgenstern R, Mancini J, ''et al.'' |title=Membrane-associated proteins in eicosanoid and glutathione metabolism (MAPEG). A widespread protein superfamily. |journal=Am. J. Respir. Crit. Care Med. |volume=161 |issue= 2 Pt 2 |pages= S20-4 |year= 2000 |pmid= 10673221 |doi= }}
*{{cite journal | author=Bigby TD |title=The leukotriene C(4) synthase gene and asthma. |journal=Am. J. Respir. Cell Mol. Biol. |volume=23 |issue= 3 |pages= 273-6 |year= 2000 |pmid= 10970815 |doi= }}
*{{cite journal | author=Penrose JF, Gagnon L, Goppelt-Struebe M, ''et al.'' |title=Purification of human leukotriene C4 synthase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 23 |pages= 11603-6 |year= 1993 |pmid= 1454853 |doi= }}
*{{cite journal | author=Nicholson DW, Ali A, Klemba MW, ''et al.'' |title=Human leukotriene C4 synthase expression in dimethyl sulfoxide-differentiated U937 cells. |journal=J. Biol. Chem. |volume=267 |issue= 25 |pages= 17849-57 |year= 1992 |pmid= 1517222 |doi= }}
*{{cite journal | author=Penrose JF, Spector J, Lam BK, ''et al.'' |title=Purification of human lung leukotriene C4 synthase and preparation of a polyclonal antibody. |journal=Am. J. Respir. Crit. Care Med. |volume=152 |issue= 1 |pages= 283-9 |year= 1995 |pmid= 7599836 |doi= }}
*{{cite journal | author=Söderström M, Morgenstern R, Hammarström S |title=Protein-protein interaction affinity chromatography of leukotriene C4 synthase. |journal=Protein Expr. Purif. |volume=6 |issue= 3 |pages= 352-6 |year= 1995 |pmid= 7663172 |doi= 10.1006/prep.1995.1046 }}
*{{cite journal | author=Welsch DJ, Creely DP, Hauser SD, ''et al.'' |title=Molecular cloning and expression of human leukotriene-C4 synthase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 21 |pages= 9745-9 |year= 1994 |pmid= 7937884 |doi= }}
*{{cite journal | author=Lam BK, Penrose JF, Freeman GJ, Austen KF |title=Expression cloning of a cDNA for human leukotriene C4 synthase, an integral membrane protein conjugating reduced glutathione to leukotriene A4. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 16 |pages= 7663-7 |year= 1994 |pmid= 8052639 |doi= }}
*{{cite journal | author=Nicholson DW, Ali A, Vaillancourt JP, ''et al.'' |title=Purification to homogeneity and the N-terminal sequence of human leukotriene C4 synthase: a homodimeric glutathione S-transferase composed of 18-kDa subunits. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 5 |pages= 2015-9 |year= 1993 |pmid= 8446623 |doi= }}
*{{cite journal | author=Penrose JF, Spector J, Baldasaro M, ''et al.'' |title=Molecular cloning of the gene for human leukotriene C4 synthase. Organization, nucleotide sequence, and chromosomal localization to 5q35. |journal=J. Biol. Chem. |volume=271 |issue= 19 |pages= 11356-61 |year= 1996 |pmid= 8626689 |doi= }}
*{{cite journal | author=Bigby TD, Hodulik CR, Arden KC, Fu L |title=Molecular cloning of the human leukotriene C4 synthase gene and assignment to chromosome 5q35. |journal=Mol. Med. |volume=2 |issue= 5 |pages= 637-46 |year= 1997 |pmid= 8898379 |doi= }}
*{{cite journal | author=Scoggan KA, Jakobsson PJ, Ford-Hutchinson AW |title=Production of leukotriene C4 in different human tissues is attributable to distinct membrane bound biosynthetic enzymes. |journal=J. Biol. Chem. |volume=272 |issue= 15 |pages= 10182-7 |year= 1997 |pmid= 9092565 |doi= }}
*{{cite journal | author=Sala A, Folco G, Henson PM, Murphy RC |title=Pharmacological modulation of human platelet leukotriene C4-synthase. |journal=Biochem. Pharmacol. |volume=53 |issue= 6 |pages= 905-8 |year= 1997 |pmid= 9113110 |doi= }}
*{{cite journal | author=Spanbroek R, Stark HJ, Janssen-Timmen U, ''et al.'' |title=5-Lipoxygenase expression in Langerhans cells of normal human epidermis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 2 |pages= 663-8 |year= 1998 |pmid= 9435249 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MAP4... {November 18, 2007 9:58:46 PM PST}
- SEARCH REDIRECT: Control Box Found: MAP4 {November 18, 2007 9:59:07 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:59:10 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:59:10 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:59:10 PM PST}
- UPDATED: Updated protein page: MAP4 {November 18, 2007 9:59:17 PM PST}
- INFO: Beginning work on MBD1... {November 18, 2007 9:59:17 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:59:59 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MBD1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1d9n.
| PDB = {{PDB2|1d9n}}, {{PDB2|1ig4}}
| Name = Methyl-CpG binding domain protein 1
| HGNCid = 6916
| Symbol = MBD1
| AltSymbols =; CXXC3; PCM1; RFT
| OMIM = 156535
| ECnumber =
| Homologene = 8414
| MGIid = 1333811
| GeneAtlas_image1 = PBB_GE_MBD1_203353_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MBD1_208595_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003714 |text = transcription corepressor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008327 |text = methyl-CpG binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0000792 |text = heterochromatin}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4152
| Hs_Ensembl = ENSG00000141644
| Hs_RefseqProtein = NP_002375
| Hs_RefseqmRNA = NM_002384
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 46047254
| Hs_GenLoc_end = 46061844
| Hs_Uniprot = Q9UIS9
| Mm_EntrezGene = 17190
| Mm_Ensembl = ENSMUSG00000024561
| Mm_RefseqmRNA = NM_013594
| Mm_RefseqProtein = NP_038622
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 74393641
| Mm_GenLoc_end = 74408054
| Mm_Uniprot = Q9Z2E2
}}
}}
'''Methyl-CpG binding domain protein 1''', also known as '''MBD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MBD1 methyl-CpG binding domain protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4152| 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 = DNA methylation is the major modification of eukaryotic genomes and plays an essential role in mammalian development. Human proteins MECP2, MBD1, MBD2, MBD3, and MBD4 comprise a family of nuclear proteins related by the presence in each of a methyl-CpG binding domain (MBD). Each of these proteins, with the exception of MBD3, is capable of binding specifically to methylated DNA. MECP2, MBD1 and MBD2 can also repress transcription from methylated gene promoters. Five transcript variants of the MBD1 are generated by alternative splicing resulting in protein isoforms that contain one MBD domain, two to three cysteine-rich (CXXC) domains, and some differences in the COOH terminus. All five transcript variants repress transcription from methylated promoters; in addition, variants with three CXXC domains also repress unmethylated promoter activity. MBD1 and MBD2 map very close to each other on chromosome 18q21.<ref name="entrez">{{cite web | title = Entrez Gene: MBD1 methyl-CpG binding domain protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4152| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{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=Cross SH, Meehan RR, Nan X, Bird A |title=A component of the transcriptional repressor MeCP1 shares a motif with DNA methyltransferase and HRX proteins. |journal=Nat. Genet. |volume=16 |issue= 3 |pages= 256-9 |year= 1997 |pmid= 9207790 |doi= 10.1038/ng0797-256 }}
*{{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=Hendrich B, Bird A |title=Identification and characterization of a family of mammalian methyl-CpG binding proteins. |journal=Mol. Cell. Biol. |volume=18 |issue= 11 |pages= 6538-47 |year= 1998 |pmid= 9774669 |doi= }}
*{{cite journal | author=Ueba T, Kaspar B, Zhao X, Gage FH |title=Repression of human fibroblast growth factor 2 by a novel transcription factor. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 10382-7 |year= 1999 |pmid= 10187827 |doi= }}
*{{cite journal | author=Hendrich B, Abbott C, McQueen H, ''et al.'' |title=Genomic structure and chromosomal mapping of the murine and human Mbd1, Mbd2, Mbd3, and Mbd4 genes. |journal=Mamm. Genome |volume=10 |issue= 9 |pages= 906-12 |year= 1999 |pmid= 10441743 |doi= }}
*{{cite journal | author=Fujita N, Takebayashi S, Okumura K, ''et al.'' |title=Methylation-mediated transcriptional silencing in euchromatin by methyl-CpG binding protein MBD1 isoforms. |journal=Mol. Cell. Biol. |volume=19 |issue= 9 |pages= 6415-26 |year= 1999 |pmid= 10454587 |doi= }}
*{{cite journal | author=Ohki I, Shimotake N, Fujita N, ''et al.'' |title=Solution structure of the methyl-CpG-binding domain of the methylation-dependent transcriptional repressor MBD1. |journal=EMBO J. |volume=18 |issue= 23 |pages= 6653-61 |year= 2000 |pmid= 10581239 |doi= 10.1093/emboj/18.23.6653 }}
*{{cite journal | author=Ng HH, Jeppesen P, Bird A |title=Active repression of methylated genes by the chromosomal protein MBD1. |journal=Mol. Cell. Biol. |volume=20 |issue= 4 |pages= 1394-406 |year= 2000 |pmid= 10648624 |doi= }}
*{{cite journal | author=Fujita N, Shimotake N, Ohki I, ''et al.'' |title=Mechanism of transcriptional regulation by methyl-CpG binding protein MBD1. |journal=Mol. Cell. Biol. |volume=20 |issue= 14 |pages= 5107-18 |year= 2000 |pmid= 10866667 |doi= }}
*{{cite journal | author=Saito M, Ishikawa F |title=The mCpG-binding domain of human MBD3 does not bind to mCpG but interacts with NuRD/Mi2 components HDAC1 and MTA2. |journal=J. Biol. Chem. |volume=277 |issue= 38 |pages= 35434-9 |year= 2002 |pmid= 12124384 |doi= 10.1074/jbc.M203455200 }}
*{{cite journal | author=Beyer KS, Blasi F, Bacchelli E, ''et al.'' |title=Mutation analysis of the coding sequence of the MECP2 gene in infantile autism. |journal=Hum. Genet. |volume=111 |issue= 4-5 |pages= 305-9 |year= 2002 |pmid= 12384770 |doi= 10.1007/s00439-002-0786-3 }}
*{{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=Patra SK, Patra A, Zhao H, ''et al.'' |title=Methyl-CpG-DNA binding proteins in human prostate cancer: expression of CXXC sequence containing MBD1 and repression of MBD2 and MeCP2. |journal=Biochem. Biophys. Res. Commun. |volume=302 |issue= 4 |pages= 759-66 |year= 2003 |pmid= 12646234 |doi= }}
*{{cite journal | author=Fujita N, Watanabe S, Ichimura T, ''et al.'' |title=MCAF mediates MBD1-dependent transcriptional repression. |journal=Mol. Cell. Biol. |volume=23 |issue= 8 |pages= 2834-43 |year= 2003 |pmid= 12665582 |doi= }}
*{{cite journal | author=Reese BE, Bachman KE, Baylin SB, Rountree MR |title=The methyl-CpG binding protein MBD1 interacts with the p150 subunit of chromatin assembly factor 1. |journal=Mol. Cell. Biol. |volume=23 |issue= 9 |pages= 3226-36 |year= 2003 |pmid= 12697822 |doi= }}
*{{cite journal | author=Fujita N, Watanabe S, Ichimura T, ''et al.'' |title=Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression. |journal=J. Biol. Chem. |volume=278 |issue= 26 |pages= 24132-8 |year= 2003 |pmid= 12711603 |doi= 10.1074/jbc.M302283200 }}
*{{cite journal | author=Carney RM, Wolpert CM, Ravan SA, ''et al.'' |title=Identification of MeCP2 mutations in a series of females with autistic disorder. |journal=Pediatr. Neurol. |volume=28 |issue= 3 |pages= 205-11 |year= 2003 |pmid= 12770674 |doi= }}
*{{cite journal | author=Georgel PT, Horowitz-Scherer RA, Adkins N, ''et al.'' |title=Chromatin compaction by human MeCP2. Assembly of novel secondary chromatin structures in the absence of DNA methylation. |journal=J. Biol. Chem. |volume=278 |issue= 34 |pages= 32181-8 |year= 2003 |pmid= 12788925 |doi= 10.1074/jbc.M305308200 }}
*{{cite journal | author=Watanabe S, Ichimura T, Fujita N, ''et al.'' |title=Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 22 |pages= 12859-64 |year= 2004 |pmid= 14555760 |doi= 10.1073/pnas.2131819100 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MTM1... {November 18, 2007 10:00:41 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:01:11 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
| 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 = Myotubularin 1
| HGNCid = 7448
| Symbol = MTM1
| AltSymbols =; CNM; MTMX; XLMTM
| OMIM = 300415
| ECnumber =
| Homologene = 37279
| MGIid = 1099452
| Function = {{GNF_GO|id=GO:0004437 |text = inositol or phosphatidylinositol phosphatase activity}} {{GNF_GO|id=GO:0004722 |text = protein serine/threonine phosphatase activity}} {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0007517 |text = muscle development}} {{GNF_GO|id=GO:0046839 |text = phospholipid dephosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4534
| Hs_Ensembl = ENSG00000171100
| Hs_RefseqProtein = NP_000243
| Hs_RefseqmRNA = NM_000252
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 149487727
| Hs_GenLoc_end = 149592453
| Hs_Uniprot = Q13496
| Mm_EntrezGene = 17772
| Mm_Ensembl = ENSMUSG00000031337
| Mm_RefseqmRNA = NM_019926
| Mm_RefseqProtein = NP_064310
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 67471323
| Mm_GenLoc_end = 67575845
| Mm_Uniprot = Q5BKQ5
}}
}}
'''Myotubularin 1''', also known as '''MTM1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MTM1 myotubularin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4534| 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 a member of a gene family that encodes tyrosine phosphatases. Myotubularin is required for muscle cell differentiation and mutations in this gene have been identified as being responsible for X-linked myotubular myopathy.<ref name="entrez">{{cite web | title = Entrez Gene: MTM1 myotubularin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4534| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Laporte J, Biancalana V, Tanner SM, ''et al.'' |title=MTM1 mutations in X-linked myotubular myopathy. |journal=Hum. Mutat. |volume=15 |issue= 5 |pages= 393-409 |year= 2000 |pmid= 10790201 |doi= 10.1002/(SICI)1098-1004(200005)15:5<393::AID-HUMU1>3.0.CO;2-R }}
*{{cite journal | author=Wishart MJ, Dixon JE |title=PTEN and myotubularin phosphatases: from 3-phosphoinositide dephosphorylation to disease. |journal=Trends Cell Biol. |volume=12 |issue= 12 |pages= 579-85 |year= 2003 |pmid= 12495846 |doi= }}
*{{cite journal | author=Laporte J, Bedez F, Bolino A, Mandel JL |title=Myotubularins, a large disease-associated family of cooperating catalytically active and inactive phosphoinositides phosphatases. |journal=Hum. Mol. Genet. |volume=12 Spec No 2 |issue= |pages= R285-92 |year= 2004 |pmid= 12925573 |doi= 10.1093/hmg/ddg273 }}
*{{cite journal | author=Magnussen E |title=[In memoriam: Elisabeth Larsen] |journal=Sygeplejersken |volume=75 |issue= 9 |pages= 16-7 |year= 1975 |pmid= 1090027 |doi= }}
*{{cite journal | author=Liechti-Gallati S, Müller B, Grimm T, ''et al.'' |title=X-linked centronuclear myopathy: mapping the gene to Xq28. |journal=Neuromuscul. Disord. |volume=1 |issue= 4 |pages= 239-45 |year= 1992 |pmid= 1822801 |doi= }}
*{{cite journal | author=Laporte J, Hu LJ, Kretz C, ''et al.'' |title=A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast. |journal=Nat. Genet. |volume=13 |issue= 2 |pages= 175-82 |year= 1996 |pmid= 8640223 |doi= 10.1038/ng0696-175 }}
*{{cite journal | author=de Gouyon BM, Zhao W, Laporte J, ''et al.'' |title=Characterization of mutations in the myotubularin gene in twenty six patients with X-linked myotubular myopathy. |journal=Hum. Mol. Genet. |volume=6 |issue= 9 |pages= 1499-504 |year= 1998 |pmid= 9285787 |doi= }}
*{{cite journal | author=Laporte J, Guiraud-Chaumeil C, Vincent MC, ''et al.'' |title=Mutations in the MTM1 gene implicated in X-linked myotubular myopathy. ENMC International Consortium on Myotubular Myopathy. European Neuro-Muscular Center. |journal=Hum. Mol. Genet. |volume=6 |issue= 9 |pages= 1505-11 |year= 1998 |pmid= 9305655 |doi= }}
*{{cite journal | author=Tanner SM, Laporte J, Guiraud-Chaumeil C, Liechti-Gallati S |title=Confirmation of prenatal diagnosis results of X-linked recessive myotubular myopathy by mutational screening, and description of three new mutations in the MTM1 gene. |journal=Hum. Mutat. |volume=11 |issue= 1 |pages= 62-8 |year= 1998 |pmid= 9450905 |doi= 10.1002/(SICI)1098-1004(1998)11:1<62::AID-HUMU10>3.0.CO;2-X }}
*{{cite journal | author=Cui X, De Vivo I, Slany R, ''et al.'' |title=Association of SET domain and myotubularin-related proteins modulates growth control. |journal=Nat. Genet. |volume=18 |issue= 4 |pages= 331-7 |year= 1998 |pmid= 9537414 |doi= 10.1038/ng0498-331 }}
*{{cite journal | author=Laporte J, Blondeau F, Buj-Bello A, ''et al.'' |title=Characterization of the myotubularin dual specificity phosphatase gene family from yeast to human. |journal=Hum. Mol. Genet. |volume=7 |issue= 11 |pages= 1703-12 |year= 1998 |pmid= 9736772 |doi= }}
*{{cite journal | author=Laporte J, Guiraud-Chaumeil C, Tanner SM, ''et al.'' |title=Genomic organization of the MTM1 gene implicated in X-linked myotubular myopathy. |journal=Eur. J. Hum. Genet. |volume=6 |issue= 4 |pages= 325-30 |year= 1998 |pmid= 9781038 |doi= 10.1038/sj.ejhg.5200189 }}
*{{cite journal | author=Kioschis P, Wiemann S, Heiss NS, ''et al.'' |title=Genomic organization of a 225-kb region in Xq28 containing the gene for X-linked myotubular myopathy (MTM1) and a related gene (MTMR1). |journal=Genomics |volume=54 |issue= 2 |pages= 256-66 |year= 1999 |pmid= 9828128 |doi= 10.1006/geno.1998.5560 }}
*{{cite journal | author=Nishino I, Minami N, Kobayashi O, ''et al.'' |title=MTM1 gene mutations in Japanese patients with the severe infantile form of myotubular myopathy. |journal=Neuromuscul. Disord. |volume=8 |issue= 7 |pages= 453-8 |year= 1999 |pmid= 9829274 |doi= }}
*{{cite journal | author=Tanner SM, Schneider V, Thomas NS, ''et al.'' |title=Characterization of 34 novel and six known MTM1 gene mutations in 47 unrelated X-linked myotubular myopathy patients. |journal=Neuromuscul. Disord. |volume=9 |issue= 1 |pages= 41-9 |year= 1999 |pmid= 10063835 |doi= }}
*{{cite journal | author=Häne BG, Rogers RC, Schwartz CE |title=Germline mosaicism in X-linked myotubular myopathy. |journal=Clin. Genet. |volume=56 |issue= 1 |pages= 77-81 |year= 1999 |pmid= 10466421 |doi= }}
*{{cite journal | author=Buj-Bello A, Biancalana V, Moutou C, ''et al.'' |title=Identification of novel mutations in the MTM1 gene causing severe and mild forms of X-linked myotubular myopathy. |journal=Hum. Mutat. |volume=14 |issue= 4 |pages= 320-5 |year= 1999 |pmid= 10502779 |doi= 10.1002/(SICI)1098-1004(199910)14:4<320::AID-HUMU7>3.0.CO;2-O }}
*{{cite journal | author=Taylor GS, Maehama T, Dixon JE |title=Inaugural article: myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 16 |pages= 8910-5 |year= 2000 |pmid= 10900271 |doi= 10.1073/pnas.160255697 }}
*{{cite journal | author=Blondeau F, Laporte J, Bodin S, ''et al.'' |title=Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway. |journal=Hum. Mol. Genet. |volume=9 |issue= 15 |pages= 2223-9 |year= 2001 |pmid= 11001925 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MUT... {November 18, 2007 10:01:11 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:01:40 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 = Methylmalonyl Coenzyme A mutase
| HGNCid = 7526
| Symbol = MUT
| AltSymbols =; MCM
| OMIM = 609058
| ECnumber =
| Homologene = 20097
| MGIid = 97239
| GeneAtlas_image1 = PBB_GE_MUT_202959_at_tn.png
| GeneAtlas_image2 = PBB_GE_MUT_202960_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004494 |text = methylmalonyl-CoA mutase activity}} {{GNF_GO|id=GO:0031419 |text = cobalamin binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0050897 |text = cobalt ion binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0009791 |text = post-embryonic development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4594
| Hs_Ensembl = ENSG00000146085
| Hs_RefseqProtein = NP_000246
| Hs_RefseqmRNA = NM_000255
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 49506958
| Hs_GenLoc_end = 49538811
| Hs_Uniprot = P22033
| Mm_EntrezGene = 17850
| Mm_Ensembl = ENSMUSG00000023921
| Mm_RefseqmRNA = NM_008650
| Mm_RefseqProtein = NP_032676
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 40398191
| Mm_GenLoc_end = 40425133
| Mm_Uniprot = Q3UFU2
}}
}}
'''Methylmalonyl Coenzyme A mutase''', also known as '''MUT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MUT methylmalonyl Coenzyme A mutase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4594| 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 = MUT encodes the mitochondrial enzymne methylmalonyl Coenzyme A mutase. In humans, MUT is a vitamin B12-dependent enzyme which catalyzes the isomerization of methylmalonyl-CoA to succinyl-CoA, while in other species this enzyme may have different functions. Mutations in MUT may lead to various types of methylmalonic aciduria.<ref name="entrez">{{cite web | title = Entrez Gene: MUT methylmalonyl Coenzyme A mutase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4594| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ledley FD, Rosenblatt DS |title=Mutations in mut methylmalonic acidemia: clinical and enzymatic correlations. |journal=Hum. Mutat. |volume=9 |issue= 1 |pages= 1-6 |year= 1997 |pmid= 8990001 |doi= 10.1002/(SICI)1098-1004(1997)9:1<1::AID-HUMU1>3.0.CO;2-E }}
*{{cite journal | author=Ludwig ML, Matthews RG |title=Structure-based perspectives on B12-dependent enzymes. |journal=Annu. Rev. Biochem. |volume=66 |issue= |pages= 269-313 |year= 1997 |pmid= 9242908 |doi= 10.1146/annurev.biochem.66.1.269 }}
*{{cite journal | author=Lubrano R, Elli M, Rossi M, ''et al.'' |title=Renal transplant in methylmalonic acidemia: could it be the best option? Report on a case at 10 years and review of the literature. |journal=Pediatr. Nephrol. |volume=22 |issue= 8 |pages= 1209-14 |year= 2007 |pmid= 17401587 |doi= 10.1007/s00467-007-0460-z }}
*{{cite journal | author=Frenkel EP, Kitchens RL |title=Intracellular localization of hepatic propionyl-CoA carboxylase and methylmalonyl-CoA mutase in humans and normal and vitamin B12 deficient rats. |journal=Br. J. Haematol. |volume=31 |issue= 4 |pages= 501-13 |year= 1978 |pmid= 24458 |doi= }}
*{{cite journal | author=Crane AM, Jansen R, Andrews ER, Ledley FD |title=Cloning and expression of a mutant methylmalonyl coenzyme A mutase with altered cobalamin affinity that causes mut- methylmalonic aciduria. |journal=J. Clin. Invest. |volume=89 |issue= 2 |pages= 385-91 |year= 1992 |pmid= 1346616 |doi= }}
*{{cite journal | author=Crane AM, Martin LS, Valle D, Ledley FD |title=Phenotype of disease in three patients with identical mutations in methylmalonyl CoA mutase. |journal=Hum. Genet. |volume=89 |issue= 3 |pages= 259-64 |year= 1992 |pmid= 1351030 |doi= }}
*{{cite journal | author=Raff ML, Crane AM, Jansen R, ''et al.'' |title=Genetic characterization of a MUT locus mutation discriminating heterogeneity in mut0 and mut- methylmalonic aciduria by interallelic complementation. |journal=J. Clin. Invest. |volume=87 |issue= 1 |pages= 203-7 |year= 1991 |pmid= 1670635 |doi= }}
*{{cite journal | author=Jansen R, Ledley FD |title=Heterozygous mutations at the mut locus in fibroblasts with mut0 methylmalonic acidemia identified by polymerase-chain-reaction cDNA cloning. |journal=Am. J. Hum. Genet. |volume=47 |issue= 5 |pages= 808-14 |year= 1990 |pmid= 1977311 |doi= }}
*{{cite journal | author=Nham SU, Wilkemeyer MF, Ledley FD |title=Structure of the human methylmalonyl-CoA mutase (MUT) locus. |journal=Genomics |volume=8 |issue= 4 |pages= 710-6 |year= 1991 |pmid= 1980486 |doi= }}
*{{cite journal | author=Ledley FD, Lumetta M, Nguyen PN, ''et al.'' |title=Molecular cloning of L-methylmalonyl-CoA mutase: gene transfer and analysis of mut cell lines. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 10 |pages= 3518-21 |year= 1988 |pmid= 2453061 |doi= }}
*{{cite journal | author=Jansen R, Kalousek F, Fenton WA, ''et al.'' |title=Cloning of full-length methylmalonyl-CoA mutase from a cDNA library using the polymerase chain reaction. |journal=Genomics |volume=4 |issue= 2 |pages= 198-205 |year= 1989 |pmid= 2567699 |doi= }}
*{{cite journal | author=Fenton WA, Hack AM, Kraus JP, Rosenberg LE |title=Immunochemical studies of fibroblasts from patients with methylmalonyl-CoA mutase apoenzyme deficiency: detection of a mutation interfering with mitochondrial import. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 5 |pages= 1421-4 |year= 1987 |pmid= 2881300 |doi= }}
*{{cite journal | author=Zoghbi HY, O'Brien WE, Ledley FD |title=Linkage relationships of the human methylmalonyl CoA mutase to the HLA and D6S4 loci on chromosome 6. |journal=Genomics |volume=3 |issue= 4 |pages= 396-8 |year= 1989 |pmid= 2907507 |doi= }}
*{{cite journal | author=Kolhouse JF, Utley C, Allen RH |title=Isolation and characterization of methylmalonyl-CoA mutase from human placenta. |journal=J. Biol. Chem. |volume=255 |issue= 7 |pages= 2708-12 |year= 1980 |pmid= 6102092 |doi= }}
*{{cite journal | author=Fenton WA, Hack AM, Willard HF, ''et al.'' |title=Purification and properties of methylmalonyl coenzyme A mutase from human liver. |journal=Arch. Biochem. Biophys. |volume=214 |issue= 2 |pages= 815-23 |year= 1982 |pmid= 6124211 |doi= }}
*{{cite journal | author=Qureshi AA, Crane AM, Matiaszuk NV, ''et al.'' |title=Cloning and expression of mutations demonstrating intragenic complementation in mut0 methylmalonic aciduria. |journal=J. Clin. Invest. |volume=93 |issue= 4 |pages= 1812-9 |year= 1994 |pmid= 7909321 |doi= }}
*{{cite journal | author=Crane AM, Ledley FD |title=Clustering of mutations in methylmalonyl CoA mutase associated with mut- methylmalonic acidemia. |journal=Am. J. Hum. Genet. |volume=55 |issue= 1 |pages= 42-50 |year= 1994 |pmid= 7912889 |doi= }}
*{{cite journal | author=Janata J, Kogekar N, Fenton WA |title=Expression and kinetic characterization of methylmalonyl-CoA mutase from patients with the mut- phenotype: evidence for naturally occurring interallelic complementation. |journal=Hum. Mol. Genet. |volume=6 |issue= 9 |pages= 1457-64 |year= 1998 |pmid= 9285782 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NME2... {November 18, 2007 10:01:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:02:10 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_NME2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1be4.
| PDB = {{PDB2|1be4}}, {{PDB2|1bhn}}, {{PDB2|1nsk}}, {{PDB2|1nue}}
| Name = Non-metastatic cells 2, protein (NM23B) expressed in
| HGNCid = 7850
| Symbol = NME2
| AltSymbols =; MGC111212; NDPKB; NM23-H2; NM23B; puf
| OMIM = 156491
| ECnumber =
| Homologene = 39553
| MGIid = 97356
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0004550 |text = nucleoside diphosphate kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0001726 |text = ruffle}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0030027 |text = lamellipodium}}
| Process = {{GNF_GO|id=GO:0006183 |text = GTP biosynthetic process}} {{GNF_GO|id=GO:0006228 |text = UTP biosynthetic process}} {{GNF_GO|id=GO:0006241 |text = CTP biosynthetic process}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007595 |text = lactation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0009117 |text = nucleotide metabolic process}} {{GNF_GO|id=GO:0009142 |text = nucleoside triphosphate biosynthetic process}} {{GNF_GO|id=GO:0030879 |text = mammary gland development}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4831
| Hs_Ensembl =
| Hs_RefseqProtein = NP_001018147
| Hs_RefseqmRNA = NM_001018137
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 18103
| Mm_Ensembl = ENSMUSG00000020857
| Mm_RefseqmRNA = NM_001077529
| Mm_RefseqProtein = NP_001070997
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 93765906
| Mm_GenLoc_end = 93772346
| Mm_Uniprot = Q5NC82
}}
}}
'''Non-metastatic cells 2, protein (NM23B) expressed in''', also known as '''NME2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NME2 non-metastatic cells 2, protein (NM23B) expressed in| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4831| 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 = Nucleoside diphosphate kinase (NDK) exists as a hexamer composed of 'A' (encoded by NME1) and 'B' (encoded by this gene) isoforms. Multiple alternatively spliced transcript variants encoding the same isoform have been found for this gene. Co-transcription of this gene and the neighboring upstream gene (NME1) generates naturally-occurring transcripts (NME1-NME2) which encode a fusion protein comprised of sequence sharing identity with each individual gene product.<ref name="entrez">{{cite web | title = Entrez Gene: NME2 non-metastatic cells 2, protein (NM23B) expressed in| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4831| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Gilles AM, Presecan E, Vonica A, Lascu I |title=Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme. |journal=J. Biol. Chem. |volume=266 |issue= 14 |pages= 8784-9 |year= 1991 |pmid= 1851158 |doi= }}
*{{cite journal | author=Stahl JA, Leone A, Rosengard AM, ''et al.'' |title=Identification of a second human nm23 gene, nm23-H2. |journal=Cancer Res. |volume=51 |issue= 1 |pages= 445-9 |year= 1991 |pmid= 1988104 |doi= }}
*{{cite journal | author=Rosengard AM, Krutzsch HC, Shearn A, ''et al.'' |title=Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila development. |journal=Nature |volume=342 |issue= 6246 |pages= 177-80 |year= 1989 |pmid= 2509941 |doi= 10.1038/342177a0 }}
*{{cite journal | author=Webb PA, Perisic O, Mendola CE, ''et al.'' |title=The crystal structure of a human nucleoside diphosphate kinase, NM23-H2. |journal=J. Mol. Biol. |volume=251 |issue= 4 |pages= 574-87 |year= 1995 |pmid= 7658474 |doi= }}
*{{cite journal | author=Chandrasekharappa SC, Gross LA, King SE, Collins FS |title=The human NME2 gene lies within 18kb of NME1 in chromosome 17. |journal=Genes Chromosomes Cancer |volume=6 |issue= 4 |pages= 245-8 |year= 1993 |pmid= 7685630 |doi= }}
*{{cite journal | author=Ji L, Arcinas M, Boxer LM |title=The transcription factor, Nm23H2, binds to and activates the translocated c-myc allele in Burkitt's lymphoma. |journal=J. Biol. Chem. |volume=270 |issue= 22 |pages= 13392-8 |year= 1995 |pmid= 7768941 |doi= }}
*{{cite journal | author=MacDonald NJ, De la Rosa A, Benedict MA, ''et al.'' |title=A serine phosphorylation of Nm23, and not its nucleoside diphosphate kinase activity, correlates with suppression of tumor metastatic potential. |journal=J. Biol. Chem. |volume=268 |issue= 34 |pages= 25780-9 |year= 1994 |pmid= 8245015 |doi= }}
*{{cite journal | author=Backer JM, Mendola CE, Kovesdi I, ''et al.'' |title=Chromosomal localization and nucleoside diphosphate kinase activity of human metastasis-suppressor genes NM23-1 and NM23-2. |journal=Oncogene |volume=8 |issue= 2 |pages= 497-502 |year= 1993 |pmid= 8381224 |doi= }}
*{{cite journal | author=Postel EH, Berberich SJ, Flint SJ, Ferrone CA |title=Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis. |journal=Science |volume=261 |issue= 5120 |pages= 478-80 |year= 1993 |pmid= 8392752 |doi= }}
*{{cite journal | author=Kelsell DP, Black DM, Solomon E, Spurr NK |title=Localization of a second NM23 gene, NME2, to chromosome 17q21-q22. |journal=Genomics |volume=17 |issue= 2 |pages= 522-4 |year= 1993 |pmid= 8406509 |doi= 10.1006/geno.1993.1362 }}
*{{cite journal | author=Engel M, Véron M, Theisinger B, ''et al.'' |title=A novel serine/threonine-specific protein phosphotransferase activity of Nm23/nucleoside-diphosphate kinase. |journal=Eur. J. Biochem. |volume=234 |issue= 1 |pages= 200-7 |year= 1996 |pmid= 8529641 |doi= }}
*{{cite journal | author=Guignard F, Markert M |title=The nucleoside diphosphate kinase of human neutrophils. |journal=Biochem. J. |volume=316 ( Pt 1) |issue= |pages= 233-8 |year= 1996 |pmid= 8645210 |doi= }}
*{{cite journal | author=Moréra S, Lacombe ML, Xu Y, ''et al.'' |title=X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2 A resolution. |journal=Structure |volume=3 |issue= 12 |pages= 1307-14 |year= 1996 |pmid= 8747457 |doi= }}
*{{cite journal | author=Paravicini G, Steinmayr M, André E, Becker-André M |title=The metastasis suppressor candidate nucleotide diphosphate kinase NM23 specifically interacts with members of the ROR/RZR nuclear orphan receptor subfamily. |journal=Biochem. Biophys. Res. Commun. |volume=227 |issue= 1 |pages= 82-7 |year= 1996 |pmid= 8858107 |doi= 10.1006/bbrc.1996.1471 }}
*{{cite journal | author=Nosaka K, Kawahara M, Masuda M, ''et al.'' |title=Association of nucleoside diphosphate kinase nm23-H2 with human telomeres. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 2 |pages= 342-8 |year= 1998 |pmid= 9480811 |doi= 10.1006/bbrc.1997.8097 }}
*{{cite journal | author=Pinon VP, Millot G, Munier A, ''et al.'' |title=Cytoskeletal association of the A and B nucleoside diphosphate kinases of interphasic but not mitotic human carcinoma cell lines: specific nuclear localization of the B subunit. |journal=Exp. Cell Res. |volume=246 |issue= 2 |pages= 355-67 |year= 1999 |pmid= 9925751 |doi= 10.1006/excr.1998.4318 }}
*{{cite journal | author=Negroni A, Venturelli D, Tanno B, ''et al.'' |title=Neuroblastoma specific effects of DR-nm23 and its mutant forms on differentiation and apoptosis. |journal=Cell Death Differ. |volume=7 |issue= 9 |pages= 843-50 |year= 2000 |pmid= 11042679 |doi= 10.1038/sj.cdd.4400720 }}
*{{cite journal | author=Roymans D, Willems R, Vissenberg K, ''et al.'' |title=Nucleoside diphosphate kinase beta (Nm23-R1/NDPKbeta) is associated with intermediate filaments and becomes upregulated upon cAMP-induced differentiation of rat C6 glioma. |journal=Exp. Cell Res. |volume=261 |issue= 1 |pages= 127-38 |year= 2000 |pmid= 11082283 |doi= 10.1006/excr.2000.5037 }}
*{{cite journal | author=Baillat G, Gaillard S, Castets F, Monneron A |title=Interactions of phocein with nucleoside-diphosphate kinase, Eps15, and Dynamin I. |journal=J. Biol. Chem. |volume=277 |issue= 21 |pages= 18961-6 |year= 2002 |pmid= 11872741 |doi= 10.1074/jbc.M108818200 }}
*{{cite journal | author=Fournier HN, Dupé-Manet S, Bouvard D, ''et al.'' |title=Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha ) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement. |journal=J. Biol. Chem. |volume=277 |issue= 23 |pages= 20895-902 |year= 2002 |pmid= 11919189 |doi= 10.1074/jbc.M200200200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NT5E... {November 18, 2007 10:02:10 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:02:58 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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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 = 5'-nucleotidase, ecto (CD73)
| HGNCid = 8021
| Symbol = NT5E
| AltSymbols =; CD73; E5NT; NT; NT5; NTE; eN; eNT
| OMIM = 129190
| ECnumber =
| Homologene = 1895
| MGIid = 99782
| GeneAtlas_image1 = PBB_GE_NT5E_203939_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0008253 |text = 5'-nucleotidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016788 |text = hydrolase activity, acting on ester bonds}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006259 |text = DNA metabolic process}} {{GNF_GO|id=GO:0009166 |text = nucleotide catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4907
| Hs_Ensembl = ENSG00000135318
| Hs_RefseqProtein = NP_002517
| Hs_RefseqmRNA = NM_002526
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 86216528
| Hs_GenLoc_end = 86262215
| Hs_Uniprot = P21589
| Mm_EntrezGene = 23959
| Mm_Ensembl = ENSMUSG00000032420
| Mm_RefseqmRNA = NM_011851
| Mm_RefseqProtein = NP_035981
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 88125533
| Mm_GenLoc_end = 88169982
| Mm_Uniprot = Q0VEE0
}}
}}
'''5'-nucleotidase, ecto (CD73)''', also known as '''NT5E''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NT5E 5'-nucleotidase, ecto (CD73)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4907| 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 = Ecto-5-prime-nucleotidase (5-prime-ribonucleotide phosphohydrolase; EC 3.1.3.5) catalyzes the conversion at neutral pH of purine 5-prime mononucleotides to nucleosides, the preferred substrate being AMP. The enzyme consists of a dimer of 2 identical 70-kD subunits bound by a glycosyl phosphatidyl inositol linkage to the external face of the plasma membrane. The enzyme is used as a marker of lymphocyte differentiation. Consequently, a deficiency of NT5 occurs in a variety of immunodeficiency diseases (e.g., see MIM 102700, MIM 300300). Other forms of 5-prime nucleotidase exist in the cytoplasm and lysosomes and can be distinguished from ecto-NT5 by their substrate affinities, requirement for divalent magnesium ion, activation by ATP, and inhibition by inorganic phosphate.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: NT5E 5'-nucleotidase, ecto (CD73)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4907| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Resta R, Thompson LF |title=T cell signalling through CD73. |journal=Cell. Signal. |volume=9 |issue= 2 |pages= 131-9 |year= 1997 |pmid= 9113412 |doi= }}
*{{cite journal | author=Kirchhoff C, Hale G |title=Cell-to-cell transfer of glycosylphosphatidylinositol-anchored membrane proteins during sperm maturation. |journal=Mol. Hum. Reprod. |volume=2 |issue= 3 |pages= 177-84 |year= 1997 |pmid= 9238677 |doi= }}
*{{cite journal | author=Resta R, Yamashita Y, Thompson LF |title=Ecto-enzyme and signaling functions of lymphocyte CD73. |journal=Immunol. Rev. |volume=161 |issue= |pages= 95-109 |year= 1998 |pmid= 9553767 |doi= }}
*{{cite journal | author=Rosi F, Carlucci F, Marinello E, Tabucchi A |title=Ecto-5'-nucleotidase in B-cell chronic lymphocytic leukemia. |journal=Biomed. Pharmacother. |volume=56 |issue= 2 |pages= 100-4 |year= 2002 |pmid= 12000134 |doi= }}
*{{cite journal | author=Babiychuk EB, Draeger A |title=Regulation of ecto-5'-nucleotidase activity via Ca2+-dependent, annexin 2-mediated membrane rearrangement? |journal=Biochem. Soc. Trans. |volume=34 |issue= Pt 3 |pages= 374-6 |year= 2006 |pmid= 16709165 |doi= 10.1042/BST0340374 }}
*{{cite journal | author=Stefanovic V, Mandel P, Rosenberg A |title=Ecto-5'-nucleotidase of intact cultured C6 rat glioma cells. |journal=J. Biol. Chem. |volume=251 |issue= 13 |pages= 3900-5 |year= 1976 |pmid= 819433 |doi= }}
*{{cite journal | author=Misumi Y, Ogata S, Ohkubo K, ''et al.'' |title=Primary structure of human placental 5'-nucleotidase and identification of the glycolipid anchor in the mature form. |journal=Eur. J. Biochem. |volume=191 |issue= 3 |pages= 563-9 |year= 1990 |pmid= 2129526 |doi= }}
*{{cite journal | author=Thomson LF, Ruedi JM, Glass A, ''et al.'' |title=Production and characterization of monoclonal antibodies to the glycosyl phosphatidylinositol-anchored lymphocyte differentiation antigen ecto-5'-nucleotidase (CD73). |journal=Tissue Antigens |volume=35 |issue= 1 |pages= 9-19 |year= 1990 |pmid= 2137649 |doi= }}
*{{cite journal | author=Klemens MR, Sherman WR, Holmberg NJ, ''et al.'' |title=Characterization of soluble vs membrane-bound human placental 5'-nucleotidase. |journal=Biochem. Biophys. Res. Commun. |volume=172 |issue= 3 |pages= 1371-7 |year= 1990 |pmid= 2173922 |doi= }}
*{{cite journal | author=Boyle JM, Hey Y, Guerts van Kessel A, Fox M |title=Assignment of ecto-5'-nucleotidase to human chromosome 6. |journal=Hum. Genet. |volume=81 |issue= 1 |pages= 88-92 |year= 1989 |pmid= 2848759 |doi= }}
*{{cite journal | author=Vlahović P, Stefanović V |title=Effect of dopamine on ecto-5'-nucleotidase expression in human glomerular mesangial cells. |journal=Archives internationales de physiologie, de biochimie et de biophysique |volume=102 |issue= 3 |pages= 171-3 |year= 1995 |pmid= 8000038 |doi= }}
*{{cite journal | author=Hansen KR, Resta R, Webb CF, Thompson LF |title=Isolation and characterization of the promoter of the human 5'-nucleotidase (CD73)-encoding gene. |journal=Gene |volume=167 |issue= 1-2 |pages= 307-12 |year= 1996 |pmid= 8566797 |doi= }}
*{{cite journal | author=Airas L, Jalkanen S |title=CD73 mediates adhesion of B cells to follicular dendritic cells. |journal=Blood |volume=88 |issue= 5 |pages= 1755-64 |year= 1996 |pmid= 8781432 |doi= }}
*{{cite journal | author=Airas L, Niemelä J, Salmi M, ''et al.'' |title=Differential regulation and function of CD73, a glycosyl-phosphatidylinositol-linked 70-kD adhesion molecule, on lymphocytes and endothelial cells. |journal=J. Cell Biol. |volume=136 |issue= 2 |pages= 421-31 |year= 1997 |pmid= 9015312 |doi= }}
*{{cite journal | author=Strohmeier GR, Lencer WI, Patapoff TW, ''et al.'' |title=Surface expression, polarization, and functional significance of CD73 in human intestinal epithelia. |journal=J. Clin. Invest. |volume=99 |issue= 11 |pages= 2588-601 |year= 1997 |pmid= 9169488 |doi= }}
*{{cite journal | author=Aumüller G, Renneberg H, Schiemann PJ, ''et al.'' |title=The role of apocrine released proteins in the post-testicular regulation of human sperm function. |journal=Adv. Exp. Med. Biol. |volume=424 |issue= |pages= 193-219 |year= 1998 |pmid= 9361795 |doi= }}
*{{cite journal | author=Rosi F, Agostinho AB, Carlucci F, ''et al.'' |title=Behaviour of human lymphocytic isoenzymes of 5'-nucleotidase. |journal=Life Sci. |volume=62 |issue= 25 |pages= 2257-66 |year= 1998 |pmid= 9651114 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NTF3... {November 18, 2007 10:02:58 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:03:33 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_NTF3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1b8k.
| PDB = {{PDB2|1b8k}}, {{PDB2|1bnd}}, {{PDB2|1nt3}}
| Name = Neurotrophin 3
| HGNCid = 8023
| Symbol = NTF3
| AltSymbols =; NT3; HDNF; MGC129711; NGF-2; NGF2
| OMIM = 162660
| ECnumber =
| Homologene = 1896
| MGIid = 97380
| GeneAtlas_image1 = PBB_GE_NTF3_206706_at_tn.png
| Function = {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0016023 |text = cytoplasmic membrane-bound vesicle}}
| Process = {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007274 |text = neuromuscular synaptic transmission}} {{GNF_GO|id=GO:0007403 |text = glial cell fate determination}} {{GNF_GO|id=GO:0007411 |text = axon guidance}} {{GNF_GO|id=GO:0007420 |text = brain development}} {{GNF_GO|id=GO:0007422 |text = peripheral nervous system development}} {{GNF_GO|id=GO:0008544 |text = epidermis development}} {{GNF_GO|id=GO:0021675 |text = nerve development}} {{GNF_GO|id=GO:0042490 |text = mechanoreceptor differentiation}} {{GNF_GO|id=GO:0043523 |text = regulation of neuron apoptosis}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0048484 |text = enteric nervous system development}} {{GNF_GO|id=GO:0048699 |text = generation of neurons}} {{GNF_GO|id=GO:0051145 |text = smooth muscle cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4908
| Hs_Ensembl = ENSG00000185652
| Hs_RefseqProtein = NP_002518
| Hs_RefseqmRNA = NM_002527
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 5473527
| Hs_GenLoc_end = 5474725
| Hs_Uniprot = P20783
| Mm_EntrezGene = 18205
| Mm_Ensembl = ENSMUSG00000049107
| Mm_RefseqmRNA = NM_008742
| Mm_RefseqProtein = NP_032768
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 126067031
| Mm_GenLoc_end = 126130540
| Mm_Uniprot = Q3V1A4
}}
}}
'''Neurotrophin 3''', also known as '''NTF3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NTF3 neurotrophin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4908| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.<ref name="entrez">{{cite web | title = Entrez Gene: NTF3 neurotrophin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4908| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kalcheim C, Carmeli C, Rosenthal A |title=Neurotrophin 3 is a mitogen for cultured neural crest cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 5 |pages= 1661-5 |year= 1992 |pmid= 1542658 |doi= }}
*{{cite journal | author=Maisonpierre PC, Le Beau MM, Espinosa R, ''et al.'' |title=Human and rat brain-derived neurotrophic factor and neurotrophin-3: gene structures, distributions, and chromosomal localizations. |journal=Genomics |volume=10 |issue= 3 |pages= 558-68 |year= 1991 |pmid= 1889806 |doi= }}
*{{cite journal | author=Ozçelik T, Rosenthal A, Francke U |title=Chromosomal mapping of brain-derived neurotrophic factor and neurotrophin-3 genes in man and mouse. |journal=Genomics |volume=10 |issue= 3 |pages= 569-75 |year= 1991 |pmid= 1889807 |doi= }}
*{{cite journal | author=Hallböök F, Ibáñez CF, Persson H |title=Evolutionary studies of the nerve growth factor family reveal a novel member abundantly expressed in Xenopus ovary. |journal=Neuron |volume=6 |issue= 5 |pages= 845-58 |year= 1991 |pmid= 2025430 |doi= }}
*{{cite journal | author=Jones KR, Reichardt LF |title=Molecular cloning of a human gene that is a member of the nerve growth factor family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 20 |pages= 8060-4 |year= 1990 |pmid= 2236018 |doi= }}
*{{cite journal | author=Rosenthal A, Goeddel DV, Nguyen T, ''et al.'' |title=Primary structure and biological activity of a novel human neurotrophic factor. |journal=Neuron |volume=4 |issue= 5 |pages= 767-73 |year= 1990 |pmid= 2344409 |doi= }}
*{{cite journal | author=Kaisho Y, Yoshimura K, Nakahama K |title=Cloning and expression of a cDNA encoding a novel human neurotrophic factor. |journal=FEBS Lett. |volume=266 |issue= 1-2 |pages= 187-91 |year= 1990 |pmid= 2365067 |doi= }}
*{{cite journal | author=Ernfors P, Lee KF, Kucera J, Jaenisch R |title=Lack of neurotrophin-3 leads to deficiencies in the peripheral nervous system and loss of limb proprioceptive afferents. |journal=Cell |volume=77 |issue= 4 |pages= 503-12 |year= 1994 |pmid= 7514502 |doi= }}
*{{cite journal | author=Robinson RC, Radziejewski C, Stuart DI, Jones EY |title=Structure of the brain-derived neurotrophic factor/neurotrophin 3 heterodimer. |journal=Biochemistry |volume=34 |issue= 13 |pages= 4139-46 |year= 1995 |pmid= 7703225 |doi= }}
*{{cite journal | author=Hattori M, Nanko S |title=Association of neurotrophin-3 gene variant with severe forms of schizophrenia. |journal=Biochem. Biophys. Res. Commun. |volume=209 |issue= 2 |pages= 513-8 |year= 1995 |pmid= 7733919 |doi= 10.1006/bbrc.1995.1531 }}
*{{cite journal | author=Tessarollo L, Vogel KS, Palko ME, ''et al.'' |title=Targeted mutation in the neurotrophin-3 gene results in loss of muscle sensory neurons. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 25 |pages= 11844-8 |year= 1995 |pmid= 7991545 |doi= }}
*{{cite journal | author=Rydén M, Ibáñez CF |title=Binding of neurotrophin-3 to p75LNGFR, TrkA, and TrkB mediated by a single functional epitope distinct from that recognized by trkC. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5623-7 |year= 1996 |pmid= 8621424 |doi= }}
*{{cite journal | author=Hui JO, Le J, Katta V, ''et al.'' |title=Human neurotrophin-3: a one-step peptide mapping method and complete disulfide characterization of the recombinant protein. |journal=J. Protein Chem. |volume=15 |issue= 4 |pages= 351-8 |year= 1996 |pmid= 8819011 |doi= }}
*{{cite journal | author=Donovan MJ, Hahn R, Tessarollo L, Hempstead BL |title=Identification of an essential nonneuronal function of neurotrophin 3 in mammalian cardiac development. |journal=Nat. Genet. |volume=14 |issue= 2 |pages= 210-3 |year= 1996 |pmid= 8841198 |doi= 10.1038/ng1096-210 }}
*{{cite journal | author=Arinami T, Takekoshi K, Itokawa M, ''et al.'' |title=Failure to find associations of the CA repeat polymorphism in the first intron and the Gly-63/Glu-63 polymorphism of the neurotrophin-3 gene with schizophrenia. |journal=Psychiatr. Genet. |volume=6 |issue= 1 |pages= 13-5 |year= 1996 |pmid= 8925252 |doi= }}
*{{cite journal | author=Urfer R, Tsoulfas P, O'Connell L, ''et al.'' |title=High resolution mapping of the binding site of TrkA for nerve growth factor and TrkC for neurotrophin-3 on the second immunoglobulin-like domain of the Trk receptors. |journal=J. Biol. Chem. |volume=273 |issue= 10 |pages= 5829-40 |year= 1998 |pmid= 9488719 |doi= }}
*{{cite journal | author=Suenaga M, Ohmae H, Tsuji S, ''et al.'' |title=Renaturation of recombinant human neurotrophin-3 from inclusion bodies using a suppressor agent of aggregation. |journal=Biotechnol. Appl. Biochem. |volume=28 ( Pt 2) |issue= |pages= 119-24 |year= 1998 |pmid= 9756741 |doi= }}
*{{cite journal | author=Hochhaus F, Koehne P, Schäper C, ''et al.'' |title=Elevated nerve growth factor and neurotrophin-3 levels in cerebrospinal fluid of children with hydrocephalus. |journal=BMC pediatrics |volume=1 |issue= |pages= 2 |year= 2003 |pmid= 11580868 |doi= }}
*{{cite journal | author=Kobayashi H, Gleich GJ, Butterfield JH, Kita H |title=Human eosinophils produce neurotrophins and secrete nerve growth factor on immunologic stimuli. |journal=Blood |volume=99 |issue= 6 |pages= 2214-20 |year= 2002 |pmid= 11877300 |doi= }}
*{{cite journal | author=Hattori M, Kunugi H, Akahane A, ''et al.'' |title=Novel polymorphisms in the promoter region of the neurotrophin-3 gene and their associations with schizophrenia. |journal=Am. J. Med. Genet. |volume=114 |issue= 3 |pages= 304-9 |year= 2002 |pmid= 11920853 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on OPRD1... {November 18, 2007 10:03:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:03:58 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 = Opioid receptor, delta 1
| HGNCid = 8153
| Symbol = OPRD1
| AltSymbols =; OPRD
| OMIM = 165195
| ECnumber =
| Homologene = 20252
| MGIid = 97438
| GeneAtlas_image1 = PBB_GE_OPRD1_207792_at_tn.png
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004986 |text = delta-opioid receptor activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007187 |text = G-protein signaling, coupled to cyclic nucleotide second messenger}} {{GNF_GO|id=GO:0007193 |text = G-protein signaling, adenylate cyclase inhibiting pathway}} {{GNF_GO|id=GO:0007218 |text = neuropeptide signaling pathway}} {{GNF_GO|id=GO:0007600 |text = sensory perception}} {{GNF_GO|id=GO:0008344 |text = adult locomotory behavior}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4985
| Hs_Ensembl = ENSG00000116329
| Hs_RefseqProtein = NP_000902
| Hs_RefseqmRNA = NM_000911
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 29011241
| Hs_GenLoc_end = 29062795
| Hs_Uniprot = P41143
| Mm_EntrezGene = 18386
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_973497
| Mm_RefseqProtein = XP_978591
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Opioid receptor, delta 1''', also known as '''OPRD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: OPRD1 opioid receptor, delta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4985| 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=Narita M, Funada M, Suzuki T |title=Regulations of opioid dependence by opioid receptor types. |journal=Pharmacol. Ther. |volume=89 |issue= 1 |pages= 1-15 |year= 2001 |pmid= 11316510 |doi= }}
*{{cite journal | author=Evans CJ, Keith DE, Morrison H, ''et al.'' |title=Cloning of a delta opioid receptor by functional expression. |journal=Science |volume=258 |issue= 5090 |pages= 1952-5 |year= 1993 |pmid= 1335167 |doi= }}
*{{cite journal | author=Offermanns S, Schultz G, Rosenthal W |title=Evidence for opioid receptor-mediated activation of the G-proteins, Go and Gi2, in membranes of neuroblastoma x glioma (NG108-15) hybrid cells. |journal=J. Biol. Chem. |volume=266 |issue= 6 |pages= 3365-8 |year= 1991 |pmid= 1671672 |doi= }}
*{{cite journal | author=Simonin F, Befort K, Gavériaux-Ruff C, ''et al.'' |title=The human delta-opioid receptor: genomic organization, cDNA cloning, functional expression, and distribution in human brain. |journal=Mol. Pharmacol. |volume=46 |issue= 6 |pages= 1015-21 |year= 1995 |pmid= 7808419 |doi= }}
*{{cite journal | author=Befort K, Mattéi MG, Roeckel N, Kieffer B |title=Chromosomal localization of the delta opioid receptor gene to human 1p34.3-p36.1 and mouse 4D bands by in situ hybridization. |journal=Genomics |volume=20 |issue= 1 |pages= 143-5 |year= 1994 |pmid= 8020949 |doi= }}
*{{cite journal | author=Knapp RJ, Malatynska E, Fang L, ''et al.'' |title=Identification of a human delta opioid receptor: cloning and expression. |journal=Life Sci. |volume=54 |issue= 25 |pages= PL463-9 |year= 1994 |pmid= 8201839 |doi= }}
*{{cite journal | author=Georgoussi Z, Carr C, Milligan G |title=Direct measurements of in situ interactions of rat brain opioid receptors with the guanine nucleotide-binding protein Go. |journal=Mol. Pharmacol. |volume=44 |issue= 1 |pages= 62-9 |year= 1993 |pmid= 8393523 |doi= }}
*{{cite journal | author=Bzdega T, Chin H, Kim H, ''et al.'' |title=Regional expression and chromosomal localization of the delta opiate receptor gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 20 |pages= 9305-9 |year= 1993 |pmid= 8415697 |doi= }}
*{{cite journal | author=Ho MK, Wong YH |title=Functional role of amino-terminal serine16 and serine27 of G alphaZ in receptor and effector coupling. |journal=J. Neurochem. |volume=68 |issue= 6 |pages= 2514-22 |year= 1997 |pmid= 9166747 |doi= }}
*{{cite journal | author=Hedin KE, Bell MP, Kalli KR, ''et al.'' |title=Delta-opioid receptors expressed by Jurkat T cells enhance IL-2 secretion by increasing AP-1 complexes and activity of the NF-AT/AP-1-binding promoter element. |journal=J. Immunol. |volume=159 |issue= 11 |pages= 5431-40 |year= 1998 |pmid= 9548483 |doi= }}
*{{cite journal | author=Jordan BA, Devi LA |title=G-protein-coupled receptor heterodimerization modulates receptor function. |journal=Nature |volume=399 |issue= 6737 |pages= 697-700 |year= 1999 |pmid= 10385123 |doi= 10.1038/21441 }}
*{{cite journal | author=Petaja-Repo UE, Hogue M, Laperriere A, ''et al.'' |title=Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor. |journal=J. Biol. Chem. |volume=275 |issue= 18 |pages= 13727-36 |year= 2000 |pmid= 10788493 |doi= }}
*{{cite journal | author=Gelernter J, Kranzler HR |title=Variant detection at the delta opioid receptor (OPRD1) locus and population genetics of a novel variant affecting protein sequence. |journal=Hum. Genet. |volume=107 |issue= 1 |pages= 86-8 |year= 2000 |pmid= 10982041 |doi= }}
*{{cite journal | author=Guo J, Wu Y, Zhang W, ''et al.'' |title=Identification of G protein-coupled receptor kinase 2 phosphorylation sites responsible for agonist-stimulated delta-opioid receptor phosphorylation. |journal=Mol. Pharmacol. |volume=58 |issue= 5 |pages= 1050-6 |year= 2000 |pmid= 11040053 |doi= }}
*{{cite journal | author=Gomes I, Jordan BA, Gupta A, ''et al.'' |title=Heterodimerization of mu and delta opioid receptors: A role in opiate synergy. |journal=J. Neurosci. |volume=20 |issue= 22 |pages= RC110 |year= 2001 |pmid= 11069979 |doi= }}
*{{cite journal | author=Xu W, Chen C, Huang P, ''et al.'' |title=The conserved cysteine 7.38 residue is differentially accessible in the binding-site crevices of the mu, delta, and kappa opioid receptors. |journal=Biochemistry |volume=39 |issue= 45 |pages= 13904-15 |year= 2000 |pmid= 11076532 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Saeed RW, Stefano GB, Murga JD, ''et al.'' |title=Expression of functional delta opioid receptors in vascular smooth muscle. |journal=Int. J. Mol. Med. |volume=6 |issue= 6 |pages= 673-7 |year= 2001 |pmid= 11078827 |doi= }}
*{{cite journal | author=Xiang B, Yu GH, Guo J, ''et al.'' |title=Heterologous activation of protein kinase C stimulates phosphorylation of delta-opioid receptor at serine 344, resulting in beta-arrestin- and clathrin-mediated receptor internalization. |journal=J. Biol. Chem. |volume=276 |issue= 7 |pages= 4709-16 |year= 2001 |pmid= 11085981 |doi= 10.1074/jbc.M006187200 }}
*{{cite journal | author=Yeo A, Samways DS, Fowler CE, ''et al.'' |title=Coincident signalling between the Gi/Go-coupled delta-opioid receptor and the Gq-coupled m3 muscarinic receptor at the level of intracellular free calcium in SH-SY5Y cells. |journal=J. Neurochem. |volume=76 |issue= 6 |pages= 1688-700 |year= 2001 |pmid= 11259487 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on P2RX1... {November 18, 2007 10:03:58 PM PST}
- SEARCH REDIRECT: Control Box Found: P2RX1 {November 18, 2007 10:04:24 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:04:27 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:04:27 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:04:27 PM PST}
- UPDATED: Updated protein page: P2RX1 {November 18, 2007 10:04:33 PM PST}
- INFO: Beginning work on PCBP1... {November 18, 2007 10:04:33 PM PST}
- SEARCH REDIRECT: Control Box Found: PCBP1 {November 18, 2007 10:04:59 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:05:00 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:05:00 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:05:00 PM PST}
- UPDATED: Updated protein page: PCBP1 {November 18, 2007 10:05:06 PM PST}
- INFO: Beginning work on PCBP2... {November 18, 2007 10:05:06 PM PST}
- SEARCH REDIRECT: Control Box Found: PCBP2 {November 18, 2007 10:09:08 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:09:10 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:09:10 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:09:10 PM PST}
- UPDATED: Updated protein page: PCBP2 {November 18, 2007 10:09:16 PM PST}
- INFO: Beginning work on PPP2R4... {November 18, 2007 10:09:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:09:48 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_PPP2R4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2g62.
| PDB = {{PDB2|2g62}}, {{PDB2|2hv6}}, {{PDB2|2hv7}}, {{PDB2|2ixm}}
| Name = Protein phosphatase 2A activator, regulatory subunit 4
| HGNCid = 9308
| Symbol = PPP2R4
| AltSymbols =; MGC2184; PP2A; PR53; PTPA
| OMIM = 600756
| ECnumber =
| Homologene = 6149
| MGIid = 1346006
| GeneAtlas_image1 = PBB_GE_PPP2R4_208874_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_PPP2R4_206452_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_PPP2R4_216105_x_at_tn.png
| Function = {{GNF_GO|id=GO:0008160 |text = protein tyrosine phosphatase activator activity}} {{GNF_GO|id=GO:0008601 |text = protein phosphatase type 2A regulator activity}} {{GNF_GO|id=GO:0019211 |text = phosphatase activator activity}} {{GNF_GO|id=GO:0046982 |text = protein heterodimerization activity}}
| Component = {{GNF_GO|id=GO:0000159 |text = protein phosphatase type 2A complex}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5524
| Hs_Ensembl = ENSG00000119383
| Hs_RefseqProtein = NP_066954
| Hs_RefseqmRNA = NM_021131
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 130913050
| Hs_GenLoc_end = 130951046
| Hs_Uniprot = Q15257
| Mm_EntrezGene = 110854
| Mm_Ensembl = ENSMUSG00000039515
| Mm_RefseqmRNA = NM_138748
| Mm_RefseqProtein = NP_620087
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 30238059
| Mm_GenLoc_end = 30269813
| Mm_Uniprot = Q543N6
}}
}}
'''Protein phosphatase 2A activator, regulatory subunit 4''', also known as '''PPP2R4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PPP2R4 protein phosphatase 2A activator, regulatory subunit 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5524| 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 = Protein phosphatase 2A is one of the four major Ser/Thr phosphatases and is implicated in the negative control of cell growth and division. Protein phosphatase 2A holoenzymes are heterotrimeric proteins composed of a structural subunit A, a catalytic subunit C, and a regulatory subunit B. The regulatory subunit is encoded by a diverse set of genes that have been grouped into the B/PR55, B'/PR61, and B''/PR72 families. These different regulatory subunits confer distinct enzymatic specificities and intracellular localizations to the holozenzyme. The product of this gene belongs to the B' family. This gene encodes a specific phosphotyrosyl phosphatase activator of the dimeric form of protein phosphatase 2A. Alternative splicing results in multiple transcript variants encoding different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: PPP2R4 protein phosphatase 2A activator, regulatory subunit 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5524| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Andersen JL, Planelles V |title=The role of Vpr in HIV-1 pathogenesis. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 43-51 |year= 2005 |pmid= 15638722 |doi= }}
*{{cite journal | author=Le Rouzic E, Benichou S |title=The Vpr protein from HIV-1: distinct roles along the viral life cycle. |journal=Retrovirology |volume=2 |issue= |pages= 11 |year= 2006 |pmid= 15725353 |doi= 10.1186/1742-4690-2-11 }}
*{{cite journal | author=Zhao RY, Elder RT |title=Viral infections and cell cycle G2/M regulation. |journal=Cell Res. |volume=15 |issue= 3 |pages= 143-9 |year= 2005 |pmid= 15780175 |doi= 10.1038/sj.cr.7290279 }}
*{{cite journal | author=Zhao RY, Bukrinsky M, Elder RT |title=HIV-1 viral protein R (Vpr) & host cellular responses. |journal=Indian J. Med. Res. |volume=121 |issue= 4 |pages= 270-86 |year= 2005 |pmid= 15817944 |doi= }}
*{{cite journal | author=Soprano KJ, Purev E, Vuocolo S, Soprano DR |title=Rb2/p130 and protein phosphatase 2A: key mediators of ovarian carcinoma cell growth suppression by all-trans retinoic acid. |journal=Oncogene |volume=25 |issue= 38 |pages= 5315-25 |year= 2006 |pmid= 16936753 |doi= 10.1038/sj.onc.1209679 }}
*{{cite journal | author=Jakes S, Mellgren RL, Schlender KK |title=Isolation and characterization of an inhibitor-sensitive and a polycation-stimulated protein phosphatase from rat liver nuclei. |journal=Biochim. Biophys. Acta |volume=888 |issue= 1 |pages= 135-42 |year= 1986 |pmid= 3017441 |doi= }}
*{{cite journal | author=Turowski P, Fernandez A, Favre B, ''et al.'' |title=Differential methylation and altered conformation of cytoplasmic and nuclear forms of protein phosphatase 2A during cell cycle progression. |journal=J. Cell Biol. |volume=129 |issue= 2 |pages= 397-410 |year= 1995 |pmid= 7721943 |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=Cayla X, Van Hoof C, Bosch M, ''et al.'' |title=Molecular cloning, expression, and characterization of PTPA, a protein that activates the tyrosyl phosphatase activity of protein phosphatase 2A. |journal=J. Biol. Chem. |volume=269 |issue= 22 |pages= 15668-75 |year= 1994 |pmid= 8195217 |doi= }}
*{{cite journal | author=Van Hoof C, Aly MS, Garcia A, ''et al.'' |title=Structure and chromosomal localization of the human gene of the phosphotyrosyl phosphatase activator (PTPA) of protein phosphatase 2A. |journal=Genomics |volume=28 |issue= 2 |pages= 261-72 |year= 1996 |pmid= 8530035 |doi= 10.1006/geno.1995.1140 }}
*{{cite journal | author=Okamoto K, Kamibayashi C, Serrano M, ''et al.'' |title=p53-dependent association between cyclin G and the B' subunit of protein phosphatase 2A. |journal=Mol. Cell. Biol. |volume=16 |issue= 11 |pages= 6593-602 |year= 1996 |pmid= 8887688 |doi= }}
*{{cite journal | author=Tung HY, De Rocquigny H, Zhao LJ, ''et al.'' |title=Direct activation of protein phosphatase-2A0 by HIV-1 encoded protein complex NCp7:vpr. |journal=FEBS Lett. |volume=401 |issue= 2-3 |pages= 197-201 |year= 1997 |pmid= 9013886 |doi= }}
*{{cite journal | author=Hériché JK, Lebrin F, Rabilloud T, ''et al.'' |title=Regulation of protein phosphatase 2A by direct interaction with casein kinase 2alpha. |journal=Science |volume=276 |issue= 5314 |pages= 952-5 |year= 1997 |pmid= 9139659 |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=Ruediger R, Brewis N, Ohst K, Walter G |title=Increasing the ratio of PP2A core enzyme to holoenzyme inhibits Tat-stimulated HIV-1 transcription and virus production. |journal=Virology |volume=238 |issue= 2 |pages= 432-43 |year= 1998 |pmid= 9400615 |doi= 10.1006/viro.1997.8873 }}
*{{cite journal | author=Ogris E, Du X, Nelson KC, ''et al.'' |title=A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A. |journal=J. Biol. Chem. |volume=274 |issue= 20 |pages= 14382-91 |year= 1999 |pmid= 10318862 |doi= }}
*{{cite journal | author=Janssens V, Van Hoof C, De Baere I, ''et al.'' |title=Functional analysis of the promoter region of the human phosphotyrosine phosphatase activator gene: Yin Yang 1 is essential for core promoter activity. |journal=Biochem. J. |volume=344 Pt 3 |issue= |pages= 755-63 |year= 2000 |pmid= 10585862 |doi= }}
*{{cite journal | author=Janssens V, van Hoof C, Martens E, ''et al.'' |title=Identification and characterization of alternative splice products encoded by the human phosphotyrosyl phosphatase activator gene. |journal=Eur. J. Biochem. |volume=267 |issue= 14 |pages= 4406-13 |year= 2000 |pmid= 10880964 |doi= }}
*{{cite journal | author=Hrimech M, Yao XJ, Branton PE, Cohen EA |title=Human immunodeficiency virus type 1 Vpr-mediated G(2) cell cycle arrest: Vpr interferes with cell cycle signaling cascades by interacting with the B subunit of serine/threonine protein phosphatase 2A. |journal=EMBO J. |volume=19 |issue= 15 |pages= 3956-67 |year= 2000 |pmid= 10921877 |doi= 10.1093/emboj/19.15.3956 }}
*{{cite journal | author=Elder RT, Yu M, Chen M, ''et al.'' |title=HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25. |journal=Virology |volume=287 |issue= 2 |pages= 359-70 |year= 2001 |pmid= 11531413 |doi= 10.1006/viro.2001.1007 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMB2... {November 18, 2007 10:09:48 PM PST}
- SEARCH REDIRECT: Control Box Found: PSMB2 {November 18, 2007 10:10:25 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:10:26 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:10:26 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:10:26 PM PST}
- UPDATED: Updated protein page: PSMB2 {November 18, 2007 10:10:33 PM PST}
- INFO: Beginning work on PSMD12... {November 18, 2007 10:11:44 PM PST}
- REDIRECT: Protein Redirected to: PSMD12 {November 18, 2007 10:12:04 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:12:07 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:12:07 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:12:07 PM PST}
- UPDATED: Updated protein page: PSMD12 {November 18, 2007 10:12:13 PM PST}
- INFO: Beginning work on PSMD8... {November 18, 2007 10:10:33 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:11:44 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Proteasome (prosome, macropain) 26S subunit, non-ATPase, 8
| HGNCid = 9566
| Symbol = PSMD8
| AltSymbols =; HIP6; HYPF; MGC1660; Nin1p; S14; p31
| OMIM =
| ECnumber =
| Homologene = 37686
| MGIid = 1888669
| GeneAtlas_image1 = PBB_GE_PSMD8_200820_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSMD8_gnf1h08609_s_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005838 |text = proteasome regulatory particle (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5714
| Hs_Ensembl = ENSG00000099341
| Hs_RefseqProtein = NP_002803
| Hs_RefseqmRNA = NM_002812
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 43557061
| Hs_GenLoc_end = 43566303
| Hs_Uniprot = P48556
| Mm_EntrezGene = 57296
| Mm_Ensembl = ENSMUSG00000030591
| Mm_RefseqmRNA = XM_001001968
| Mm_RefseqProtein = XP_001001968
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 28883015
| Mm_GenLoc_end = 28889291
| Mm_Uniprot = Q3TG45
}}
}}
'''Proteasome (prosome, macropain) 26S subunit, non-ATPase, 8''', also known as '''PSMD8''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMD8 proteasome (prosome, macropain) 26S subunit, non-ATPase, 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5714| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a non-ATPase subunit of the 19S regulator. A pseudogene has been identified on chromosome 1.<ref name="entrez">{{cite web | title = Entrez Gene: PSMD8 proteasome (prosome, macropain) 26S subunit, non-ATPase, 8| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5714| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue= |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
*{{cite journal | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi= }}
*{{cite journal | author=Kominami K, DeMartino GN, Moomaw CR, ''et al.'' |title=Nin1p, a regulatory subunit of the 26S proteasome, is necessary for activation of Cdc28p kinase of Saccharomyces cerevisiae. |journal=EMBO J. |volume=14 |issue= 13 |pages= 3105-15 |year= 1995 |pmid= 7621825 |doi= }}
*{{cite journal | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi= }}
*{{cite journal | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi= }}
*{{cite journal | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
*{{cite journal | author=Mulder LC, Muesing MA |title=Degradation of HIV-1 integrase by the N-end rule pathway. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29749-53 |year= 2000 |pmid= 10893419 |doi= 10.1074/jbc.M004670200 }}
*{{cite journal | author=Li T, Duan W, Yang H, ''et al.'' |title=Identification of two proteins, S14 and UIP1, that interact with UCH37. |journal=FEBS Lett. |volume=488 |issue= 3 |pages= 201-5 |year= 2001 |pmid= 11163772 |doi= }}
*{{cite journal | author=Sheehy AM, Gaddis NC, Choi JD, Malim MH |title=Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. |journal=Nature |volume=418 |issue= 6898 |pages= 646-50 |year= 2002 |pmid= 12167863 |doi= 10.1038/nature00939 }}
*{{cite journal | author=Huang X, Seifert U, Salzmann U, ''et al.'' |title=The RTP site shared by the HIV-1 Tat protein and the 11S regulator subunit alpha is crucial for their effects on proteasome function including antigen processing. |journal=J. Mol. Biol. |volume=323 |issue= 4 |pages= 771-82 |year= 2002 |pmid= 12419264 |doi= }}
*{{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=Gaddis NC, Chertova E, Sheehy AM, ''et al.'' |title=Comprehensive investigation of the molecular defect in vif-deficient human immunodeficiency virus type 1 virions. |journal=J. Virol. |volume=77 |issue= 10 |pages= 5810-20 |year= 2003 |pmid= 12719574 |doi= }}
*{{cite journal | author=Lecossier D, Bouchonnet F, Clavel F, Hance AJ |title=Hypermutation of HIV-1 DNA in the absence of the Vif protein. |journal=Science |volume=300 |issue= 5622 |pages= 1112 |year= 2003 |pmid= 12750511 |doi= 10.1126/science.1083338 }}
*{{cite journal | author=Zhang H, Yang B, Pomerantz RJ, ''et al.'' |title=The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA. |journal=Nature |volume=424 |issue= 6944 |pages= 94-8 |year= 2003 |pmid= 12808465 |doi= 10.1038/nature01707 }}
*{{cite journal | author=Mangeat B, Turelli P, Caron G, ''et al.'' |title=Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. |journal=Nature |volume=424 |issue= 6944 |pages= 99-103 |year= 2003 |pmid= 12808466 |doi= 10.1038/nature01709 }}
*{{cite journal | author=Harris RS, Bishop KN, Sheehy AM, ''et al.'' |title=DNA deamination mediates innate immunity to retroviral infection. |journal=Cell |volume=113 |issue= 6 |pages= 803-9 |year= 2003 |pmid= 12809610 |doi= }}
*{{cite journal | author=Harris RS, Sheehy AM, Craig HM, ''et al.'' |title=DNA deamination: not just a trigger for antibody diversification but also a mechanism for defense against retroviruses. |journal=Nat. Immunol. |volume=4 |issue= 7 |pages= 641-3 |year= 2003 |pmid= 12830140 |doi= 10.1038/ni0703-641 }}
*{{cite journal | author=Gu Y, Sundquist WI |title=Good to CU. |journal=Nature |volume=424 |issue= 6944 |pages= 21-2 |year= 2003 |pmid= 12840737 |doi= 10.1038/424021a }}
*{{cite journal | author=Mariani R, Chen D, Schröfelbauer B, ''et al.'' |title=Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif. |journal=Cell |volume=114 |issue= 1 |pages= 21-31 |year= 2003 |pmid= 12859895 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTPN2... {November 18, 2007 10:12:13 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 10:12:40 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_PTPN2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1l8k.
| PDB = {{PDB2|1l8k}}
| Name = Protein tyrosine phosphatase, non-receptor type 2
| HGNCid = 9650
| Symbol = PTPN2
| AltSymbols =; PTPT; TC-PTP; TCELLPTP; TCPTP
| OMIM = 176887
| ECnumber =
| Homologene = 7497
| MGIid = 97806
| Function = {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0008286 |text = insulin receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5771
| Hs_Ensembl =
| Hs_RefseqProtein = NP_002819
| Hs_RefseqmRNA = NM_002828
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 19255
| Mm_Ensembl = ENSMUSG00000024539
| Mm_RefseqmRNA = NM_008977
| Mm_RefseqProtein = NP_033003
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 67797358
| Mm_GenLoc_end = 67849964
| Mm_Uniprot = Q06180
}}
}}
'''Protein tyrosine phosphatase, non-receptor type 2''', also known as '''PTPN2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPN2 protein tyrosine phosphatase, non-receptor type 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5771| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. Members of the PTP family share a highly conserved catalytic motif, which is essential for the catalytic activity. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. Epidermal growth factor receptor and the adaptor protein Shc were reported to be substrates of this PTP, which suggested the roles in growth factor mediated cell signaling. Three alternatively spliced variants of this gene, which encode isoforms differing at their extreme C-termini, have been described. The different C-termini are thought to determine the substrate specificity, as well as the cellular localization of the isoforms. Two highly related but distinctly processed pseudogenes that localize to distinct chromosomes have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: PTPN2 protein tyrosine phosphatase, non-receptor type 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5771| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mosinger B, Tillmann U, Westphal H, Tremblay ML |title=Cloning and characterization of a mouse cDNA encoding a cytoplasmic protein-tyrosine-phosphatase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 2 |pages= 499-503 |year= 1992 |pmid= 1731319 |doi= }}
*{{cite journal | author=Swarup G, Kamatkar S, Radha V, Rema V |title=Molecular cloning and expression of a protein-tyrosine phosphatase showing homology with transcription factors Fos and Jun. |journal=FEBS Lett. |volume=280 |issue= 1 |pages= 65-9 |year= 1991 |pmid= 1849097 |doi= }}
*{{cite journal | author=Brown-Shimer S, Johnson KA, Lawrence JB, ''et al.'' |title=Molecular cloning and chromosome mapping of the human gene encoding protein phosphotyrosyl phosphatase 1B. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 13 |pages= 5148-52 |year= 1990 |pmid= 2164224 |doi= }}
*{{cite journal | author=Cool DE, Tonks NK, Charbonneau H, ''et al.'' |title=cDNA isolated from a human T-cell library encodes a member of the protein-tyrosine-phosphatase family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 14 |pages= 5257-61 |year= 1989 |pmid= 2546150 |doi= }}
*{{cite journal | author=Lorenzen JA, Dadabay CY, Fischer EH |title=COOH-terminal sequence motifs target the T cell protein tyrosine phosphatase to the ER and nucleus. |journal=J. Cell Biol. |volume=131 |issue= 3 |pages= 631-43 |year= 1995 |pmid= 7593185 |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=Johnson CV, Cool DE, Glaccum MB, ''et al.'' |title=Isolation and mapping of human T-cell protein tyrosine phosphatase sequences: localization of genes and pseudogenes discriminated using fluorescence hybridization with genomic versus cDNA probes. |journal=Genomics |volume=16 |issue= 3 |pages= 619-29 |year= 1993 |pmid= 8325634 |doi= 10.1006/geno.1993.1239 }}
*{{cite journal | author=Tiganis T, Flint AJ, Adam SA, Tonks NK |title=Association of the T-cell protein tyrosine phosphatase with nuclear import factor p97. |journal=J. Biol. Chem. |volume=272 |issue= 34 |pages= 21548-57 |year= 1997 |pmid= 9261175 |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=Tiganis T, Bennett AM, Ravichandran KS, Tonks NK |title=Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase. |journal=Mol. Cell. Biol. |volume=18 |issue= 3 |pages= 1622-34 |year= 1998 |pmid= 9488479 |doi= }}
*{{cite journal | author=Tiganis T, Kemp BE, Tonks NK |title=The protein-tyrosine phosphatase TCPTP regulates epidermal growth factor receptor-mediated and phosphatidylinositol 3-kinase-dependent signaling. |journal=J. Biol. Chem. |volume=274 |issue= 39 |pages= 27768-75 |year= 1999 |pmid= 10488121 |doi= }}
*{{cite journal | author=Aoki N, Matsuda T |title=A nuclear protein tyrosine phosphatase TC-PTP is a potential negative regulator of the PRL-mediated signaling pathway: dephosphorylation and deactivation of signal transducer and activator of transcription 5a and 5b by TC-PTP in nucleus. |journal=Mol. Endocrinol. |volume=16 |issue= 1 |pages= 58-69 |year= 2002 |pmid= 11773439 |doi= }}
*{{cite journal | author=Iversen LF, Moller KB, Pedersen AK, ''et al.'' |title=Structure determination of T cell protein-tyrosine phosphatase. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19982-90 |year= 2002 |pmid= 11907034 |doi= 10.1074/jbc.M200567200 }}
*{{cite journal | author=Simoncic PD, Lee-Loy A, Barber DL, ''et al.'' |title=The T cell protein tyrosine phosphatase is a negative regulator of janus family kinases 1 and 3. |journal=Curr. Biol. |volume=12 |issue= 6 |pages= 446-53 |year= 2002 |pmid= 11909529 |doi= }}
*{{cite journal | author=ten Hoeve J, de Jesus Ibarra-Sanchez M, Fu Y, ''et al.'' |title=Identification of a nuclear Stat1 protein tyrosine phosphatase. |journal=Mol. Cell. Biol. |volume=22 |issue= 16 |pages= 5662-8 |year= 2002 |pmid= 12138178 |doi= }}
*{{cite journal | author=Zhu W, Mustelin T, David M |title=Arginine methylation of STAT1 regulates its dephosphorylation by T cell protein tyrosine phosphatase. |journal=J. Biol. Chem. |volume=277 |issue= 39 |pages= 35787-90 |year= 2002 |pmid= 12171910 |doi= 10.1074/jbc.C200346200 }}
*{{cite journal | author=Yamamoto T, Sekine Y, Kashima K, ''et al.'' |title=The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation. |journal=Biochem. Biophys. Res. Commun. |volume=297 |issue= 4 |pages= 811-7 |year= 2002 |pmid= 12359225 |doi= }}
*{{cite journal | author=Gupta S, Radha V, Sudhakar Ch, Swarup G |title=A nuclear protein tyrosine phosphatase activates p53 and induces caspase-1-dependent apoptosis. |journal=FEBS Lett. |volume=532 |issue= 1-2 |pages= 61-6 |year= 2003 |pmid= 12459463 |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=Galic S, Klingler-Hoffmann M, Fodero-Tavoletti MT, ''et al.'' |title=Regulation of insulin receptor signaling by the protein tyrosine phosphatase TCPTP. |journal=Mol. Cell. Biol. |volume=23 |issue= 6 |pages= 2096-108 |year= 2003 |pmid= 12612081 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RPA2... {November 18, 2007 10:13:43 PM PST}
- SEARCH REDIRECT: Control Box Found: RPA2 {November 18, 2007 10:16:17 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:16:19 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:16:19 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:16:19 PM PST}
- UPDATED: Updated protein page: RPA2 {November 18, 2007 10:16:24 PM PST}
- INFO: Beginning work on UPF1... {November 18, 2007 10:12:40 PM PST}
- SEARCH REDIRECT: Control Box Found: UPF1 {November 18, 2007 10:13:32 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 10:13:34 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 10:13:34 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 10:13:34 PM PST}
- UPDATED: Updated protein page: UPF1 {November 18, 2007 10:13:43 PM PST}
end log.
