Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 22:47, 18 November 2007 (UTC)
[edit]Conflict: Ambiguous Proteins (2)
[edit]Proteins without matches (9)
[edit]Proteins with a High Potential Match (8)
[edit]Redirected Proteins (6)
[edit]Manual Inspection (Page not found) (19)
[edit]
Protein Status Grid - Date: 22:47, 18 November 2007 (UTC)
[edit]Vebose Log - Date: 22:47, 18 November 2007 (UTC)
[edit]- INFO: Beginning work on AIFM1... {November 18, 2007 2:34:02 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:34:48 PM PST}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_AIFM1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gv4.
| PDB = {{PDB2|1gv4}}, {{PDB2|1m6i}}
| Name = Apoptosis-inducing factor, mitochondrion-associated, 1
| HGNCid = 8768
| Symbol = AIFM1
| AltSymbols =; AIF; MGC111425; PDCD8
| OMIM = 300169
| ECnumber =
| Homologene = 3100
| MGIid = 1349419
| GeneAtlas_image1 = PBB_GE_AIFM1_205512_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0015036 |text = disulfide oxidoreductase activity}}
| Component = {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005792 |text = microsome}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006309 |text = DNA fragmentation during apoptosis}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0008630 |text = DNA damage response, signal transduction resulting in induction of apoptosis}} {{GNF_GO|id=GO:0045454 |text = cell redox homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9131
| Hs_Ensembl = ENSG00000156709
| Hs_RefseqProtein = NP_004199
| Hs_RefseqmRNA = NM_004208
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 129091018
| Hs_GenLoc_end = 129127489
| Hs_Uniprot = O95831
| Mm_EntrezGene = 26926
| Mm_Ensembl = ENSMUSG00000036932
| Mm_RefseqmRNA = NM_012019
| Mm_RefseqProtein = NP_036149
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 44719571
| Mm_GenLoc_end = 44758053
| Mm_Uniprot = Q1L6K5
}}
}}
'''Apoptosis-inducing factor, mitochondrion-associated, 1''', also known as '''AIFM1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AIFM1 apoptosis-inducing factor, mitochondrion-associated, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9131| 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 flavoprotein essential for nuclear disassembly in apoptotic cells that is found in the mitochondrial intermembrane space in healthy cells. Induction of apoptosis results in the translocation of this protein to the nucleus where it effects chromosome condensation and fragmentation. In addition, this gene product induces mitochondria to release the apoptogenic proteins cytochrome c and caspase-9. Three alternative transcripts encoding different isoforms have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: AIFM1 apoptosis-inducing factor, mitochondrion-associated, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9131| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Daugas E, Nochy D, Ravagnan L, ''et al.'' |title=Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis. |journal=FEBS Lett. |volume=476 |issue= 3 |pages= 118-23 |year= 2000 |pmid= 10913597 |doi= }}
*{{cite journal | author=Ferri KF, Jacotot E, Blanco J, ''et al.'' |title=Mitochondrial control of cell death induced by HIV-1-encoded proteins. |journal=Ann. N. Y. Acad. Sci. |volume=926 |issue= |pages= 149-64 |year= 2001 |pmid= 11193032 |doi= }}
*{{cite journal | author=Candé C, Cohen I, Daugas E, ''et al.'' |title=Apoptosis-inducing factor (AIF): a novel caspase-independent death effector released from mitochondria. |journal=Biochimie |volume=84 |issue= 2-3 |pages= 215-22 |year= 2002 |pmid= 12022952 |doi= }}
*{{cite journal | author=Castedo M, Perfettini JL, Andreau K, ''et al.'' |title=Mitochondrial apoptosis induced by the HIV-1 envelope. |journal=Ann. N. Y. Acad. Sci. |volume=1010 |issue= |pages= 19-28 |year= 2004 |pmid= 15033690 |doi= }}
*{{cite journal | author=Moon HS, Yang JS |title=Role of HIV Vpr as a regulator of apoptosis and an effector on bystander cells. |journal=Mol. Cells |volume=21 |issue= 1 |pages= 7-20 |year= 2006 |pmid= 16511342 |doi= }}
*{{cite journal | author=Glass L |title=Classification of biological networks by their qualitative dynamics. |journal=J. Theor. Biol. |volume=54 |issue= 1 |pages= 85-107 |year= 1976 |pmid= 1202295 |doi= }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi= }}
*{{cite journal | author=Susin SA, Zamzami N, Castedo M, ''et al.'' |title=The central executioner of apoptosis: multiple connections between protease activation and mitochondria in Fas/APO-1/CD95- and ceramide-induced apoptosis. |journal=J. Exp. Med. |volume=186 |issue= 1 |pages= 25-37 |year= 1997 |pmid= 9206994 |doi= }}
*{{cite journal | author=Susin SA, Lorenzo HK, Zamzami N, ''et al.'' |title=Mitochondrial release of caspase-2 and -9 during the apoptotic process. |journal=J. Exp. Med. |volume=189 |issue= 2 |pages= 381-94 |year= 1999 |pmid= 9892620 |doi= }}
*{{cite journal | author=Susin SA, Lorenzo HK, Zamzami N, ''et al.'' |title=Molecular characterization of mitochondrial apoptosis-inducing factor. |journal=Nature |volume=397 |issue= 6718 |pages= 441-6 |year= 1999 |pmid= 9989411 |doi= 10.1038/17135 }}
*{{cite journal | author=Daugas E, Susin SA, Zamzami N, ''et al.'' |title=Mitochondrio-nuclear translocation of AIF in apoptosis and necrosis. |journal=FASEB J. |volume=14 |issue= 5 |pages= 729-39 |year= 2000 |pmid= 10744629 |doi= }}
*{{cite journal | author=Joza N, Susin SA, Daugas E, ''et al.'' |title=Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death. |journal=Nature |volume=410 |issue= 6828 |pages= 549-54 |year= 2002 |pmid= 11279485 |doi= 10.1038/35069004 }}
*{{cite journal | author=Ravagnan L, Gurbuxani S, Susin SA, ''et al.'' |title=Heat-shock protein 70 antagonizes apoptosis-inducing factor. |journal=Nat. Cell Biol. |volume=3 |issue= 9 |pages= 839-43 |year= 2001 |pmid= 11533664 |doi= 10.1038/ncb0901-839 }}
*{{cite journal | author=Ye H, Cande C, Stephanou NC, ''et al.'' |title=DNA binding is required for the apoptogenic action of apoptosis inducing factor. |journal=Nat. Struct. Biol. |volume=9 |issue= 9 |pages= 680-4 |year= 2002 |pmid= 12198487 |doi= 10.1038/nsb836 }}
*{{cite journal | author=Roumier T, Vieira HL, Castedo M, ''et al.'' |title=The C-terminal moiety of HIV-1 Vpr induces cell death via a caspase-independent mitochondrial pathway. |journal=Cell Death Differ. |volume=9 |issue= 11 |pages= 1212-9 |year= 2003 |pmid= 12404120 |doi= 10.1038/sj.cdd.4401089 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ATXN1... {November 18, 2007 2:25:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:26:26 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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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_ATXN1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1oa8.
| PDB = {{PDB2|1oa8}}
| Name = Ataxin 1
| HGNCid = 10548
| Symbol = ATXN1
| AltSymbols =; ATX1; D6S504E; SCA1
| OMIM = 601556
| ECnumber =
| Homologene = 281
| MGIid = 104783
| GeneAtlas_image1 = PBB_GE_ATXN1_203232_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ATXN1_203231_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0042405 |text = nuclear inclusion body}}
| Process = {{GNF_GO|id=GO:0008219 |text = cell death}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6310
| Hs_Ensembl = ENSG00000124788
| Hs_RefseqProtein = NP_000323
| Hs_RefseqmRNA = NM_000332
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 16407320
| Hs_GenLoc_end = 16869703
| Hs_Uniprot = P54253
| Mm_EntrezGene = 20238
| Mm_Ensembl = ENSMUSG00000046876
| Mm_RefseqmRNA = NM_009124
| Mm_RefseqProtein = NP_033150
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 45565865
| Mm_GenLoc_end = 45975948
| Mm_Uniprot = Q8C866
}}
}}
'''Ataxin 1''', also known as '''ATXN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ATXN1 ataxin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6310| 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 autosomal dominant cerebellar ataxias (ADCA) are a heterogeneous group of neurodegenerative disorders characterized by progressive degeneration of the cerebellum, brain stem and spinal cord. Clinically, ADCA has been divided into three groups: ADCA types I-III. ADCAI is genetically heterogeneous, with five genetic loci, designated spinocerebellar ataxia (SCA) 1, 2, 3, 4 and 6, being assigned to five different chromosomes. ADCAII, which always presents with retinal degeneration (SCA7), and ADCAIII often referred to as the `pure' cerebellar syndrome (SCA5), are most likely homogeneous disorders. Several SCA genes have been cloned and shown to contain CAG repeats in their coding regions. ADCA is caused by the expansion of the CAG repeats, producing an elongated polyglutamine tract in the corresponding protein. The expanded repeats are variable in size and unstable, usually increasing in size when transmitted to successive generations. The function of the ataxins is not known. This locus has been mapped to chromosome 6, and it has been determined that the diseased allele contains 41-81 CAG repeats, compared to 6-39 in the normal allele. Several transcript variants in the 5' UTR have been described; however, their full-length nature is not known.<ref name="entrez">{{cite web | title = Entrez Gene: ATXN1 ataxin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6310| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Stevanin G, Dürr A, Brice A |title=Clinical and molecular advances in autosomal dominant cerebellar ataxias: from genotype to phenotype and physiopathology. |journal=Eur. J. Hum. Genet. |volume=8 |issue= 1 |pages= 4-18 |year= 2000 |pmid= 10713882 |doi= 10.1038/sj.ejhg.5200403 }}
*{{cite journal | author=Volz A, Fonatsch C, Ziegler A |title=Regional mapping of the gene for autosomal dominant spinocerebellar ataxia (SCA1) by localizing the closely linked D6S89 locus to 6p24.2----p23.05. |journal=Cytogenet. Cell Genet. |volume=60 |issue= 1 |pages= 37-9 |year= 1992 |pmid= 1582256 |doi= }}
*{{cite journal | author=Servadio A, Koshy B, Armstrong D, ''et al.'' |title=Expression analysis of the ataxin-1 protein in tissues from normal and spinocerebellar ataxia type 1 individuals. |journal=Nat. Genet. |volume=10 |issue= 1 |pages= 94-8 |year= 1995 |pmid= 7647801 |doi= 10.1038/ng0595-94 }}
*{{cite journal | author=Banfi S, Servadio A, Chung MY, ''et al.'' |title=Identification and characterization of the gene causing type 1 spinocerebellar ataxia. |journal=Nat. Genet. |volume=7 |issue= 4 |pages= 513-20 |year= 1994 |pmid= 7951322 |doi= 10.1038/ng0894-513 }}
*{{cite journal | author=Orr HT, Chung MY, Banfi S, ''et al.'' |title=Expansion of an unstable trinucleotide CAG repeat in spinocerebellar ataxia type 1. |journal=Nat. Genet. |volume=4 |issue= 3 |pages= 221-6 |year= 1993 |pmid= 8358429 |doi= 10.1038/ng0793-221 }}
*{{cite journal | author=Goldfarb LG, Vasconcelos O, Platonov FA, ''et al.'' |title=Unstable triplet repeat and phenotypic variability of spinocerebellar ataxia type 1. |journal=Ann. Neurol. |volume=39 |issue= 4 |pages= 500-6 |year= 1996 |pmid= 8619528 |doi= 10.1002/ana.410390412 }}
*{{cite journal | author=Quan F, Janas J, Popovich BW |title=A novel CAG repeat configuration in the SCA1 gene: implications for the molecular diagnostics of spinocerebellar ataxia type 1. |journal=Hum. Mol. Genet. |volume=4 |issue= 12 |pages= 2411-3 |year= 1996 |pmid= 8634720 |doi= }}
*{{cite journal | author=Koshy B, Matilla T, Burright EN, ''et al.'' |title=Spinocerebellar ataxia type-1 and spinobulbar muscular atrophy gene products interact with glyceraldehyde-3-phosphate dehydrogenase. |journal=Hum. Mol. Genet. |volume=5 |issue= 9 |pages= 1311-8 |year= 1997 |pmid= 8872471 |doi= }}
*{{cite journal | author=Burright EN, Davidson JD, Duvick LA, ''et al.'' |title=Identification of a self-association region within the SCA1 gene product, ataxin-1. |journal=Hum. Mol. Genet. |volume=6 |issue= 4 |pages= 513-8 |year= 1997 |pmid= 9097953 |doi= }}
*{{cite journal | author=Skinner PJ, Koshy BT, Cummings CJ, ''et al.'' |title=Ataxin-1 with an expanded glutamine tract alters nuclear matrix-associated structures. |journal=Nature |volume=389 |issue= 6654 |pages= 971-4 |year= 1997 |pmid= 9353120 |doi= 10.1038/40153 }}
*{{cite journal | author=Matilla A, Koshy BT, Cummings CJ, ''et al.'' |title=The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1. |journal=Nature |volume=389 |issue= 6654 |pages= 974-8 |year= 1997 |pmid= 9353121 |doi= 10.1038/40159 }}
*{{cite journal | author=Davidson JD, Riley B, Burright EN, ''et al.'' |title=Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein. |journal=Hum. Mol. Genet. |volume=9 |issue= 15 |pages= 2305-12 |year= 2001 |pmid= 11001934 |doi= }}
*{{cite journal | author=Yue S, Serra HG, Zoghbi HY, Orr HT |title=The spinocerebellar ataxia type 1 protein, ataxin-1, has RNA-binding activity that is inversely affected by the length of its polyglutamine tract. |journal=Hum. Mol. Genet. |volume=10 |issue= 1 |pages= 25-30 |year= 2001 |pmid= 11136710 |doi= }}
*{{cite journal | author=Savić D, Topisirović I, Keckarević M, ''et al.'' |title=Is the 31 CAG repeat allele of the spinocerebellar ataxia 1 (SCA1) gene locus non-specifically associated with trinucleotide expansion diseases? |journal=Psychiatr. Genet. |volume=11 |issue= 4 |pages= 201-5 |year= 2002 |pmid= 11807410 |doi= }}
*{{cite journal | author=Zühlke C, Dalski A, Hellenbroich Y, ''et al.'' |title=Spinocerebellar ataxia type 1 (SCA1): phenotype-genotype correlation studies in intermediate alleles. |journal=Eur. J. Hum. Genet. |volume=10 |issue= 3 |pages= 204-9 |year= 2002 |pmid= 11973625 |doi= 10.1038/sj.ejhg.5200788 }}
*{{cite journal | author=Okazawa H, Rich T, Chang A, ''et al.'' |title=Interaction between mutant ataxin-1 and PQBP-1 affects transcription and cell death. |journal=Neuron |volume=34 |issue= 5 |pages= 701-13 |year= 2002 |pmid= 12062018 |doi= }}
*{{cite journal | author=Hong S, Kim SJ, Ka S, ''et al.'' |title=USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product. |journal=Mol. Cell. Neurosci. |volume=20 |issue= 2 |pages= 298-306 |year= 2002 |pmid= 12093161 |doi= }}
*{{cite journal | author=Stenoien DL, Mielke M, Mancini MA |title=Intranuclear ataxin1 inclusions contain both fast- and slow-exchanging components. |journal=Nat. Cell Biol. |volume=4 |issue= 10 |pages= 806-10 |year= 2002 |pmid= 12360291 |doi= 10.1038/ncb859 }}
*{{cite journal | author=Poux C, van Rheede T, Madsen O, de Jong WW |title=Sequence gaps join mice and men: phylogenetic evidence from deletions in two proteins. |journal=Mol. Biol. Evol. |volume=19 |issue= 11 |pages= 2035-7 |year= 2003 |pmid= 12411613 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on AZU1... {November 18, 2007 2:18:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:19:43 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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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_AZU1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1a7s.
| PDB = {{PDB2|1a7s}}, {{PDB2|1ae5}}, {{PDB2|1fy1}}, {{PDB2|1fy3}}
| Name = Azurocidin 1 (cationic antimicrobial protein 37)
| HGNCid = 913
| Symbol = AZU1
| AltSymbols =; AZAMP; AZU; CAP37; HBP; HUMAZUR; NAZC
| OMIM = 162815
| ECnumber =
| Homologene = 74404
| MGIid =
| GeneAtlas_image1 = PBB_GE_AZU1_214575_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0015643 |text = toxin binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0042582 |text = azurophil granule}}
| Process = {{GNF_GO|id=GO:0001774 |text = microglial cell activation}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007205 |text = protein kinase C activation}} {{GNF_GO|id=GO:0008347 |text = glial cell migration}} {{GNF_GO|id=GO:0042117 |text = monocyte activation}} {{GNF_GO|id=GO:0042535 |text = positive regulation of tumor necrosis factor biosynthetic process}} {{GNF_GO|id=GO:0043114 |text = regulation of vascular permeability}} {{GNF_GO|id=GO:0045123 |text = cellular extravasation}} {{GNF_GO|id=GO:0045348 |text = positive regulation of MHC class II biosynthetic process}} {{GNF_GO|id=GO:0045785 |text = positive regulation of cell adhesion}} {{GNF_GO|id=GO:0048246 |text = macrophage chemotaxis}} {{GNF_GO|id=GO:0050725 |text = positive regulation of interleukin-1 beta biosynthetic process}} {{GNF_GO|id=GO:0050754 |text = positive regulation of fractalkine biosynthetic process}} {{GNF_GO|id=GO:0050766 |text = positive regulation of phagocytosis}} {{GNF_GO|id=GO:0050829 |text = defense response to Gram-negative bacterium}} {{GNF_GO|id=GO:0050930 |text = induction of positive chemotaxis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 566
| Hs_Ensembl = ENSG00000172232
| Hs_RefseqProtein = NP_001691
| Hs_RefseqmRNA = NM_001700
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 776097
| Hs_GenLoc_end = 783017
| Hs_Uniprot = P20160
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Azurocidin 1 (cationic antimicrobial protein 37)''', also known as '''AZU1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AZU1 azurocidin 1 (cationic antimicrobial protein 37)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=566| 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 = Azurophil granules, specialized lysosomes of the neutrophil, contain at least 10 proteins implicated in the killing of microorganisms. The protein encoded by this gene is an azurophil granule antibiotic protein, with monocyte chemotactic and antibacterial activity. It is also an important multifunctional inflammatory mediator. This encoded protein is a member of the serine protease gene family but it is not a serine proteinase, because the active site serine and histidine residues are replaced. The genes encoding this protein, neutrophil elastase 2, and proteinase 3 are in a cluster located at chromosome 19pter. All 3 genes are expressed coordinately and their protein products are packaged together into azurophil granules during neutrophil differentiation.<ref name="entrez">{{cite web | title = Entrez Gene: AZU1 azurocidin 1 (cationic antimicrobial protein 37)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=566| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Morgan JG, Pereira HA, Sukiennicki T, ''et al.'' |title=Human neutrophil granule cationic protein CAP37 is a specific macrophage chemotaxin that shares homology with inflammatory proteinases. |journal=Adv. Exp. Med. Biol. |volume=305 |issue= |pages= 89-96 |year= 1992 |pmid= 1755383 |doi= }}
*{{cite journal | author=Watorek W |title=Azurocidin -- inactive serine proteinase homolog acting as a multifunctional inflammatory mediator. |journal=Acta Biochim. Pol. |volume=50 |issue= 3 |pages= 743-52 |year= 2004 |pmid= 14515154 |doi= 035003743 }}
*{{cite journal | author=Zimmer M, Medcalf RL, Fink TM, ''et al.'' |title=Three human elastase-like genes coordinately expressed in the myelomonocyte lineage are organized as a single genetic locus on 19pter. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 17 |pages= 8215-9 |year= 1992 |pmid= 1518849 |doi= }}
*{{cite journal | author=Green BG, Weston H, Ashe BM, ''et al.'' |title=PMN elastases: a comparison of the specificity of human isozymes and the enzyme from other species toward substrates and inhibitors. |journal=Arch. Biochem. Biophys. |volume=286 |issue= 1 |pages= 284-92 |year= 1991 |pmid= 1897955 |doi= }}
*{{cite journal | author=Morgan JG, Sukiennicki T, Pereira HA, ''et al.'' |title=Cloning of the cDNA for the serine protease homolog CAP37/azurocidin, a microbicidal and chemotactic protein from human granulocytes. |journal=J. Immunol. |volume=147 |issue= 9 |pages= 3210-4 |year= 1991 |pmid= 1919011 |doi= }}
*{{cite journal | author=Flodgaard H, Ostergaard E, Bayne S, ''et al.'' |title=Covalent structure of two novel neutrophile leucocyte-derived proteins of porcine and human origin. Neutrophile elastase homologues with strong monocyte and fibroblast chemotactic activities. |journal=Eur. J. Biochem. |volume=197 |issue= 2 |pages= 535-47 |year= 1991 |pmid= 2026172 |doi= }}
*{{cite journal | author=Almeida RP, Melchior M, Campanelli D, ''et al.'' |title=Complementary DNA sequence of human neutrophil azurocidin, an antibiotic with extensive homology to serine proteases. |journal=Biochem. Biophys. Res. Commun. |volume=177 |issue= 2 |pages= 688-95 |year= 1991 |pmid= 2049091 |doi= }}
*{{cite journal | author=Pohl J, Pereira HA, Martin NM, Spitznagel JK |title=Amino acid sequence of CAP37, a human neutrophil granule-derived antibacterial and monocyte-specific chemotactic glycoprotein structurally similar to neutrophil elastase. |journal=FEBS Lett. |volume=272 |issue= 1-2 |pages= 200-4 |year= 1990 |pmid= 2226832 |doi= }}
*{{cite journal | author=Campanelli D, Detmers PA, Nathan CF, Gabay JE |title=Azurocidin and a homologous serine protease from neutrophils. Differential antimicrobial and proteolytic properties. |journal=J. Clin. Invest. |volume=85 |issue= 3 |pages= 904-15 |year= 1990 |pmid= 2312733 |doi= }}
*{{cite journal | author=Pereira HA, Shafer WM, Pohl J, ''et al.'' |title=CAP37, a human neutrophil-derived chemotactic factor with monocyte specific activity. |journal=J. Clin. Invest. |volume=85 |issue= 5 |pages= 1468-76 |year= 1990 |pmid= 2332502 |doi= }}
*{{cite journal | author=Wilde CG, Snable JL, Griffith JE, Scott RW |title=Characterization of two azurphil granule proteases with active-site homology to neutrophil elastase. |journal=J. Biol. Chem. |volume=265 |issue= 4 |pages= 2038-41 |year= 1990 |pmid= 2404977 |doi= }}
*{{cite journal | author=Pereira HA, Spitznagel JK, Pohl J, ''et al.'' |title=CAP 37, a 37 kD human neutrophil granule cationic protein shares homology with inflammatory proteinases. |journal=Life Sci. |volume=46 |issue= 3 |pages= 189-96 |year= 1990 |pmid= 2406527 |doi= }}
*{{cite journal | author=Gabay JE, Scott RW, Campanelli D, ''et al.'' |title=Antibiotic proteins of human polymorphonuclear leukocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 14 |pages= 5610-4 |year= 1989 |pmid= 2501794 |doi= }}
*{{cite journal | author=Pereira HA, Erdem I, Pohl J, Spitznagel JK |title=Synthetic bactericidal peptide based on CAP37: a 37-kDa human neutrophil granule-associated cationic antimicrobial protein chemotactic for monocytes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 10 |pages= 4733-7 |year= 1993 |pmid= 8506327 |doi= }}
*{{cite journal | author=Chertov O, Michiel DF, Xu L, ''et al.'' |title=Identification of defensin-1, defensin-2, and CAP37/azurocidin as T-cell chemoattractant proteins released from interleukin-8-stimulated neutrophils. |journal=J. Biol. Chem. |volume=271 |issue= 6 |pages= 2935-40 |year= 1996 |pmid= 8621683 |doi= }}
*{{cite journal | author=Iversen LF, Kastrup JS, Bjørn SE, ''et al.'' |title=Structure of HBP, a multifunctional protein with a serine proteinase fold. |journal=Nat. Struct. Biol. |volume=4 |issue= 4 |pages= 265-8 |year= 1997 |pmid= 9095193 |doi= }}
*{{cite journal | author=Karlsen S, Iversen LF, Larsen IK, ''et al.'' |title=Atomic resolution structure of human HBP/CAP37/azurocidin. |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=54 |issue= Pt 4 |pages= 598-609 |year= 1998 |pmid= 9761855 |doi= }}
*{{cite journal | author=Olofsson AM, Vestberg M, Herwald H, ''et al.'' |title=Heparin-binding protein targeted to mitochondrial compartments protects endothelial cells from apoptosis. |journal=J. Clin. Invest. |volume=104 |issue= 7 |pages= 885-94 |year= 1999 |pmid= 10510329 |doi= }}
*{{cite journal | author=Lindmark A, Garwicz D, Rasmussen PB, ''et al.'' |title=Characterization of the biosynthesis, processing, and sorting of human HBP/CAP37/azurocidin. |journal=J. Leukoc. Biol. |volume=66 |issue= 4 |pages= 634-43 |year= 1999 |pmid= 10534120 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on C2... {November 18, 2007 2:19:43 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:20:24 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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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_C2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2i6q.
| PDB = {{PDB2|2i6q}}, {{PDB2|2i6s}}, {{PDB2|2odp}}, {{PDB2|2odq}}
| Name = Complement component 2
| HGNCid = 1248
| Symbol = C2
| AltSymbols =; CO2; DKFZp779M0311
| OMIM = 217000
| ECnumber =
| Homologene = 45
| MGIid = 88226
| GeneAtlas_image1 = PBB_GE_C2_203052_at_tn.png
| Function = {{GNF_GO|id=GO:0003813 |text = classical-complement-pathway C3/C5 convertase activity}} {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005603 |text = complement component C2 complex}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006958 |text = complement activation, classical pathway}} {{GNF_GO|id=GO:0045087 |text = innate immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 717
| Hs_Ensembl = ENSG00000166278
| Hs_RefseqProtein = NP_000054
| Hs_RefseqmRNA = NM_000063
| Hs_GenLoc_db =
| Hs_GenLoc_chr = c6_COX
| Hs_GenLoc_start = 32030300
| Hs_GenLoc_end = 32048254
| Hs_Uniprot = P06681
| Mm_EntrezGene = 12263
| Mm_Ensembl = ENSMUSG00000024372
| Mm_RefseqmRNA = NM_013484
| Mm_RefseqProtein = NP_038512
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 34470664
| Mm_GenLoc_end = 34490119
| Mm_Uniprot = O70350
}}
}}
'''Complement component 2''', also known as '''C2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: C2 complement component 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=717| 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 = Component C2 is part of the classical pathway of complement system. Activated C1 cleaves C2 into C2a and C2b. C2a leads to activation of C3. Deficiency of C2 has been reported to associated with certain autoimmune diseases.<ref name="entrez">{{cite web | title = Entrez Gene: C2 complement component 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=717| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bartholomew WR, Shanahan TC |title=Complement components and receptors: deficiencies and disease associations. |journal=Immunol. Ser. |volume=52 |issue= |pages= 33-51 |year= 1991 |pmid= 2091785 |doi= }}
*{{cite journal | author=Campbell RD |title=The molecular genetics and polymorphism of C2 and factor B. |journal=Br. Med. Bull. |volume=43 |issue= 1 |pages= 37-49 |year= 1988 |pmid= 3315100 |doi= }}
*{{cite journal | author=Yu CY |title=Molecular genetics of the human MHC complement gene cluster. |journal=Exp. Clin. Immunogenet. |volume=15 |issue= 4 |pages= 213-30 |year= 1999 |pmid= 10072631 |doi= }}
*{{cite journal | author=Lutsenko SM, Kharchenko VG, Bachurin VI, Lomakin MM |title=[Circulating blood volume and regional hemodynamics in acute gastrointestinal hemorrhage] |journal=Sovetskaia meditsina |volume= |issue= 2 |pages= 38-41 |year= 1976 |pmid= 1084023 |doi= }}
*{{cite journal | author=Zhu ZB, Hsieh SL, Bentley DR, ''et al.'' |title=A variable number of tandem repeats locus within the human complement C2 gene is associated with a retroposon derived from a human endogenous retrovirus. |journal=J. Exp. Med. |volume=175 |issue= 6 |pages= 1783-7 |year= 1992 |pmid= 1350302 |doi= }}
*{{cite journal | author=Lappin DF, Guc D, Hill A, ''et al.'' |title=Effect of interferon-gamma on complement gene expression in different cell types. |journal=Biochem. J. |volume=281 ( Pt 2) |issue= |pages= 437-42 |year= 1992 |pmid= 1531292 |doi= }}
*{{cite journal | author=Johnson CA, Densen P, Hurford RK, ''et al.'' |title=Type I human complement C2 deficiency. A 28-base pair gene deletion causes skipping of exon 6 during RNA splicing. |journal=J. Biol. Chem. |volume=267 |issue= 13 |pages= 9347-53 |year= 1992 |pmid= 1577763 |doi= }}
*{{cite journal | author=Lappin DF, Birnie GD, Whaley K |title=Interferon-mediated transcriptional and post-transcriptional modulation of complement gene expression in human monocytes. |journal=Eur. J. Biochem. |volume=194 |issue= 1 |pages= 177-84 |year= 1991 |pmid= 1701385 |doi= }}
*{{cite journal | author=Horiuchi T, Macon KJ, Kidd VJ, Volanakis JE |title=cDNA cloning and expression of human complement component C2. |journal=J. Immunol. |volume=142 |issue= 6 |pages= 2105-11 |year= 1989 |pmid= 2493504 |doi= }}
*{{cite journal | author=Cole FS, Whitehead AS, Auerbach HS, ''et al.'' |title=The molecular basis for genetic deficiency of the second component of human complement. |journal=N. Engl. J. Med. |volume=313 |issue= 1 |pages= 11-6 |year= 1985 |pmid= 2582254 |doi= }}
*{{cite journal | author=Bentley DR |title=Primary structure of human complement component C2. Homology to two unrelated protein families. |journal=Biochem. J. |volume=239 |issue= 2 |pages= 339-45 |year= 1987 |pmid= 2949737 |doi= }}
*{{cite journal | author=Bentley DR, Campbell RD, Cross SJ |title=DNA polymorphism of the C2 locus. |journal=Immunogenetics |volume=22 |issue= 4 |pages= 377-90 |year= 1985 |pmid= 2997031 |doi= }}
*{{cite journal | author=Kam CM, McRae BJ, Harper JW, ''et al.'' |title=Human complement proteins D, C2, and B. Active site mapping with peptide thioester substrates. |journal=J. Biol. Chem. |volume=262 |issue= 8 |pages= 3444-51 |year= 1987 |pmid= 3546307 |doi= }}
*{{cite journal | author=Wu LC, Morley BJ, Campbell RD |title=Cell-specific expression of the human complement protein factor B gene: evidence for the role of two distinct 5'-flanking elements. |journal=Cell |volume=48 |issue= 2 |pages= 331-42 |year= 1987 |pmid= 3643061 |doi= }}
*{{cite journal | author=Gagnon J |title=Structure and activation of complement components C2 and factor B. |journal=Philos. Trans. R. Soc. Lond., B, Biol. Sci. |volume=306 |issue= 1129 |pages= 301-9 |year= 1984 |pmid= 6149575 |doi= }}
*{{cite journal | author=Bentley DR, Porter RR |title=Isolation of cDNA clones for human complement component C2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=81 |issue= 4 |pages= 1212-5 |year= 1984 |pmid= 6199794 |doi= }}
*{{cite journal | author=Parkes C, Gagnon J, Kerr MA |title=The reaction of iodine and thiol-blocking reagents with human complement components C2 and factor B. Purification and N-terminal amino acid sequence of a peptide from C2a containing a free thiol group. |journal=Biochem. J. |volume=213 |issue= 1 |pages= 201-9 |year= 1983 |pmid= 6555044 |doi= }}
*{{cite journal | author=Kerr MA, Gagnon J |title=The purification and properties of the second component of guinea-pig complement. |journal=Biochem. J. |volume=205 |issue= 1 |pages= 59-67 |year= 1982 |pmid= 6922702 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CD19... {November 18, 2007 2:20:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:20:50 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 = CD19 molecule
| HGNCid = 1633
| Symbol = CD19
| AltSymbols =; B4; MGC12802
| OMIM = 107265
| ECnumber =
| Homologene = 1341
| MGIid = 88319
| GeneAtlas_image1 = PBB_GE_CD19_206398_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005057 |text = receptor signaling protein activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}}
| Process = {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 930
| Hs_Ensembl = ENSG00000177455
| Hs_RefseqProtein = NP_001761
| Hs_RefseqmRNA = NM_001770
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 28850779
| Hs_GenLoc_end = 28858164
| Hs_Uniprot = P15391
| Mm_EntrezGene = 12478
| Mm_Ensembl = ENSMUSG00000030724
| Mm_RefseqmRNA = NM_009844
| Mm_RefseqProtein = NP_033974
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 126199599
| Mm_GenLoc_end = 126205984
| Mm_Uniprot = Q3TA95
}}
}}
'''CD19 molecule''', also known as '''CD19''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CD19 CD19 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=930| 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 = Lymphocytes proliferate and differentiate in response to various concentrations of different antigens. The ability of the B cell to respond in a specific, yet sensitive manner to the various antigens is achieved with the use of low-affinity antigen receptors. This gene encodes a cell surface molecule which assembles with the antigen receptor of B lymphocytes in order to decrease the threshold for antigen receptor-dependent stimulation.<ref name="entrez">{{cite web | title = Entrez Gene: CD19 CD19 molecule| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=930| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ishikawa H, Tsuyama N, Mahmoud MS, ''et al.'' |title=CD19 expression and growth inhibition of tumours in human multiple myeloma. |journal=Leuk. Lymphoma |volume=43 |issue= 3 |pages= 613-6 |year= 2003 |pmid= 12002767 |doi= }}
*{{cite journal | author=Zhou LJ, Ord DC, Omori SA, Tedder TF |title=Structure of the genes encoding the CD19 antigen of human and mouse B lymphocytes. |journal=Immunogenetics |volume=35 |issue= 2 |pages= 102-11 |year= 1992 |pmid= 1370948 |doi= }}
*{{cite journal | author=Carter RH, Fearon DT |title=CD19: lowering the threshold for antigen receptor stimulation of B lymphocytes. |journal=Science |volume=256 |issue= 5053 |pages= 105-7 |year= 1992 |pmid= 1373518 |doi= }}
*{{cite journal | author=Kozmik Z, Wang S, Dörfler P, ''et al.'' |title=The promoter of the CD19 gene is a target for the B-cell-specific transcription factor BSAP. |journal=Mol. Cell. Biol. |volume=12 |issue= 6 |pages= 2662-72 |year= 1992 |pmid= 1375324 |doi= }}
*{{cite journal | author=Bradbury LE, Kansas GS, Levy S, ''et al.'' |title=The CD19/CD21 signal transducing complex of human B lymphocytes includes the target of antiproliferative antibody-1 and Leu-13 molecules. |journal=J. Immunol. |volume=149 |issue= 9 |pages= 2841-50 |year= 1992 |pmid= 1383329 |doi= }}
*{{cite journal | author=Matsumoto AK, Kopicky-Burd J, Carter RH, ''et al.'' |title=Intersection of the complement and immune systems: a signal transduction complex of the B lymphocyte-containing complement receptor type 2 and CD19. |journal=J. Exp. Med. |volume=173 |issue= 1 |pages= 55-64 |year= 1991 |pmid= 1702139 |doi= }}
*{{cite journal | author=Zhou LJ, Ord DC, Hughes AL, Tedder TF |title=Structure and domain organization of the CD19 antigen of human, mouse, and guinea pig B lymphocytes. Conservation of the extensive cytoplasmic domain. |journal=J. Immunol. |volume=147 |issue= 4 |pages= 1424-32 |year= 1991 |pmid= 1714482 |doi= }}
*{{cite journal | author=Stamenkovic I, Seed B |title=CD19, the earliest differentiation antigen of the B cell lineage, bears three extracellular immunoglobulin-like domains and an Epstein-Barr virus-related cytoplasmic tail. |journal=J. Exp. Med. |volume=168 |issue= 3 |pages= 1205-10 |year= 1988 |pmid= 2459292 |doi= }}
*{{cite journal | author=Tedder TF, Isaacs CM |title=Isolation of cDNAs encoding the CD19 antigen of human and mouse B lymphocytes. A new member of the immunoglobulin superfamily. |journal=J. Immunol. |volume=143 |issue= 2 |pages= 712-7 |year= 1989 |pmid= 2472450 |doi= }}
*{{cite journal | author=Ord DC, Edelhoff S, Dushkin H, ''et al.'' |title=CD19 maps to a region of conservation between human chromosome 16 and mouse chromosome 7. |journal=Immunogenetics |volume=39 |issue= 5 |pages= 322-8 |year= 1994 |pmid= 7513297 |doi= }}
*{{cite journal | author=Weng WK, Jarvis L, LeBien TW |title=Signaling through CD19 activates Vav/mitogen-activated protein kinase pathway and induces formation of a CD19/Vav/phosphatidylinositol 3-kinase complex in human B cell precursors. |journal=J. Biol. Chem. |volume=269 |issue= 51 |pages= 32514-21 |year= 1995 |pmid= 7528218 |doi= }}
*{{cite journal | author=Myers DE, Jun X, Waddick KG, ''et al.'' |title=Membrane-associated CD19-LYN complex is an endogenous p53-independent and Bc1-2-independent regulator of apoptosis in human B-lineage lymphoma cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 21 |pages= 9575-9 |year= 1995 |pmid= 7568175 |doi= }}
*{{cite journal | author=Chalupny NJ, Aruffo A, Esselstyn JM, ''et al.'' |title=Specific binding of Fyn and phosphatidylinositol 3-kinase to the B cell surface glycoprotein CD19 through their src homology 2 domains. |journal=Eur. J. Immunol. |volume=25 |issue= 10 |pages= 2978-84 |year= 1995 |pmid= 7589101 |doi= }}
*{{cite journal | author=Tuscano JM, Engel P, Tedder TF, ''et al.'' |title=Involvement of p72syk kinase, p53/56lyn kinase and phosphatidyl inositol-3 kinase in signal transduction via the human B lymphocyte antigen CD22. |journal=Eur. J. Immunol. |volume=26 |issue= 6 |pages= 1246-52 |year= 1996 |pmid= 8647200 |doi= }}
*{{cite journal | author=Carter RH, Doody GM, Bolen JB, Fearon DT |title=Membrane IgM-induced tyrosine phosphorylation of CD19 requires a CD19 domain that mediates association with components of the B cell antigen receptor complex. |journal=J. Immunol. |volume=158 |issue= 7 |pages= 3062-9 |year= 1997 |pmid= 9120258 |doi= }}
*{{cite journal | author=Husson H, Mograbi B, Schmid-Antomarchi H, ''et al.'' |title=CSF-1 stimulation induces the formation of a multiprotein complex including CSF-1 receptor, c-Cbl, PI 3-kinase, Crk-II and Grb2. |journal=Oncogene |volume=14 |issue= 19 |pages= 2331-8 |year= 1997 |pmid= 9178909 |doi= 10.1038/sj.onc.1201074 }}
*{{cite journal | author=Khine AA, Firtel M, Lingwood CA |title=CD77-dependent retrograde transport of CD19 to the nuclear membrane: functional relationship between CD77 and CD19 during germinal center B-cell apoptosis. |journal=J. Cell. Physiol. |volume=176 |issue= 2 |pages= 281-92 |year= 1998 |pmid= 9648915 |doi= 10.1002/(SICI)1097-4652(199808)176:2<281::AID-JCP6>3.0.CO;2-K }}
*{{cite journal | author=Thunberg U, Gidlöf C, Bånghagen M, ''et al.'' |title=HpaII polymerase chain reaction restriction fragment length polymorphism in the human CD19 gene on 16p11. |journal=Hum. Hered. |volume=48 |issue= 4 |pages= 230-1 |year= 1998 |pmid= 9694255 |doi= }}
*{{cite journal | author=Horváth G, Serru V, Clay D, ''et al.'' |title=CD19 is linked to the integrin-associated tetraspans CD9, CD81, and CD82. |journal=J. Biol. Chem. |volume=273 |issue= 46 |pages= 30537-43 |year= 1998 |pmid= 9804823 |doi= }}
*{{cite journal | author=Buhl AM, Cambier JC |title=Phosphorylation of CD19 Y484 and Y515, and linked activation of phosphatidylinositol 3-kinase, are required for B cell antigen receptor-mediated activation of Bruton's tyrosine kinase. |journal=J. Immunol. |volume=162 |issue= 8 |pages= 4438-46 |year= 1999 |pmid= 10201980 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CHAT... {November 18, 2007 2:20:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:21:12 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
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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_CHAT_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2fy2.
| PDB = {{PDB2|2fy2}}, {{PDB2|2fy3}}, {{PDB2|2fy4}}, {{PDB2|2fy5}}
| Name = Choline acetyltransferase
| HGNCid = 1912
| Symbol = CHAT
| AltSymbols =; CMS1A; CMS1A2
| OMIM = 118490
| ECnumber =
| Homologene = 40693
| MGIid = 88392
| GeneAtlas_image1 = PBB_GE_CHAT_221197_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004102 |text = choline O-acetyltransferase activity}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0007274 |text = neuromuscular synaptic transmission}} {{GNF_GO|id=GO:0007517 |text = muscle development}} {{GNF_GO|id=GO:0007529 |text = establishment of synaptic specificity at neuromuscular junction}} {{GNF_GO|id=GO:0007622 |text = rhythmic behavior}} {{GNF_GO|id=GO:0007628 |text = adult walking behavior}} {{GNF_GO|id=GO:0016358 |text = dendrite development}} {{GNF_GO|id=GO:0030182 |text = neuron differentiation}} {{GNF_GO|id=GO:0042136 |text = neurotransmitter biosynthetic process}} {{GNF_GO|id=GO:0043179 |text = rhythmic excitation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1103
| Hs_Ensembl = ENSG00000070748
| Hs_RefseqProtein = NP_065574
| Hs_RefseqmRNA = NM_020549
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 50487147
| Hs_GenLoc_end = 50543156
| Hs_Uniprot = P28329
| Mm_EntrezGene = 12647
| Mm_Ensembl = ENSMUSG00000021919
| Mm_RefseqmRNA = NM_009891
| Mm_RefseqProtein = NP_034021
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 31237212
| Mm_GenLoc_end = 31294918
| Mm_Uniprot = Q8BQN4
}}
}}
'''Choline acetyltransferase''', also known as '''CHAT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CHAT choline acetyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1103| 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 = Cholinergic systems are implicated in numerous neurologic functions. Alteration in some cholinergic neurons may account for the disturbances of Alzheimer disease. The protein encoded by this gene synthesizes the neurotransmitter acetylcholine. Alternative splice variants have been found that contain alternative 5' untranslated exons. Three of the four described splice variants encode identical 69 kDa proteins while one variant encodes both the 69 kDa and a larger 82 kDa protein.<ref name="entrez">{{cite web | title = Entrez Gene: CHAT choline acetyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1103| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Oda Y |title=Choline acetyltransferase: the structure, distribution and pathologic changes in the central nervous system. |journal=Pathol. Int. |volume=49 |issue= 11 |pages= 921-37 |year= 2000 |pmid= 10594838 |doi= }}
*{{cite journal | author=Oda Y, Nakanishi I, Deguchi T |title=A complementary DNA for human choline acetyltransferase induces two forms of enzyme with different molecular weights in cultured cells. |journal=Brain Res. Mol. Brain Res. |volume=16 |issue= 3-4 |pages= 287-94 |year= 1993 |pmid= 1337937 |doi= }}
*{{cite journal | author=Toussaint JL, Geoffroy V, Schmitt M, ''et al.'' |title=Human choline acetyltransferase (CHAT): partial gene sequence and potential control regions. |journal=Genomics |volume=12 |issue= 2 |pages= 412-6 |year= 1992 |pmid= 1339386 |doi= }}
*{{cite journal | author=Lorenzi MV, Trinidad AC, Zhang R, Strauss WL |title=Two mRNAs are transcribed from the human gene for choline acetyltransferase. |journal=DNA Cell Biol. |volume=11 |issue= 8 |pages= 593-603 |year= 1992 |pmid= 1388731 |doi= }}
*{{cite journal | author=Misawa H, Ishii K, Deguchi T |title=Gene expression of mouse choline acetyltransferase. Alternative splicing and identification of a highly active promoter region. |journal=J. Biol. Chem. |volume=267 |issue= 28 |pages= 20392-9 |year= 1992 |pmid= 1400357 |doi= }}
*{{cite journal | author=Cervini R, Rocchi M, DiDonato S, Finocchiaro G |title=Isolation and sub-chromosomal localization of a DNA fragment of the human choline acetyltransferase gene. |journal=Neurosci. Lett. |volume=132 |issue= 2 |pages= 191-4 |year= 1992 |pmid= 1784419 |doi= }}
*{{cite journal | author=Strauss WL, Kemper RR, Jayakar P, ''et al.'' |title=Human choline acetyltransferase gene maps to region 10q11-q22.2 by in situ hybridization. |journal=Genomics |volume=9 |issue= 2 |pages= 396-8 |year= 1991 |pmid= 1840566 |doi= }}
*{{cite journal | author=Viegas-Péquignot E, Berrard S, Brice A, ''et al.'' |title=Localization of a 900-bp-long fragment of the human choline acetyltransferase gene to 10q11.2 by nonradioactive in situ hybridization. |journal=Genomics |volume=9 |issue= 1 |pages= 210-2 |year= 1991 |pmid= 2004764 |doi= }}
*{{cite journal | author=Itoh N, Slemmon JR, Hawke DH, ''et al.'' |title=Cloning of Drosophila choline acetyltransferase cDNA. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 11 |pages= 4081-5 |year= 1986 |pmid= 3086876 |doi= }}
*{{cite journal | author=Hersh LB, Takane K, Gylys K, ''et al.'' |title=Conservation of amino acid sequences between human and porcine choline acetyltransferase. |journal=J. Neurochem. |volume=51 |issue= 6 |pages= 1843-5 |year= 1988 |pmid= 3183663 |doi= }}
*{{cite journal | author=Berrard S, Brice A, Lottspeich F, ''et al.'' |title=cDNA cloning and complete sequence of porcine choline acetyltransferase: in vitro translation of the corresponding RNA yields an active protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 24 |pages= 9280-4 |year= 1988 |pmid= 3480542 |doi= }}
*{{cite journal | author=Chireux MA, Le Van Thai A, Weber MJ |title=Human choline acetyltransferase gene: localization of alternative first exons. |journal=J. Neurosci. Res. |volume=40 |issue= 4 |pages= 427-38 |year= 1995 |pmid= 7616604 |doi= 10.1002/jnr.490400402 }}
*{{cite journal | author=Bausero P, Schmitt M, Toussaint JL, ''et al.'' |title=Identification and analysis of the human choline acetyltransferase gene promoter. |journal=Neuroreport |volume=4 |issue= 3 |pages= 287-90 |year= 1993 |pmid= 7682855 |doi= }}
*{{cite journal | author=Quirin-Stricker C, Nappey V, Simoni P, ''et al.'' |title=Trans-activation by thyroid hormone receptors of the 5' flanking region of the human ChAT gene. |journal=Brain Res. Mol. Brain Res. |volume=23 |issue= 3 |pages= 253-65 |year= 1994 |pmid= 8057782 |doi= }}
*{{cite journal | author=Erickson JD, Varoqui H, Schäfer MK, ''et al.'' |title=Functional identification of a vesicular acetylcholine transporter and its expression from a "cholinergic" gene locus. |journal=J. Biol. Chem. |volume=269 |issue= 35 |pages= 21929-32 |year= 1994 |pmid= 8071310 |doi= }}
*{{cite journal | author=Kengaku M, Misawa H, Deguchi T |title=Multiple mRNA species of choline acetyltransferase from rat spinal cord. |journal=Brain Res. Mol. Brain Res. |volume=18 |issue= 1-2 |pages= 71-6 |year= 1993 |pmid= 8479291 |doi= }}
*{{cite journal | author=Misawa H, Matsuura J, Oda Y, ''et al.'' |title=Human choline acetyltransferase mRNAs with different 5'-region produce a 69-kDa major translation product. |journal=Brain Res. Mol. Brain Res. |volume=44 |issue= 2 |pages= 323-33 |year= 1997 |pmid= 9073174 |doi= }}
*{{cite journal | author=Lönnerberg P, Ibáñez CF |title=Novel, testis-specific mRNA transcripts encoding N-terminally truncated choline acetyltransferase. |journal=Mol. Reprod. Dev. |volume=53 |issue= 3 |pages= 274-81 |year= 1999 |pmid= 10369388 |doi= 10.1002/(SICI)1098-2795(199907)53:3<274::AID-MRD3>3.0.CO;2-8 }}
*{{cite journal | author=Sakakibara A, Hattori S |title=Chat, a Cas/HEF1-associated adaptor protein that integrates multiple signaling pathways. |journal=J. Biol. Chem. |volume=275 |issue= 9 |pages= 6404-10 |year= 2000 |pmid= 10692442 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IL24... {November 18, 2007 2:38:04 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:39:19 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 = Interleukin 24
| HGNCid = 11346
| Symbol = IL24
| AltSymbols =; C49A; FISP; IL-24; IL10B; MDA7; Mob-5; ST16; mda-7
| OMIM = 604136
| ECnumber =
| Homologene = 4991
| MGIid = 2135548
| GeneAtlas_image1 = PBB_GE_IL24_206569_at_tn.png
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 11009
| Hs_Ensembl = ENSG00000162892
| Hs_RefseqProtein = NP_006841
| Hs_RefseqmRNA = NM_006850
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 205137411
| Hs_GenLoc_end = 205144107
| Hs_Uniprot = Q13007
| Mm_EntrezGene = 93672
| Mm_Ensembl = ENSMUSG00000026420
| Mm_RefseqmRNA = NM_053095
| Mm_RefseqProtein = NP_444325
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 132709620
| Mm_GenLoc_end = 132714885
| Mm_Uniprot = Q925S4
}}
}}
'''Interleukin 24''', also known as '''IL24''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: IL24 interleukin 24| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11009| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the IL10 family of cytokines. It was identified as a gene induced during terminal differentiation in melanoma cells. The protein encoded by this gene can induce apoptosis selectively in various cancer cells. Overexpression of this gene leads to elevated expression of several GADD family genes, which correlates with the induction of apoptosis. The phosphorylation of mitogen-activated protein kinase 14 (MAPK7/P38), and heat shock 27kDa protein 1 (HSPB2/HSP27) are found to be induced by this gene in melanoma cells, but not in normal immortal melanocytes. Alternatively spliced transcript variants encoding distinct isoforms have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: IL24 interleukin 24| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11009| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sauane M, Gopalkrishnan RV, Sarkar D, ''et al.'' |title=MDA-7/IL-24: novel cancer growth suppressing and apoptosis inducing cytokine. |journal=Cytokine Growth Factor Rev. |volume=14 |issue= 1 |pages= 35-51 |year= 2003 |pmid= 12485618 |doi= }}
*{{cite journal | author=Jiang H, Lin JJ, Su ZZ, ''et al.'' |title=Subtraction hybridization identifies a novel melanoma differentiation associated gene, mda-7, modulated during human melanoma differentiation, growth and progression. |journal=Oncogene |volume=11 |issue= 12 |pages= 2477-86 |year= 1996 |pmid= 8545104 |doi= }}
*{{cite journal | author=Jiang H, Su ZZ, Lin JJ, ''et al.'' |title=The melanoma differentiation associated gene mda-7 suppresses cancer cell growth. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 17 |pages= 9160-5 |year= 1996 |pmid= 8799171 |doi= }}
*{{cite journal | author=Su ZZ, Madireddi MT, Lin JJ, ''et al.'' |title=The cancer growth suppressor gene mda-7 selectively induces apoptosis in human breast cancer cells and inhibits tumor growth in nude mice. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 24 |pages= 14400-5 |year= 1998 |pmid= 9826712 |doi= }}
*{{cite journal | author=Madireddi MT, Dent P, Fisher PB |title=AP-1 and C/EBP transcription factors contribute to mda-7 gene promoter activity during human melanoma differentiation. |journal=J. Cell. Physiol. |volume=185 |issue= 1 |pages= 36-46 |year= 2000 |pmid= 10942517 |doi= 10.1002/1097-4652(200010)185:1<36::AID-JCP3>3.0.CO;2-V }}
*{{cite journal | author=Blumberg H, Conklin D, Xu WF, ''et al.'' |title=Interleukin 20: discovery, receptor identification, and role in epidermal function. |journal=Cell |volume=104 |issue= 1 |pages= 9-19 |year= 2001 |pmid= 11163236 |doi= }}
*{{cite journal | author=Huang EY, Madireddi MT, Gopalkrishnan RV, ''et al.'' |title=Genomic structure, chromosomal localization and expression profile of a novel melanoma differentiation associated (mda-7) gene with cancer specific growth suppressing and apoptosis inducing properties. |journal=Oncogene |volume=20 |issue= 48 |pages= 7051-63 |year= 2001 |pmid= 11704829 |doi= 10.1038/sj.onc.1204897 }}
*{{cite journal | author=Wang M, Tan Z, Zhang R, ''et al.'' |title=Interleukin 24 (MDA-7/MOB-5) signals through two heterodimeric receptors, IL-22R1/IL-20R2 and IL-20R1/IL-20R2. |journal=J. Biol. Chem. |volume=277 |issue= 9 |pages= 7341-7 |year= 2002 |pmid= 11706020 |doi= 10.1074/jbc.M106043200 }}
*{{cite journal | author=Ellerhorst JA, Prieto VG, Ekmekcioglu S, ''et al.'' |title=Loss of MDA-7 expression with progression of melanoma. |journal=J. Clin. Oncol. |volume=20 |issue= 4 |pages= 1069-74 |year= 2002 |pmid= 11844832 |doi= }}
*{{cite journal | author=Caudell EG, Mumm JB, Poindexter N, ''et al.'' |title=The protein product of the tumor suppressor gene, melanoma differentiation-associated gene 7, exhibits immunostimulatory activity and is designated IL-24. |journal=J. Immunol. |volume=168 |issue= 12 |pages= 6041-6 |year= 2002 |pmid= 12055212 |doi= }}
*{{cite journal | author=Saeki T, Mhashilkar A, Swanson X, ''et al.'' |title=Inhibition of human lung cancer growth following adenovirus-mediated mda-7 gene expression in vivo. |journal=Oncogene |volume=21 |issue= 29 |pages= 4558-66 |year= 2002 |pmid= 12085234 |doi= 10.1038/sj.onc.1205553 }}
*{{cite journal | author=Sarkar D, Su ZZ, Lebedeva IV, ''et al.'' |title=mda-7 (IL-24) Mediates selective apoptosis in human melanoma cells by inducing the coordinated overexpression of the GADD family of genes by means of p38 MAPK. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 15 |pages= 10054-9 |year= 2002 |pmid= 12114539 |doi= 10.1073/pnas.152327199 }}
*{{cite journal | author=Garn H, Schmidt A, Grau V, ''et al.'' |title=IL-24 is expressed by rat and human macrophages. |journal=Immunobiology |volume=205 |issue= 3 |pages= 321-34 |year= 2003 |pmid= 12182458 |doi= }}
*{{cite journal | author=Parrish-Novak J, Xu W, Brender T, ''et al.'' |title=Interleukins 19, 20, and 24 signal through two distinct receptor complexes. Differences in receptor-ligand interactions mediate unique biological functions. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47517-23 |year= 2003 |pmid= 12351624 |doi= 10.1074/jbc.M205114200 }}
*{{cite journal | author=Sarkar D, Su ZZ, Lebedeva IV, ''et al.'' |title=mda-7 (IL-24): signaling and functional roles. |journal=BioTechniques |volume=Suppl |issue= |pages= 30-9 |year= 2003 |pmid= 12395925 |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=Ekmekcioglu S, Ellerhorst JA, Mumm JB, ''et al.'' |title=Negative association of melanoma differentiation-associated gene (mda-7) and inducible nitric oxide synthase (iNOS) in human melanoma: MDA-7 regulates iNOS expression in melanoma cells. |journal=Mol. Cancer Ther. |volume=2 |issue= 1 |pages= 9-17 |year= 2003 |pmid= 12533668 |doi= }}
*{{cite journal | author=Su ZZ, Lebedeva IV, Sarkar D, ''et al.'' |title=Melanoma differentiation associated gene-7, mda-7/IL-24, selectively induces growth suppression, apoptosis and radiosensitization in malignant gliomas in a p53-independent manner. |journal=Oncogene |volume=22 |issue= 8 |pages= 1164-80 |year= 2003 |pmid= 12606943 |doi= 10.1038/sj.onc.1206062 }}
*{{cite journal | author=Sauane M, Gopalkrishnan RV, Lebedeva I, ''et al.'' |title=Mda-7/IL-24 induces apoptosis of diverse cancer cell lines through JAK/STAT-independent pathways. |journal=J. Cell. Physiol. |volume=196 |issue= 2 |pages= 334-45 |year= 2003 |pmid= 12811827 |doi= 10.1002/jcp.10309 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LILRB1... {November 18, 2007 2:36:19 PM PST}
- SEARCH REDIRECT: Control Box Found: LILRB1 {November 18, 2007 2:37:47 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 2:37:49 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 2:37:49 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 2:37:49 PM PST}
- UPDATED: Updated protein page: LILRB1 {November 18, 2007 2:38:04 PM PST}
- INFO: Beginning work on NPHS2... {November 18, 2007 2:30:45 PM PST}
- SEARCH REDIRECT: Control Box Found: NPHS2 {November 18, 2007 2:31:36 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 2:31:44 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 2:31:44 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 2:31:44 PM PST}
- UPDATED: Updated protein page: NPHS2 {November 18, 2007 2:31:59 PM PST}
- INFO: Beginning work on PIAS2... {November 18, 2007 2:31:59 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:34:02 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 = Protein inhibitor of activated STAT, 2
| HGNCid = 17311
| Symbol = PIAS2
| AltSymbols =; MGC102682; MIZ1; PIASX-ALPHA; PIASX-BETA; SIZ2; ZMIZ4; miz
| OMIM = 603567
| ECnumber =
| Homologene = 20979
| MGIid = 1096566
| GeneAtlas_image1 = PBB_GE_PIAS2_37433_at_tn.png
| GeneAtlas_image2 = PBB_GE_PIAS2_214442_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_PIAS2_214593_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0019789 |text = SUMO ligase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0050681 |text = androgen receptor binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0016925 |text = protein sumoylation}} {{GNF_GO|id=GO:0030521 |text = androgen receptor signaling pathway}} {{GNF_GO|id=GO:0045893 |text = positive regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9063
| Hs_Ensembl = ENSG00000078043
| Hs_RefseqProtein = XP_001129747
| Hs_RefseqmRNA = XM_001129747
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 42646058
| Hs_GenLoc_end = 42751464
| Hs_Uniprot = O75928
| Mm_EntrezGene = 17344
| Mm_Ensembl = ENSMUSG00000025423
| Mm_RefseqmRNA = XM_990156
| Mm_RefseqProtein = XP_995250
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 77301699
| Mm_GenLoc_end = 77357244
| Mm_Uniprot = Q3V3U5
}}
}}
'''Protein inhibitor of activated STAT, 2''', also known as '''PIAS2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PIAS2 protein inhibitor of activated STAT, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9063| 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=Cookson MR |title=Pathways to Parkinsonism. |journal=Neuron |volume=37 |issue= 1 |pages= 7-10 |year= 2003 |pmid= 12526767 |doi= }}
*{{cite journal | author=Wu L, Wu H, Ma L, ''et al.'' |title=Miz1, a novel zinc finger transcription factor that interacts with Msx2 and enhances its affinity for DNA. |journal=Mech. Dev. |volume=65 |issue= 1-2 |pages= 3-17 |year= 1997 |pmid= 9256341 |doi= }}
*{{cite journal | author=Liu B, Liao J, Rao X, ''et al.'' |title=Inhibition of Stat1-mediated gene activation by PIAS1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 18 |pages= 10626-31 |year= 1998 |pmid= 9724754 |doi= }}
*{{cite journal | author=Moilanen AM, Karvonen U, Poukka H, ''et al.'' |title=A testis-specific androgen receptor coregulator that belongs to a novel family of nuclear proteins. |journal=J. Biol. Chem. |volume=274 |issue= 6 |pages= 3700-4 |year= 1999 |pmid= 9920921 |doi= }}
*{{cite journal | author=Minty A, Dumont X, Kaghad M, Caput D |title=Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36316-23 |year= 2000 |pmid= 10961991 |doi= 10.1074/jbc.M004293200 }}
*{{cite journal | author=Kotaja N, Aittomäki S, Silvennoinen O, ''et al.'' |title=ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation. |journal=Mol. Endocrinol. |volume=14 |issue= 12 |pages= 1986-2000 |year= 2001 |pmid= 11117529 |doi= }}
*{{cite journal | author=Gross M, Liu B, Tan J, ''et al.'' |title=Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells. |journal=Oncogene |volume=20 |issue= 29 |pages= 3880-7 |year= 2001 |pmid= 11439351 |doi= 10.1038/sj.onc.1204489 }}
*{{cite journal | author=Takahashi K, Taira T, Niki T, ''et al.'' |title=DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor. |journal=J. Biol. Chem. |volume=276 |issue= 40 |pages= 37556-63 |year= 2001 |pmid= 11477070 |doi= 10.1074/jbc.M101730200 }}
*{{cite journal | author=Schmidt D, Müller S |title=Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 5 |pages= 2872-7 |year= 2002 |pmid= 11867732 |doi= 10.1073/pnas.052559499 }}
*{{cite journal | author=Tan JA, Hall SH, Hamil KG, ''et al.'' |title=Protein inhibitors of activated STAT resemble scaffold attachment factors and function as interacting nuclear receptor coregulators. |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 16993-7001 |year= 2002 |pmid= 11877418 |doi= 10.1074/jbc.M109217200 }}
*{{cite journal | author=Nishida T, Yasuda H |title=PIAS1 and PIASxalpha function as SUMO-E3 ligases toward androgen receptor and repress androgen receptor-dependent transcription. |journal=J. Biol. Chem. |volume=277 |issue= 44 |pages= 41311-7 |year= 2003 |pmid= 12177000 |doi= 10.1074/jbc.M206741200 }}
*{{cite journal | author=Tussie-Luna MI, Michel B, Hakre S, Roy AL |title=The SUMO ubiquitin-protein isopeptide ligase family member Miz1/PIASxbeta /Siz2 is a transcriptional cofactor for TFII-I. |journal=J. Biol. Chem. |volume=277 |issue= 45 |pages= 43185-93 |year= 2003 |pmid= 12193603 |doi= 10.1074/jbc.M207635200 }}
*{{cite journal | author=Tussié-Luna MI, Bayarsaihan D, Seto E, ''et al.'' |title=Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxbeta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 20 |pages= 12807-12 |year= 2002 |pmid= 12239342 |doi= 10.1073/pnas.192464499 }}
*{{cite journal | author=Miyauchi Y, Yogosawa S, Honda R, ''et al.'' |title=Sumoylation of Mdm2 by protein inhibitor of activated STAT (PIAS) and RanBP2 enzymes. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 50131-6 |year= 2003 |pmid= 12393906 |doi= 10.1074/jbc.M208319200 }}
*{{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=Arora T, Liu B, He H, ''et al.'' |title=PIASx is a transcriptional co-repressor of signal transducer and activator of transcription 4. |journal=J. Biol. Chem. |volume=278 |issue= 24 |pages= 21327-30 |year= 2003 |pmid= 12716907 |doi= 10.1074/jbc.C300119200 }}
*{{cite journal | author=Ohshima T, Shimotohno K |title=Transforming growth factor-beta-mediated signaling via the p38 MAP kinase pathway activates Smad-dependent transcription through SUMO-1 modification of Smad4. |journal=J. Biol. Chem. |volume=278 |issue= 51 |pages= 50833-42 |year= 2004 |pmid= 14514699 |doi= 10.1074/jbc.M307533200 }}
*{{cite journal | author=Lee BH, Yoshimatsu K, Maeda A, ''et al.'' |title=Association of the nucleocapsid protein of the Seoul and Hantaan hantaviruses with small ubiquitin-like modifier-1-related molecules. |journal=Virus Res. |volume=98 |issue= 1 |pages= 83-91 |year= 2004 |pmid= 14609633 |doi= }}
*{{cite journal | author=Lehner B, Semple JI, Brown SE, ''et al.'' |title=Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region. |journal=Genomics |volume=83 |issue= 1 |pages= 153-67 |year= 2004 |pmid= 14667819 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMB7... {November 18, 2007 2:21:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:21:41 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PSMB7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1iru.
| PDB = {{PDB2|1iru}}
| Name = Proteasome (prosome, macropain) subunit, beta type, 7
| HGNCid = 9544
| Symbol = PSMB7
| AltSymbols =; Z
| OMIM = 604030
| ECnumber =
| Homologene = 2093
| MGIid = 107637
| GeneAtlas_image1 = PBB_GE_PSMB7_200786_at_tn.png
| Function = {{GNF_GO|id=GO:0004298 |text = threonine endopeptidase activity}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005839 |text = proteasome core complex (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5695
| Hs_Ensembl = ENSG00000136930
| Hs_RefseqProtein = NP_002790
| Hs_RefseqmRNA = NM_002799
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 126155566
| Hs_GenLoc_end = 126217542
| Hs_Uniprot = Q99436
| Mm_EntrezGene = 19177
| Mm_Ensembl = ENSMUSG00000026750
| Mm_RefseqmRNA = NM_011187
| Mm_RefseqProtein = NP_035317
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 38410046
| Mm_GenLoc_end = 38465927
| Mm_Uniprot = Q5D098
}}
}}
'''Proteasome (prosome, macropain) subunit, beta type, 7''', also known as '''PSMB7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMB7 proteasome (prosome, macropain) subunit, beta type, 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5695| 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 proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure 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. 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 member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit in the proteasome. Expression of this catalytic subunit is downregulated by gamma interferon and proteolytic processing is required to generate a mature subunit. This subunit is not present in the immunoproteasome and is replaced by catalytic subunit 2i (proteasome beta 10 subunit).<ref name="entrez">{{cite web | title = Entrez Gene: PSMB7 proteasome (prosome, macropain) subunit, beta type, 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5695| 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=Rivett AJ, Bose S, Brooks P, Broadfoot KI |title=Regulation of proteasome complexes by gamma-interferon and phosphorylation. |journal=Biochimie |volume=83 |issue= 3-4 |pages= 363-6 |year= 2001 |pmid= 11295498 |doi= }}
*{{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=Kristensen P, Johnsen AH, Uerkvitz W, ''et al.'' |title=Human proteasome subunits from 2-dimensional gels identified by partial sequencing. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 3 |pages= 1785-9 |year= 1995 |pmid= 7811265 |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=Hisamatsu H, Shimbara N, Saito Y, ''et al.'' |title=Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma. |journal=J. Exp. Med. |volume=183 |issue= 4 |pages= 1807-16 |year= 1996 |pmid= 8666937 |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=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=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=O'Hare T, Wiens GD, Whitcomb EA, ''et al.'' |title=Cutting edge: proteasome involvement in the degradation of unassembled Ig light chains. |journal=J. Immunol. |volume=163 |issue= 1 |pages= 11-4 |year= 1999 |pmid= 10384092 |doi= }}
*{{cite journal | author=Elenich LA, Nandi D, Kent AE, ''et al.'' |title=The complete primary structure of mouse 20S proteasomes. |journal=Immunogenetics |volume=49 |issue= 10 |pages= 835-42 |year= 1999 |pmid= 10436176 |doi= }}
*{{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=Feng Y, Longo DL, Ferris DK |title=Polo-like kinase interacts with proteasomes and regulates their activity. |journal=Cell Growth Differ. |volume=12 |issue= 1 |pages= 29-37 |year= 2001 |pmid= 11205743 |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= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMC6... {November 18, 2007 2:21:41 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:22:27 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Proteasome (prosome, macropain) 26S subunit, ATPase, 6
| HGNCid = 9553
| Symbol = PSMC6
| AltSymbols =; CADP44; MGC12520; P44; SUG2; p42
| OMIM = 602708
| ECnumber =
| Homologene = 2099
| MGIid = 1914339
| GeneAtlas_image1 = PBB_GE_PSMC6_201699_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}} {{GNF_GO|id=GO:0030674 |text = protein binding, bridging}}
| Component = {{GNF_GO|id=GO:0000502 |text = proteasome complex (sensu Eukaryota)}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0030163 |text = protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5706
| Hs_Ensembl = ENSG00000100519
| Hs_RefseqProtein = NP_002797
| Hs_RefseqmRNA = NM_002806
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 52243668
| Hs_GenLoc_end = 52264463
| Hs_Uniprot = P62333
| Mm_EntrezGene = 67089
| Mm_Ensembl = ENSMUSG00000021832
| Mm_RefseqmRNA = NM_025959
| Mm_RefseqProtein = NP_080235
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 44251722
| Mm_GenLoc_end = 44271565
| Mm_Uniprot = Q14AQ1
}}
}}
'''Proteasome (prosome, macropain) 26S subunit, ATPase, 6''', also known as '''PSMC6''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMC6 proteasome (prosome, macropain) 26S subunit, ATPase, 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5706| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the ATPase subunits, a member of the triple-A family of ATPases which have a chaperone-like activity. Pseudogenes have been identified on chromosomes 8 and 12.<ref name="entrez">{{cite web | title = Entrez Gene: PSMC6 proteasome (prosome, macropain) 26S subunit, ATPase, 6| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5706| 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=Hastings R, Walker G, Eyheralde I, ''et al.'' |title=Activator complexes containing the proteasomal regulatory ATPases S10b (SUG2) and S6 (TBP1) in different tissues and organisms. |journal=Mol. Biol. Rep. |volume=26 |issue= 1-2 |pages= 35-8 |year= 1999 |pmid= 10363644 |doi= }}
*{{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=DeMartino GN, Proske RJ, Moomaw CR, ''et al.'' |title=Identification, purification, and characterization of a PA700-dependent activator of the proteasome. |journal=J. Biol. Chem. |volume=271 |issue= 6 |pages= 3112-8 |year= 1996 |pmid= 8621709 |doi= }}
*{{cite journal | author=Fujiwara T, Watanabe TK, Tanaka K, ''et al.'' |title=cDNA cloning of p42, a shared subunit of two proteasome regulatory proteins, reveals a novel member of the AAA protein family. |journal=FEBS Lett. |volume=387 |issue= 2-3 |pages= 184-8 |year= 1996 |pmid= 8674546 |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=Tipler CP, Hutchon SP, Hendil K, ''et al.'' |title=Purification and characterization of 26S proteasomes from human and mouse spermatozoa. |journal=Mol. Hum. Reprod. |volume=3 |issue= 12 |pages= 1053-60 |year= 1998 |pmid= 9464850 |doi= }}
*{{cite journal | author=Tanahashi N, Suzuki M, Fujiwara T, ''et al.'' |title=Chromosomal localization and immunological analysis of a family of human 26S proteasomal ATPases. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 1 |pages= 229-32 |year= 1998 |pmid= 9473509 |doi= }}
*{{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=Russell SJ, Steger KA, Johnston SA |title=Subcellular localization, stoichiometry, and protein levels of 26 S proteasome subunits in yeast. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21943-52 |year= 1999 |pmid= 10419517 |doi= }}
*{{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=Russell SJ, Gonzalez F, Joshua-Tor L, Johnston SA |title=Selective chemical inactivation of AAA proteins reveals distinct functions of proteasomal ATPases. |journal=Chem. Biol. |volume=8 |issue= 10 |pages= 941-50 |year= 2002 |pmid= 11590019 |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=Reiser G, Bernstein HG |title=Neurons and plaques of Alzheimer's disease patients highly express the neuronal membrane docking protein p42IP4/centaurin alpha. |journal=Neuroreport |volume=13 |issue= 18 |pages= 2417-9 |year= 2003 |pmid= 12499840 |doi= 10.1097/01.wnr.0000048005.96487.10 }}
*{{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= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSMD1... {November 18, 2007 2:22:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:23:03 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, 1
| HGNCid = 9554
| Symbol = PSMD1
| AltSymbols =; MGC133040; MGC133041; P112; S1
| OMIM =
| ECnumber =
| Homologene = 2100
| MGIid = 1917497
| GeneAtlas_image1 = PBB_GE_PSMD1_201198_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSMD1_201199_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005488 |text = binding}}
| 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}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5707
| Hs_Ensembl = ENSG00000173692
| Hs_RefseqProtein = NP_002798
| Hs_RefseqmRNA = NM_002807
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 231629836
| Hs_GenLoc_end = 231745712
| Hs_Uniprot = Q99460
| Mm_EntrezGene = 70247
| Mm_Ensembl = ENSMUSG00000026229
| Mm_RefseqmRNA = NM_027357
| Mm_RefseqProtein = NP_081633
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 87895790
| Mm_GenLoc_end = 87970466
| Mm_Uniprot = A0JLU3
}}
}}
'''Proteasome (prosome, macropain) 26S subunit, non-ATPase, 1''', also known as '''PSMD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMD1 proteasome (prosome, macropain) 26S subunit, non-ATPase, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5707| 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 the largest non-ATPase subunit of the 19S regulator lid, which is responsible for substrate recognition and binding.<ref name="entrez">{{cite web | title = Entrez Gene: PSMD1 proteasome (prosome, macropain) 26S subunit, non-ATPase, 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5707| 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=Yokota K, Kagawa S, Shimizu Y, ''et al.'' |title=CDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3p. |journal=Mol. Biol. Cell |volume=7 |issue= 6 |pages= 853-70 |year= 1997 |pmid= 8816993 |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=Lüders J, Demand J, Höhfeld J |title=The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome. |journal=J. Biol. Chem. |volume=275 |issue= 7 |pages= 4613-7 |year= 2000 |pmid= 10671488 |doi= }}
*{{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=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 PSMD13... {November 18, 2007 2:23:36 PM PST}
- SEARCH REDIRECT: Control Box Found: PSMD13 {November 18, 2007 2:24:06 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 2:24:10 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 2:24:10 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 2:24:10 PM PST}
- UPDATED: Updated protein page: PSMD13 {November 18, 2007 2:24:16 PM PST}
- INFO: Beginning work on PSMD2... {November 18, 2007 2:23:03 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:23:36 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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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 = Proteasome (prosome, macropain) 26S subunit, non-ATPase, 2
| HGNCid = 9559
| Symbol = PSMD2
| AltSymbols =; MGC14274; P97; S2; TRAP2
| OMIM = 606223
| ECnumber =
| Homologene = 2101
| MGIid = 1096584
| GeneAtlas_image1 = PBB_GE_PSMD2_200830_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| 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}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5708
| Hs_Ensembl = ENSG00000175166
| Hs_RefseqProtein = NP_002799
| Hs_RefseqmRNA = NM_002808
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 185499189
| Hs_GenLoc_end = 185509531
| Hs_Uniprot = Q13200
| Mm_EntrezGene = 21762
| Mm_Ensembl = ENSMUSG00000006998
| Mm_RefseqmRNA = NM_134101
| Mm_RefseqProtein = NP_598862
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 20565229
| Mm_GenLoc_end = 20576955
| Mm_Uniprot = Q3TI61
}}
}}
'''Proteasome (prosome, macropain) 26S subunit, non-ATPase, 2''', also known as '''PSMD2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMD2 proteasome (prosome, macropain) 26S subunit, non-ATPase, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5708| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the non-ATPase subunits of the 19S regulator lid. In addition to participation in proteasome function, this subunit may also participate in the TNF signalling pathway since it interacts with the tumor necrosis factor type 1 receptor. A pseudogene has been identified on chromosome 1.<ref name="entrez">{{cite web | title = Entrez Gene: PSMD2 proteasome (prosome, macropain) 26S subunit, non-ATPase, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5708| 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=Boldin MP, Mett IL, Wallach D |title=A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its 'death domain'. |journal=FEBS Lett. |volume=367 |issue= 1 |pages= 39-44 |year= 1995 |pmid= 7601280 |doi= }}
*{{cite journal | author=Song HY, Donner DB |title=Association of a RING finger protein with the cytoplasmic domain of the human type-2 tumour necrosis factor receptor. |journal=Biochem. J. |volume=309 ( Pt 3) |issue= |pages= 825-9 |year= 1995 |pmid= 7639698 |doi= }}
*{{cite journal | author=Tsurumi C, Shimizu Y, Saeki M, ''et al.'' |title=cDNA cloning and functional analysis of the p97 subunit of the 26S proteasome, a polypeptide identical to the type-1 tumor-necrosis-factor-receptor-associated protein-2/55.11. |journal=Eur. J. Biochem. |volume=239 |issue= 3 |pages= 912-21 |year= 1996 |pmid= 8774743 |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=Dunbar JD, Song HY, Guo D, ''et al.'' |title=Two-hybrid cloning of a gene encoding TNF receptor-associated protein 2, a protein that interacts with the intracellular domain of the type 1 TNF receptor: identity with subunit 2 of the 26S protease. |journal=J. Immunol. |volume=158 |issue= 9 |pages= 4252-9 |year= 1997 |pmid= 9126987 |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=Gorbea C, Taillandier D, Rechsteiner M |title=Mapping subunit contacts in the regulatory complex of the 26 S proteasome. S2 and S5b form a tetramer with ATPase subunits S4 and S7. |journal=J. Biol. Chem. |volume=275 |issue= 2 |pages= 875-82 |year= 2000 |pmid= 10625621 |doi= }}
*{{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=You J, Pickart CM |title=A HECT domain E3 enzyme assembles novel polyubiquitin chains. |journal=J. Biol. Chem. |volume=276 |issue= 23 |pages= 19871-8 |year= 2001 |pmid= 11278995 |doi= 10.1074/jbc.M100034200 }}
*{{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=You J, Wang M, Aoki T, ''et al.'' |title=Proteolytic targeting of transcriptional regulator TIP120B by a HECT domain E3 ligase. |journal=J. Biol. Chem. |volume=278 |issue= 26 |pages= 23369-75 |year= 2003 |pmid= 12692129 |doi= 10.1074/jbc.M212887200 }}
*{{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 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAB3A... {November 18, 2007 2:24:59 PM PST}
- SEARCH: Multiple Conflicting Pages. Need Resolution. {November 18, 2007 2:25:23 PM PST}
- AMBIGUITY: More than one potential page found for updating, RAB3A RAB3A {November 18, 2007 2:25:23 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_RAB3A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1zbd.
| PDB = {{PDB2|1zbd}}, {{PDB2|3rab}}
| Name = RAB3A, member RAS oncogene family
| HGNCid = 9777
| Symbol = RAB3A
| AltSymbols =;
| OMIM = 179490
| ECnumber =
| Homologene = 20629
| MGIid = 97843
| GeneAtlas_image1 = PBB_GE_RAB3A_204974_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0008021 |text = synaptic vesicle}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0007269 |text = neurotransmitter secretion}} {{GNF_GO|id=GO:0015031 |text = protein transport}} {{GNF_GO|id=GO:0017157 |text = regulation of exocytosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5864
| Hs_Ensembl = ENSG00000105649
| Hs_RefseqProtein = NP_002857
| Hs_RefseqmRNA = NM_002866
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 18168611
| Hs_GenLoc_end = 18175839
| Hs_Uniprot = P20336
| Mm_EntrezGene = 19339
| Mm_Ensembl = ENSMUSG00000031840
| Mm_RefseqmRNA = NM_009001
| Mm_RefseqProtein = NP_033027
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 73684845
| Mm_GenLoc_end = 73687077
| Mm_Uniprot = Q0PD63
}}
}}
'''RAB3A, member RAS oncogene family''', also known as '''RAB3A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAB3A RAB3A, member RAS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5864| 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=Khosravi-Far R, Lutz RJ, Cox AD, ''et al.'' |title=Isoprenoid modification of rab proteins terminating in CC or CXC motifs. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 14 |pages= 6264-8 |year= 1991 |pmid= 1648736 |doi= }}
*{{cite journal | author=Zahraoui A, Touchot N, Chardin P, Tavitian A |title=The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion. |journal=J. Biol. Chem. |volume=264 |issue= 21 |pages= 12394-401 |year= 1989 |pmid= 2501306 |doi= }}
*{{cite journal | author=Rousseau-Merck MF, Zahraoui A, Bernheim A, ''et al.'' |title=Chromosome mapping of the human ras-related rab3A gene to 19p13.2. |journal=Genomics |volume=5 |issue= 4 |pages= 694-8 |year= 1990 |pmid= 2687157 |doi= }}
*{{cite journal | author=Brondyk WH, McKiernan CJ, Fortner KA, ''et al.'' |title=Interaction cloning of Rabin3, a novel protein that associates with the Ras-like GTPase Rab3A. |journal=Mol. Cell. Biol. |volume=15 |issue= 3 |pages= 1137-43 |year= 1995 |pmid= 7532276 |doi= }}
*{{cite journal | author=Farnsworth CC, Seabra MC, Ericsson LH, ''et al.'' |title=Rab geranylgeranyl transferase catalyzes the geranylgeranylation of adjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 25 |pages= 11963-7 |year= 1995 |pmid= 7991565 |doi= }}
*{{cite journal | author=McKiernan CJ, Brondyk WH, Macara IG |title=The Rab3A GTPase interacts with multiple factors through the same effector domain. Mutational analysis of cross-linking of Rab3A to a putative target protein. |journal=J. Biol. Chem. |volume=268 |issue= 32 |pages= 24449-52 |year= 1993 |pmid= 8226995 |doi= }}
*{{cite journal | author=Trask B, Fertitta A, Christensen M, ''et al.'' |title=Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers. |journal=Genomics |volume=15 |issue= 1 |pages= 133-45 |year= 1993 |pmid= 8432525 |doi= }}
*{{cite journal | author=Johannes L, Perez F, Laran-Chich MP, ''et al.'' |title=Characterization of the interaction of the monomeric GTP-binding protein Rab3a with geranylgeranyl transferase II. |journal=Eur. J. Biochem. |volume=239 |issue= 2 |pages= 362-8 |year= 1996 |pmid= 8706741 |doi= }}
*{{cite journal | author=Burton JL, Slepnev V, De Camilli PV |title=An evolutionarily conserved domain in a subfamily of Rabs is crucial for the interaction with the guanyl nucleotide exchange factor Mss4. |journal=J. Biol. Chem. |volume=272 |issue= 6 |pages= 3663-8 |year= 1997 |pmid= 9013620 |doi= }}
*{{cite journal | author=Geppert M, Goda Y, Stevens CF, Südhof TC |title=The small GTP-binding protein Rab3A regulates a late step in synaptic vesicle fusion. |journal=Nature |volume=387 |issue= 6635 |pages= 810-4 |year= 1997 |pmid= 9194562 |doi= 10.1038/42954 }}
*{{cite journal | author=Martincic I, Peralta ME, Ngsee JK |title=Isolation and characterization of a dual prenylated Rab and VAMP2 receptor. |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 26991-8 |year= 1997 |pmid= 9341137 |doi= }}
*{{cite journal | author=Ostermeier C, Brunger AT |title=Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A. |journal=Cell |volume=96 |issue= 3 |pages= 363-74 |year= 1999 |pmid= 10025402 |doi= }}
*{{cite journal | author=Jung YJ, Lee TH, Lee JY, ''et al.'' |title=Phosphatidic acid is important to the translocation of Rab3A from the cytosol to phospholipid membranes. |journal=Neuroreport |volume=10 |issue= 13 |pages= 2859-63 |year= 1999 |pmid= 10511453 |doi= }}
*{{cite journal | author=Sullivan M, Olsen AS, Houslay MD |title=Genomic organisation of the human cyclic AMP-specific phosphodiesterase PDE4C gene and its chromosomal localisation to 19p13.1, between RAB3A and JUND. |journal=Cell. Signal. |volume=11 |issue= 10 |pages= 735-42 |year= 2000 |pmid= 10574328 |doi= }}
*{{cite journal | author=Clabecq A, Henry JP, Darchen F |title=Biochemical characterization of Rab3-GTPase-activating protein reveals a mechanism similar to that of Ras-GAP. |journal=J. Biol. Chem. |volume=275 |issue= 41 |pages= 31786-91 |year= 2000 |pmid= 10859313 |doi= 10.1074/jbc.M003705200 }}
*{{cite journal | author=Haynes LP, Evans GJ, Morgan A, Burgoyne RD |title=A direct inhibitory role for the Rab3-specific effector, Noc2, in Ca2+-regulated exocytosis in neuroendocrine cells. |journal=J. Biol. Chem. |volume=276 |issue= 13 |pages= 9726-32 |year= 2001 |pmid= 11134008 |doi= 10.1074/jbc.M006959200 }}
*{{cite journal | author=Zhang Y, Luan Z, Liu A, Hu G |title=The scaffolding protein CASK mediates the interaction between rabphilin3a and beta-neurexins. |journal=FEBS Lett. |volume=497 |issue= 2-3 |pages= 99-102 |year= 2001 |pmid= 11377421 |doi= }}
*{{cite journal | author=Luo HR, Saiardi A, Nagata E, ''et al.'' |title=GRAB: a physiologic guanine nucleotide exchange factor for Rab3A, which interacts with inositol hexakisphosphate kinase. |journal=Neuron |volume=31 |issue= 3 |pages= 439-51 |year= 2001 |pmid= 11516400 |doi= }}
*{{cite journal | author=Piiper A, Leser J, Lutz MP, ''et al.'' |title=Subcellular distribution and function of Rab3A-D in pancreatic acinar AR42J cells. |journal=Biochem. Biophys. Res. Commun. |volume=287 |issue= 3 |pages= 746-51 |year= 2001 |pmid= 11563859 |doi= 10.1006/bbrc.2001.5651 }}
*{{cite journal | author=Kuroda TS, Fukuda M, Ariga H, Mikoshiba K |title=The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain. |journal=J. Biol. Chem. |volume=277 |issue= 11 |pages= 9212-8 |year= 2002 |pmid= 11773082 |doi= 10.1074/jbc.M112414200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAB4A... {November 18, 2007 2:25:23 PM PST}
- SEARCH: Multiple Conflicting Pages. Need Resolution. {November 18, 2007 2:25:44 PM PST}
- AMBIGUITY: More than one potential page found for updating, RAB4A RAB4A {November 18, 2007 2:25:44 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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| 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_RAB4A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1yu9.
| PDB = {{PDB2|1yu9}}, {{PDB2|1z0k}}, {{PDB2|2bmd}}, {{PDB2|2bme}}
| Name = RAB4A, member RAS oncogene family
| HGNCid = 9781
| Symbol = RAB4A
| AltSymbols =; RAB4
| OMIM = 179511
| ECnumber =
| Homologene = 55834
| MGIid = 105069
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003924 |text = GTPase activity}} {{GNF_GO|id=GO:0005525 |text = GTP binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0007264 |text = small GTPase mediated signal transduction}} {{GNF_GO|id=GO:0015031 |text = protein transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5867
| Hs_Ensembl =
| Hs_RefseqProtein = NP_004569
| Hs_RefseqmRNA = NM_004578
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 19341
| Mm_Ensembl = ENSMUSG00000019478
| Mm_RefseqmRNA = NM_009003
| Mm_RefseqProtein = NP_033029
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 126692115
| Mm_GenLoc_end = 126721377
| Mm_Uniprot = Q3TSQ6
}}
}}
'''RAB4A, member RAS oncogene family''', also known as '''RAB4A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAB4A RAB4A, member RAS oncogene family| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5867| 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=Stibbs HH, Seed JR |title=Short-term metabolism of (14-C) tryptophan in rats infected with Trypanosoma brucei gambiense. |journal=J. Infect. Dis. |volume=131 |issue= 4 |pages= 459-62 |year= 1975 |pmid= 1117200 |doi= }}
*{{cite journal | author=van der Sluijs P, Hull M, Huber LA, ''et al.'' |title=Reversible phosphorylation--dephosphorylation determines the localization of rab4 during the cell cycle. |journal=EMBO J. |volume=11 |issue= 12 |pages= 4379-89 |year= 1992 |pmid= 1425574 |doi= }}
*{{cite journal | author=Bailly E, McCaffrey M, Touchot N, ''et al.'' |title=Phosphorylation of two small GTP-binding proteins of the Rab family by p34cdc2. |journal=Nature |volume=350 |issue= 6320 |pages= 715-8 |year= 1991 |pmid= 1902553 |doi= 10.1038/350715a0 }}
*{{cite journal | author=Rousseau-Merck MF, Zahraoui A, Touchot N, ''et al.'' |title=Chromosome assignment of four RAS-related RAB genes. |journal=Hum. Genet. |volume=86 |issue= 4 |pages= 350-4 |year= 1991 |pmid= 1999336 |doi= }}
*{{cite journal | author=Zahraoui A, Touchot N, Chardin P, Tavitian A |title=The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion. |journal=J. Biol. Chem. |volume=264 |issue= 21 |pages= 12394-401 |year= 1989 |pmid= 2501306 |doi= }}
*{{cite journal | author=Cormont M, Tanti JF, Zahraoui A, ''et al.'' |title=Rab4 is phosphorylated by the insulin-activated extracellular-signal-regulated kinase ERK1. |journal=Eur. J. Biochem. |volume=219 |issue= 3 |pages= 1081-5 |year= 1994 |pmid= 8112321 |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=Karniguian A, Zahraoui A, Tavitian A |title=Identification of small GTP-binding rab proteins in human platelets: thrombin-induced phosphorylation of rab3B, rab6, and rab8 proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 16 |pages= 7647-51 |year= 1993 |pmid= 8356066 |doi= }}
*{{cite journal | author=Valentijn JA, LaCivita DQ, Gumkowski FD, Jamieson JD |title=Rab4 associates with the actin terminal web in developing rat pancreatic acinar cells. |journal=Eur. J. Cell Biol. |volume=72 |issue= 1 |pages= 1-8 |year= 1997 |pmid= 9013719 |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=Vitale G, Rybin V, Christoforidis S, ''et al.'' |title=Distinct Rab-binding domains mediate the interaction of Rabaptin-5 with GTP-bound Rab4 and Rab5. |journal=EMBO J. |volume=17 |issue= 7 |pages= 1941-51 |year= 1998 |pmid= 9524117 |doi= 10.1093/emboj/17.7.1941 }}
*{{cite journal | author=Bucci C, Chiariello M, Lattero D, ''et al.'' |title=Interaction cloning and characterization of the cDNA encoding the human prenylated rab acceptor (PRA1). |journal=Biochem. Biophys. Res. Commun. |volume=258 |issue= 3 |pages= 657-62 |year= 1999 |pmid= 10329441 |doi= 10.1006/bbrc.1999.0651 }}
*{{cite journal | author=Shisheva A, Chinni SR, DeMarco C |title=General role of GDP dissociation inhibitor 2 in membrane release of Rab proteins: modulations of its functional interactions by in vitro and in vivo structural modifications. |journal=Biochemistry |volume=38 |issue= 36 |pages= 11711-21 |year= 1999 |pmid= 10512627 |doi= }}
*{{cite journal | author=Nagelkerken B, Van Anken E, Van Raak M, ''et al.'' |title=Rabaptin4, a novel effector of the small GTPase rab4a, is recruited to perinuclear recycling vesicles. |journal=Biochem. J. |volume=346 Pt 3 |issue= |pages= 593-601 |year= 2000 |pmid= 10698684 |doi= }}
*{{cite journal | author=Gerez L, Mohrmann K, van Raak M, ''et al.'' |title=Accumulation of rab4GTP in the cytoplasm and association with the peptidyl-prolyl isomerase pin1 during mitosis. |journal=Mol. Biol. Cell |volume=11 |issue= 7 |pages= 2201-11 |year= 2000 |pmid= 10888662 |doi= }}
*{{cite journal | author=Li L, Omata W, Kojima I, Shibata H |title=Direct interaction of Rab4 with syntaxin 4. |journal=J. Biol. Chem. |volume=276 |issue= 7 |pages= 5265-73 |year= 2001 |pmid= 11063739 |doi= 10.1074/jbc.M003883200 }}
*{{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=Cormont M, Mari M, Galmiche A, ''et al.'' |title=A FYVE-finger-containing protein, Rabip4, is a Rab4 effector involved in early endosomal traffic. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 4 |pages= 1637-42 |year= 2001 |pmid= 11172003 |doi= 10.1073/pnas.031586998 }}
*{{cite journal | author=Bielli A, Thörnqvist PO, Hendrick AG, ''et al.'' |title=The small GTPase Rab4A interacts with the central region of cytoplasmic dynein light intermediate chain-1. |journal=Biochem. Biophys. Res. Commun. |volume=281 |issue= 5 |pages= 1141-53 |year= 2001 |pmid= 11243854 |doi= 10.1006/bbrc.2001.4468 }}
*{{cite journal | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAD1... {November 18, 2007 2:24:16 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:24:58 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 = RAD1 homolog (S. pombe)
| HGNCid = 9806
| Symbol = RAD1
| AltSymbols =; HRAD1; REC1
| OMIM = 603153
| ECnumber =
| Homologene = 37695
| MGIid = 1316678
| GeneAtlas_image1 = PBB_GE_RAD1_204460_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RAD1_204461_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_RAD1_210216_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008408 |text = 3'-5' exonuclease activity}} {{GNF_GO|id=GO:0008853 |text = exodeoxyribonuclease III activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0000075 |text = cell cycle checkpoint}} {{GNF_GO|id=GO:0000077 |text = DNA damage checkpoint}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0007128 |text = meiotic prophase I}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5810
| Hs_Ensembl = ENSG00000113456
| Hs_RefseqProtein = NP_002844
| Hs_RefseqmRNA = NM_002853
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 34941122
| Hs_GenLoc_end = 34954139
| Hs_Uniprot = O60671
| Mm_EntrezGene = 19355
| Mm_Ensembl = ENSMUSG00000022248
| Mm_RefseqmRNA = NM_011232
| Mm_RefseqProtein = NP_035362
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 10430759
| Mm_GenLoc_end = 10440784
| Mm_Uniprot = Q9QWZ1
}}
}}
'''RAD1 homolog (S. pombe)''', also known as '''RAD1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RAD1 RAD1 homolog (S. pombe)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5810| 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 component of a heterotrimeric cell cycle checkpoint complex, known as the 9-1-1 complex, that is activated to stop cell cycle progression in response to DNA damage or incomplete DNA replication. The 9-1-1 complex is recruited by RAD17 to affected sites where it may attract specialized DNA polymerases and other DNA repair effectors. Alternatively spliced transcript variants encoding different isoforms of this gene have been described.<ref name="entrez">{{cite web | title = Entrez Gene: RAD1 RAD1 homolog (S. pombe)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5810| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bardwell AJ, Bardwell L, Johnson DK, Friedberg EC |title=Yeast DNA recombination and repair proteins Rad1 and Rad10 constitute a complex in vivo mediated by localized hydrophobic domains. |journal=Mol. Microbiol. |volume=8 |issue= 6 |pages= 1177-88 |year= 1993 |pmid= 8361362 |doi= }}
*{{cite journal | author=Parker AE, Van de Weyer I, Laus MC, ''et al.'' |title=A human homologue of the Schizosaccharomyces pombe rad1+ checkpoint gene encodes an exonuclease. |journal=J. Biol. Chem. |volume=273 |issue= 29 |pages= 18332-9 |year= 1998 |pmid= 9660799 |doi= }}
*{{cite journal | author=Udell CM, Lee SK, Davey S |title=HRAD1 and MRAD1 encode mammalian homologues of the fission yeast rad1(+) cell cycle checkpoint control gene. |journal=Nucleic Acids Res. |volume=26 |issue= 17 |pages= 3971-6 |year= 1998 |pmid= 9705507 |doi= }}
*{{cite journal | author=Freire R, Murguía JR, Tarsounas M, ''et al.'' |title=Human and mouse homologs of Schizosaccharomyces pombe rad1(+) and Saccharomyces cerevisiae RAD17: linkage to checkpoint control and mammalian meiosis. |journal=Genes Dev. |volume=12 |issue= 16 |pages= 2560-73 |year= 1998 |pmid= 9716408 |doi= }}
*{{cite journal | author=Bluyssen HA, van Os RI, Naus NC, ''et al.'' |title=A human and mouse homolog of the Schizosaccharomyces pombe rad1+ cell cycle checkpoint control gene. |journal=Genomics |volume=54 |issue= 2 |pages= 331-7 |year= 1999 |pmid= 9828137 |doi= 10.1006/geno.1998.5582 }}
*{{cite journal | author=Marathi UK, Dahlen M, Sunnerhagen P, ''et al.'' |title=RAD1, a human structural homolog of the Schizosaccharomyces pombe RAD1 cell cycle checkpoint gene. |journal=Genomics |volume=54 |issue= 2 |pages= 344-7 |year= 1999 |pmid= 9828139 |doi= 10.1006/geno.1998.5589 }}
*{{cite journal | author=Volkmer E, Karnitz LM |title=Human homologs of Schizosaccharomyces pombe rad1, hus1, and rad9 form a DNA damage-responsive protein complex. |journal=J. Biol. Chem. |volume=274 |issue= 2 |pages= 567-70 |year= 1999 |pmid= 9872989 |doi= }}
*{{cite journal | author=Dean FB, Lian L, O'Donnell M |title=cDNA cloning and gene mapping of human homologs for Schizosaccharomyces pombe rad17, rad1, and hus1 and cloning of homologs from mouse, Caenorhabditis elegans, and Drosophila melanogaster. |journal=Genomics |volume=54 |issue= 3 |pages= 424-36 |year= 1999 |pmid= 9878245 |doi= 10.1006/geno.1998.5587 }}
*{{cite journal | author=St Onge RP, Udell CM, Casselman R, Davey S |title=The human G2 checkpoint control protein hRAD9 is a nuclear phosphoprotein that forms complexes with hRAD1 and hHUS1. |journal=Mol. Biol. Cell |volume=10 |issue= 6 |pages= 1985-95 |year= 1999 |pmid= 10359610 |doi= }}
*{{cite journal | author=Hang H, Lieberman HB |title=Physical interactions among human checkpoint control proteins HUS1p, RAD1p, and RAD9p, and implications for the regulation of cell cycle progression. |journal=Genomics |volume=65 |issue= 1 |pages= 24-33 |year= 2000 |pmid= 10777662 |doi= 10.1006/geno.2000.6142 }}
*{{cite journal | author=Cai RL, Yan-Neale Y, Cueto MA, ''et al.'' |title=HDAC1, a histone deacetylase, forms a complex with Hus1 and Rad9, two G2/M checkpoint Rad proteins. |journal=J. Biol. Chem. |volume=275 |issue= 36 |pages= 27909-16 |year= 2000 |pmid= 10846170 |doi= 10.1074/jbc.M000168200 }}
*{{cite journal | author=Burtelow MA, Kaufmann SH, Karnitz LM |title=Retention of the human Rad9 checkpoint complex in extraction-resistant nuclear complexes after DNA damage. |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26343-8 |year= 2000 |pmid= 10852904 |doi= 10.1074/jbc.M001244200 }}
*{{cite journal | author=Rauen M, Burtelow MA, Dufault VM, Karnitz LM |title=The human checkpoint protein hRad17 interacts with the PCNA-like proteins hRad1, hHus1, and hRad9. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29767-71 |year= 2000 |pmid= 10884395 |doi= 10.1074/jbc.M005782200 }}
*{{cite journal | author=Burtelow MA, Roos-Mattjus PM, Rauen M, ''et al.'' |title=Reconstitution and molecular analysis of the hRad9-hHus1-hRad1 (9-1-1) DNA damage responsive checkpoint complex. |journal=J. Biol. Chem. |volume=276 |issue= 28 |pages= 25903-9 |year= 2001 |pmid= 11340080 |doi= 10.1074/jbc.M102946200 }}
*{{cite journal | author=Bao S, Tibbetts RS, Brumbaugh KM, ''et al.'' |title=ATR/ATM-mediated phosphorylation of human Rad17 is required for genotoxic stress responses. |journal=Nature |volume=411 |issue= 6840 |pages= 969-74 |year= 2001 |pmid= 11418864 |doi= 10.1038/35082110 }}
*{{cite journal | author=Xiang SL, Kumano T, Iwasaki SI, ''et al.'' |title=The J domain of Tpr2 regulates its interaction with the proapoptotic and cell-cycle checkpoint protein, Rad9. |journal=Biochem. Biophys. Res. Commun. |volume=287 |issue= 4 |pages= 932-40 |year= 2001 |pmid= 11573955 |doi= 10.1006/bbrc.2001.5685 }}
*{{cite journal | author=Zou L, Cortez D, Elledge SJ |title=Regulation of ATR substrate selection by Rad17-dependent loading of Rad9 complexes onto chromatin. |journal=Genes Dev. |volume=16 |issue= 2 |pages= 198-208 |year= 2002 |pmid= 11799063 |doi= 10.1101/gad.950302 }}
*{{cite journal | author=Griffith JD, Lindsey-Boltz LA, Sancar A |title=Structures of the human Rad17-replication factor C and checkpoint Rad 9-1-1 complexes visualized by glycerol spray/low voltage microscopy. |journal=J. Biol. Chem. |volume=277 |issue= 18 |pages= 15233-6 |year= 2002 |pmid= 11907025 |doi= 10.1074/jbc.C200129200 }}
*{{cite journal | author=Hang H, Zhang Y, Dunbrack RL, ''et al.'' |title=Identification and characterization of a paralog of human cell cycle checkpoint gene HUS1. |journal=Genomics |volume=79 |issue= 4 |pages= 487-92 |year= 2002 |pmid= 11944979 |doi= 10.1006/geno.2002.6737 }}
*{{cite journal | author=Hirai I, Wang HG |title=A role of the C-terminal region of human Rad9 (hRad9) in nuclear transport of the hRad9 checkpoint complex. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 25722-7 |year= 2002 |pmid= 11994305 |doi= 10.1074/jbc.M203079200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SNAI1... {November 18, 2007 2:26:26 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:27:27 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Snail homolog 1 (Drosophila)
| HGNCid = 11128
| Symbol = SNAI1
| AltSymbols =; SLUGH2; SNA; SNAH; dJ710H13.1
| OMIM = 604238
| ECnumber =
| Homologene = 4363
| MGIid = 98330
| GeneAtlas_image1 = PBB_GE_SNAI1_219480_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{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:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001502 |text = cartilage condensation}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007399 |text = nervous system development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6615
| Hs_Ensembl = ENSG00000124216
| Hs_RefseqProtein = NP_005976
| Hs_RefseqmRNA = NM_005985
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 48032934
| Hs_GenLoc_end = 48038825
| Hs_Uniprot = O95863
| Mm_EntrezGene = 20613
| Mm_Ensembl = ENSMUSG00000042821
| Mm_RefseqmRNA = NM_011427
| Mm_RefseqProtein = NP_035557
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 167229432
| Mm_GenLoc_end = 167234019
| Mm_Uniprot = Q4FK48
}}
}}
'''Snail homolog 1 (Drosophila)''', also known as '''SNAI1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SNAI1 snail homolog 1 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6615| 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 Drosophila embryonic protein snail is a zinc finger transcriptional repressor which downregulates the expression of ectodermal genes within the mesoderm. The nuclear protein encoded by this gene is structurally similar to the Drosophila snail protein, and is also thought to be critical for mesoderm formation in the developing embryo. At least two variants of a similar processed pseudogene have been found on chromosome 2.<ref name="entrez">{{cite web | title = Entrez Gene: SNAI1 snail homolog 1 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6615| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Twigg SR, Wilkie AO |title=Characterisation of the human snail (SNAI1) gene and exclusion as a major disease gene in craniosynostosis. |journal=Hum. Genet. |volume=105 |issue= 4 |pages= 320-6 |year= 1999 |pmid= 10543399 |doi= }}
*{{cite journal | author=Paznekas WA, Okajima K, Schertzer M, ''et al.'' |title=Genomic organization, expression, and chromosome location of the human SNAIL gene (SNAI1) and a related processed pseudogene (SNAI1P). |journal=Genomics |volume=62 |issue= 1 |pages= 42-9 |year= 2000 |pmid= 10585766 |doi= 10.1006/geno.1999.6010 }}
*{{cite journal | author=Batlle E, Sancho E, Francí C, ''et al.'' |title=The transcription factor snail is a repressor of E-cadherin gene expression in epithelial tumour cells. |journal=Nat. Cell Biol. |volume=2 |issue= 2 |pages= 84-9 |year= 2000 |pmid= 10655587 |doi= 10.1038/35000034 }}
*{{cite journal | author=Smith S, Metcalfe JA, Elgar G |title=Identification and analysis of two snail genes in the pufferfish (Fugu rubripes) and mapping of human SNA to 20q. |journal=Gene |volume=247 |issue= 1-2 |pages= 119-28 |year= 2000 |pmid= 10773451 |doi= }}
*{{cite journal | author=Okubo T, Truong TK, Yu B, ''et al.'' |title=Down-regulation of promoter 1.3 activity of the human aromatase gene in breast tissue by zinc-finger protein, snail (SnaH). |journal=Cancer Res. |volume=61 |issue= 4 |pages= 1338-46 |year= 2001 |pmid= 11245431 |doi= }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal | author=Blanco MJ, Moreno-Bueno G, Sarrio D, ''et al.'' |title=Correlation of Snail expression with histological grade and lymph node status in breast carcinomas. |journal=Oncogene |volume=21 |issue= 20 |pages= 3241-6 |year= 2002 |pmid= 12082640 |doi= 10.1038/sj.onc.1205416 }}
*{{cite journal | author=Guaita S, Puig I, Franci C, ''et al.'' |title=Snail induction of epithelial to mesenchymal transition in tumor cells is accompanied by MUC1 repression and ZEB1 expression. |journal=J. Biol. Chem. |volume=277 |issue= 42 |pages= 39209-16 |year= 2002 |pmid= 12161443 |doi= 10.1074/jbc.M206400200 }}
*{{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=Yokoyama K, Kamata N, Fujimoto R, ''et al.'' |title=Increased invasion and matrix metalloproteinase-2 expression by Snail-induced mesenchymal transition in squamous cell carcinomas. |journal=Int. J. Oncol. |volume=22 |issue= 4 |pages= 891-8 |year= 2003 |pmid= 12632084 |doi= }}
*{{cite journal | author=Ikenouchi J, Matsuda M, Furuse M, Tsukita S |title=Regulation of tight junctions during the epithelium-mesenchyme transition: direct repression of the gene expression of claudins/occludin by Snail. |journal=J. Cell. Sci. |volume=116 |issue= Pt 10 |pages= 1959-67 |year= 2004 |pmid= 12668723 |doi= 10.1242/jcs.00389 }}
*{{cite journal | author=Domínguez D, Montserrat-Sentís B, Virgós-Soler A, ''et al.'' |title=Phosphorylation regulates the subcellular location and activity of the snail transcriptional repressor. |journal=Mol. Cell. Biol. |volume=23 |issue= 14 |pages= 5078-89 |year= 2003 |pmid= 12832491 |doi= }}
*{{cite journal | author=Imai T, Horiuchi A, Wang C, ''et al.'' |title=Hypoxia attenuates the expression of E-cadherin via up-regulation of SNAIL in ovarian carcinoma cells. |journal=Am. J. Pathol. |volume=163 |issue= 4 |pages= 1437-47 |year= 2003 |pmid= 14507651 |doi= }}
*{{cite journal | author=Miyoshi A, Kitajima Y, Sumi K, ''et al.'' |title=Snail and SIP1 increase cancer invasion by upregulating MMP family in hepatocellular carcinoma cells. |journal=Br. J. Cancer |volume=90 |issue= 6 |pages= 1265-73 |year= 2004 |pmid= 15026811 |doi= 10.1038/sj.bjc.6601685 }}
*{{cite journal | author=Ohkubo T, Ozawa M |title=The transcription factor Snail downregulates the tight junction components independently of E-cadherin downregulation. |journal=J. Cell. Sci. |volume=117 |issue= Pt 9 |pages= 1675-85 |year= 2004 |pmid= 15075229 |doi= 10.1242/jcs.01004 }}
*{{cite journal | author=Barberà MJ, Puig I, Domínguez D, ''et al.'' |title=Regulation of Snail transcription during epithelial to mesenchymal transition of tumor cells. |journal=Oncogene |volume=23 |issue= 44 |pages= 7345-54 |year= 2004 |pmid= 15286702 |doi= 10.1038/sj.onc.1207990 }}
*{{cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, ''et al.'' |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130-5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 }}
*{{cite journal | author=Kajita M, McClinic KN, Wade PA |title=Aberrant expression of the transcription factors snail and slug alters the response to genotoxic stress. |journal=Mol. Cell. Biol. |volume=24 |issue= 17 |pages= 7559-66 |year= 2004 |pmid= 15314165 |doi= 10.1128/MCB.24.17.7559-7566.2004 }}
*{{cite journal | author=Zhou BP, Deng J, Xia W, ''et al.'' |title=Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition. |journal=Nat. Cell Biol. |volume=6 |issue= 10 |pages= 931-40 |year= 2004 |pmid= 15448698 |doi= 10.1038/ncb1173 }}
*{{cite journal | author=Saito T, Oda Y, Kawaguchi K, ''et al.'' |title=E-cadherin mutation and Snail overexpression as alternative mechanisms of E-cadherin inactivation in synovial sarcoma. |journal=Oncogene |volume=23 |issue= 53 |pages= 8629-38 |year= 2004 |pmid= 15467754 |doi= 10.1038/sj.onc.1207960 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SNCG... {November 18, 2007 2:27:27 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:27:54 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Synuclein, gamma (breast cancer-specific protein 1)
| HGNCid = 11141
| Symbol = SNCG
| AltSymbols =; SR; BCSG1
| OMIM = 602998
| ECnumber =
| Homologene = 2322
| MGIid = 1298397
| GeneAtlas_image1 = PBB_GE_SNCG_209877_at_tn.png
| Function =
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0030424 |text = axon}} {{GNF_GO|id=GO:0043025 |text = cell soma}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6623
| Hs_Ensembl = ENSG00000173267
| Hs_RefseqProtein = NP_003078
| Hs_RefseqmRNA = NM_003087
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 88708365
| Hs_GenLoc_end = 88712997
| Hs_Uniprot = O76070
| Mm_EntrezGene = 20618
| Mm_Ensembl = ENSMUSG00000023064
| Mm_RefseqmRNA = NM_011430
| Mm_RefseqProtein = NP_035560
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 33199367
| Mm_GenLoc_end = 33203752
| Mm_Uniprot = Q5GQ64
}}
}}
'''Synuclein, gamma (breast cancer-specific protein 1)''', also known as '''SNCG''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SNCG synuclein, gamma (breast cancer-specific protein 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6623| 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 = Synuclein-gamma is a member of the synuclein family of proteins which are believed to be involved in the pathogenesis of neurodegenerative diseases. High levels of SNCG have been identified in advanced breast carcinomas suggesting a correlation between overexpression of SNCG and breast tumor development.<ref name="entrez">{{cite web | title = Entrez Gene: SNCG synuclein, gamma (breast cancer-specific protein 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6623| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=George JM |title=The synucleins. |journal=Genome Biol. |volume=3 |issue= 1 |pages= REVIEWS3002 |year= 2002 |pmid= 11806835 |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=Ji H, Liu YE, Jia T, ''et al.'' |title=Identification of a breast cancer-specific gene, BCSG1, by direct differential cDNA sequencing. |journal=Cancer Res. |volume=57 |issue= 4 |pages= 759-64 |year= 1997 |pmid= 9044857 |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=Ninkina NN, Alimova-Kost MV, Paterson JW, ''et al.'' |title=Organization, expression and polymorphism of the human persyn gene. |journal=Hum. Mol. Genet. |volume=7 |issue= 9 |pages= 1417-24 |year= 1998 |pmid= 9700196 |doi= }}
*{{cite journal | author=Lavedan C, Leroy E, Dehejia A, ''et al.'' |title=Identification, localization and characterization of the human gamma-synuclein gene. |journal=Hum. Genet. |volume=103 |issue= 1 |pages= 106-12 |year= 1998 |pmid= 9737786 |doi= }}
*{{cite journal | author=Buchman VL, Hunter HJ, Pinõn LG, ''et al.'' |title=Persyn, a member of the synuclein family, has a distinct pattern of expression in the developing nervous system. |journal=J. Neurosci. |volume=18 |issue= 22 |pages= 9335-41 |year= 1998 |pmid= 9801372 |doi= }}
*{{cite journal | author=Lavedan C, Buchholtz S, Auburger G, ''et al.'' |title=Absence of mutation in the beta- and gamma-synuclein genes in familial autosomal dominant Parkinson's disease. |journal=DNA Res. |volume=5 |issue= 6 |pages= 401-2 |year= 1999 |pmid= 10048491 |doi= }}
*{{cite journal | author=Surguchov A, Surgucheva I, Solessio E, Baehr W |title=Synoretin--A new protein belonging to the synuclein family. |journal=Mol. Cell. Neurosci. |volume=13 |issue= 2 |pages= 95-103 |year= 1999 |pmid= 10192768 |doi= 10.1006/mcne.1999.0735 }}
*{{cite journal | author=Duda JE, Shah U, Arnold SE, ''et al.'' |title=The expression of alpha-, beta-, and gamma-synucleins in olfactory mucosa from patients with and without neurodegenerative diseases. |journal=Exp. Neurol. |volume=160 |issue= 2 |pages= 515-22 |year= 2000 |pmid= 10619569 |doi= 10.1006/exnr.1999.7228 }}
*{{cite journal | author=Souza JM, Giasson BI, Lee VM, Ischiropoulos H |title=Chaperone-like activity of synucleins. |journal=FEBS Lett. |volume=474 |issue= 1 |pages= 116-9 |year= 2000 |pmid= 10828462 |doi= }}
*{{cite journal | author=Pronin AN, Morris AJ, Surguchov A, Benovic JL |title=Synucleins are a novel class of substrates for G protein-coupled receptor kinases. |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26515-22 |year= 2000 |pmid= 10852916 |doi= 10.1074/jbc.M003542200 }}
*{{cite journal | author=Galvin JE, Schuck TM, Lee VM, Trojanowski JQ |title=Differential expression and distribution of alpha-, beta-, and gamma-synuclein in the developing human substantia nigra. |journal=Exp. Neurol. |volume=168 |issue= 2 |pages= 347-55 |year= 2001 |pmid= 11259122 |doi= 10.1006/exnr.2000.7615 }}
*{{cite journal | author=Surguchov A, Palazzo RE, Surgucheva I |title=Gamma synuclein: subcellular localization in neuronal and non-neuronal cells and effect on signal transduction. |journal=Cell Motil. Cytoskeleton |volume=49 |issue= 4 |pages= 218-28 |year= 2002 |pmid= 11746666 |doi= 10.1002/cm.1035 }}
*{{cite journal | author=Uversky VN, Li J, Souillac P, ''et al.'' |title=Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins. |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 11970-8 |year= 2002 |pmid= 11812782 |doi= 10.1074/jbc.M109541200 }}
*{{cite journal | author=Lu A, Zhang F, Gupta A, Liu J |title=Blockade of AP1 transactivation abrogates the abnormal expression of breast cancer-specific gene 1 in breast cancer cells. |journal=J. Biol. Chem. |volume=277 |issue= 35 |pages= 31364-72 |year= 2002 |pmid= 12072430 |doi= 10.1074/jbc.M201060200 }}
*{{cite journal | author=Pan ZZ, Bruening W, Giasson BI, ''et al.'' |title=Gamma-synuclein promotes cancer cell survival and inhibits stress- and chemotherapy drug-induced apoptosis by modulating MAPK pathways. |journal=J. Biol. Chem. |volume=277 |issue= 38 |pages= 35050-60 |year= 2002 |pmid= 12121974 |doi= 10.1074/jbc.M201650200 }}
*{{cite journal | author=Li QX, Campbell BC, McLean CA, ''et al.'' |title=Platelet alpha- and gamma-synucleins in Parkinson's disease and normal control subjects. |journal=J. Alzheimers Dis. |volume=4 |issue= 4 |pages= 309-15 |year= 2003 |pmid= 12446933 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SYP... {November 18, 2007 2:27:54 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:28:26 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Synaptophysin
| HGNCid = 11506
| Symbol = SYP
| AltSymbols =;
| OMIM = 313475
| ECnumber =
| Homologene = 2391
| MGIid = 98467
| GeneAtlas_image1 = PBB_GE_SYP_213200_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015485 |text = cholesterol binding}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0019717 |text = synaptosome}} {{GNF_GO|id=GO:0030285 |text = integral to synaptic vesicle membrane}} {{GNF_GO|id=GO:0045202 |text = synapse}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0016188 |text = synaptic vesicle maturation}} {{GNF_GO|id=GO:0048499 |text = synaptic vesicle membrane organization and biogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6855
| Hs_Ensembl = ENSG00000102003
| Hs_RefseqProtein = NP_003170
| Hs_RefseqmRNA = NM_003179
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 48931201
| Hs_GenLoc_end = 48943606
| Hs_Uniprot = P08247
| Mm_EntrezGene = 20977
| Mm_Ensembl = ENSMUSG00000031144
| Mm_RefseqmRNA = NM_009305
| Mm_RefseqProtein = NP_033331
| Mm_GenLoc_db =
| Mm_GenLoc_chr = X
| Mm_GenLoc_start = 6795643
| Mm_GenLoc_end = 6810210
| Mm_Uniprot = Q62277
}}
}}
'''Synaptophysin''', also known as '''SYP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SYP synaptophysin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6855| 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 = Synaptophysin (p38) is an integral membrane protein of small synaptic vesicles in brain and endocrine cells.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: SYP synaptophysin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6855| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kalina M, Lukinius A, Grimelius L, ''et al.'' |title=Ultrastructural localization of synaptophysin to the secretory granules of normal glucagon and insulin cells in human islets of Langerhans. |journal=Ultrastructural pathology |volume=15 |issue= 3 |pages= 215-9 |year= 1991 |pmid= 1908157 |doi= }}
*{{cite journal | author=Ozçelik T, Lafreniere RG, Archer BT, ''et al.'' |title=Synaptophysin: structure of the human gene and assignment to the X chromosome in man and mouse. |journal=Am. J. Hum. Genet. |volume=47 |issue= 3 |pages= 551-61 |year= 1990 |pmid= 1975480 |doi= }}
*{{cite journal | author=Goto S, Hirano A, Pearson J |title=Calcineurin and synaptophysin in the human spinal cord of normal individuals and patients with familial dysautonomia. |journal=Acta Neuropathol. |volume=79 |issue= 6 |pages= 647-52 |year= 1990 |pmid= 2163183 |doi= }}
*{{cite journal | author=Südhof TC, Lottspeich F, Greengard P, ''et al.'' |title=The cDNA and derived amino acid sequences for rat and human synaptophysin. |journal=Nucleic Acids Res. |volume=15 |issue= 22 |pages= 9607 |year= 1988 |pmid= 3120152 |doi= }}
*{{cite journal | author=de Koning JP, Schelen AM, Dong F, ''et al.'' |title=Specific involvement of tyrosine 764 of human granulocyte colony-stimulating factor receptor in signal transduction mediated by p145/Shc/GRB2 or p90/GRB2 complexes. |journal=Blood |volume=87 |issue= 1 |pages= 132-40 |year= 1996 |pmid= 8547634 |doi= }}
*{{cite journal | author=Zhang PJ, Rosenblum MK |title=Synaptophysin expression in the human spinal cord. Diagnostic implications of an immunohistochemical study. |journal=Am. J. Surg. Pathol. |volume=20 |issue= 3 |pages= 273-6 |year= 1997 |pmid= 8772779 |doi= }}
*{{cite journal | author=Bouwens L, Lu WG, De Krijger R |title=Proliferation and differentiation in the human fetal endocrine pancreas. |journal=Diabetologia |volume=40 |issue= 4 |pages= 398-404 |year= 1997 |pmid= 9112016 |doi= }}
*{{cite journal | author=Fisher SE, Ciccodicola A, Tanaka K, ''et al.'' |title=Sequence-based exon prediction around the synaptophysin locus reveals a gene-rich area containing novel genes in human proximal Xp. |journal=Genomics |volume=45 |issue= 2 |pages= 340-7 |year= 1998 |pmid= 9344658 |doi= 10.1006/geno.1997.4941 }}
*{{cite journal | author=Maggiano N, Lauriola L, Serra FG, ''et al.'' |title=Detection of synaptophysin-producing cells in human thymus by immunohistochemistry and nonradioactive in situ hybridization. |journal=J. Histochem. Cytochem. |volume=47 |issue= 2 |pages= 237-43 |year= 1999 |pmid= 9889259 |doi= }}
*{{cite journal | author=Portela-Gomes GM, Stridsberg M, Johansson H, Grimelius L |title=Co-localization of synaptophysin with different neuroendocrine hormones in the human gastrointestinal tract. |journal=Histochem. Cell Biol. |volume=111 |issue= 1 |pages= 49-54 |year= 1999 |pmid= 9930883 |doi= }}
*{{cite journal | author=Davidsson P, Gottfries J, Bogdanovic N, ''et al.'' |title=The synaptic-vesicle-specific proteins rab3a and synaptophysin are reduced in thalamus and related cortical brain regions in schizophrenic brains. |journal=Schizophr. Res. |volume=40 |issue= 1 |pages= 23-9 |year= 1999 |pmid= 10541003 |doi= }}
*{{cite journal | author=Cassiman D, van Pelt J, De Vos R, ''et al.'' |title=Synaptophysin: A novel marker for human and rat hepatic stellate cells. |journal=Am. J. Pathol. |volume=155 |issue= 6 |pages= 1831-9 |year= 1999 |pmid= 10595912 |doi= }}
*{{cite journal | author=Thiele C, Hannah MJ, Fahrenholz F, Huttner WB |title=Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles. |journal=Nat. Cell Biol. |volume=2 |issue= 1 |pages= 42-9 |year= 2000 |pmid= 10620806 |doi= 10.1038/71366 }}
*{{cite journal | author=Nag TC, Wadhwa S |title=Differential expression of syntaxin-1 and synaptophysin in the developing and adult human retina. |journal=J. Biosci. |volume=26 |issue= 2 |pages= 179-91 |year= 2001 |pmid= 11426054 |doi= }}
*{{cite journal | author=Bhangu PS, Genever PG, Spencer GJ, ''et al.'' |title=Evidence for targeted vesicular glutamate exocytosis in osteoblasts. |journal=Bone |volume=29 |issue= 1 |pages= 16-23 |year= 2001 |pmid= 11472886 |doi= }}
*{{cite journal | author=Roudenok V, Kühnel W |title=The development of synaptophysin immunoreactivity in the human sympathetic ganglia. |journal=Ann. Anat. |volume=183 |issue= 4 |pages= 345-51 |year= 2001 |pmid= 11508360 |doi= }}
*{{cite journal | author=Wheeler TC, Chin LS, Li Y, ''et al.'' |title=Regulation of synaptophysin degradation by mammalian homologues of seven in absentia. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10273-82 |year= 2002 |pmid= 11786535 |doi= 10.1074/jbc.M107857200 }}
*{{cite journal | author=Ulfig N, Chan WY |title=Expression of a kinase anchoring protein 79 and synaptophysin in the developing human red nucleus. |journal=Neurosignals |volume=11 |issue= 2 |pages= 95-102 |year= 2003 |pmid= 12077483 |doi= }}
*{{cite journal | author=Yao I, Iida J, Nishimura W, Hata Y |title=Synaptic and nuclear localization of brain-enriched guanylate kinase-associated protein. |journal=J. Neurosci. |volume=22 |issue= 13 |pages= 5354-64 |year= 2002 |pmid= 12097487 |doi= 20026505 }}
*{{cite journal | author=Wistow G, Bernstein SL, Wyatt MK, ''et al.'' |title=Expressed sequence tag analysis of human retina for the NEIBank Project: retbindin, an abundant, novel retinal cDNA and alternative splicing of other retina-preferred gene transcripts. |journal=Mol. Vis. |volume=8 |issue= |pages= 196-204 |year= 2002 |pmid= 12107411 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TCEB2... {November 18, 2007 2:28:26 PM PST}
- SEARCH REDIRECT: Control Box Found: TCEB2 {November 18, 2007 2:28:50 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 2:28:52 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 2:28:52 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 2:28:52 PM PST}
- UPDATED: Updated protein page: TCEB2 {November 18, 2007 2:28:58 PM PST}
- INFO: Beginning work on TIAM1... {November 18, 2007 2:28:58 PM PST}
- SEARCH REDIRECT: Control Box Found: TIAM1 {November 18, 2007 2:29:32 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 2:29:33 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 2:29:33 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 2:29:33 PM PST}
- UPDATED: Updated protein page: TIAM1 {November 18, 2007 2:29:40 PM PST}
- INFO: Beginning work on TJP2... {November 18, 2007 2:34:49 PM PST}
- SEARCH REDIRECT: Control Box Found: TJP2 {November 18, 2007 2:36:04 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 2:36:05 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 2:36:05 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 2:36:05 PM PST}
- UPDATED: Updated protein page: TJP2 {November 18, 2007 2:36:18 PM PST}
- INFO: Beginning work on TMPO... {November 18, 2007 2:29:40 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 2:30:44 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 = PBB_Protein_TMPO_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gjj.
| PDB = {{PDB2|1gjj}}, {{PDB2|1h9e}}, {{PDB2|1h9f}}
| Name = Thymopoietin
| HGNCid = 11875
| Symbol = TMPO
| AltSymbols =; TP; LAP2; CMD1T; MGC61508; PRO0868
| OMIM = 188380
| ECnumber =
| Homologene = 31144
| MGIid = 106920
| GeneAtlas_image1 = PBB_GE_TMPO_209753_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_TMPO_209754_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_TMPO_203432_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0005521 |text = lamin binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005635 |text = nuclear envelope}} {{GNF_GO|id=GO:0005694 |text = chromosome}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0045449 |text = regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7112
| Hs_Ensembl = ENSG00000120802
| Hs_RefseqProtein = NP_001027454
| Hs_RefseqmRNA = NM_001032283
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 97433527
| Hs_GenLoc_end = 97468250
| Hs_Uniprot = P42167
| Mm_EntrezGene = 21917
| Mm_Ensembl = ENSMUSG00000019961
| Mm_RefseqmRNA = NM_001080129
| Mm_RefseqProtein = NP_001073598
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 90578420
| Mm_GenLoc_end = 90611277
| Mm_Uniprot = Q61033
}}
}}
'''Thymopoietin''', also known as '''TMPO''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TMPO thymopoietin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7112| 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=Dechat T, Vlcek S, Foisner R |title=Review: lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics. |journal=J. Struct. Biol. |volume=129 |issue= 2-3 |pages= 335-45 |year= 2000 |pmid= 10806084 |doi= 10.1006/jsbi.2000.4212 }}
*{{cite journal | author=Twomey JJ, Goldstein G, Lewis VM, ''et al.'' |title=Bioassay determinations of thymopoietin and thymic hormone levels in human plasma. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=74 |issue= 6 |pages= 2541-5 |year= 1977 |pmid= 302007 |doi= }}
*{{cite journal | author=Heavner GA, Audhya T, Goldstein G |title=Peptide analogs of thymopentin distinguish distinct thymopoietin receptor specificities on two human T cell lines. |journal=Regul. Pept. |volume=27 |issue= 2 |pages= 257-62 |year= 1990 |pmid= 2158125 |doi= }}
*{{cite journal | author=Audhya T, Schlesinger DH, Goldstein G |title=Isolation and complete amino acid sequence of human thymopoietin and splenin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 11 |pages= 3545-9 |year= 1987 |pmid= 3473468 |doi= }}
*{{cite journal | author=Fuccello A, Audhya T, Talle MA, Goldstein G |title=Immunoassay for bovine serum thymopoietin: discrimination from splenin by monoclonal antibodies. |journal=Arch. Biochem. Biophys. |volume=228 |issue= 1 |pages= 292-8 |year= 1984 |pmid= 6364989 |doi= }}
*{{cite journal | author=Harris CA, Andryuk PJ, Cline S, ''et al.'' |title=Three distinct human thymopoietins are derived from alternatively spliced mRNAs. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 14 |pages= 6283-7 |year= 1994 |pmid= 7517549 |doi= }}
*{{cite journal | author=Hara H, Hayashi K, Ohta K, ''et al.'' |title=A new thymopoietin precursor gene from human thymus. |journal=Biochem. Mol. Biol. Int. |volume=34 |issue= 5 |pages= 927-33 |year= 1995 |pmid= 7703909 |doi= }}
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}}
{{refend}}
{{protein-stub}}
end log.
