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UniProtKB/Swiss-Prot entry O95817


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BAG3_HUMAN
Primary accession number O95817
Secondary accession numbers A8K5L8 Q3B763 Q9NT20 Q9P120
Integrated into Swiss-Prot on January 11, 2001
Sequence was last modified on January 11, 2001 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 91)
Name and origin of the protein
Protein name BAG family molecular chaperone regulator 3
Synonyms BAG-3
Bcl-2-associated athanogene 3
Bcl-2-binding protein Bis
Docking protein CAIR-1
Gene name
Name: BAG3
Synonyms: BIS
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.274.2.781; PubMed=9873016 [NCBI, ExPASy, EBI, Israel, Japan]
Takayama S., Xie Z., Reed J.C.;
"An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators.";
J. Biol. Chem. 274:781-786(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-151.
DOI=10.1038/sj.onc.1203043; PubMed=10597216 [NCBI, ExPASy, EBI, Israel, Japan]
Lee J.H., Takahashi T., Yasuhara N., Inazawa J., Kamada S., Tsujimoto Y.;
"Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell death.";
Oncogene 18:6183-6190(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/sj.onc.1203797; PubMed=10980614 [NCBI, ExPASy, EBI, Israel, Japan]
Doong H., Price J., Kim Y.S., Gasbarre C., Probst J., Liotta L.A., Blanchette J., Rizzo K., Kohn E.;
"CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-gamma and Hsp70/Hsc70.";
Oncogene 19:4385-4395(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan]
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Lung, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-279 AND SER-377, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-247, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, AND MASS SPECTROMETRY.
TISSUE=T-cell;
DOI=10.1038/nmeth776; PubMed=16094384 [NCBI, ExPASy, EBI, Israel, Japan]
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry.";
Nat. Methods 2:591-598(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-285 AND SER-289, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-279; THR-285; SER-289 AND SER-291, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-136; TYR-240; THR-285 AND SER-289, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-173; THR-285; SER-289 AND SER-291, AND MASS SPECTROMETRY.
DOI=10.1021/pr0705441; PubMed=18220336 [NCBI, ExPASy, EBI, Israel, Japan]
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-406, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-275; SER-279; THR-285; SER-289; SER-291; SER-377; SER-386 AND THR-406, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF095193; AAD16122.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF127139; AAF26839.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF071218; AAF69592.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291333; BAF84022.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL137582; CAB70824.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006418; AAH06418.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014656; AAH14656.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC107786; AAI07787.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00641582; -.
RefSeq NP_004272.2; -.
UniGene Hs.523309
3D structure databases
HSSP O95429; 1M7K. [HSSP ENTRY / PDB]
SMR O95817; 396-498.
ModBase O95817.
Protein-protein interaction databases
IntAct O95817; 4.
PTM databases
PhosphoSite O95817; -.
Organism-specific databases
GeneCards GC10P121400; -.
H-InvDB HIX0009255; -.
HGNC HGNC:939; BAG3.
GenAtlas BAG3.
MIM 603883; gene. [NCBI / EBI]
PharmGKB PA25239; -.
Gene expression databases
ArrayExpress O95817; -.
Bgee O95817; -.
CleanEx HS_BAG3; -.
GermOnline ENSG00000151929; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from MGI).
GO:0006916; Biological process: anti-apoptosis (non-traceable author statement from UniProtKB).
GO:0006915; Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0006457; Biological process: protein folding (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR003103; Apoptosis_reg_Bcl-2_prot_BAG.
IPR001202; WW_Rsp5_WWP.
Graphical view of domain structure.
Pfam PF02179; BAG; 1.
PF00397; WW; 1.
Pfam graphical view of domain structure.
SMART SM00264; BAG; 1.
SM00456; WW; 1.
SMART graphical view of domain structure.
PROSITE PS51035; BAG; 1.
PS01159; WW_DOMAIN_1; 1.
PS50020; WW_DOMAIN_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas O95817; -.
PRIDE O95817; -.
Genome annotation databases
Ensembl ENSG00000151929; Homo sapiens. [Contig view]
GeneID 9531; -.
KEGG hsa:9531; -.
Phylogenomic databases
HOGENOM O95817; -.
HOVERGEN O95817; -.
OMA O95817; IPVIHEQ.
Other
NextBio 35732; -.
PMAP-CutDB O95817; -.
SOURCE BAG3; Homo sapiens.
ProtoNet O95817.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Apoptosis; Chaperone; Phosphoprotein; Polymorphism; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   575  575     BAG family molecular chaperone regulator 3. PRO_0000088868
DOMAIN   20    54  35     WW 1. 
DOMAIN   124   154  31     WW 2. 
DOMAIN   421   498  78     BAG. 
COMPBIAS   180   187  8     Poly-Ser. 
MOD_RES   134   134        Phosphoserine. 
MOD_RES   136   136        Phosphoserine. 
MOD_RES   171   171        Phosphoserine. 
MOD_RES   173   173        Phosphoserine. 
MOD_RES   194   194        Phosphoserine. 
MOD_RES   240   240        Phosphotyrosine. 
MOD_RES   247   247        Phosphotyrosine. 
MOD_RES   274   274        Phosphoserine. 
MOD_RES   275   275        Phosphoserine. 
MOD_RES   279   279        Phosphoserine. 
MOD_RES   285   285        Phosphothreonine. 
MOD_RES   289   289        Phosphoserine. 
MOD_RES   291   291        Phosphoserine. 
MOD_RES   377   377        Phosphoserine. 
MOD_RES   385   385        Phosphoserine (By similarity). 
MOD_RES   386   386        Phosphoserine. 
MOD_RES   406   406        Phosphothreonine. 
VARIANT   71    71  1     R -> Q (in dbSNP:rs35434411 [NCBI]). VAR_048344 
VARIANT   151   151  1     C -> R (in dbSNP:rs2234962 [NCBI]). VAR_048345 
VARIANT   405   405  1     A -> V (in dbSNP:rs11199064 [NCBI]). VAR_048346 
VARIANT   407   407  1     P -> L (in dbSNP:rs3858340 [NCBI]). VAR_048347 
CONFLICT   227   227        Q -> K (in Ref. 1; AAD16122). 
CONFLICT   237   237        Q -> R (in Ref. 1; AAD16122). 
CONFLICT   304   304        Missing (in Ref. 5; CAB70824). 
Sequence information
Length: 575 AA [This is the length of the unprocessed precursor] Molecular weight: 61595 Da [This is the MW of the unprocessed precursor] CRC64: A6328A44F37A406A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSAATHSPMM QVASGNGDRD PLPPGWEIKI DPQTGWPFFV DHNSRTTTWN DPRVPSEGPK 

        70         80         90        100        110        120 
ETPSSANGPS REGSRLPPAR EGHPVYPQLR PGYIPIPVLH EGAENRQVHP FHVYPQPGMQ 

       130        140        150        160        170        180 
RFRTEAAAAA PQRSQSPLRG MPETTQPDKQ CGQVAAAAAA QPPASHGPER SQSPAASDCS 

       190        200        210        220        230        240 
SSSSSASLPS SGRSSLGSHQ LPRGYISIPV IHEQNVTRPA AQPSFHQAQK THYPAQQGEY 

       250        260        270        280        290        300 
QTHQPVYHKI QGDDWEPRPL RAASPFRSSV QGASSREGSP ARSSTPLHSP SPIRVHTVVD 

       310        320        330        340        350        360 
RPQQPMTHRE TAPVSQPENK PESKPGPVGP ELPPGHIPIQ VIRKEVDSKP VSQKPPPPSE 

       370        380        390        400        410        420 
KVEVKVPPAP VPCPPPSPGP SAVPSSPKSV ATEERAAPST APAEATPPKP GEAEAPPKHP 

       430        440        450        460        470        480 
GVLKVEAILE KVQGLEQAVD NFEGKKTDKK YLMIEEYLTK ELLALDSVDP EGRADVRQAR 

       490        500        510        520        530        540 
RDGVRKVQTI LEKLEQKAID VPGQVQVYEL QPSNLEADQP LQAIMEMGAV AADKGKKNAG 

       550        560        570 
NAEDPHTETQ QPEATAAATS NPSSMTDTPG NPAAP 

O95817 in FASTA format

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