Reviewed, UniProtKB/Swiss-Prot O95817 (BAG3_HUMAN)

Names and origin

Protein names

Recommended name:
    BAG family molecular chaperone regulator 3
      Short name=BAG-3
Alternative name(s):
    Bcl-2-associated athanogene 3
    Bcl-2-binding protein Bis
    Docking protein CAIR-1

Gene names

Name:	BAG3
Synonyms:	BIS

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	575 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Has anti-apoptotic activity.
Subunit structure	Binds to the ATPase domain of HSP70/HSC chaperones. Binds to Bcl-2 and PLC-gamma.
Sequence similarities	Contains 1 BAG domain. Contains 2 WW domains.

Ontologies

Keywords
Biological process	Apoptosis
Coding sequence diversity	Polymorphism
Domain	Repeat
Molecular function	Chaperone
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	anti-apoptosis Ref.2 Non-traceable author statement. Source: UniProtKB apoptosis Inferred from electronic annotation. Source: UniProtKB-KW protein folding Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Ref.2 Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 575	575	BAG family molecular chaperone regulator 3		PRO_0000088868
Regions
	Domain	20 – 54	35	WW 1
	Domain	124 – 154	31	WW 2
	Domain	421 – 498	78	BAG
	Compositional bias	180 – 187	8	Poly-Ser
Amino acid modifications
	Modified residue	134	1	Phosphoserine Ref.13
	Modified residue	136	1	Phosphoserine Ref.13
	Modified residue	171	1	Phosphoserine Ref.15
	Modified residue	173	1	Phosphoserine Ref.15 Ref.14
	Modified residue	194	1	Phosphoserine Ref.12
	Modified residue	240	1	Phosphotyrosine Ref.13 Ref.9
	Modified residue	247	1	Phosphotyrosine Ref.8
	Modified residue	274	1	Phosphoserine Ref.17
	Modified residue	275	1	Phosphoserine Ref.17 Ref.7 Ref.11
	Modified residue	279	1	Phosphoserine Ref.17 Ref.7 Ref.11
	Modified residue	285	1	Phosphothreonine Ref.13 Ref.15 Ref.17 Ref.11 Ref.10
	Modified residue	289	1	Phosphoserine Ref.13 Ref.15 Ref.17 Ref.11 Ref.10
	Modified residue	291	1	Phosphoserine Ref.15 Ref.17 Ref.11
	Modified residue	377	1	Phosphoserine Ref.17 Ref.7
	Modified residue	385	1	Phosphoserine By similarity
	Modified residue	386	1	Phosphoserine Ref.17
	Modified residue	406	1	Phosphothreonine Ref.17 Ref.16
Natural variations
	Natural variant	71	1	R → Q: dbSNP rs35434411.		VAR_048344
	Natural variant	151	1	C → R: dbSNP rs2234962. Ref.2		VAR_048345
	Natural variant	405	1	A → V: dbSNP rs11199064.		VAR_048346
	Natural variant	407	1	P → L: dbSNP rs3858340.		VAR_048347
Experimental info
	Sequence conflict	227	1	Q → K in AAD16122. Ref.1
	Sequence conflict	237	1	Q → R in AAD16122. Ref.1
	Sequence conflict	304	1	Missing in CAB70824. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	O95817-1 [UniParc]. Last modified January 11, 2001. Version 3. Checksum: A6328A44F37A406A	FASTA	575	61,595
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators." Takayama S., Xie Z., Reed J.C. J. Biol. Chem. 274:781-786(1999) [PubMed: 9873016] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell death." Lee J.H., Takahashi T., Yasuhara N., Inazawa J., Kamada S., Tsujimoto Y. Oncogene 18:6183-6190(1999) [PubMed: 10597216] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-151.
[3]	"CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-gamma and Hsp70/Hsc70." Doong H., Price J., Kim Y.S., Gasbarre C., Probst J., Liotta L.A., Blanchette J., Rizzo K., Kohn E. Oncogene 19:4385-4395(2000) [PubMed: 10980614] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tongue.
[5]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Lung and Placenta.
[7]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-279 AND SER-377, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." 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. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-247, MASS SPECTROMETRY.
[9]	"Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry." Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J., Bodenmiller B., Watts J.D., Hood L., Aebersold R. Nat. Methods 2:591-598(2005) [PubMed: 16094384] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, MASS SPECTROMETRY. Tissue: T-cell.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-285 AND SER-289, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; SER-279; THR-285; SER-289 AND SER-291, MASS SPECTROMETRY. Tissue: Epithelium.
[12]	"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." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-136; TYR-240; THR-285 AND SER-289, MASS SPECTROMETRY.
[14]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, MASS SPECTROMETRY.
[15]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-173; THR-285; SER-289 AND SER-291, MASS SPECTROMETRY.
[16]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-406, MASS SPECTROMETRY.
[17]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274; SER-275; SER-279; THR-285; SER-289; SER-291; SER-377; SER-386 AND THR-406, MASS SPECTROMETRY.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF095193 mRNA. Translation: AAD16122.2. AF127139 mRNA. Translation: AAF26839.1. AF071218 mRNA. Translation: AAF69592.2. AK291333 mRNA. Translation: BAF84022.1. AL137582 mRNA. Translation: CAB70824.1. BC006418 mRNA. Translation: AAH06418.1. BC014656 mRNA. Translation: AAH14656.1. BC107786 mRNA. Translation: AAI07787.1.
IPI	IPI00641582.
RefSeq	NP_004272.2.
UniGene	Hs.523309
3D structure databases
HSSP	HSSP built from PDB template 1M7K based on UniProtKB O95429.
SMR	O95817. Positions 396-498.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95817. 4 interactions.
PTM databases
PhosphoSite	O95817.
Proteomic databases
PeptideAtlas	O95817.
PRIDE	O95817.
Genome annotation databases
Ensembl	ENSG00000151929. Homo sapiens. [Contig view]
GeneID	9531.
KEGG	hsa:9531.
Organism-specific databases
GeneCards	GC10P121400.
H-InvDB	HIX0009255.
HGNC	HGNC:939. BAG3.
MIM	603883. gene.
PharmGKB	PA25239.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	O95817.
HOVERGEN	O95817.
OMA	O95817. IPVIHEQ.
Gene expression databases
ArrayExpress	O95817.
Bgee	O95817.
CleanEx	HS_BAG3.
GermOnline	ENSG00000151929. Homo sapiens.
Family and domain databases
InterPro	IPR003103. Apoptosis_reg_Bcl-2_prot_BAG. IPR001202. WW_Rsp5_WWP. [Graphical view]
Pfam	PF02179. BAG. 1 hit. PF00397. WW. 1 hit. [Graphical view]
SMART	SM00264. BAG. 1 hit. SM00456. WW. 1 hit. [Graphical view]
PROSITE	PS51035. BAG. 1 hit. PS01159. WW_DOMAIN_1. 1 hit. PS50020. WW_DOMAIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	35732.
PMAP-CutDB	O95817.
SOURCE	Search...

Entry information

Entry name

BAG3_HUMAN

Accession

Primary (citable) accession number: O95817
Secondary accession number(s): A8K5L8 , Q3B763, Q9NT20, Q9P120

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	January 11, 2001
Last modified:	June 16, 2009
This is version 91 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)