O95817 (BAG3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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.
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 HSP/HSC70 chaperones. Binds to Bcl-2 and PLC-gamma.
Involvement in disease	Defects in BAG3 are the cause of myopathy myofibrillar type 6 (MFM6) [MIM:612954]. A neuromuscular disorder that results in early-onset, severe, progressive, diffuse muscle weakness associated with cardiomyopathy, severe respiratory insufficiency during adolescence, and a rigid spine in some patients. At ultrastructural level, muscle fibers display structural alterations consisting of replacement of the normal myofibrillar markings by small, dense granules, or larger hyaline masses, or amorphous material. Ref.21 Ref.23 Ref.25 Defects in BAG3 are the cause of cardiomyopathy dilated type 1HH (CMD1HH) [MIM:613881]. CMD1HH is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. Ref.22 Ref.24 Ref.25
Sequence similarities	Contains 1 BAG domain. Contains 2 WW domains.

Ontologies

Keywords
Biological process	Apoptosis
Coding sequence diversity	Polymorphism
Disease	Cardiomyopathy Disease mutation Myofibrillar myopathy
Domain	Repeat
Molecular function	Chaperone
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	anti-apoptosis Non-traceable author statement Ref.2. Source: UniProtKB apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW protein folding Non-traceable author statement Ref.1. Source: UniProtKB
Cellular component	cytosol Inferred from direct assay Ref.2. Source: MGI plasma membrane Inferred from direct assay. Source: HPA
Molecular function	chaperone binding Inferred from electronic annotation. Source: InterPro
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.14 Ref.15 Ref.18
	Modified residue	194	1	Phosphoserine Ref.12
	Modified residue	240	1	Phosphotyrosine Ref.9 Ref.13
	Modified residue	247	1	Phosphotyrosine Ref.8
	Modified residue	274	1	Phosphoserine Ref.17
	Modified residue	275	1	Phosphoserine Ref.7 Ref.11 Ref.17
	Modified residue	279	1	Phosphoserine Ref.7 Ref.11 Ref.17
	Modified residue	284	1	Phosphoserine Ref.18
	Modified residue	285	1	Phosphothreonine Ref.10 Ref.11 Ref.13 Ref.15 Ref.17 Ref.18
	Modified residue	289	1	Phosphoserine Ref.10 Ref.11 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19
	Modified residue	291	1	Phosphoserine Ref.11 Ref.15 Ref.17 Ref.18
	Modified residue	377	1	Phosphoserine Ref.7 Ref.17 Ref.18
	Modified residue	381	1	Phosphoserine Ref.18
	Modified residue	385	1	Phosphoserine Ref.18
	Modified residue	386	1	Phosphoserine Ref.17 Ref.18
	Modified residue	406	1	Phosphothreonine Ref.16 Ref.17 Ref.18
Natural variations
	Natural variant	71	1	R → Q. Ref.24 Corresponds to variant rs35434411 [ dbSNP | Ensembl ].		VAR_048344
	Natural variant	71	1	R → W in CMD1HH. Ref.22		VAR_065479
	Natural variant	77	1	P → L. Ref.24 Corresponds to variant rs141355480 [ dbSNP | Ensembl ].		VAR_066777
	Natural variant	94	1	I → F. Ref.24 Corresponds to variant rs145393807 [ dbSNP | Ensembl ].		VAR_066778
	Natural variant	115	1	P → S. Ref.24		VAR_066779
	Natural variant	151	1	C → R. Ref.2 Ref.24 Corresponds to variant rs2234962 [ dbSNP | Ensembl ].		VAR_048345
	Natural variant	155	1	A → T. Ref.24 Corresponds to variant rs61756328 [ dbSNP | Ensembl ].		VAR_066780
	Natural variant	209	1	P → L in MFM6; interferes with the differentiation of skeletal muscle cells; does not cause functional alterations in cardiomyocyte cells. Ref.21 Ref.23 Ref.25 Corresponds to variant rs121918312 [ dbSNP | Ensembl ].		VAR_063089
	Natural variant	218	1	R → W in CMD1HH; interferes with the assembly of Z-disks; increases stress-induced apoptosis. Ref.25		VAR_066781
	Natural variant	258	1	R → W Polymorphism with no functional consequences. Ref.23 Ref.25 Corresponds to variant rs117671123 [ dbSNP | Ensembl ].		VAR_066782
	Natural variant	300	1	D → N. Ref.25 Corresponds to variant rs78439745 [ dbSNP | Ensembl ].		VAR_066783
	Natural variant	380	1	P → S. Ref.24 Corresponds to variant rs144692954 [ dbSNP | Ensembl ].		VAR_066784
	Natural variant	405	1	A → V. Corresponds to variant rs11199064 [ dbSNP | Ensembl ].		VAR_048346
	Natural variant	407	1	P → L. Ref.24 Ref.25 Corresponds to variant rs3858340 [ dbSNP | Ensembl ].		VAR_048347
	Natural variant	455	1	E → K in CMD1HH. Ref.24		VAR_066785
	Natural variant	462	1	L → P in CMD1HH; interferes with the assembly of Z-disks; increases stress-induced apoptosis. Ref.25		VAR_066786
	Natural variant	468	1	V → M in CMD1HH. Ref.24		VAR_066787
	Natural variant	477	1	R → H in CMD1HH. Ref.22		VAR_065480
	Natural variant	553	1	E → D. Ref.25		VAR_066788
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 [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., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder 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: Cervix carcinoma.
[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: Leukemic 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: Cervix carcinoma.
[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: Cervix carcinoma.
[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: Cervix carcinoma.
[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. Tissue: Embryonic kidney.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[18]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-284; THR-285; SER-289; SER-291; SER-377; SER-381; SER-385; SER-386 AND THR-406, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[19]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"Mutation in BAG3 causes severe dominant childhood muscular dystrophy." Selcen D., Muntoni F., Burton B.K., Pegoraro E., Sewry C., Bite A.V., Engel A.G. Ann. Neurol. 65:83-89(2009) [PubMed: 19085932] [Abstract] Cited for: VARIANT MFM6 LEU-209.
[22]	"Genome-wide studies of copy number variation and exome sequencing identify rare variants in BAG3 as a cause of dilated cardiomyopathy." Norton N., Li D., Rieder M.J., Siegfried J.D., Rampersaud E., Zuchner S., Mangos S., Gonzalez-Quintana J., Wang L., McGee S., Reiser J., Martin E., Nickerson D.A., Hershberger R.E. Am. J. Hum. Genet. 88:273-282(2011) [PubMed: 21353195] [Abstract] Cited for: VARIANTS CMD1HH TRP-71 AND HIS-477.
[23]	"BAG3-related myofibrillar myopathy in a Chinese family." Lee H., Cherk S., Chan S., Wong S., Tong T., Ho W., Chan A., Lee K., Mak C. Clin. Genet. 0:0-0(2011) [PubMed: 21361913] [Abstract] Cited for: VARIANT MFM6 LEU-209, VARIANT TRP-258.
[24]	"A genome-wide association study identifies two loci associated with heart failure due to dilated cardiomyopathy." Villard E., Perret C., Gary F., Proust C., Dilanian G., Hengstenberg C., Ruppert V., Arbustini E., Wichter T., Germain M., Dubourg O., Tavazzi L., Aumont M.C., DeGroote P., Fauchier L., Trochu J.N., Gibelin P., Aupetit J.F. , Stark K., Erdmann J., Hetzer R., Roberts A.M., Barton P.J., Regitz-Zagrosek V., Aslam U., Duboscq-Bidot L., Meyborg M., Maisch B., Madeira H., Waldenstrom A., Galve E., Cleland J.G., Dorent R., Roizes G., Zeller T., Blankenberg S., Goodall A.H., Cook S., Tregouet D.A., Tiret L., Isnard R., Komajda M., Charron P., Cambien F. Eur. Heart J. 32:1065-1076(2011) [PubMed: 21459883] [Abstract] Cited for: VARIANTS GLN-71; LEU-77; PHE-94; SER-115; ARG-151; THR-155; SER-380 AND LEU-407, VARIANTS CMD1HH LYS-455 AND MET-468.
[25]	"Dilated cardiomyopathy-associated BAG3 mutations impair Z-disc assembly and enhance sensitivity to apoptosis in cardiomyocytes." Arimura T., Ishikawa T., Nunoda S., Kawai S., Kimura A. Hum. Mutat. 32:1481-1491(2011) [PubMed: 21898660] [Abstract] Cited for: VARIANTS CMD1HH TRP-218 AND PRO-462, VARIANTS TRP-258; ASN-300; LEU-407 AND ASP-553, CHARACTERIZATION OF VARIANTS CMD1HH TRP-218 AND PRO-462, CHARACTERIZATION OF VARIANT MFM6 LEU-209, CHARACTERIZATION OF VARIANT TRP-258.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. NM_004281.3.
UniGene	Hs.523309.
3D structure databases
ProteinModelPortal	O95817.
SMR	O95817. Positions 19-55, 396-498.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95817. 8 interactions.
STRING	O95817.
PTM databases
PhosphoSite	O95817.
Proteomic databases
PeptideAtlas	O95817.
PRIDE	O95817.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000369085; ENSP00000358081; ENSG00000151929.
GeneID	9531.
KEGG	hsa:9531.
UCSC	uc001lem.1. human.
Organism-specific databases
CTD	9531.
GeneCards	GC10P121400.
H-InvDB	HIX0009255.
HGNC	HGNC:939. BAG3.
HPA	HPA018493. HPA020586.
MIM	603883. gene. 612954. phenotype. 613881. phenotype.
neXtProt	NX_O95817.
Orphanet	154. Familial isolated dilated cardiomyopathy. 199340. Muscular dystrophy, Selcen type.
PharmGKB	PA25239.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08274.
HOGENOM	HBG714179.
HOVERGEN	HBG003419.
InParanoid	O95817.
OMA	KKYLMIE.
PhylomeDB	O95817.
Gene expression databases
ArrayExpress	O95817.
Bgee	O95817.
CleanEx	HS_BAG3.
Genevestigator	O95817.
GermOnline	ENSG00000151929. Homo sapiens.
Family and domain databases
InterPro	IPR003103. BAG_domain. IPR001202. WW_Rsp5_WWP. [Graphical view]
Gene3D	G3DSA:2.20.70.10. G3DSA:2.20.70.10. 1 hit.
KO	K09557.
Pfam	PF02179. BAG. 1 hit. PF00397. WW. 1 hit. [Graphical view]
SMART	SM00264. BAG. 1 hit. SM00456. WW. 1 hit. [Graphical view]
SUPFAM	SSF51045. WW_Rsp5_WWP. 1 hit.
PROSITE	PS51035. BAG. 1 hit. PS01159. WW_DOMAIN_1. 1 hit. PS50020. WW_DOMAIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
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:	January 25, 2012
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.