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O95817 (BAG3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length575 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Interacts with DNAJB6. Ref.14

Involvement in disease

Myopathy, myofibrillar, 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.17 Ref.19

Cardiomyopathy, dilated 1HH (CMD1HH) [MIM:613881]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.18 Ref.19

Sequence similarities

Contains 1 BAG domain.

Contains 2 WW domains.

Ontologies

Keywords
   Biological processApoptosis
   Coding sequence diversityPolymorphism
   DiseaseCardiomyopathy
Disease mutation
Myofibrillar myopathy
   DomainRepeat
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbrain development

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from direct assay Ref.2. Source: MGI

negative regulation of apoptotic process

Non-traceable author statement Ref.2. Source: UniProtKB

negative regulation of striated muscle cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

protein folding

Non-traceable author statement Ref.1. Source: UniProtKB

protein stabilization

Inferred from electronic annotation. Source: Ensembl

spinal cord development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentZ disc

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from direct assay Ref.2. Source: MGI

neuron projection

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionprotein binding

Inferred from physical interaction Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SQSTM1Q135013EBI-747185,EBI-307104

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 575574BAG family molecular chaperone regulator 3
PRO_0000088868

Regions

Domain20 – 5435WW 1
Domain124 – 15431WW 2
Domain421 – 49878BAG
Compositional bias180 – 1878Poly-Ser

Amino acid modifications

Modified residue21N-acetylserine Ref.12
Modified residue1981Phosphoserine Ref.12
Modified residue2741Phosphoserine Ref.10
Modified residue2751Phosphoserine Ref.10
Modified residue2791Phosphoserine Ref.10
Modified residue2851Phosphothreonine Ref.10
Modified residue2891Phosphoserine Ref.10 Ref.12
Modified residue2911Phosphoserine Ref.10
Modified residue3771Phosphoserine Ref.9 Ref.10 Ref.12
Modified residue3851Phosphoserine By similarity
Modified residue3861Phosphoserine Ref.10 Ref.12
Modified residue4061Phosphothreonine Ref.10 Ref.12

Natural variations

Natural variant711R → Q. Ref.18
Corresponds to variant rs35434411 [ dbSNP | Ensembl ].
VAR_048344
Natural variant711R → W in CMD1HH. Ref.16
VAR_065479
Natural variant771P → L. Ref.18
Corresponds to variant rs141355480 [ dbSNP | Ensembl ].
VAR_066777
Natural variant941I → F. Ref.18
Corresponds to variant rs145393807 [ dbSNP | Ensembl ].
VAR_066778
Natural variant1151P → S. Ref.18
VAR_066779
Natural variant1511C → R. Ref.2 Ref.18
Corresponds to variant rs2234962 [ dbSNP | Ensembl ].
VAR_048345
Natural variant1551A → T. Ref.18
Corresponds to variant rs61756328 [ dbSNP | Ensembl ].
VAR_066780
Natural variant2091P → L in MFM6; interferes with the differentiation of skeletal muscle cells; does not cause functional alterations in cardiomyocyte cells. Ref.15 Ref.17 Ref.19
Corresponds to variant rs121918312 [ dbSNP | Ensembl ].
VAR_063089
Natural variant2181R → W in CMD1HH; interferes with the assembly of Z-disks; increases stress-induced apoptosis. Ref.19
VAR_066781
Natural variant2581R → W Polymorphism with no functional consequences. Ref.17 Ref.19
Corresponds to variant rs117671123 [ dbSNP | Ensembl ].
VAR_066782
Natural variant3001D → N. Ref.19
Corresponds to variant rs78439745 [ dbSNP | Ensembl ].
VAR_066783
Natural variant3801P → S. Ref.18
Corresponds to variant rs144692954 [ dbSNP | Ensembl ].
VAR_066784
Natural variant4051A → V.
Corresponds to variant rs11199064 [ dbSNP | Ensembl ].
VAR_048346
Natural variant4071P → L. Ref.18 Ref.19
Corresponds to variant rs3858340 [ dbSNP | Ensembl ].
VAR_048347
Natural variant4551E → K in CMD1HH. Ref.18
VAR_066785
Natural variant4621L → P in CMD1HH; interferes with the assembly of Z-disks; increases stress-induced apoptosis. Ref.19
VAR_066786
Natural variant4681V → M in CMD1HH. Ref.18
VAR_066787
Natural variant4771R → H in CMD1HH. Ref.16
VAR_065480
Natural variant5531E → D. Ref.19
VAR_066788

Experimental info

Sequence conflict2271Q → K in AAD16122. Ref.1
Sequence conflict2371Q → R in AAD16122. Ref.1
Sequence conflict3041Missing in CAB70824. Ref.5

Sequences

Sequence LengthMass (Da)Tools
O95817 [UniParc].

Last modified January 11, 2001. Version 3.
Checksum: A6328A44F37A406A

FASTA57561,595
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain, Lung and Placenta.
[7]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198; SER-289; SER-377; SER-386 AND THR-406, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Mutations affecting the cytoplasmic functions of the co-chaperone DNAJB6 cause limb-girdle muscular dystrophy."
Sarparanta J., Jonson P.H., Golzio C., Sandell S., Luque H., Screen M., McDonald K., Stajich J.M., Mahjneh I., Vihola A., Raheem O., Penttila S., Lehtinen S., Huovinen S., Palmio J., Tasca G., Ricci E., Hackman P. expand/collapse author list , Hauser M., Katsanis N., Udd B.
Nat. Genet. 44:450-455(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNAJB6.
[15]"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] [Europe PMC] [Abstract]
Cited for: VARIANT MFM6 LEU-209.
[16]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1HH TRP-71 AND HIS-477.
[17]"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. 81:394-398(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MFM6 LEU-209, VARIANT TRP-258.
[18]"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. expand/collapse author list , 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] [Europe PMC] [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.
[19]"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] [Europe PMC] [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.

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.
CCDSCCDS7615.1.
RefSeqNP_004272.2. NM_004281.3.
UniGeneHs.523309.

3D structure databases

ProteinModelPortalO95817.
SMRO95817. Positions 19-55, 396-498.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114907. 409 interactions.
DIPDIP-41273N.
IntActO95817. 14 interactions.
MINTMINT-208995.
STRING9606.ENSP00000358081.

PTM databases

PhosphoSiteO95817.

Proteomic databases

MaxQBO95817.
PaxDbO95817.
PeptideAtlasO95817.
PRIDEO95817.

Protocols and materials databases

DNASU9531.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369085; ENSP00000358081; ENSG00000151929.
GeneID9531.
KEGGhsa:9531.
UCSCuc001lel.3. human.

Organism-specific databases

CTD9531.
GeneCardsGC10P121400.
GeneReviewsBAG3.
HGNCHGNC:939. BAG3.
HPAHPA018493.
HPA020586.
MIM603883. gene.
612954. phenotype.
613881. phenotype.
neXtProtNX_O95817.
Orphanet154. Familial isolated dilated cardiomyopathy.
199340. Muscular dystrophy, Selcen type.
PharmGKBPA25239.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238690.
HOGENOMHOG000050234.
HOVERGENHBG003419.
InParanoidO95817.
KOK09557.
OMAVYPQLRP.
OrthoDBEOG75B85S.
PhylomeDBO95817.
TreeFamTF102013.

Enzyme and pathway databases

SignaLinkO95817.

Gene expression databases

ArrayExpressO95817.
BgeeO95817.
CleanExHS_BAG3.
GenevestigatorO95817.

Family and domain databases

Gene3D1.20.58.120. 1 hit.
InterProIPR003103. BAG_domain.
IPR001202. WW_dom.
[Graphical view]
PfamPF02179. BAG. 1 hit.
PF00397. WW. 1 hit.
[Graphical view]
SMARTSM00264. BAG. 1 hit.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMSSF51045. SSF51045. 1 hit.
PROSITEPS51035. BAG. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiBAG3.
GenomeRNAi9531.
NextBio35732.
PMAP-CutDBO95817.
PROO95817.
SOURCESearch...

Entry information

Entry nameBAG3_HUMAN
AccessionPrimary (citable) accession number: O95817
Secondary accession number(s): A8K5L8 expand/collapse secondary AC list , Q3B763, Q9NT20, Q9P120
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2001
Last modified: July 9, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM