[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Liver; DOI=10.1073/pnas.92.25.11465; PubMed=8524784 [NCBI, ExPASy, EBI, Israel, Japan] Zeiner M., Gehring U.; "A protein that interacts with members of the nuclear hormone receptor family: identification and cDNA cloning."; Proc. Natl. Acad. Sci. U.S.A. 92:11465-11469(1995).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Mammary gland; DOI=10.1006/geno.1996.0389; PubMed=8812483 [NCBI, ExPASy, EBI, Israel, Japan] Takayama S., Kochel K., Irie S., Inazawa J., Abe T., Sato T., Druck T., Huebner K., Reed J.C.; "Cloning of cDNAs encoding the human BAG1 protein and localization of the human BAG1 gene to chromosome 9p12."; Genomics 35:494-498(1996).
[3]	SEQUENCE REVISION TO N-TERMINUS; 79; 84; 90; 245 AND 293. Takayama S.; Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ANTI-APOPTOTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION WITH STK19. TISSUE=T-cell; DOI=10.1002/ijc.21259; PubMed=15986447 [NCBI, ExPASy, EBI, Israel, Japan] Wadle A., Mischo A., Henrich P.P., Stenner-Lieven F., Scherer C., Imig J., Petersen G., Pfreundschuh M., Renner C.; "Characterization of Hap/BAG-1 variants as RP1 binding proteins with antiapoptotic activity."; Int. J. Cancer 117:896-904(2005).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Cervix, and Lung; 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).
[6]	INTERACTION WITH SIAH1. DOI=10.1093/emboj/17.10.2736; PubMed=9582267 [NCBI, ExPASy, EBI, Israel, Japan] Matsuzawa S., Takayama S., Froesch B.A., Zapata J.M., Reed J.C.; "p53-inducible human homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1."; EMBO J. 17:2736-2747(1998).
[7]	FUNCTION. 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).
[8]	INTERACTION WITH NR3C1. DOI=10.1083/jcb.146.5.929; PubMed=10477749 [NCBI, ExPASy, EBI, Israel, Japan] Schneikert J., Huebner S., Martin E., Cato A.B.C.; "A nuclear action of the eukaryotic cochaperone RAP46 in downregulation of glucocorticoid receptor activity."; J. Cell Biol. 146:929-940(1999).
[9]	INTERACTION WITH PPP1R15A, AND FUNCTION. DOI=10.1128/MCB.23.10.3477-3486.2003; PubMed=12724406 [NCBI, ExPASy, EBI, Israel, Japan] Hung W.J., Roberson R.S., Taft J., Wu D.Y.; "Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functions."; Mol. Cell. Biol. 23:3477-3486(2003).
[10]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 222-334 IN COMPLEX WITH HSC70. DOI=10.1126/science.1057268; PubMed=11222862 [NCBI, ExPASy, EBI, Israel, Japan] Sondermann H., Scheufler C., Schneider C., Hohfeld J., Hartl F.U., Moarefi I.; "Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors."; Science 291:1553-1557(2001).
[11]	STRUCTURE BY NMR OF 72-152. RIKEN structural genomics initiative (RSGI); "Solution structure of the ubiquitin domain of Bcl-2 binding athanogene-1."; Submitted (AUG-2005) to the PDB data bank.

Comments

FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli.
SUBUNIT: Binds to the ATPase domain of HSP70/HSC chaperones. Binds to BCL2 and NR3C1. Interacts with N-terminal region of STK19. Interacts with PPP1R15A. Isoform 2 doesn't interact with HSP70/HSC or BCL2.
INTERACTION:
P19120:HSPA8 (xeno); NbExp=1; IntAct=EBI-1030678, EBI-907802;
SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. Note=Isoform2 localizes to the cytoplasm and shuttles into the nucleus in response to heat shock.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	1
Isoform ID	Q99933-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	BAG1V, HAPV
Isoform ID	Q99933-2
Features which should be applied to build the isoform sequence: VSP_000453.

PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation (Probable).
DISEASE: May be linked to the cryptophthalmos syndrome (Fraser syndrome), an autosomal recessive disorder characterized by the failure of eyes fissures to form during embryogenesis, webbed fingers, and atresia of ear canals, anus, vagina, alimentary tract, or larynx. All these developmental processes require cell death.
SIMILARITY: Contains 1 BAG domain.
SIMILARITY: Contains 1 ubiquitin-like domain.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org//Genes/BAG1ID742ch9p13.html";.

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

Z35491; CAA84624.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U46917; AAD11467.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF022224; AAC34258.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF116273; AAD25045.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001936; AAH01936.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014774; AAH14774.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00218546; -.
IPI00300531; -.

UniGene

Hs.377484

3D structure databases

PDB

1HX1; X-ray; 1.90 A; B=222-334.	[ExPASy / RCSB / EBI]
1WXV; NMR; -; A=143-223.	[ExPASy / RCSB / EBI]
3FZF; X-ray; 2.20 A; B=222-334.	[ExPASy / RCSB / EBI]
3FZH; X-ray; 2.00 A; B=222-334.	[ExPASy / RCSB / EBI]
3FZK; X-ray; 2.10 A; B=222-334.	[ExPASy / RCSB / EBI]
3FZL; X-ray; 2.20 A; B=222-334.	[ExPASy / RCSB / EBI]
3FZM; X-ray; 2.30 A; B=222-334.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1HX1; -.
1WXV; -.
3FZF; -.
3FZH; -.
3FZK; -.
3FZL; -.
3FZM; -.

SMR

Q99933; 216-345.

ModBase

Q99933.

Protein-protein interaction databases

DIP

DIP:3341N; -.

IntAct

Q99933; 1.

Enzyme and pathway databases

Pathway_Interaction_DB

met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met).

Organism-specific databases

GeneCards

GC09M033245; -.

H-InvDB

HIX0007978; -.
HIX0080318; -.

HGNC:937; BAG1.

CAB002486; -.
HPA018121; -.

MIM

601497; gene. [NCBI / EBI]

PharmGKB

PA25237; -.

Gene expression databases

Q99933; -.

Q99933; -.

HS_BAG1; -.

ENSG00000107262; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (traceable author statement from ProtInc).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from LIFEdb).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0005057;	Molecular function: receptor signaling protein activity (traceable author statement from ProtInc).
GO:0006916;	Biological process: anti-apoptosis (traceable author statement from ProtInc).
GO:0006915;	Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0007166;	Biological process: cell surface receptor linked signal transduction (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR003103; Apoptosis_reg_Bcl-2_prot_BAG.
IPR017093; Molecular_chp_reg_BAG_1.
IPR000626; Ubiquitin.
IPR019954; Ubiquitin_CS.
IPR019955; Ubiquitin_supergroup.
Graphical view of domain structure.

Pfam

PF02179; BAG; 1.
PF00240; ubiquitin; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF037029; BAG_1; 1.

SMART

SM00264; BAG; 1.
SM00213; UBQ; 1.
SMART graphical view of domain structure.

PROSITE

PS51035; BAG; 1.
PS00299; UBIQUITIN_1; FALSE_NEG.
PS50053; UBIQUITIN_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

Q99933; -.

Genome annotation databases

Ensembl

ENSG00000107262; Homo sapiens. [Contig view]

Phylogenomic databases

HOVERGEN

Q99933; -.

Other

BAG1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Apoptosis; Chaperone; Cytoplasm; Nucleus; Repeat; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 345`	`345`	`BAG family molecular chaperone regulator 1.`	`PRO_0000088865`
`REPEAT`	`96 101`	`6`	`1.`
`REPEAT`	`102 107`	`6`	`2.`
`REPEAT`	`108 113`	`6`	`3.`
`REPEAT`	`114 119`	`6`	`4.`
`REPEAT`	`120 125`	`6`	`5.`
`REPEAT`	`126 131`	`6`	`6.`
`REPEAT`	`132 137`	`6`	`7.`
`DOMAIN`	`144 224`	`81`	`Ubiquitin-like.`
`DOMAIN`	`246 326`	`81`	`BAG.`
`REGION`	`96 137`	`42`	`7 X 6 AA tandem repeat of E-E-X(4).`
`REGION`	`216 345`	`130`	`Interaction with PPP1R15A.`
`COMPBIAS`	`4 82`	`79`	`Arg-rich.`
`VAR_SEQ`	`302 345`		`KDSRLKRKGLVKKVQAFLAECDTVEQNICQETERLQSTN` `FALAE -> PTLTLVLNEK (in isoform 2).`	`VSP_000453`
`CONFLICT`	`79 79`		`R -> F (in Ref. 2; AAD11467).`
`CONFLICT`	`84 84`		`E -> K (in Ref. 2; AAD11467).`
`CONFLICT`	`90 90`		`E -> K (in Ref. 2; AAD11467).`
`CONFLICT`	`245 245`		`D -> N (in Ref. 2; AAD11467).`
`CONFLICT`	`293 293`		`D -> H (in Ref. 2; AAD11467).`
`STRAND`	`72 78`	`7`
`STRAND`	`80 88`	`9`
`STRAND`	`92 96`	`5`
`HELIX`	`99 109`	`11`
`TURN`	`114 116`	`3`
`STRAND`	`118 121`	`4`
`STRAND`	`124 126`	`3`
`STRAND`	`129 132`	`4`
`HELIX`	`133 136`	`4`
`STRAND`	`140 148`	`9`
`HELIX`	`224 259`	`36`
`HELIX`	`264 272`	`9`
`HELIX`	`275 292`	`18`
`HELIX`	`302 326`	`25`

Sequence information

Length: 345 AA [This is the length of the unprocessed precursor]

Molecular weight: 38878 Da [This is the MW of the unprocessed precursor]

CRC64: 9895EF082D73335B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAQRGGARRP RGDRERLGSR LRALRPGREP RQSEPPAQRG PPPSRRPPAR STASGHDRPT 

        70         80         90        100        110        120 
RGAAAGARRP RMKKKTRRRS TRSEELTRSE ELTLSEEATW SEEATQSEEA TQGEEMNRSQ 

       130        140        150        160        170        180 
EVTRDEESTR SEEVTREEMA AAGLTVTVTH SNEKHDLHVT SQQGSSEPVV QDLAQVVEEV 

       190        200        210        220        230        240 
IGVPQSFQKL IFKGKSLKEM ETPLSALGIQ DGCRVMLIGK KNSPQEEVEL KKLKHLEKSV 

       250        260        270        280        290        300 
EKIADQLEEL NKELTGIQQG FLPKDLQAEA LCKLDRRVKA TIEQFMKILE EIDTLILPEN 

       310        320        330        340 
FKDSRLKRKG LVKKVQAFLA ECDTVEQNIC QETERLQSTN FALAE

Q99933 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools