[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 [LARGE SCALE MRNA]. TISSUE=Brain; DOI=10.1093/dnares/5.6.355; PubMed=10048485 [NCBI, ExPASy, EBI, Israel, Japan] Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.; "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."; DNA Res. 5:355-364(1998).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; 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).
[4]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[5]	STRUCTURE BY NMR OF 275-351. RIKEN structural genomics initiative (RSGI); "Solution structure of the BAG domain (275-350) of BAG-family molecular chaperone regulator-5."; Submitted (DEC-2006) to the PDB data bank.

Comments

FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 (By similarity).
SUBUNIT: Binds to the ATPase domain of HSP70/HSC chaperones. Binds PARK2 (By similarity).
SIMILARITY: Contains 4 BAG domains.

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

AF095195; AAD16124.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB020680; BAA74896.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC044216; AAH44216.2; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050551; AAH50551.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00007731; -.

RefSeq

NP_001015048.1; -.
NP_001015049.1; -.
NP_004864.1; -.

UniGene

Hs.5443

3D structure databases

PDB

2D9D; NMR; -; A=275-350.

[ExPASy / RCSB / EBI]

2D9D; -.

Q9UL15; 1-89.

Protein-protein interaction databases

IntAct

Q9UL15; 2.

Organism-specific databases

GC14M103093; -.

HIX0012003; -.

HGNC:941; BAG5.

HPA016429; -.

603885; gene. [NCBI / EBI]

PharmGKB

PA25241; -.

HUGE

KIAA0873.

Gene expression databases

Q9UL15; -.

Q9UL15; -.

HS_BAG5; -.

ENSG00000166170; Homo sapiens.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from electronic annotation from InterPro).
GO:0006915;	Biological process: apoptosis (inferred from electronic annotation from InterPro).
GO:0006457;	Biological process: protein folding (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR003103; Apoptosis_reg_Bcl-2_prot_BAG.
Graphical view of domain structure.

Pfam

PF02179; BAG; 4.
Pfam graphical view of domain structure.

SMART

SM00264; BAG; 4.
SMART graphical view of domain structure.

PROSITE

PS51035; BAG; 4.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

Q9UL15; -.

Genome annotation databases

Ensembl

ENSG00000166170; Homo sapiens. [Contig view]

GeneID

9529; -.

KEGG

hsa:9529; -.

Phylogenomic databases

HOGENOM

Q9UL15; -.

HOVERGEN

Q9UL15; -.

Other

35720; -.

BAG5; Homo sapiens.

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

Keywords

3D-structure; Chaperone; Repeat.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 447`	`447`	`BAG family molecular chaperone regulator 5.`	`PRO_0000088872`
`DOMAIN`	`9 86`	`78`	`BAG 1.`
`DOMAIN`	`182 260`	`79`	`BAG 2.`
`DOMAIN`	`275 350`	`76`	`BAG 3.`
`DOMAIN`	`365 442`	`78`	`BAG 4.`
`CONFLICT`	`157 157`		`C -> W (in Ref. 3; AAH50551).`

Sequence information

Length: 447 AA [This is the length of the unprocessed precursor]

Molecular weight: 51200 Da [This is the MW of the unprocessed precursor]

CRC64: 0D3F7EA6B612C1F5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDMGNQHPSI SRLQEIQKEV KSVEQQVIGF SGLSDDKNYK KLERILTKQL FEIDSVDTEG 

        70         80         90        100        110        120 
KGDIQQARKR AAQETERLLK ELEQNANHPH RIEIQNIFEE AQSLVREKIV PFYNGGNCVT 

       130        140        150        160        170        180 
DEFEEGIQDI ILRLTHVKTG GKISLRKARY HTLTKICAVQ EIIEDCMKKQ PSLPLSEDAH 

       190        200        210        220        230        240 
PSVAKINFVM CEVNKARGVL IALLMGVNNN ETCRHLSCVL SGLIADLDAL DVCGRTEIRN 

       250        260        270        280        290        300 
YRREVVEDIN KLLKYLDLEE EADTTKAFDL RQNHSILKIE KVLKRMREIK NELLQAQNPS 

       310        320        330        340        350        360 
ELYLSSKTEL QGLIGQLDEV SLEKNPCIRE ARRRAVIEVQ TLITYIDLKE ALEKRKLFAC 

       370        380        390        400        410        420 
EEHPSHKAVW NVLGNLSEIQ GEVLSFDGNR TDKNYIRLEE LLTKQLLALD AVDPQGEEKC 

       430        440 
KAARKQAVRL AQNILSYLDL KSDEWEY

Q9UL15 in FASTA format

View entry in raw text format (no links)
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	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