Q9UL15 (BAG5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
BAG family molecular chaperone regulator 5
Short name=BAG-5

Alternative name(s):
Bcl-2-associated athanogene 5

Gene names

Name:	BAG5
Synonyms:	KIAA0873

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	447 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Inhibits both auto-ubiquitination of PARK2 and ubiquitination of target proteins by PARK2 By similarity. May function as a nucleotide exchange factor for HSP/HSP70, promoting ADP release, and activating Hsp70-mediated refolding. Ref.7
Subunit structure	Binds to the ATPase domain of HSP/HSC70 chaperones. Binds PARK2 By similarity. Ref.7
Domain	The fifth BAG domain is responsible for the interaction with HSP70 nucleotide-binding domain. Ref.7
Sequence similarities	Contains 5 BAG domains.
Sequence caution	The sequence BAA74896.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Molecular function	Chaperone
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of protein refolding Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of ubiquitin-protein ligase activity Inferred from sequence or structural similarity. Source: BHF-UCL neuron death Inferred from sequence or structural similarity. Source: BHF-UCL protein folding Traceable author statement. Source: ProtInc regulation of inclusion body assembly Inferred from mutant phenotype. Source: BHF-UCL
Cellular component	inclusion body Inferred from direct assay. Source: BHF-UCL perinuclear region of cytoplasm Inferred from direct assay. Source: BHF-UCL
Molecular function	chaperone binding Inferred from physical interaction. Source: BHF-UCL ubiquitin protein ligase binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UL15-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UL15-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRFHWLPTLSEPFDRNQELETCIRPLWTPSGSACETEHNKSM

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 447

447

BAG family molecular chaperone regulator 5

PRO_0000088872

Regions

Domain

9 – 86

78

BAG 1

Domain

95 – 167

73

BAG 2

Domain

182 – 260

79

BAG 3

Domain

275 – 350

76

BAG 4

Domain

365 – 442

78

BAG 5

Amino acid modifications

Modified residue

278

1

N6-acetyllysine Ref.5

Natural variations

Alternative sequence

1

1

M → MRFHWLPTLSEPFDRNQELE TCIRPLWTPSGSACETEHNK SM in isoform 2.

VSP_037996

Natural variant

157

1

C → W. Ref.4
Corresponds to variant rs17854644 [ dbSNP | Ensembl ].

VAR_058712

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

447

Helix Strand Turn

Details...

Helix

277 – 295

19

Turn

299 – 301

3

Helix

302 – 310

9

Helix

317 – 320

4

Helix

326 – 350

25

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 0D3F7EA6B612C1F5	FASTA	447	51,200
	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
	Isoform 2 [UniParc]. Checksum: 7A901A14F9B07AC2	FASTA	488	56,027
	10 20 30 40 50 60 MRFHWLPTLS EPFDRNQELE TCIRPLWTPS GSACETEHNK SMDMGNQHPS ISRLQEIQKE 70 80 90 100 110 120 VKSVEQQVIG FSGLSDDKNY KKLERILTKQ LFEIDSVDTE GKGDIQQARK RAAQETERLL 130 140 150 160 170 180 KELEQNANHP HRIEIQNIFE EAQSLVREKI VPFYNGGNCV TDEFEEGIQD IILRLTHVKT 190 200 210 220 230 240 GGKISLRKAR YHTLTKICAV QEIIEDCMKK QPSLPLSEDA HPSVAKINFV MCEVNKARGV 250 260 270 280 290 300 LIALLMGVNN NETCRHLSCV LSGLIADLDA LDVCGRTEIR NYRREVVEDI NKLLKYLDLE 310 320 330 340 350 360 EEADTTKAFD LRQNHSILKI EKVLKRMREI KNELLQAQNP SELYLSSKTE LQGLIGQLDE 370 380 390 400 410 420 VSLEKNPCIR EARRRAVIEV QTLITYIDLK EALEKRKLFA CEEHPSHKAV WNVLGNLSEI 430 440 450 460 470 480 QGEVLSFDGN RTDKNYIRLE ELLTKQLLAL DAVDPQGEEK CKAARKQAVR LAQNILSYLD LKSDEWEY

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] (ISOFORM 1).
[2]	"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." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:355-364(1998) [PubMed: 10048485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed: 12508121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] (ISOFORMS 1 AND 2), VARIANT TRP-157. Tissue: Brain.
[5]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-278, MASS SPECTROMETRY.
[6]	"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].
[7]	"The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange." Arakawa A., Handa N., Ohsawa N., Shida M., Kigawa T., Hayashi F., Shirouzu M., Yokoyama S. Structure 18:309-319(2010) [PubMed: 20223214] [Abstract] Cited for: STRUCTURE BY NMR OF 275-350, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 341-447 IN COMPLEX WITH HSPA1, DOMAIN BAG, FUNCTION, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF095195 mRNA. Translation: AAD16124.2.
AB020680 mRNA. Translation: BAA74896.1. Different initiation.
AL139300 Genomic DNA. No translation available.
BC044216 mRNA. Translation: AAH44216.2.
BC050551 mRNA. Translation: AAH50551.1.

IPI

IPI00007731.
IPI00556027.

RefSeq

NP_001015048.1. NM_001015048.2.
NP_001015049.1. NM_001015049.2.
NP_004864.1. NM_004873.3.

UniGene

Hs.5443.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D9D	NMR	-	A	275-350	[»]
3A8Y	X-ray	2.30	C/D	341-447	[»]

ProteinModelPortal

Q9UL15.

SMR

Q9UL15. Positions 1-89, 178-259, 276-447.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-53428N.

IntAct

Q9UL15. 5 interactions.

MINT

MINT-1147557.

STRING

Q9UL15.

PTM databases

PhosphoSite

Q9UL15.

Polymorphism databases

DMDM

12643895.

Proteomic databases

PRIDE

Q9UL15.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000299204; ENSP00000299204; ENSG00000166170.
ENST00000337322; ENSP00000338814; ENSG00000166170.
ENST00000445922; ENSP00000391713; ENSG00000166170.

GeneID

9529.

KEGG

hsa:9529.

UCSC

uc001ynh.1. human.

Organism-specific databases

CTD

9529.

GeneCards

GC14M104022.

H-InvDB

HIX0012003.

HGNC

HGNC:941. BAG5.

HPA

HPA016429.

MIM

603885. gene.

neXtProt

NX_Q9UL15.

PharmGKB

PA25241.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG13028.

GeneTree

ENSGT00530000063256.

HOGENOM

HBG713028.

HOVERGEN

HBG004810.

InParanoid

Q9UL15.

OMA

YIRLEEL.

OrthoDB

EOG46T31D.

PhylomeDB

Q9UL15.

Gene expression databases

ArrayExpress

Q9UL15.

Bgee

Q9UL15.

CleanEx

HS_BAG5.

Genevestigator

Q9UL15.

GermOnline

ENSG00000166170. Homo sapiens.

Family and domain databases

InterPro

IPR003103. BAG_domain.
[Graphical view]

KO

K09559.

Pfam

PF02179. BAG. 4 hits.
[Graphical view]

SMART

SM00264. BAG. 4 hits.
[Graphical view]

PROSITE

PS51035. BAG. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

35720.

SOURCE

Search...

Entry information

Entry name

BAG5_HUMAN

Accession

Primary (citable) accession number: Q9UL15
Secondary accession number(s): O94950, Q86W59

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 95 of the entry and version 1 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.