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Protein

BAG family molecular chaperone regulator 5

Gene

BAG5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

GO - Molecular functioni

  • adenyl-nucleotide exchange factor activity Source: Reactome
  • chaperone binding Source: BHF-UCL
  • protein kinase binding Source: ParkinsonsUK-UCL
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  • Golgi organization Source: ParkinsonsUK-UCL
  • negative regulation of neuron projection development Source: ParkinsonsUK-UCL
  • negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  • negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
  • negative regulation of protein refolding Source: BHF-UCL
  • negative regulation of protein ubiquitination Source: ParkinsonsUK-UCL
  • negative regulation of ubiquitin-protein transferase activity Source: BHF-UCL
  • neuron death Source: BHF-UCL
  • protein folding Source: ProtInc
  • regulation of cellular response to heat Source: Reactome
  • regulation of inclusion body assembly Source: BHF-UCL
  • regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciZFISH:ENSG00000166170-MONOMER.
ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
BAG family molecular chaperone regulator 5
Short name:
BAG-5
Alternative name(s):
Bcl-2-associated athanogene 5
Gene namesi
Name:BAG5
Synonyms:KIAA0873
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:941. BAG5.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: ParkinsonsUK-UCL
  • inclusion body Source: BHF-UCL
  • membrane Source: UniProtKB
  • mitochondrion Source: ParkinsonsUK-UCL
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

DisGeNETi9529.
OpenTargetsiENSG00000166170.
PharmGKBiPA25241.

Polymorphism and mutation databases

BioMutaiBAG5.
DMDMi12643895.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000888721 – 447BAG family molecular chaperone regulator 5Add BLAST447

Proteomic databases

EPDiQ9UL15.
PaxDbiQ9UL15.
PeptideAtlasiQ9UL15.
PRIDEiQ9UL15.

PTM databases

iPTMnetiQ9UL15.
PhosphoSitePlusiQ9UL15.

Expressioni

Gene expression databases

BgeeiENSG00000166170.
CleanExiHS_BAG5.
ExpressionAtlasiQ9UL15. baseline and differential.
GenevisibleiQ9UL15. HS.

Organism-specific databases

HPAiHPA016429.

Interactioni

Subunit structurei

Binds to the ATPase domain of HSP/HSC70 chaperones. Binds PARK2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q53FC72EBI-356517,EBI-9356749
BANPQ8N9N53EBI-356517,EBI-744695
CCDC155Q8N6L03EBI-356517,EBI-749265
FAM118BQ9BPY33EBI-356517,EBI-726822
HSPA1BP081076EBI-356517,EBI-629985
LRRK1Q38SD23EBI-356517,EBI-1050422
LRRK2Q5S00712EBI-356517,EBI-5323863
MAD1L1Q9Y6D96EBI-356517,EBI-742610
THAP1Q9NVV95EBI-356517,EBI-741515
TRIM27P143735EBI-356517,EBI-719493

GO - Molecular functioni

  • chaperone binding Source: BHF-UCL
  • protein kinase binding Source: ParkinsonsUK-UCL
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi114905. 41 interactors.
DIPiDIP-53428N.
IntActiQ9UL15. 41 interactors.
MINTiMINT-1147557.
STRINGi9606.ENSP00000338814.

Structurei

Secondary structure

1447
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi277 – 295Combined sources19
Turni299 – 301Combined sources3
Helixi302 – 317Combined sources16
Helixi318 – 320Combined sources3
Helixi326 – 350Combined sources25
Turni356 – 358Combined sources3
Helixi364 – 384Combined sources21
Helixi393 – 410Combined sources18
Helixi418 – 442Combined sources25

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D9DNMR-A275-350[»]
3A8YX-ray2.30C/D341-447[»]
ProteinModelPortaliQ9UL15.
SMRiQ9UL15.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UL15.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini9 – 86BAG 1PROSITE-ProRule annotationAdd BLAST78
Domaini95 – 167BAG 2PROSITE-ProRule annotationAdd BLAST73
Domaini182 – 260BAG 3PROSITE-ProRule annotationAdd BLAST79
Domaini275 – 350BAG 4PROSITE-ProRule annotationAdd BLAST76
Domaini365 – 442BAG 5PROSITE-ProRule annotationAdd BLAST78

Domaini

The fifth BAG domain is responsible for the interaction with HSP70 nucleotide-binding domain.1 Publication

Sequence similaritiesi

Contains 5 BAG domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4361. Eukaryota.
ENOG4111WNH. LUCA.
GeneTreeiENSGT00530000063256.
HOGENOMiHOG000070447.
HOVERGENiHBG004810.
InParanoidiQ9UL15.
KOiK09559.
OMAiANHPHRI.
OrthoDBiEOG091G08LY.
PhylomeDBiQ9UL15.
TreeFamiTF102014.

Family and domain databases

Gene3Di1.20.58.120. 4 hits.
InterProiIPR003103. BAG_domain.
[Graphical view]
PfamiPF02179. BAG. 4 hits.
[Graphical view]
SMARTiSM00264. BAG. 4 hits.
[Graphical view]
SUPFAMiSSF63491. SSF63491. 4 hits.
PROSITEiPS51035. BAG. 4 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UL15-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MDMGNQHPSI SRLQEIQKEV KSVEQQVIGF SGLSDDKNYK KLERILTKQL
60 70 80 90 100
FEIDSVDTEG KGDIQQARKR AAQETERLLK ELEQNANHPH RIEIQNIFEE
110 120 130 140 150
AQSLVREKIV PFYNGGNCVT DEFEEGIQDI ILRLTHVKTG GKISLRKARY
160 170 180 190 200
HTLTKICAVQ EIIEDCMKKQ PSLPLSEDAH PSVAKINFVM CEVNKARGVL
210 220 230 240 250
IALLMGVNNN ETCRHLSCVL SGLIADLDAL DVCGRTEIRN YRREVVEDIN
260 270 280 290 300
KLLKYLDLEE EADTTKAFDL RQNHSILKIE KVLKRMREIK NELLQAQNPS
310 320 330 340 350
ELYLSSKTEL QGLIGQLDEV SLEKNPCIRE ARRRAVIEVQ TLITYIDLKE
360 370 380 390 400
ALEKRKLFAC EEHPSHKAVW NVLGNLSEIQ GEVLSFDGNR TDKNYIRLEE
410 420 430 440
LLTKQLLALD AVDPQGEEKC KAARKQAVRL AQNILSYLDL KSDEWEY
Length:447
Mass (Da):51,200
Last modified:May 1, 2000 - v1
Checksum:i0D3F7EA6B612C1F5
GO
Isoform 2 (identifier: Q9UL15-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:488
Mass (Da):56,027
Checksum:i7A901A14F9B07AC2
GO

Sequence cautioni

The sequence BAA74896 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_058712157C → W.1 PublicationCorresponds to variant rs17854644dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0379961M → MRFHWLPTLSEPFDRNQELE TCIRPLWTPSGSACETEHNK SM in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41995.1. [Q9UL15-2]
CCDS9982.1. [Q9UL15-1]
RefSeqiNP_001015048.1. NM_001015048.2. [Q9UL15-1]
NP_001015049.1. NM_001015049.2. [Q9UL15-2]
NP_004864.1. NM_004873.3. [Q9UL15-1]
UniGeneiHs.5443.

Genome annotation databases

EnsembliENST00000299204; ENSP00000299204; ENSG00000166170. [Q9UL15-1]
ENST00000337322; ENSP00000338814; ENSG00000166170. [Q9UL15-2]
ENST00000445922; ENSP00000391713; ENSG00000166170. [Q9UL15-1]
GeneIDi9529.
KEGGihsa:9529.
UCSCiuc001ynh.3. human. [Q9UL15-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41995.1. [Q9UL15-2]
CCDS9982.1. [Q9UL15-1]
RefSeqiNP_001015048.1. NM_001015048.2. [Q9UL15-1]
NP_001015049.1. NM_001015049.2. [Q9UL15-2]
NP_004864.1. NM_004873.3. [Q9UL15-1]
UniGeneiHs.5443.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2D9DNMR-A275-350[»]
3A8YX-ray2.30C/D341-447[»]
ProteinModelPortaliQ9UL15.
SMRiQ9UL15.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114905. 41 interactors.
DIPiDIP-53428N.
IntActiQ9UL15. 41 interactors.
MINTiMINT-1147557.
STRINGi9606.ENSP00000338814.

PTM databases

iPTMnetiQ9UL15.
PhosphoSitePlusiQ9UL15.

Polymorphism and mutation databases

BioMutaiBAG5.
DMDMi12643895.

Proteomic databases

EPDiQ9UL15.
PaxDbiQ9UL15.
PeptideAtlasiQ9UL15.
PRIDEiQ9UL15.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000299204; ENSP00000299204; ENSG00000166170. [Q9UL15-1]
ENST00000337322; ENSP00000338814; ENSG00000166170. [Q9UL15-2]
ENST00000445922; ENSP00000391713; ENSG00000166170. [Q9UL15-1]
GeneIDi9529.
KEGGihsa:9529.
UCSCiuc001ynh.3. human. [Q9UL15-1]

Organism-specific databases

CTDi9529.
DisGeNETi9529.
GeneCardsiBAG5.
HGNCiHGNC:941. BAG5.
HPAiHPA016429.
MIMi603885. gene.
neXtProtiNX_Q9UL15.
OpenTargetsiENSG00000166170.
PharmGKBiPA25241.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4361. Eukaryota.
ENOG4111WNH. LUCA.
GeneTreeiENSGT00530000063256.
HOGENOMiHOG000070447.
HOVERGENiHBG004810.
InParanoidiQ9UL15.
KOiK09559.
OMAiANHPHRI.
OrthoDBiEOG091G08LY.
PhylomeDBiQ9UL15.
TreeFamiTF102014.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000166170-MONOMER.
ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

EvolutionaryTraceiQ9UL15.
GeneWikiiBAG5.
GenomeRNAii9529.
PROiQ9UL15.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000166170.
CleanExiHS_BAG5.
ExpressionAtlasiQ9UL15. baseline and differential.
GenevisibleiQ9UL15. HS.

Family and domain databases

Gene3Di1.20.58.120. 4 hits.
InterProiIPR003103. BAG_domain.
[Graphical view]
PfamiPF02179. BAG. 4 hits.
[Graphical view]
SMARTiSM00264. BAG. 4 hits.
[Graphical view]
SUPFAMiSSF63491. SSF63491. 4 hits.
PROSITEiPS51035. BAG. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBAG5_HUMAN
AccessioniPrimary (citable) accession number: Q9UL15
Secondary accession number(s): O94950, Q86W59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.