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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

  1. chaperone binding Source: BHF-UCL
  2. protein kinase binding Source: ParkinsonsUK-UCL
  3. ubiquitin protein ligase binding Source: BHF-UCL

GO - Biological processi

  1. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  2. negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
  3. negative regulation of protein refolding Source: BHF-UCL
  4. negative regulation of protein ubiquitination Source: ParkinsonsUK-UCL
  5. negative regulation of ubiquitin-protein transferase activity Source: BHF-UCL
  6. neuron death Source: BHF-UCL
  7. protein folding Source: ProtInc
  8. regulation of inclusion body assembly Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

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
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:941. BAG5.

Subcellular locationi

GO - Cellular componenti

  1. inclusion body Source: BHF-UCL
  2. membrane Source: UniProtKB
  3. mitochondrion Source: ParkinsonsUK-UCL
  4. nucleus Source: UniProtKB
  5. perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25241.

Polymorphism and mutation databases

BioMutaiBAG5.
DMDMi12643895.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447BAG family molecular chaperone regulator 5PRO_0000088872Add
BLAST

Proteomic databases

MaxQBiQ9UL15.
PaxDbiQ9UL15.
PRIDEiQ9UL15.

PTM databases

PhosphoSiteiQ9UL15.

Expressioni

Gene expression databases

BgeeiQ9UL15.
CleanExiHS_BAG5.
ExpressionAtlasiQ9UL15. baseline and differential.
GenevestigatoriQ9UL15.

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
MAD1L1Q9Y6D94EBI-356517,EBI-742610
THAP1Q9NVV93EBI-356517,EBI-741515
TRIM27P143733EBI-356517,EBI-719493

Protein-protein interaction databases

BioGridi114905. 27 interactions.
DIPiDIP-53428N.
IntActiQ9UL15. 25 interactions.
MINTiMINT-1147557.
STRINGi9606.ENSP00000338814.

Structurei

Secondary structure

1
447
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi277 – 29519Combined sources
Turni299 – 3013Combined sources
Helixi302 – 31716Combined sources
Helixi318 – 3203Combined sources
Helixi326 – 35025Combined sources
Turni356 – 3583Combined sources
Helixi364 – 38421Combined sources
Helixi393 – 41018Combined sources
Helixi418 – 44225Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9DNMR-A275-350[»]
3A8YX-ray2.30C/D341-447[»]
ProteinModelPortaliQ9UL15.
SMRiQ9UL15. Positions 1-89, 276-447.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UL15.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 8678BAG 1PROSITE-ProRule annotationAdd
BLAST
Domaini95 – 16773BAG 2PROSITE-ProRule annotationAdd
BLAST
Domaini182 – 26079BAG 3PROSITE-ProRule annotationAdd
BLAST
Domaini275 – 35076BAG 4PROSITE-ProRule annotationAdd
BLAST
Domaini365 – 44278BAG 5PROSITE-ProRule annotationAdd
BLAST

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

eggNOGiNOG262724.
GeneTreeiENSGT00530000063256.
HOGENOMiHOG000070447.
HOVERGENiHBG004810.
InParanoidiQ9UL15.
KOiK09559.
OMAiDMGNQHP.
OrthoDBiEOG7WX08F.
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]
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 BAA74896.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti157 – 1571C → W.1 Publication
Corresponds to variant rs17854644 [ dbSNP | Ensembl ].
VAR_058712

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MRFHWLPTLSEPFDRNQELE TCIRPLWTPSGSACETEHNK SM in isoform 2. 1 PublicationVSP_037996

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.2. human. [Q9UL15-2]
uc001yni.2. human. [Q9UL15-1]

Polymorphism and mutation databases

BioMutaiBAG5.

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9DNMR-A275-350[»]
3A8YX-ray2.30C/D341-447[»]
ProteinModelPortaliQ9UL15.
SMRiQ9UL15. Positions 1-89, 276-447.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114905. 27 interactions.
DIPiDIP-53428N.
IntActiQ9UL15. 25 interactions.
MINTiMINT-1147557.
STRINGi9606.ENSP00000338814.

PTM databases

PhosphoSiteiQ9UL15.

Polymorphism and mutation databases

BioMutaiBAG5.
DMDMi12643895.

Proteomic databases

MaxQBiQ9UL15.
PaxDbiQ9UL15.
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.2. human. [Q9UL15-2]
uc001yni.2. human. [Q9UL15-1]

Organism-specific databases

CTDi9529.
GeneCardsiGC14M104022.
HGNCiHGNC:941. BAG5.
HPAiHPA016429.
MIMi603885. gene.
neXtProtiNX_Q9UL15.
PharmGKBiPA25241.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG262724.
GeneTreeiENSGT00530000063256.
HOGENOMiHOG000070447.
HOVERGENiHBG004810.
InParanoidiQ9UL15.
KOiK09559.
OMAiDMGNQHP.
OrthoDBiEOG7WX08F.
PhylomeDBiQ9UL15.
TreeFamiTF102014.

Miscellaneous databases

EvolutionaryTraceiQ9UL15.
GeneWikiiBAG5.
GenomeRNAii9529.
NextBioi35720.
PROiQ9UL15.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UL15.
CleanExiHS_BAG5.
ExpressionAtlasiQ9UL15. baseline and differential.
GenevestigatoriQ9UL15.

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]
PROSITEiPS51035. BAG. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT TRP-157.
    Tissue: Brain.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy."
    Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.
    Nature 504:291-295(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARK2.
  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] [Europe PMC] [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.

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: April 29, 2015
This is version 124 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

External Data

Dasty 3

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 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.