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Protein

BAG family molecular chaperone regulator 3

Gene

Bag3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70. Has anti-apoptotic activity. Plays a role in the HSF1 nucleocytoplasmic transport.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone
Biological processApoptosis

Enzyme and pathway databases

ReactomeiR-MMU-3371453. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
BAG family molecular chaperone regulator 3
Short name:
BAG-3
Alternative name(s):
Bcl-2-associated athanogene 3
Bcl-2-binding protein Bis
Gene namesi
Name:Bag3
Synonyms:Bis
ORF Names:MNCb-2243
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1352493. Bag3.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Colocalizes with HSF1 to the nucleus upon heat stress.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: MGI
  • neuron projection Source: Ensembl
  • nucleus Source: UniProtKB
  • plasma membrane Source: MGI
  • Z disc Source: MGI

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000888692 – 577BAG family molecular chaperone regulator 3Add BLAST576

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei138PhosphoserineCombined sources1
Modified residuei141Omega-N-methylarginineCombined sources1
Modified residuei179PhosphoserineBy similarity1
Modified residuei204PhosphoserineBy similarity1
Modified residuei267Omega-N-methylarginineCombined sources1
Modified residuei280PhosphoserineBy similarity1
Modified residuei281PhosphoserineBy similarity1
Modified residuei285PhosphoserineBy similarity1
Modified residuei291PhosphothreonineCombined sources1
Modified residuei297PhosphoserineCombined sources1
Modified residuei380PhosphoserineCombined sources1
Modified residuei382PhosphoserineCombined sources1
Modified residuei390PhosphoserineCombined sources1
Cross-linki450Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9JLV1.
PaxDbiQ9JLV1.
PRIDEiQ9JLV1.

PTM databases

iPTMnetiQ9JLV1.
PhosphoSitePlusiQ9JLV1.
SwissPalmiQ9JLV1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000030847.
CleanExiMM_BAG3.
GenevisibleiQ9JLV1. MM.

Interactioni

Subunit structurei

Binds to the ATPase domain of HSP70/HSC70 chaperones. Interacts with BCL2. Interacts with phospholipase C-gamma proteins. Interacts with DNAJB6. Interacts (via BAG domain) with HSF1; this interaction occurs in normal and heat-shocked cells. Interacts with HSPA8 (via NBD), HSPA1A (via NBD) and HSPA1B (via NBD). Interacts (via WW domain 1) with SYNPO2 (via PPPY motif).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
EBNA-LPQ8AZK72EBI-309231,EBI-1185167From Epstein-Barr virus (strain B95-8).

GO - Molecular functioni

  • cadherin binding Source: MGI
  • chaperone binding Source: InterPro
  • protein complex binding Source: MGI

Protein-protein interaction databases

BioGridi205891. 6 interactors.
IntActiQ9JLV1. 6 interactors.
MINTiMINT-4124913.
STRINGi10090.ENSMUSP00000033136.

Structurei

Secondary structure

1577
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi417 – 420Combined sources4
Helixi425 – 445Combined sources21
Beta strandi451 – 453Combined sources3
Helixi454 – 471Combined sources18
Helixi479 – 503Combined sources25

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UK5NMR-A406-503[»]
ProteinModelPortaliQ9JLV1.
SMRiQ9JLV1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JLV1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 56WW 1PROSITE-ProRule annotationAdd BLAST35
Domaini126 – 157WW 2PROSITE-ProRule annotationAdd BLAST32
Domaini426 – 503BAGPROSITE-ProRule annotationAdd BLAST78

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi186 – 193Poly-Ser8

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0940. Eukaryota.
KOG4361. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00530000063256.
HOGENOMiHOG000050234.
HOVERGENiHBG003419.
InParanoidiQ9JLV1.
KOiK09557.
OMAiVYPQLRP.
OrthoDBiEOG091G08LY.
TreeFamiTF102013.

Family and domain databases

Gene3Di1.20.58.120. 1 hit.
InterProiView protein in InterPro
IPR003103. BAG_domain.
IPR001202. WW_dom.
PfamiView protein in Pfam
PF02179. BAG. 1 hit.
PF00397. WW. 1 hit.
SMARTiView protein in SMART
SM00264. BAG. 1 hit.
SM00456. WW. 1 hit.
SUPFAMiSSF51045. SSF51045. 1 hit.
SSF63491. SSF63491. 1 hit.
PROSITEiView protein in PROSITE
PS51035. BAG. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JLV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAATQSPMM QMASGNGASD RDPLPPGWEI KIDPQTGWPF FVDHNSRTTT
60 70 80 90 100
WNDPRVPPEG PKDTASSANG PSRDGSRLLP IREGHPIYPQ LRPGYIPIPV
110 120 130 140 150
LHEGSENRQP HLFHAYSQPG VQRFRTEAAA ATPQRSQSPL RGGMTEAAQT
160 170 180 190 200
DKQCGQMPAT ATTAAAQPPT AHGPERSQSP AASDCSSSSS SASLPSSGRS
210 220 230 240 250
SLGSHQLPRG YIPIPVIHEQ NITRPAAQPS FHQAQKTHYP AQQGEYQPQQ
260 270 280 290 300
PVYHKIQGDD WEPRPLRAAS PFRSPVRGAS SREGSPARSG TPVHCPSPIR
310 320 330 340 350
VHTVVDRPQP MTHREPPPVT QPENKPESKP GPAGPDLPPG HIPIQVIRRE
360 370 380 390 400
ADSKPVSQKS PPPAEKVEVK VSSAPIPCPS PSPAPSAVPS PPKNVAAEQK
410 420 430 440 450
AAPSPAPAEP AAPKSGEAET PPKHPGVLKV EAILEKVQGL EQAVDSFEGK
460 470 480 490 500
KTDKKYLMIE EYLTKELLAL DSVDPEGRAD VRQARRDGVR KVQTILEKLE
510 520 530 540 550
QKAIDVPGQV QVYELQPSNL EAEQPLQEIM GAVVADKDKK GPENKDPQTE
560 570
SQQLEAKAAT PPNPSNPADS AGNLVAP
Length:577
Mass (Da):61,860
Last modified:July 27, 2011 - v2
Checksum:i7BBF296A4A2EF7E3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74D → N in AAF26840 (PubMed:10597216).Curated1
Sequence conflicti527Q → P in AAF26840 (PubMed:10597216).Curated1
Sequence conflicti539K → E in BAA95066 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130471 mRNA. Translation: AAF26840.1.
AB041583 mRNA. Translation: BAA95066.1.
AK007414 mRNA. Translation: BAB25024.1.
AK016510 mRNA. Translation: BAB30278.1.
AK036675 mRNA. Translation: BAC29531.1.
CH466531 Genomic DNA. Translation: EDL17651.1.
CCDSiCCDS21898.1.
RefSeqiNP_038891.4. NM_013863.5.
UniGeneiMm.84073.

Genome annotation databases

EnsembliENSMUST00000033136; ENSMUSP00000033136; ENSMUSG00000030847.
GeneIDi29810.
KEGGimmu:29810.
UCSCiuc009jzb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF130471 mRNA. Translation: AAF26840.1.
AB041583 mRNA. Translation: BAA95066.1.
AK007414 mRNA. Translation: BAB25024.1.
AK016510 mRNA. Translation: BAB30278.1.
AK036675 mRNA. Translation: BAC29531.1.
CH466531 Genomic DNA. Translation: EDL17651.1.
CCDSiCCDS21898.1.
RefSeqiNP_038891.4. NM_013863.5.
UniGeneiMm.84073.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UK5NMR-A406-503[»]
ProteinModelPortaliQ9JLV1.
SMRiQ9JLV1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205891. 6 interactors.
IntActiQ9JLV1. 6 interactors.
MINTiMINT-4124913.
STRINGi10090.ENSMUSP00000033136.

PTM databases

iPTMnetiQ9JLV1.
PhosphoSitePlusiQ9JLV1.
SwissPalmiQ9JLV1.

Proteomic databases

MaxQBiQ9JLV1.
PaxDbiQ9JLV1.
PRIDEiQ9JLV1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033136; ENSMUSP00000033136; ENSMUSG00000030847.
GeneIDi29810.
KEGGimmu:29810.
UCSCiuc009jzb.2. mouse.

Organism-specific databases

CTDi9531.
MGIiMGI:1352493. Bag3.

Phylogenomic databases

eggNOGiKOG0940. Eukaryota.
KOG4361. Eukaryota.
COG5021. LUCA.
GeneTreeiENSGT00530000063256.
HOGENOMiHOG000050234.
HOVERGENiHBG003419.
InParanoidiQ9JLV1.
KOiK09557.
OMAiVYPQLRP.
OrthoDBiEOG091G08LY.
TreeFamiTF102013.

Enzyme and pathway databases

ReactomeiR-MMU-3371453. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

EvolutionaryTraceiQ9JLV1.
PROiPR:Q9JLV1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030847.
CleanExiMM_BAG3.
GenevisibleiQ9JLV1. MM.

Family and domain databases

Gene3Di1.20.58.120. 1 hit.
InterProiView protein in InterPro
IPR003103. BAG_domain.
IPR001202. WW_dom.
PfamiView protein in Pfam
PF02179. BAG. 1 hit.
PF00397. WW. 1 hit.
SMARTiView protein in SMART
SM00264. BAG. 1 hit.
SM00456. WW. 1 hit.
SUPFAMiSSF51045. SSF51045. 1 hit.
SSF63491. SSF63491. 1 hit.
PROSITEiView protein in PROSITE
PS51035. BAG. 1 hit.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiBAG3_MOUSE
AccessioniPrimary (citable) accession number: Q9JLV1
Secondary accession number(s): Q9CQL3, Q9JJC7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: July 27, 2011
Last modified: May 10, 2017
This is version 143 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.