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UniProtKB - Q9Z1R2 (BAG6_MOUSE)

UniProt

Q9Z1R2 - BAG6_MOUSE

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Protein

Large proline-rich protein BAG6

Gene

Bag6

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

Functioni

Chaperone that plays a key role in various processes such as apoptosis, insertion of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane and regulation of chromatin. Key component of the BAG6/BAT3 complex, a cytosolic multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. BAG6/BAT3 acts by facilitating TA membrane proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins and transfers them to ASNA1/TRC40 for targeting to the endoplasmic reticulum membrane. Moreover, it regulates the stability and the degradation of proteins by the proteasome. For instance, it is required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, may play a role in immuno-proteasomes to generate antigenic peptides via targeted degradation, thereby playing a role in antigen presentation in immune response. It is also involved in ubiquitin-mediated proteasomal degradation of proteins of the secretory pathway that are mislocalized to the cytosol. Binds the mislocalized proteins, preventing their aggregation in the cytosol, and promotes their ubiquitination. Participates in endoplasmic reticulum stress-induced apoptosis via its interaction with AIFM1/AIF by regulating AIFM1/AIF stability and preventing its degradation. Also required during spermatogenesis for synaptonemal complex assembly via its interaction with HSPA2, by inhibiting polyubiquitination and subsequent proteasomal degradation of HSPA2.By similarity3 Publications
Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2).By similarity
Can be released from tumor and dendritic cells in membrane vesicles or exosomes, and engage NCR3 thereby promoting natural killer cells (NK) activation and cytotoxicity.By similarity

GO - Molecular functioni

  • Hsp70 protein binding Source: UniProtKB
  • misfolded protein binding Source: MGI
  • polyubiquitin binding Source: UniProtKB
  • proteasome binding Source: UniProtKB
  • ribosome binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: MGI
  • ubiquitin-specific protease binding Source: MGI

GO - Biological processi

  • antigen processing and presentation of peptide antigen via MHC class I Source: UniProtKB
  • brain development Source: UniProtKB
  • cell differentiation Source: UniProtKB-KW
  • chromatin modification Source: UniProtKB-KW
  • embryo development Source: UniProtKB
  • internal peptidyl-lysine acetylation Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
  • kidney development Source: UniProtKB
  • lung development Source: UniProtKB
  • maintenance of unfolded protein involved in ERAD pathway Source: MGI
  • negative regulation of apoptotic process Source: MGI
  • negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
  • negative regulation of proteolysis Source: UniProtKB
  • positive regulation of ERAD pathway Source: MGI
  • protein stabilization Source: UniProtKB
  • regulation of apoptotic process Source: UniProtKB
  • regulation of cell proliferation Source: Ensembl
  • spermatogenesis Source: UniProtKB
  • synaptonemal complex assembly Source: UniProtKB
  • tail-anchored membrane protein insertion into ER membrane Source: UniProtKB
  • transport Source: UniProtKB-KW
  • ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Chromatin regulator

Keywords - Biological processi

Apoptosis, Differentiation, Immunity, Spermatogenesis, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Large proline-rich protein BAG6
Alternative name(s):
BAG family molecular chaperone regulator 6
BCL2-associated athanogene 6
Short name:
BAG-6
Short name:
BAG6
HLA-B-associated transcript 3
Protein Scythe
Gene namesi
Name:Bag6
Synonyms:Bat3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1919439. Bag6.

Subcellular locationi

  • Cytoplasm › cytosol 1 Publication
  • Nucleus By similarity

    • Note: The C-terminal fragment generated by caspase-3 is cytoplasmic. Also found in extracellular vesicular exosomes in some tumor cells (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Lethality associated with pronounced developmental defects in the lung, kidney and brain. Lethality is either embryonic consecutive to abnormal brain development or perinatal associated with pronounced developmental defects in the lung and kidney. These developmental defects were associated with widespread aberrant apoptosis and proliferation. Lethality can be partially rescued in an ICR genetic background: mice are slightly smaller in size than their wild-type counterparts and show impaired genotoxic stress responses.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11541154Large proline-rich protein BAG6PRO_0000114898Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei96 – 961PhosphoserineBy similarity
Modified residuei117 – 1171PhosphothreonineBy similarity
Modified residuei986 – 9861PhosphoserineBy similarity
Modified residuei995 – 9951PhosphoserineCombined sources
Modified residuei1075 – 10751PhosphothreonineBy similarity
Modified residuei1103 – 11031PhosphoserineBy similarity
Modified residuei1139 – 11391PhosphoserineBy similarity

Post-translational modificationi

Cleavage by caspase-3 releases a C-terminal peptide that plays a role in ricin-induced apoptosis.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1023 – 10242Cleavage; by caspase-3By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9Z1R2.
MaxQBiQ9Z1R2.
PaxDbiQ9Z1R2.
PRIDEiQ9Z1R2.

PTM databases

iPTMnetiQ9Z1R2.
PhosphoSiteiQ9Z1R2.

Expressioni

Gene expression databases

BgeeiENSMUSG00000024392.
CleanExiMM_BAT3.
ExpressionAtlasiQ9Z1R2. baseline and differential.
GenevisibleiQ9Z1R2. MM.

Interactioni

Subunit structurei

Component of the BAT3 complex, at least composed of BAG6/BAT3, UBL4A and GET4/TRC35. Interacts with AIFM1, CTCFL, HSPA2 and p300/EP300. Interacts with ricin A chain. Interacts with NCR3. Interacts (via ubiquitin-like domain) with RNF126; required for BAG6-dependent ubiquitination of proteins mislocalized to the cytosol.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Camk2aP11798-23EBI-644645,EBI-400402
Tnfrsf11aO353054EBI-644645,EBI-647362

GO - Molecular functioni

  • Hsp70 protein binding Source: UniProtKB
  • misfolded protein binding Source: MGI
  • polyubiquitin binding Source: UniProtKB
  • proteasome binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: MGI
  • ubiquitin-specific protease binding Source: MGI

Protein-protein interaction databases

BioGridi230309. 4 interactions.
DIPiDIP-49391N.
IntActiQ9Z1R2. 7 interactions.
MINTiMINT-1563095.
STRINGi10090.ENSMUSP00000025250.

Structurei

3D structure databases

ProteinModelPortaliQ9Z1R2.
SMRiQ9Z1R2. Positions 13-87, 1079-1134.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 9276Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST
Repeati237 – 271351Add
BLAST
Repeati416 – 444292Add
BLAST
Repeati597 – 624283Add
BLAST
Repeati630 – 658294Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni237 – 6584224 X 29 AA approximate repeatsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi196 – 27479Pro-richAdd
BLAST
Compositional biasi395 – 720326Pro-richAdd
BLAST
Compositional biasi564 – 61047Ala-richAdd
BLAST

Sequence similaritiesi

Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG4248. Eukaryota.
ENOG410XS9P. LUCA.
GeneTreeiENSGT00390000016199.
HOVERGENiHBG002193.
InParanoidiQ9Z1R2.
OMAiPMWSSRR.
OrthoDBiEOG091G0XSR.
PhylomeDBiQ9Z1R2.
TreeFamiTF328437.

Family and domain databases

InterProiIPR021925. DUF3538.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF12057. DUF3538. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z1R2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPSDSASTA MEEPDSLEVL VKTLDSQTRT FIVGAQMNVK EFKEHIAASV 
        60         70         80         90        100
SIPSEKQRLI YQGRVLQDDK KLQEYNVGGK VIHLVERAPP QTQLPSGASS 
       110        120        130        140        150
GTGSASATHG GAPLPGTRGP GASVHDRNAN SYVMVGTFNL PSDGSAVDVH 
       160        170        180        190        200
INMEQAPIQS EPRVRLVMAQ HMIRDIQTLL SRMECRGGTQ AQASQPPPQT 
       210        220        230        240        250
PQTVASETVA LNSQTSEPVE SEAPPREPME SEEMEERPPT QTPELAPSGP 
       260        270        280        290        300
APAGPAPAGP APAPETNAPN HPSPAEHVEV LQELQRLQRR LQPFLQRYCE 
       310        320        330        340        350
VLGAAATTDY NNNHEGREED QRLINLVGES LRLLGNTFVA LSDLRCNLAC 
       360        370        380        390        400
APPRHLHVVR PMSHYTTPMV LQQAAIPIQI NVGTTVTMTG NGARPPPAPG 
       410        420        430        440        450
AEAATPGSAQ ATSLPPSSTT VDSSTEGAPP PGPAPPPASS HPRVIRISHQ 
       460        470        480        490        500
SVEPVVMMHM NIQDSGAQPG GVPSAPTGPL GPPGHGQTLG QQVPGFPTAP 
       510        520        530        540        550
TRVVIARPTP PQARPSHPGG PPVSGALQGA GLGTNTSLAQ MVSGLVGQLL 
       560        570        580        590        600
MQPVLVAQGT PGMAQAQAQA QAQAQAQAQA PAPAPAPAPA PATASASAGT 
       610        620        630        640        650
TNTATTAGPA PGGPAQPPPP QPSAADLQFS QLLGNLLGPA GPGAGGPGMA 
       660        670        680        690        700
SPTITVAMPG VPAFLQGMTD FLQASQTAPP PPPPPPPPPP APEQQSTPPP 
       710        720        730        740        750
GSPSGGTASP GGLGPESLPP EFFTSVVQGV LSSLLGSLGA RAGSSESIAA 
       760        770        780        790        800
FIQRLSGSSN IFEPGADGAL GFFGALLSLL CQNFSMVDVV MLLHGHFQPL 
       810        820        830        840        850
QRLQPQLRSF FHQHYLGGQE PTPSNIRMAT HTLITGLEEY VRESFSLVQV 
       860        870        880        890        900
QPGVDIIRTN LEFLQEQFNS IAAHVLHCTD SGFGARLLEL CNQGLFECLA 
       910        920        930        940        950
LNLHCLGGQQ MELAAVINGR IRRMSRGVNP SLVSWLTTMM GLRLQVVLEH 
       960        970        980        990       1000
MPVGPDAILR YVRRVGDPPQ TLPEEPMEVQ GAERTSPEPQ RENASPAPGT 
      1010       1020       1030       1040       1050
TAEEAMSRGP PPAPEGGSRD EQDGASADAE PWAAAVPPEW VPIIQQDIQS 
      1060       1070       1080       1090       1100
QRKVKPQPPL SDAYLSGMPA KRRKTMQGEG PQLLLSEAVS RAAKAAGARP 
      1110       1120       1130       1140       1150
LTSPESLSRD LEAPEVQESY RQQLRSDIQK RLQEDPNYSP QRFPNAHRAF 

ADDP
Length:1,154
Mass (Da):121,037
Last modified:May 1, 1999 - v1
Checksum:i7F3FD14DF5AC1211
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti528 – 5281Missing in AAH26647 (PubMed:15489334).Curated
Sequence conflicti1012 – 10121P → S in AAH26647 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF109719 Genomic DNA. Translation: AAC82479.1.
CR974444 Genomic DNA. No translation available.
BC026647 mRNA. Translation: AAH26647.1.
CCDSiCCDS28688.1.
RefSeqiNP_476512.1. NM_057171.2.
UniGeneiMm.203962.

Genome annotation databases

EnsembliENSMUST00000025250; ENSMUSP00000025250; ENSMUSG00000024392.
GeneIDi224727.
KEGGimmu:224727.
UCSCiuc008cgb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF109719 Genomic DNA. Translation: AAC82479.1.
CR974444 Genomic DNA. No translation available.
BC026647 mRNA. Translation: AAH26647.1.
CCDSiCCDS28688.1.
RefSeqiNP_476512.1. NM_057171.2.
UniGeneiMm.203962.

3D structure databases

ProteinModelPortaliQ9Z1R2.
SMRiQ9Z1R2. Positions 13-87, 1079-1134.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230309. 4 interactions.
DIPiDIP-49391N.
IntActiQ9Z1R2. 7 interactions.
MINTiMINT-1563095.
STRINGi10090.ENSMUSP00000025250.

PTM databases

iPTMnetiQ9Z1R2.
PhosphoSiteiQ9Z1R2.

Proteomic databases

EPDiQ9Z1R2.
MaxQBiQ9Z1R2.
PaxDbiQ9Z1R2.
PRIDEiQ9Z1R2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025250; ENSMUSP00000025250; ENSMUSG00000024392.
GeneIDi224727.
KEGGimmu:224727.
UCSCiuc008cgb.2. mouse.

Organism-specific databases

CTDi7917.
MGIiMGI:1919439. Bag6.

Phylogenomic databases

eggNOGiKOG4248. Eukaryota.
ENOG410XS9P. LUCA.
GeneTreeiENSGT00390000016199.
HOVERGENiHBG002193.
InParanoidiQ9Z1R2.
OMAiPMWSSRR.
OrthoDBiEOG091G0XSR.
PhylomeDBiQ9Z1R2.
TreeFamiTF328437.

Miscellaneous databases

PROiQ9Z1R2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024392.
CleanExiMM_BAT3.
ExpressionAtlasiQ9Z1R2. baseline and differential.
GenevisibleiQ9Z1R2. MM.

Family and domain databases

InterProiIPR021925. DUF3538.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF12057. DUF3538. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBAG6_MOUSE
AccessioniPrimary (citable) accession number: Q9Z1R2
Secondary accession number(s): Q8SNA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: May 1, 1999
Last modified: September 7, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.