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Protein

BAG family molecular chaperone regulator 1

Gene

BAG1

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

Functioni

Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli.3 Publications

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell surface receptor signaling pathway Source: ProtInc
  • chaperone cofactor-dependent protein refolding Source: UniProtKB
  • negative regulation of apoptotic process Source: ProtInc
  • regulation of cellular response to heat Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

BioCyciZFISH:ENSG00000107262-MONOMER.
ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
BAG family molecular chaperone regulator 1
Short name:
BAG-1
Alternative name(s):
Bcl-2-associated athanogene 1
Gene namesi
Name:BAG1
Synonyms:HAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:937. BAG1.

Subcellular locationi

Isoform 1 :
Isoform 2 :
  • Cytoplasm
  • Nucleus

  • Note: Isoform 2 localizes to the cytoplasm and shuttles into the nucleus in response to heat shock.
Isoform 4 :
  • Cytoplasm
  • Nucleus

  • Note: Isoform 4 localizes predominantly to the cytoplasm. The cellular background in which it is expressed can influence whether it resides primarily in the cytoplasm or is also found in the nucleus. In the presence of BCL2, localizes to intracellular membranes (what appears to be the nuclear envelope and perinuclear membranes) as well as punctate cytosolic structures suggestive of mitochondria.

GO - Cellular componenti

  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi573.
OpenTargetsiENSG00000107262.
PharmGKBiPA25237.

Polymorphism and mutation databases

BioMutaiBAG1.
DMDMi296439462.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000888651 – 345BAG family molecular chaperone regulator 1Add BLAST345

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei223PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation.Curated

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ99933.
MaxQBiQ99933.
PaxDbiQ99933.
PeptideAtlasiQ99933.
PRIDEiQ99933.

PTM databases

iPTMnetiQ99933.
PhosphoSitePlusiQ99933.

Expressioni

Tissue specificityi

Isoform 4 is the most abundantly expressed isoform. It is ubiquitously expressed throughout most tissues, except the liver, colon, breast and uterine myometrium. Isoform 1 is expressed in the ovary and testis. Isoform 4 is expressed in several types of tumor cell lines, and at consistently high levels in leukemia and lymphoma cell lines. Isoform 1 is expressed in the prostate, breast and leukemia cell lines. Isoform 3 is the least abundant isoform in tumor cell lines (at protein level).1 Publication

Inductioni

Up-regulated during differentiation of bladder epithelial cells and down-regulated during differentiation of prostate epithelium.1 Publication

Gene expression databases

BgeeiENSG00000107262.
CleanExiHS_BAG1.
ExpressionAtlasiQ99933. baseline and differential.
GenevisibleiQ99933. HS.

Organism-specific databases

HPAiCAB002486.
HPA018121.

Interactioni

Subunit structurei

Homodimer. Forms a heteromeric complex with HSP70/HSC70. Binds to the ATPase domain of HSP/HSC70 chaperones. Isoform 1, isoform 3 and isoform 4 but not isoform 2 interact with HSPA8/HSC70. Interacts with NR3C1. Interacts with the N-terminal region of STK19. Interacts with PPP1R15A. Interacts with BCL2 in an ATP-dependent manner. Isoform 2 does not interact with BCL2.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q53FC72EBI-1030678,EBI-9356749
Q96BE02EBI-1030678,EBI-9356686
HSPA8P1114210EBI-1030678,EBI-351896
HSPA8Q96IS65EBI-1030678,EBI-10289199
PSMD2Q132005EBI-1030678,EBI-357648
STUB1Q9UNE72EBI-1030678,EBI-357085
TRIM23P364065EBI-1030678,EBI-740098
TRIM27P143733EBI-1030678,EBI-719493

Protein-protein interaction databases

BioGridi107049. 86 interactors.
DIPiDIP-3341N.
IntActiQ99933. 40 interactors.
MINTiMINT-189058.
STRINGi9606.ENSP00000420514.

Structurei

Secondary structure

1345
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi144 – 149Combined sources6
Beta strandi151 – 159Combined sources9
Beta strandi163 – 167Combined sources5
Helixi170 – 180Combined sources11
Turni185 – 187Combined sources3
Beta strandi189 – 192Combined sources4
Beta strandi195 – 197Combined sources3
Beta strandi200 – 203Combined sources4
Helixi204 – 207Combined sources4
Beta strandi211 – 219Combined sources9
Helixi224 – 259Combined sources36
Helixi264 – 272Combined sources9
Helixi275 – 292Combined sources18
Helixi302 – 326Combined sources25

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HX1X-ray1.90B222-334[»]
1WXVNMR-A144-222[»]
3FZFX-ray2.20B222-334[»]
3FZHX-ray2.00B222-334[»]
3FZKX-ray2.10B222-334[»]
3FZLX-ray2.20B222-334[»]
3FZMX-ray2.30B222-334[»]
3LDQX-ray1.90B222-334[»]
3M3ZX-ray2.10B222-334[»]
5AQFX-ray1.88B/D222-334[»]
5AQGX-ray2.24B/D/F222-334[»]
5AQHX-ray2.00B222-334[»]
5AQIX-ray1.98B/D222-334[»]
5AQJX-ray1.96B/D/F222-334[»]
5AQKX-ray2.09B222-334[»]
5AQLX-ray1.69B/D222-334[»]
5AQMX-ray1.63B/D222-334[»]
5AQNX-ray2.45B/D/F222-334[»]
5AQOX-ray2.12B/D/F222-334[»]
5AQPX-ray2.08B/D/F222-334[»]
5AQQX-ray2.72B/D/F222-334[»]
5AQRX-ray1.91B/D/F222-334[»]
5AQSX-ray2.00B/D222-334[»]
5AQTX-ray1.90B222-334[»]
5AQUX-ray1.92B222-334[»]
5AQVX-ray1.75B222-334[»]
ProteinModelPortaliQ99933.
SMRiQ99933.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99933.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati96 – 10116
Repeati102 – 10726
Repeati108 – 11336
Repeati114 – 11946
Repeati120 – 12556
Repeati126 – 13166
Repeati132 – 13776
Domaini144 – 224Ubiquitin-likePROSITE-ProRule annotationAdd BLAST81
Domaini246 – 326BAGPROSITE-ProRule annotationAdd BLAST81

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni96 – 1377 X 6 AA tandem repeat of E-E-X(4)Add BLAST42
Regioni172 – 219Interaction with HSPA8Add BLAST48
Regioni216 – 345Interaction with PPP1R15A1 PublicationAdd BLAST130

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi4 – 82Arg-richAdd BLAST79

Sequence similaritiesi

Contains 1 BAG domain.PROSITE-ProRule annotation
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IHYI. Eukaryota.
ENOG4111SUG. LUCA.
GeneTreeiENSGT00450000040296.
HOVERGENiHBG000236.
InParanoidiQ99933.
KOiK09555.
PhylomeDBiQ99933.

Family and domain databases

Gene3Di1.20.58.120. 1 hit.
InterProiIPR003103. BAG_domain.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF02179. BAG. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00264. BAG. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF63491. SSF63491. 1 hit.
PROSITEiPS51035. BAG. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform 1 (identifier: Q99933-1) [UniParc]FASTAAdd to basket
Also known as: BAG-1L, p50

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
MAQRGGARRP RGDRERLGSR LRALRPGREP RQSEPPAQRG PPPSGRPPAR
60 70 80 90 100
STASGHDRPT RGAAAGARRP RMKKKTRRRS TRSEELTRSE ELTLSEEATW
110 120 130 140 150
SEEATQSEEA TQGEEMNRSQ EVTRDEESTR SEEVTREEMA AAGLTVTVTH
160 170 180 190 200
SNEKHDLHVT SQQGSSEPVV QDLAQVVEEV IGVPQSFQKL IFKGKSLKEM
210 220 230 240 250
ETPLSALGIQ DGCRVMLIGK KNSPQEEVEL KKLKHLEKSV EKIADQLEEL
260 270 280 290 300
NKELTGIQQG FLPKDLQAEA LCKLDRRVKA TIEQFMKILE EIDTLILPEN
310 320 330 340
FKDSRLKRKG LVKKVQAFLA ECDTVEQNIC QETERLQSTN FALAE
Length:345
Mass (Da):38,779
Last modified:May 18, 2010 - v4
Checksum:i8B40EF078C66335F
GO
Isoform 2 (identifier: Q99933-2) [UniParc]FASTAAdd to basket
Also known as: BAG1V, HAPV

The sequence of this isoform differs from the canonical sequence as follows:
     302-345: KDSRLKRKGLVKKVQAFLAECDTVEQNICQETERLQSTNFALAE → PTLTLVLNEK

Note: Produced by alternative splicing.
Show »
Length:311
Mass (Da):34,866
Checksum:i1F94BA55E21694D3
GO
Isoform 3 (identifier: Q99933-3) [UniParc]FASTAAdd to basket
Also known as: BAG-1M, RAP46

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: Missing.

Note: Produced by alternative initiation at Met-72 of isoform 1.
Show »
Length:274
Mass (Da):31,117
Checksum:iC13E200ED63A2CF0
GO
Isoform 4 (identifier: Q99933-4) [UniParc]FASTAAdd to basket
Also known as: BAG-1, p32

The sequence of this isoform differs from the canonical sequence as follows:
     1-115: Missing.

Note: Produced by alternative initiation at Met-116 of isoform 1.
Show »
Length:230
Mass (Da):25,989
Checksum:iD4B34A8F54DE684D
GO

Sequence cautioni

The sequence AAD11467 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAD25045 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD96469 differs from that shown. Unusual initiator. The initiator methionine is coded by a non-canonical CTG leucine codon.Curated
The sequence CAA84624 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAH72516 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAH72518 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAH72741 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAH72742 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAW58515 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti45G → R in AAC34258 (PubMed:8812483).Curated1
Sequence conflicti45G → R in BAD96469 (Ref. 5) Curated1
Sequence conflicti45G → R in AAH01936 (PubMed:15489334).Curated1
Sequence conflicti45G → R in AAH14774 (PubMed:15489334).Curated1
Sequence conflicti79R → F in AAD11467 (PubMed:8812483).Curated1
Sequence conflicti84E → K in AAD11467 (PubMed:8812483).Curated1
Sequence conflicti90E → K in AAD11467 (PubMed:8812483).Curated1
Sequence conflicti245D → N in AAD11467 (PubMed:8812483).Curated1
Sequence conflicti293D → H in AAD11467 (PubMed:8812483).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0383941 – 115Missing in isoform 4. CuratedAdd BLAST115
Alternative sequenceiVSP_0383951 – 71Missing in isoform 3. CuratedAdd BLAST71
Alternative sequenceiVSP_000453302 – 345KDSRL…FALAE → PTLTLVLNEK in isoform 2. 1 PublicationAdd BLAST44

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35491 mRNA. Translation: CAA84624.1. Different initiation.
U46917 mRNA. Translation: AAD11467.1. Different initiation.
AF022224 mRNA. Translation: AAC34258.1.
AF116273 mRNA. Translation: AAD25045.1. Different initiation.
AK222749 mRNA. Translation: BAD96469.1. Different initiation.
AL161445, AL356472 Genomic DNA. Translation: CAH72516.1. Sequence problems.
AL161445, AL356472 Genomic DNA. Translation: CAH72517.1.
AL161445, AL356472 Genomic DNA. Translation: CAH72518.1. Sequence problems.
AL356472, AL161445 Genomic DNA. Translation: CAH72741.1. Sequence problems.
AL356472, AL161445 Genomic DNA. Translation: CAH72742.1. Sequence problems.
AL356472, AL161445 Genomic DNA. Translation: CAH72743.1.
CH471071 Genomic DNA. Translation: EAW58514.1.
CH471071 Genomic DNA. Translation: EAW58515.1. Sequence problems.
BC001936 mRNA. Translation: AAH01936.2.
BC014774 mRNA. Translation: AAH14774.2.
CCDSiCCDS35004.1. [Q99933-1]
CCDS55301.1. [Q99933-4]
RefSeqiNP_001165886.1. NM_001172415.1. [Q99933-4]
NP_004314.5. NM_004323.5.
UniGeneiHs.377484.

Genome annotation databases

EnsembliENST00000379704; ENSP00000369026; ENSG00000107262. [Q99933-4]
GeneIDi573.
KEGGihsa:573.
UCSCiuc064sos.1. human. [Q99933-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35491 mRNA. Translation: CAA84624.1. Different initiation.
U46917 mRNA. Translation: AAD11467.1. Different initiation.
AF022224 mRNA. Translation: AAC34258.1.
AF116273 mRNA. Translation: AAD25045.1. Different initiation.
AK222749 mRNA. Translation: BAD96469.1. Different initiation.
AL161445, AL356472 Genomic DNA. Translation: CAH72516.1. Sequence problems.
AL161445, AL356472 Genomic DNA. Translation: CAH72517.1.
AL161445, AL356472 Genomic DNA. Translation: CAH72518.1. Sequence problems.
AL356472, AL161445 Genomic DNA. Translation: CAH72741.1. Sequence problems.
AL356472, AL161445 Genomic DNA. Translation: CAH72742.1. Sequence problems.
AL356472, AL161445 Genomic DNA. Translation: CAH72743.1.
CH471071 Genomic DNA. Translation: EAW58514.1.
CH471071 Genomic DNA. Translation: EAW58515.1. Sequence problems.
BC001936 mRNA. Translation: AAH01936.2.
BC014774 mRNA. Translation: AAH14774.2.
CCDSiCCDS35004.1. [Q99933-1]
CCDS55301.1. [Q99933-4]
RefSeqiNP_001165886.1. NM_001172415.1. [Q99933-4]
NP_004314.5. NM_004323.5.
UniGeneiHs.377484.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HX1X-ray1.90B222-334[»]
1WXVNMR-A144-222[»]
3FZFX-ray2.20B222-334[»]
3FZHX-ray2.00B222-334[»]
3FZKX-ray2.10B222-334[»]
3FZLX-ray2.20B222-334[»]
3FZMX-ray2.30B222-334[»]
3LDQX-ray1.90B222-334[»]
3M3ZX-ray2.10B222-334[»]
5AQFX-ray1.88B/D222-334[»]
5AQGX-ray2.24B/D/F222-334[»]
5AQHX-ray2.00B222-334[»]
5AQIX-ray1.98B/D222-334[»]
5AQJX-ray1.96B/D/F222-334[»]
5AQKX-ray2.09B222-334[»]
5AQLX-ray1.69B/D222-334[»]
5AQMX-ray1.63B/D222-334[»]
5AQNX-ray2.45B/D/F222-334[»]
5AQOX-ray2.12B/D/F222-334[»]
5AQPX-ray2.08B/D/F222-334[»]
5AQQX-ray2.72B/D/F222-334[»]
5AQRX-ray1.91B/D/F222-334[»]
5AQSX-ray2.00B/D222-334[»]
5AQTX-ray1.90B222-334[»]
5AQUX-ray1.92B222-334[»]
5AQVX-ray1.75B222-334[»]
ProteinModelPortaliQ99933.
SMRiQ99933.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107049. 86 interactors.
DIPiDIP-3341N.
IntActiQ99933. 40 interactors.
MINTiMINT-189058.
STRINGi9606.ENSP00000420514.

PTM databases

iPTMnetiQ99933.
PhosphoSitePlusiQ99933.

Polymorphism and mutation databases

BioMutaiBAG1.
DMDMi296439462.

Proteomic databases

EPDiQ99933.
MaxQBiQ99933.
PaxDbiQ99933.
PeptideAtlasiQ99933.
PRIDEiQ99933.

Protocols and materials databases

DNASUi573.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379704; ENSP00000369026; ENSG00000107262. [Q99933-4]
GeneIDi573.
KEGGihsa:573.
UCSCiuc064sos.1. human. [Q99933-1]

Organism-specific databases

CTDi573.
DisGeNETi573.
GeneCardsiBAG1.
HGNCiHGNC:937. BAG1.
HPAiCAB002486.
HPA018121.
MIMi601497. gene.
neXtProtiNX_Q99933.
OpenTargetsiENSG00000107262.
PharmGKBiPA25237.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IHYI. Eukaryota.
ENOG4111SUG. LUCA.
GeneTreeiENSGT00450000040296.
HOVERGENiHBG000236.
InParanoidiQ99933.
KOiK09555.
PhylomeDBiQ99933.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000107262-MONOMER.
ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

ChiTaRSiBAG1. human.
EvolutionaryTraceiQ99933.
GeneWikiiBAG1.
GenomeRNAii573.
PROiQ99933.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000107262.
CleanExiHS_BAG1.
ExpressionAtlasiQ99933. baseline and differential.
GenevisibleiQ99933. HS.

Family and domain databases

Gene3Di1.20.58.120. 1 hit.
InterProiIPR003103. BAG_domain.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF02179. BAG. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTiSM00264. BAG. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF63491. SSF63491. 1 hit.
PROSITEiPS51035. BAG. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBAG1_HUMAN
AccessioniPrimary (citable) accession number: Q99933
Secondary accession number(s): O75315
, Q14414, Q53H32, Q5VZE8, Q5VZE9, Q5VZF0, Q96TG2, Q9Y2V4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 18, 2010
Last modified: November 30, 2016
This is version 175 of the entry and version 4 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 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.