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Protein Page:
BAG1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
BAG1 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. 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. Up-regulated during differentiation of bladder epithelial cells and down-regulated during differentiation of prostate epithelium. 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. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Nuclear receptor co-regulator
Chromosomal Location of Human Ortholog: 9p12
Cellular Component: cytoplasm; nucleus
Molecular Function: protein binding; chaperone binding; receptor signaling protein activity
Biological Process: cell surface receptor linked signal transduction; apoptosis; negative regulation of apoptosis
Reference #:  Q99933 (UniProtKB)
Alt. Names/Synonyms: BAG family molecular chaperone regulator 1; BAG-1; BAG1; Bcl-2 associating athanogene-1 protein; Bcl-2-associated athanogene 1; Bcl-2-binding protein; BCL2-associated athanogene; glucocortoid receptor-associated protein RAP46; HAP; RAP46; receptor-associated protein, 46-KD
Gene Symbols: BAG1
Molecular weight: 38,779 Da
Basal Isoelectric point: 7.68  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

BAG1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S80-p KKKTRRRsTRsEELT
0 1 S83-p TRRRsTRsEELTRSE
0 1 S89 RsEELTRSEELTLSE
0 1 T93 LTRSEELTLSEEATW
0 1 S95 RSEELTLSEEATWSE
0 1 S119-p QGEEMNRsQEVTRDE
0 1 T145 EMAAAGLTVTVTHSN
0 4 S196-p KLIFKGKsLKEMEtP
0 1 T202-p KsLKEMEtPLSALGI
0 3 S223-p MLIGKKNsPQEEVEL
0 1 K252-ub DQLEELNkELTGIQQ
0 38 K273-ub LQAEALCkLDRRVKA
  mouse

 
S80 KKKVRPRSSQSEKVG
S83 VRPRSSQSEKVGSSS
S96-p SSRELTRsKKVtRsK
T100-p LTRsKKVtRsKNVTG
S102-p RsKKVtRsKNVTGTQ
A128 QTEEVTVAEEVTQTD
S155-p EMETPRLsVIVTHSN
S206 KLIFKGKSLKEMETP
T212 KSLKEMETPLSALGM
N233 MLIGEKSNPEEEVEL
K262 NHLQELNKELSGIQQ
K283-ub LQAEALCkLDRKVKA
  rat

 
S80 KKKVRPRSSQSEKVA
S83 VRPRSSQSEKVAHSK
S95 HSKELTRSKKLTRSK
T99 LTRSKKLTRSKKVTG
S101 RSKKLTRSKKVTGTQ
- under review  
S158 EMEPPTLSVVVTHSN
S209 KLIFKGKSLKEMETP
T215 KSLKEMETPLSALGM
N236 MLIGEKSNPEEEAEL
K265 NHLEELNKELSDIQQ
R286 LQAEALCRLDRKIKA
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