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Protein Page:
GRP58 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
GRP58 a protein disulfide isomerase found in the endoplasmic reticulum lumen. Catalyzes the rearrangement of both intrachain and interchain disulfide bonds in proteins to form the native structures. An essential component of the peptide-loading complex of the major histocompatibility complex class I pathway. Note: This description may include information from UniProtKB.
Protein type: EC 5.3.4.1; Endoplasmic reticulum; Phospholipase; Chaperone; Isomerase; Protease; Apoptosis
Cellular Component: cell surface; endoplasmic reticulum; endoplasmic reticulum lumen; melanosome
Molecular Function: protein binding; cysteine-type endopeptidase activity; protein disulfide isomerase activity; protein disulfide oxidoreductase activity; phospholipase C activity
Biological Process: antigen processing and presentation of peptide antigen via MHC class I; cellular protein metabolic process; protein folding; protein import into nucleus; cell redox homeostasis; antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; antigen processing and presentation of exogenous peptide antigen via MHC class I; protein amino acid N-linked glycosylation via asparagine; signal transduction; post-translational protein modification; protein retention in ER; glycerol ether metabolic process
Reference #:  P30101 (UniProtKB)
Alt. Names/Synonyms: 58 kDa glucose-regulated protein; 58 kDa microsomal protein; Disulfide isomerase ER-60; endoplasmic reticulum P58; Endoplasmic reticulum resident protein 57; Endoplasmic reticulum resident protein 60; ER protein 57; ER protein 60; ER60; ERP57; ERP60; ERp61; glucose regulated protein, 58kDa; GRP57; GRP58; HsT17083; p58; PDIA3; phospholipase C-alpha; PI-PLC; protein disulfide isomerase family A, member 3; protein disulfide isomerase-associated 3; Protein disulfide-isomerase A3
Gene Symbols: PDIA3
Molecular weight: 56,782 Da
Basal Isoelectric point: 5.98  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

GRP58

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 2 K61-m1 APWCGHCkRLAPEyE
0 14 Y67-p CkRLAPEyEAAATRL
0 3 K94-a ANTNTCNkYGVSGYP
0 1 K94-u ANTNTCNkYGVSGYP
0 1 T102-ga YGVSGYPtLkIFRDG
0 20 K104-a VSGYPtLkIFRDGEE
0 2 K104-u VSGYPtLkIFRDGEE
0 2 Y115-p DGEEAGAyDGPRTAD
0 12 K129 DGIVSHLKKQAGPAS
0 2 T141-p PASVPLRtEEEFKKF
0 3 K146 LRtEEEFKKFISDKD
1 1 S150 EEFKKFISDKDASIV
0 1 K152 FKKFISDKDASIVGF
0 1 K173 EAHSEFLKAASNLRD
0 1 T223-p EDKTVAYtEQkMTSG
0 1 K226-a TVAYtEQkMTSGKIK
0 1 K274 VDYEKNAKGSNYWRN
0 1 K296-u KFLDAGHkLNFAVAS
0 2 K305-u NFAVASRkTFSHELS
0 1 T306 FAVASRkTFSHELSD
0 1 R329 EIPVVAIRTAKGEkF
0 2 K335-u IRTAKGEkFVMQEEF
1 1 S343 FVMQEEFSRDGKALE
0 31 K362-a DYFDGNLkRYLKSEP
0 2 K362-u DYFDGNLkRYLKSEP
0 1 R363 YFDGNLkRYLKSEPI
0 2 K425-u ELGEKLSkDPNIVIA
1 0 Y445 ANDVPSPYEVRGFPt
0 1 T452-ga YEVRGFPtIYFsPAN
1 0 Y454 VRGFPtIYFsPANKK
0 1 S456-ga GFPtIYFsPANKKLN
0 1 K460 IYFsPANKKLNPKKY
1 0 Y467 KKLNPKKYEGGRELS
0 1 T485-ga SYLQREAtNPPVIQE
  mouse

 
K61 APWCGHCKRLAPEYE
Y67 CKRLAPEYEAAATRL
K94 ANTNTCNKYGVSGYP
K94 ANTNTCNKYGVSGYP
T102 YGVSGYPTLkIFRDG
K104-a VSGYPTLkIFRDGEE
K104-u VSGYPTLkIFRDGEE
Y115 DGEEAGAYDGPRTAD
K129-a DGIVSHLkKQAGPAS
T141 PASVPLRTEEEFkKF
K146-a LRTEEEFkKFISDkD
S150 EEFkKFISDkDASVV
K152-u FkKFISDkDASVVGF
K173-u DGHSEFLkAASNLRD
T223 EDKTVAYTEKKMTSG
K226 TVAYTEKKMTSGKIK
K274-u VDYEKNAkGSNYWRN
K296 KFLDAGHKLNFAVAS
K305-u NFAVASRktFSHELS
T306-p FAVASRktFSHELSD
R329 EVPVVAIRTAKGEkF
K335-u IRTAKGEkFVMQEEF
S343 FVMQEEFSRDGKALE
K362-a EYFDGNLkRYLKSEP
K362-u EYFDGNLkRYLKSEP
R363 YFDGNLkRYLKSEPI
K425-u ELGEKLSkDPNIVIA
Y445 ANDVPSPYEVKGFPT
T452 YEVKGFPTIYFSPAN
Y454 VKGFPTIYFSPANkK
S456 GFPTIYFSPANkKLT
K460-u IYFSPANkKLTPKKY
Y467 kKLTPKKYEGGRELN
T485 SYLQREATNPPIIQE
  rat

 
K61 APWCGHCKRLAPEYE
Y67 CKRLAPEYEAAATRL
K94 ANTNTCNKYGVSGYP
K94 ANTNTCNKYGVSGYP
T102 YGVSGYPTLKIFRDG
K104 VSGYPTLKIFRDGEE
K104 VSGYPTLKIFRDGEE
Y115 DGEEAGAYDGPRTAD
K129 DGIVSHLKKQAGPAS
T141 PASVPLRTEDEFKKF
K146 LRTEDEFKKFIsDKD
S150-p DEFKKFIsDKDASVV
K152 FKKFIsDKDASVVGF
K173 DGHSEFLKAASNLRD
T223 EDKIVAYTEKKMTSG
K226 IVAYTEKKMTSGKIK
K274 VDYEKNTKGSNYWRN
K296 TFLDAGHKLNFAVAS
K305 NFAVASRKTFSHELS
T306 FAVASRKTFSHELSD
R329-m2 EIPVVAIrTAKGEKF
K335 IrTAKGEKFVMQEEF
S343-p FVMQEEFsRDGKALE
K362 EYFDGNLKrYLKSEP
K362 EYFDGNLKrYLKSEP
R363-m2 YFDGNLKrYLKSEPI
K425 ELGEKLSKDPNIVIA
Y445-p ANDVPSPyEVKGFPT
T452 yEVKGFPTIyFSPAN
Y454-p VKGFPTIyFSPANKK
S456 GFPTIyFSPANKKLT
K460 IyFSPANKKLTPKKy
Y467-p KKLTPKKyEGGRELN
T485 SYLQREATNPPIIQE
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