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Protein Page:
GPX1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
GPX1 Protects the hemoglobin in erythrocytes from oxidative breakdown. Homotetramer. Interacts with MIEN1. Belongs to the glutathione peroxidase family. Note: This description may include information from UniProtKB.
Protein type: EC 1.11.1.9; Other Amino Acids Metabolism - glutathione; Oxidoreductase; Lipid Metabolism - arachidonic acid
Chromosomal Location of Human Ortholog: 3p21.3
Cellular Component: cytoplasm; cytosol; mitochondrial matrix; mitochondrion
Molecular Function: glutathione peroxidase activity; SH3 domain binding
Biological Process: cell redox homeostasis; glutathione metabolic process; heart contraction; hydrogen peroxide catabolic process; lipoxygenase pathway; negative regulation of caspase activity; purine nucleotide catabolic process; regulation of gene expression, epigenetic; regulation of mammary gland epithelial cell proliferation; response to hydrogen peroxide; response to reactive oxygen species; response to selenium ion; UV protection
Disease: Glutathione Peroxidase Deficiency
Reference #:  P07203 (UniProtKB)
Alt. Names/Synonyms: Cellular glutathione peroxidase; Glutathione peroxidase 1; GPx-1; GPX1; GSHPx-1; GSHPX1; MGC14399; MGC88245
Gene Symbols: GPX1
Molecular weight: 22,088 Da
Basal Isoelectric point: 6.15  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

GPX1

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



 LTP 

LTP: 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.


 HTP 

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


       human

 
0 3 A7 _MCAARLAAAAAAAQ
0 1 A12 RLAAAAAAAQSVYAF
0 1 S31 LAGGEPVSLGsLRGK
0 3 S34‑p GEPVSLGsLRGKVLL
0 33 R64 TQMNELQRRLGPRGL
0 1 R64 TQMNELQRRLGPRGL
0 2 R64 TQMNELQRRLGPRGL
0 15 K88‑ac FGHQENAkNEEILNS
0 1 K88 FGHQENAKNEEILNS
0 1 K88 FGHQENAKNEEILNS
0 3 K97 EEILNSLKyVRPGGG
1 0 Y98‑p EILNSLKyVRPGGGF
0 3 K114 PNFMLFEKCEVNGAG
0 1 K114 PNFMLFEKCEVNGAG
0 16 G121 KCEVNGAGAHPLFAF
0 1 G121 KCEVNGAGAHPLFAF
0 1 G121 KCEVNGAGAHPLFAF
0 4 T145‑p DDATALMtDPkLITW
0 5 K148‑ac TALMtDPkLITWsPV
0 1 K148 TALMtDPKLITWsPV
0 13 L149 ALMtDPkLITWsPVC
0 7 S153‑p DPkLITWsPVCRNDV
0 1 K166 DVAWNFEKFLVGPDG
0 1 K166‑ub DVAWNFEkFLVGPDG
0 1 S180‑p GVPLRRYsRRFQTID
0 1 S197 PDIEALLSQGPsCA_
0 1 Q198 DIEALLSQGPsCA__
0 1 S201‑p ALLSQGPsCA_____
0 5 A203 LSQGPsCA_______
  mouse

 
S7‑p _MCAARLsAAAQsTV
S12‑p RLsAAAQsTVYAFSA
S29‑p LTGGEPVsLGSLRGK
S32 GEPVsLGSLRGKVLL
K62‑ac TEMNDLQkRLGPRGL
K62‑ub TEMNDLQkRLGPRGL
K62‑sc TEMNDLQkRLGPRGL
K86‑ac FGHQENGkNEEILNS
K86‑ub FGHQENGkNEEILNS
K86‑sc FGHQENGkNEEILNS
K95‑ac EEILNSLkYVRPGGG
Y96 EILNSLkYVRPGGGF
K112‑ac PNFTLFEkCEVNGEk
K112‑sc PNFTLFEkCEVNGEk
K119‑ac kCEVNGEkAHPLFTF
K119‑ub kCEVNGEkAHPLFTF
K119‑sc kCEVNGEkAHPLFTF
T143‑p DDPTALMtDPkyIIW
K146‑ac TALMtDPkyIIWsPV
K146‑ub TALMtDPkyIIWsPV
Y147‑p ALMtDPkyIIWsPVC
S151‑p DPkyIIWsPVCRNDI
K164‑ac DIAWNFEkFLVGPDG
K164 DIAWNFEKFLVGPDG
S178 GVPVRRYSRRFRTID
S195 PDIETLLSQQSGNs_
Q196 DIETLLSQQSGNs__
G199 TLLSQQSGNs_____
S201‑p LSQQSGNs_______
  rat

 
S7 _MSAARLSAVAQSTV
S12 RLSAVAQSTVYAFSA
S29 LAGGEPVSLGsLRGK
S32‑p GEPVSLGsLRGKVLL
K62‑ac TEMNDLQkRLGPRGL
K62 TEMNDLQKRLGPRGL
K62 TEMNDLQKRLGPRGL
K86‑ac FGHQENGkNEEILNS
K86 FGHQENGKNEEILNS
K86 FGHQENGKNEEILNS
K95‑ac EEILNSLkYVRPGGG
Y96 EILNSLkYVRPGGGF
K112‑ac PNFTLFEkCEVNGEk
K112 PNFTLFEKCEVNGEk
K119‑ac kCEVNGEkAHPLFTF
K119 kCEVNGEKAHPLFTF
K119 kCEVNGEKAHPLFTF
T143‑p DDPTALMtDPkyIIW
K146‑ac TALMtDPkyIIWSPV
K146 TALMtDPKyIIWSPV
Y147‑p ALMtDPkyIIWSPVC
S151 DPkyIIWSPVCRNDI
K164 DISWNFEKFLVGPDG
K164 DISWNFEKFLVGPDG
S178 GVPVRRYSRRFRTID
S195‑p PDIEALLskQPSNP_
K196‑ac DIEALLskQPSNP__
S199 ALLskQPSNP_____
P201 LskQPSNP_______
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