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Protein Page:
KRas (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
KRas Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Interacts with PHLPP. Interacts (active GTP-bound form preferentially) with RGS14. Alternate between an inactive form bound to GDP and an active form bound to GTP. Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase- activating protein (GAP). Belongs to the small GTPase superfamily. Ras family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: G protein, monomeric; G protein; G protein, monomeric, Ras; Motility/polarity/chemotaxis
Cellular Component: membrane; mitochondrion; plasma membrane; lipid raft
Molecular Function: protein binding; GDP binding; GTP binding; GMP binding; protein complex binding; LRR domain binding
Biological Process: regulation of long-term neuronal synaptic plasticity; axon guidance; activation of MAPKK activity; nerve growth factor receptor signaling pathway; response to glucocorticoid stimulus; activation of NF-kappaB transcription factor; positive regulation of MAP kinase activity; GTP catabolic process; small GTPase mediated signal transduction; positive regulation of cell proliferation; visual learning; negative regulation of neuron apoptosis; epidermal growth factor receptor signaling pathway; fibroblast growth factor receptor signaling pathway; positive regulation of nitric-oxide synthase activity; cytokine and chemokine mediated signaling pathway; MAPKKK cascade; response to mineralocorticoid stimulus; social behavior; regulation of synaptic transmission, GABAergic; positive regulation of Rac protein signal transduction; Ras protein signal transduction; insulin receptor signaling pathway; striated muscle cell differentiation; innate immune response; positive regulation of protein amino acid phosphorylation; blood coagulation; actin cytoskeleton organization and biogenesis; leukocyte migration
Reference #:  P01116 (UniProtKB)
Alt. Names/Synonyms: c-K-ras; c-Ki-ras; c-Kirsten-ras protein; cellular c-Ki-ras2 proto-oncogene; GTPase KRas; GTPase KRas, N-terminally processed; K-Ras; K-Ras 2; K-ras p21 protein; K-RAS2A; K-RAS2B; K-RAS4A; K-RAS4B; Ki-Ras; Kirsten rat sarcoma-2 viral (v-Ki-ras2) oncogene homolog; KRAS; KRAS1; KRAS2; NS; NS3; oncogene KRAS2; PR310 c-K-ras oncogene; RASK; RASK2; transforming protein p21; v-Ki-ras2 Kirsten rat sarcoma 2 viral oncogene homolog; v-Ki-ras2 Kirsten rat sarcoma viral oncogene homolog
Gene Symbols: KRAS
Molecular weight: 21,656 Da
Basal Isoelectric point: 6.33  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  Angiogenesis  |  B Cell Receptor Signaling  |  ErbB/HER Signaling  |  ESC Pluripotency and Differentiation  |  GPCR Signaling to MAPKs  |  Growth And Differentiation Control by MAPKs  |  IL6 Signaling  |  Inhibition of Apoptosis  |  Insulin Receptor Signaling  |  NF-kB Signaling  |  SAPK/JNK Signaling Cascades  |  T Cell Receptor Signaling  |  TGF-├č Signaling  |  Warburg Effect
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

KRas

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

► Hide Isoforms
 
0 1 T2-p ______MtEyKLVVV
0 1 Y4-p ____MtEyKLVVVGA
0 5 S39-p YDPTIEDsYRKQVVI
1 1 R41 PTIEDsYRKQVVIDG
1 1 K42 TIEDsYRKQVVIDGE
1 0 K104-ub REQIKRVkDSEDVPM
0 2 K117-ub PMVLVGNkCDLPSRT
0 33 K128-ub PSRTVDTkQAQDLAR
1 5 K147-ub PFIETSAkTRQRVED
0 1 T148 FIETSAkTRQRVEDA
0 16 Y157 QRVEDAFYTLVREIR
0 1 T158 RVEDAFYTLVREIRQ
0 1 - gap
3 0 - gap
  KRas iso2  
T2 ______MTEYKLVVV
Y4 ____MTEYKLVVVGA
S39 YDPTIEDSYRKQVVI
R41 PTIEDSYRKQVVIDG
K42 TIEDSYRKQVVIDGE
K104 REQIKRVKDSEDVPM
K117 PMVLVGNKCDLPSRT
K128 PSRTVDTKQAQDLAR
K147 PFIETSAKtRQGVDD
T148-p FIETSAKtRQGVDDA
Y157-p QGVDDAFytLVREIR
T158-p GVDDAFytLVREIRK
K179-ac KDGKKKKkKsKTKCV
S181-p GKKKKkKsKTKCVIM
  mouse

► Hide Isoforms
 
T2 ______MTEYKLVVV
Y4 ____MTEYKLVVVGA
S39-p YDPTIEDsYRKQVVI
R41 PTIEDsYRKQVVIDG
K42 TIEDsYRKQVVIDGE
K104 REQIKRVKDSEDVPM
K117-ub PMVLVGNkCDLPSRT
K128-ub PSRTVDTkQAQELAR
K147-ub PFIETSAkTRQRVED
T148 FIETSAkTRQRVEDA
Y157 QRVEDAFYTLVREIR
T158 RVEDAFYTLVREIRQ
- gap
- gap
  KRas iso2  
T2 ______MTEYKLVVV
Y4 ____MTEYKLVVVGA
S39 YDPTIEDSYRKQVVI
R41 PTIEDSYRKQVVIDG
K42 TIEDSYRKQVVIDGE
K104 REQIKRVKDSEDVPM
K117 PMVLVGNKCDLPSRT
K128 PSRTVDTKQAQELAR
K147 PFIETSAKTRQGVDD
T148 FIETSAKTRQGVDDA
Y157 QGVDDAFYTLVREIR
T158 GVDDAFYTLVREIRK
K179 KDGKKKKKKSRTRCT
S181 GKKKKKKSRTRCTVM
  rat

 
T2 ______MTEYKLVVV
Y4 ____MTEYKLVVVGA
S39 YDPTIEDSYrkQVVI
R41-m2 PTIEDSYrkQVVIDG
K42-m2 TIEDSYrkQVVIDGE
K104 REQIKRVKDSEDVPM
K117 PMVLVGNKCDLPSRT
K128-ub PSRTVDTkQAQELAR
K147 PFIETSAKTRQRVED
T148 FIETSAKTRQRVEDA
Y157 QRVEDAFYTLVREIR
T158 RVEDAFYTLVREIRQ
- gap
- gap
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