KRAS
entrez
3845
canonical
uniprot
P01116
canonical
ensembl
ENSG00000133703
resolver
ensp
ENSP00000256078
resolver
ensp
ENSP00000308495
resolver
ensp
ENSP00000508921
resolver
ensp
ENSP00000652769
resolver
genesymbol
KRAS
resolver
genesymbol_syn
KRAS2
resolver
genesymbol_syn
RASK2
resolver
hgnc
HGNC:6407
resolver
uniprot
A0ABF7PHA5
resolver
uniprot
A8K8Z5
resolver
uniprot
B0LPF9
resolver
uniprot
I1SRC5
resolver
uniprot
P01118
resolver
uniprot
Q96D10
resolver
uniprot_entry
A0ABF7PHA5_HUMAN
resolver
uniprot_entry
I1SRC5_HUMAN
resolver
uniprot_entry
RASK_HUMAN
resolver
uniprot_sec
A8K8Z5
resolver
uniprot_sec
B0LPF9
resolver
uniprot_sec
P01118
resolver
uniprot_sec
Q96D10
resolver
activity_regulation
ACTIVITY REGULATION: Alternates between an inactive form bound to GDP and an active form bound to GTP (PubMed:22566140, PubMed:22431598, PubMed:39809765). Activated by a guanine nucleotide-exchange factor (GEF) and inactivated by a GTPase-activating protein (GAP) (PubMed:22711838). Interaction with SOS1 promotes exchange of bound GDP to GTP (PubMed:22566140, PubMed:22431598, PubMed:39809765). {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:22566140, ECO:0000269|PubMed:22711838, ECO:0000269|PubMed:39809765}.
uniprot
proteins
amino_acid_sequence
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCIIM
uniprot
proteins
disease_involvement
DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes. {ECO:0000269|PubMed:8955068}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. {ECO:0000269|PubMed:17332249}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Noonan syndrome 3 (NS3) [MIM:609942]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. {ECO:0000269|PubMed:16474405, ECO:0000269|PubMed:16773572, ECO:0000269|PubMed:17056636, ECO:0000269|PubMed:17468812, ECO:0000269|PubMed:19396835, ECO:0000269|PubMed:20949621}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Gastric cancer (GASC) [MIM:613659]: A malignant disease which starts in the stomach, can spread to the esophagus or the small intestine, and can extend through the stomach wall to nearby lymph nodes and organs. It also can metastasize to other parts of the body. The term gastric cancer or gastric carcinoma refers to adenocarcinoma of the stomach that accounts for most of all gastric malignant tumors. Two main histologic types are recognized, diffuse type and intestinal type carcinomas. Diffuse tumors are poorly differentiated infiltrating lesions, resulting in thickening of the stomach. In contrast, intestinal tumors are usually exophytic, often ulcerating, and associated with intestinal metaplasia of the stomach, most often observed in sporadic disease. {ECO:0000269|PubMed:14534542, ECO:0000269|PubMed:3034404, ECO:0000269|PubMed:7773929}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Defects in KRAS are a cause of pylocytic astrocytoma (PA). Pylocytic astrocytomas are neoplasms of the brain and spinal cord derived from glial cells which vary from histologically benign forms to highly anaplastic and malignant tumors. {ECO:0000269|PubMed:16247081}.; DISEASE: Cardiofaciocutaneous syndrome 2 (CFC2) [MIM:615278]: A form of cardiofaciocutaneous syndrome, a multiple congenital anomaly disorder characterized by a distinctive facial appearance, heart defects and intellectual disability. Heart defects include pulmonic stenosis, atrial septal defects and hypertrophic cardiomyopathy. Some affected individuals present with ectodermal abnormalities such as sparse, friable hair, hyperkeratotic skin lesions and a generalized ichthyosis-like condition. Typical facial features are similar to Noonan syndrome. They include high forehead with bitemporal constriction, hypoplastic supraorbital ridges, downslanting palpebral fissures, a depressed nasal bridge, and posteriorly angulated ears with prominent helices. CFC2 patients often do not have the skin abnormalities, such as ichthyosis, hyperkeratosis, and hemangioma observed in CFC1. {ECO:0000269|PubMed:16474404, ECO:0000269|PubMed:16474405, ECO:0000269|PubMed:17056636, ECO:0000269|PubMed:20949621, ECO:0000269|PubMed:21797849}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=KRAS mutations are involved in cancer development. {ECO:0000269|PubMed:14534542, ECO:0000269|PubMed:1553789, ECO:0000269|PubMed:16533793, ECO:0000269|PubMed:24623306, ECO:0000269|PubMed:3034404, ECO:0000269|PubMed:3627975, ECO:0000269|PubMed:6092920, ECO:0000269|PubMed:6695174, ECO:0000269|PubMed:7773929}.; DISEASE: Oculoectodermal syndrome (OES) [MIM:600268]: A syndrome characterized by the association of epibulbar dermoids and aplasia cutis congenita. Affected individuals show multiple, asymmetric, atrophic, non-scarring and hairless regions that may be associated with hamartomas. Ectodermal changes include linear hyperpigmentation that may follow the lines of Blaschko and rarely epidermal nevus-like lesions. Epibulbar dermoids may be uni-or bilateral. Additional ocular anomalies such as skin tags of the upper eyelid, rarely optic nerve or retinal changes, and microphthalmia can be present. The phenotypic expression is highly variable, and various other abnormalities have occasionally been reported including growth failure, lymphedema, cardiovascular defects, as well as neurodevelopmental symptoms like developmental delay, epilepsy, learning difficulties, and behavioral abnormalities. Benign tumor-like lesions such as nonossifying fibromas of the long bones and giant cell granulomas of the jaws have repeatedly been observed and appear to be age-dependent, becoming a common manifestation in individuals aged 5 years or older. {ECO:0000269|PubMed:25808193, ECO:0000269|PubMed:26970110, ECO:0000269|PubMed:30891959}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Schimmelpenning-Feuerstein-Mims syndrome (SFM) [MIM:163200]: A disease characterized by sebaceous nevi, often on the face, associated with variable ipsilateral abnormalities of the central nervous system, ocular anomalies, and skeletal defects. Many oral manifestations have been reported, not only including hypoplastic and malformed teeth, and mucosal papillomatosis, but also ankyloglossia, hemihyperplastic tongue, intraoral nevus, giant cell granuloma, ameloblastoma, bone cysts, follicular cysts, oligodontia, and odontodysplasia. Sebaceous nevi follow the lines of Blaschko and these can continue as linear intraoral lesions, as in mucosal papillomatosis. {ECO:0000269|PubMed:30891959}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: RAS-associated autoimmune leukoproliferative disorder 2 (RALD2) [MIM:621582]: A disease characterized by lymphadenopathy, splenomegaly, and autoimmunity causing hemolytic anemia, idiopathic thrombocytopenic purpura, and neutropenia. {ECO:0000269|PubMed:21063026, ECO:0000269|PubMed:21079152}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.5.2
uniprot
proteins
function
FUNCTION: Signal transducer in the Ras-MAPK signaling pathway that regulates cell proliferation and survival (PubMed:22711838, PubMed:23698361). Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (PubMed:20949621, PubMed:39809765). Activates MAPK1/MAPK3 resulting in phosphorylation and ultimately degradation of GJA1 (By similarity). Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells in a ZNF304-dependent manner (PubMed:24623306). Recognized by LZTR1 that mediates its ubiquitination by a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex (PubMed:40934300). {ECO:0000250|UniProtKB:P08644, ECO:0000269|PubMed:20949621, ECO:0000269|PubMed:22711838, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:24623306, ECO:0000269|PubMed:39809765, ECO:0000269|PubMed:40934300}.
uniprot
proteins
mass_dalton
21656
uniprot
proteins
mutagenesis
MUTAGEN 35; /note="T->A: Increases affinity for LZTR1; alone and when associated with A-62."; /evidence="ECO:0000269|PubMed:40934300"; MUTAGEN 38; /note="D->A: Decreased interaction with MAPKAP1/SIN1."; /evidence="ECO:0000269|PubMed:34380736"; MUTAGEN 40; /note="Y->A: Decreased interaction with MAPKAP1/SIN1."; /evidence="ECO:0000269|PubMed:34380736"; MUTAGEN 61; /note="Q->L: Promotes GTP binding."; /evidence="ECO:0000269|PubMed:39809765"; MUTAGEN 62; /note="E->A: Increases affinity for LZTR1; alone and when associated with A-35."; /evidence="ECO:0000269|PubMed:40934300"; MUTAGEN 180; /note="C->S: Abolished palmitoylation on Cys; reduced palmitoylation on Lys residues."; /evidence="ECO:0000269|PubMed:29239724"; MUTAGEN 182..185; /note="KIKK->RIRR: In K-Ras-3KR; abolished lysine-palmitoylation."; /evidence="ECO:0000269|PubMed:29239724"; MUTAGEN P01116-2:185; /note="C->S: Abolished interaction with GPR131."; /evidence="ECO:0000269|PubMed:28619714
uniprot
proteins
post_translational_modification
PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). {ECO:0000269|PubMed:22711838, ECO:0000269|Ref.17}.; PTM: Palmitoylated at Lys-182, Lys-184 and Lys-185 (PubMed:29239724). Palmitoylation on lysine residues is promoted by palmitoylation at Cys-180 (PubMed:29239724). Lysine-depalmitoylation by SIRT2 promotes its localization to endomembranes in endocytic pathways (PubMed:29239724). {ECO:0000269|PubMed:29239724}.; PTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at Lys-170 in a non-degradative manner, leading to inhibit Ras signaling by decreasing Ras association with membranes. {ECO:0000305|PubMed:30442762, ECO:0000305|PubMed:30442766}.; PTM: (Microbial infection) Glucosylated at Thr-35 by P.sordellii toxin TcsL. {ECO:0000269|PubMed:19744486}.
uniprot
proteins
protein_family
Ras family
uniprot
proteins
protein_family
Small GTPase superfamily
uniprot
proteins
pubmed
14534542
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1553789
uniprot
proteins
pubmed
16247081
uniprot
proteins
pubmed
16474404
uniprot
proteins
pubmed
16474405
uniprot
proteins
pubmed
16533793
uniprot
proteins
pubmed
16773572
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17056636
uniprot
proteins
pubmed
17332249
uniprot
proteins
pubmed
17468812
uniprot
proteins
pubmed
19396835
uniprot
proteins
pubmed
19744486
uniprot
proteins
pubmed
20709748
uniprot
proteins
pubmed
20949621
uniprot
proteins
pubmed
21063026
uniprot
proteins
pubmed
21079152
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21797849
uniprot
proteins
pubmed
22431598
uniprot
proteins
pubmed
22566140
uniprot
proteins
pubmed
22711838
uniprot
proteins
pubmed
23524970
uniprot
proteins
pubmed
23698361
uniprot
proteins
pubmed
24415755
uniprot
proteins
pubmed
24623306
uniprot
proteins
pubmed
25808193
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26970110
uniprot
proteins
pubmed
27791178
uniprot
proteins
pubmed
28619714
uniprot
proteins
pubmed
29239724
uniprot
proteins
pubmed
3034404
uniprot
proteins
pubmed
30442762
uniprot
proteins
pubmed
30442766
uniprot
proteins
pubmed
30891959
uniprot
proteins
pubmed
3310850
uniprot
proteins
pubmed
34380736
uniprot
proteins
pubmed
34820593
uniprot
proteins
pubmed
35522713
uniprot
proteins
pubmed
35768504
uniprot
proteins
pubmed
35830882
uniprot
proteins
pubmed
35831509
uniprot
proteins
pubmed
36175670
uniprot
proteins
pubmed
3627975
uniprot
proteins
pubmed
3855240
uniprot
proteins
pubmed
3932274
uniprot
proteins
pubmed
39809765
uniprot
proteins
pubmed
40934300
uniprot
proteins
pubmed
6092920
uniprot
proteins
pubmed
6096811
uniprot
proteins
pubmed
6308465
uniprot
proteins
pubmed
6308466
uniprot
proteins
pubmed
6308467
uniprot
proteins
pubmed
6320174
uniprot
proteins
pubmed
6695174
uniprot
proteins
pubmed
7773929
uniprot
proteins
pubmed
8439212
uniprot
proteins
pubmed
8955068
uniprot
proteins
sequence_length
189
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22431598, ECO:0000269|PubMed:23524970, ECO:0000269|PubMed:23698361, ECO:0000269|PubMed:29239724}; Lipid-anchor {ECO:0000269|PubMed:29239724, ECO:0000305|PubMed:23698361}; Cytoplasmic side {ECO:0000305|PubMed:23698361}. Endomembrane system {ECO:0000269|PubMed:29239724}. Cytoplasm {ECO:0000269|PubMed:23524970, ECO:0000269|PubMed:23698361}.; SUBCELLULAR LOCATION: [Isoform 2B]: Cell membrane {ECO:0000269|PubMed:28619714}; Lipid-anchor {ECO:0000305|PubMed:28619714}.
uniprot
proteins