LipidDB ID

LipidDB-10116-00845

Entry Name

UniProt Accession

P08644; P46203; P97914;

Theoretical PI

6.33

Molecular Weight

21655.83

Genbank Protein ID

AAB60458.1; AAA42011.1; AAA42011.1; AAA40937.1; AAA41494.1;

Genbank Nucleotide ID

U09793; AABR03032592; M12260; M12259; M54870; M16970;

Protein Name

GTPase KRas, N-terminally processed

Protein Synonyms/Alias

K-Ras 2; Ki-Ras; c-K-ras; c-Ki-ras;

Gene Name

Kras

Gene Synonyms/Alias

Kras2;

Created Date

13-AUG-1987

Organism

Rattus norvegicus (Rat)

NCBI Taxa ID

10116

Reference

[1] Laezza C, Fiorentino L, Pisanti S, Gazzerro P, Caraglia M, Portella G, Vitale M, Bifulco M. Lovastatin induces apoptosis of k-ras-transformed thyroid cells viainhibition of ras farnesylation and by modulating redox state. J Mol Med (Berl). 2008 Dec;86(12):1341-51. doi: 10.1007/s00109-008-0396-1. Epub 2008 Sep 9.[PMID:18779944]

Functional Description

Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.

Sequence Annotation

Nucleotide-binding: 10 17 GTP.
Nucleotide-binding: 57 61 GTP.
Nucleotide-binding: 116 119 GTP.
Region: 166 185 Hypervariable region.
Motif: 32 40 Effector region.
Modified residue: 1 1 N-acetylmethionine.
Modified residue: 2 2 N-acetylthreonine; in GTPase KRas, N-terminally processed.
Modified residue: 104 104 N6-acetyllysine.
Modified residue: 186 186 Cysteine methyl ester; in isoform 2A.

Protein Length

189 AA.

Protein Sequence
(Canonical)

FASTA
(Canonical)

Gene Ontology

GO:0045121; C:membrane raft; IDA:RGD
GO:0005739; C:mitochondrion; IDA:RGD
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0019003; F:GDP binding; IDA:RGD
GO:0019002; F:GMP binding; IDA:RGD
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0030275; F:LRR domain binding; IDA:RGD
GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl
GO:0019221; P:cytokine-mediated signaling pathway; IMP:RGD
GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl
GO:0006184; P:GTP catabolic process; IEA:InterPro
GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl
GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl
GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl
GO:0010628; P:positive regulation of gene expression; IEA:Ensembl
GO:0043406; P:positive regulation of MAP kinase activity; IMP:RGD
GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:RGD
GO:0051000; P:positive regulation of nitric-oxide synthase activity; IMP:RGD
GO:0035022; P:positive regulation of Rac protein signal transduction; IEA:Ensembl
GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl
GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl
GO:0051384; P:response to glucocorticoid; IEP:RGD
GO:0051385; P:response to mineralocorticoid; IEP:RGD
GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro
GO:0035176; P:social behavior; IEP:RGD
GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl
GO:0008542; P:visual learning; IEA:Ensembl

Interpro

InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR020849; Small_GTPase_Ras

Pfam

Pfam; PF00071; Ras;

SMART

SMART; SM00173; RAS;

PROSITE

PROSITE; PS51421; RAS;

PRINTS

PRINTS; PR00449; RASTRNSFRMNG;