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P08644 (RASK_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
GTPase KRas
Alternative name(s):
K-Ras 2
Ki-Ras
c-K-ras
c-Ki-ras

Cleaved into the following chain:

  1. GTPase KRas, N-terminally processed
Gene names
Name:Kras
Synonyms:Kras2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length189 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Enzyme regulation

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).

Subunit structure

Interacts with PHLPP. Interacts (active GTP-bound form preferentially) with RGS14. Ref.6 Ref.7

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side.

Sequence similarities

Belongs to the small GTPase superfamily. Ras family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Lipoprotein
Methylation
Palmitate
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcytokine-mediated signaling pathway

Inferred from mutant phenotype. Source: RGD

positive regulation of MAP kinase activity

Inferred from mutant phenotype. Source: RGD

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype. Source: RGD

positive regulation of nitric-oxide synthase activity

Inferred from mutant phenotype. Source: RGD

response to glucocorticoid stimulus

Inferred from expression pattern. Source: RGD

response to mineralocorticoid stimulus

Inferred from expression pattern. Source: RGD

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

social behavior

Inferred from expression pattern. Source: RGD

   Cellular componentmembrane raft

Inferred from direct assay Ref.6. Source: RGD

mitochondrion

Inferred from direct assay. Source: RGD

plasma membrane

Traceable author statement. Source: Reactome

   Molecular functionGDP binding

Inferred from direct assay Ref.6. Source: RGD

GMP binding

Inferred from direct assay Ref.6. Source: RGD

GTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

LRR domain binding

Inferred from direct assay Ref.6. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoforms differ in the C-terminal region which is encoded by two alternative exons (IVA and IVB).
Isoform 2A (identifier: P08644-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2B (identifier: P08644-2)

The sequence of this isoform differs from the canonical sequence as follows:
     151-153: RVE → GVD
     165-189: QYRLKKISKEEKTPGCVKIKKCVIM → KHKEKMSKDGKKKKKKSRTRCIVM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 186186GTPase KRas
PRO_0000082644
Initiator methionine11Removed; alternate By similarity
Chain2 – 186185GTPase KRas, N-terminally processed
PRO_0000326483
Propeptide187 – 1893Removed in mature form By similarity
PRO_0000281294

Regions

Nucleotide binding10 – 178GTP
Nucleotide binding57 – 615GTP
Nucleotide binding116 – 1194GTP
Region166 – 18520Hypervariable region
Motif32 – 409Effector region

Amino acid modifications

Modified residue11N-acetylmethionine; in GTPase KRas; alternate By similarity
Modified residue21N-acetylthreonine; in GTPase KRas, N-terminally processed By similarity
Modified residue1861Cysteine methyl ester; in isoform 2A By similarity
Lipidation1801S-palmitoyl cysteine By similarity
Lipidation1861S-farnesyl cysteine; in isoform 2A By similarity

Natural variations

Alternative sequence151 – 1533RVE → GVD in isoform 2B.
VSP_011144
Alternative sequence165 – 18925QYRLK…KCVIM → KHKEKMSKDGKKKKKKSRTR CIVM in isoform 2B.
VSP_011145

Experimental info

Sequence conflict121G → C in AAA42011. Ref.3
Sequence conflict471D → H in AAA42011. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 2A [UniParc].

Last modified July 19, 2004. Version 3.
Checksum: 97345422E01D2C81

FASTA18921,656
        10         20         30         40         50         60 
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG 

        70         80         90        100        110        120 
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHHYREQI KRVKDSEDVP MVLVGNKCDL 

       130        140        150        160        170        180 
PSRTVDTKQA QELARSYGIP FIETSAKTRQ RVEDAFYTLV REIRQYRLKK ISKEEKTPGC 


VKIKKCVIM 

« Hide

Isoform 2B [UniParc] [UniParc].

Checksum: B0A55318AD158F51
Show »

FASTA18821,495

References

« Hide 'large scale' references
[1]"Activation of the K-ras gene by insertion mutations in chemically induced rat renal mesenchymal tumors."
Higinbotham K.G., Rice J.M., Buzard G.S., Perantoni A.O.
Oncogene 9:2455-2459(1994) [PubMed: 8058308] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2B), MUTAGENESIS.
Strain: Noble.
Tissue: Kidney.
[2]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed: 15057822] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[3]"Structure of the c-Ki-ras gene in a rat fibrosarcoma induced by 1,8-dinitropyrene."
Tahira T., Hayashi K., Ochiai M., Tsuchida N., Nagao M., Sugimura T.
Mol. Cell. Biol. 6:1349-1351(1986) [PubMed: 3023884] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
[4]"Nucleotide sequence of exon I of the rat c-K-ras gene."
Iritani A., Katayama N., Tahira T., Hayashi K., Tsuchida N.
Bull. Tokyo Med. Dent. Univ. 33:35-40(1986) [PubMed: 3009041] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1-37.
[5]"Characterization of c-Ki-ras oncogene alleles by direct sequencing of enzymatically amplified DNA from carcinogen-induced tumors."
McMahon G., Davis E., Wogan G.N.
Proc. Natl. Acad. Sci. U.S.A. 84:4974-4978(1987) [PubMed: 3110778] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
[6]"Suprachiasmatic nucleus circadian oscillatory protein, a novel binding partner of K-Ras in the membrane rafts, negatively regulates MAPK pathway."
Shimizu K., Okada M., Nagai K., Fukada Y.
J. Biol. Chem. 278:14920-14925(2003) [PubMed: 12594205] [Abstract]
Cited for: INTERACTION WITH PHLPP.
[7]"Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras effector."
Willard F.S., Willard M.D., Kimple A.J., Soundararajan M., Oestreich E.A., Li X., Sowa N.A., Kimple R.J., Doyle D.A., Der C.J., Zylka M.J., Snider W.D., Siderovski D.P.
PLoS ONE 4:E4884-E4884(2009) [PubMed: 19319189] [Abstract]
Cited for: INTERACTION WITH RGS14.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U09793 mRNA. Translation: AAB60458.1.
AABR03032592 Genomic DNA. No translation available.
M12260, M12259 Genomic DNA. Translation: AAA42011.1.
M54870 Genomic DNA. Translation: AAA40937.1.
M16970 Genomic DNA. Translation: AAA41494.1.
IPIIPI00203826.
IPI00210097.
PIRI58402.
RefSeqNP_113703.1. NM_031515.3.
UniGeneRn.24554.

3D structure databases

ProteinModelPortalP08644.
SMRP08644. Positions 1-167.
ModBaseSearch...

Protein-protein interaction databases

STRINGP08644.

PTM databases

PhosphoSiteP08644.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000012588; ENSRNOP00000012588; ENSRNOG00000009338.
ENSRNOT00000012887; ENSRNOP00000012887; ENSRNOG00000009338.
GeneID24525.
KEGGrno:24525.

Organism-specific databases

CTD3845.
RGD2981. Kras.

Phylogenomic databases

GeneTreeENSGT00560000076901.
HOVERGENHBG009351.
InParanoidP08644.
OMARRYNKEM.
PhylomeDBP08644.

Enzyme and pathway databases

ReactomeREACT_111984. Signal Transduction.

Gene expression databases

ArrayExpressP08644.
GenevestigatorP08644.
GermOnlineENSRNOG00000009338. Rattus norvegicus.

Family and domain databases

InterProIPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
KOK07827.
PANTHERPTHR24070. PTHR24070. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00173. RAS. 1 hit.
[Graphical view]
TIGRFAMsTIGR00231. Small_GTP. 1 hit.
PROSITEPS51421. RAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio603578.

Entry information

Entry nameRASK_RAT
AccessionPrimary (citable) accession number: P08644
Secondary accession number(s): P46203, P97914
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: July 19, 2004
Last modified: November 16, 2011
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families