Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00692
Entry Name
UniProt Accession
Theoretical PI
6.44
Molecular Weight
23480.49
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Ras-related protein R-Ras
Protein Synonyms/Alias
p23;
Gene Name
RRAS
Gene Synonyms/Alias
Created Date
01-JUL-1989
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
213
Canonical
PRKKGGGCPCVLL**
[1]
S-Palmitoylation
215
Canonical
KKGGGCPCVLL****
[2]
S-Geranylgeranylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Furuhjelm J, Peränen J. The C-terminal end of R-Ras contains a focal adhesion targeting signal. J Cell Sci. 2003 Sep 15;116(Pt 18):3729-38. Epub 2003 Jul 30.[PMID:12890755]
[2] van de Donk NW, Schotte D, Kamphuis MM, van Marion AM, van Kessel B, Bloem AC,Lokhorst HM. Protein geranylgeranylation is critical for the regulation ofsurvival and proliferation of lymphoma tumor cells. Clin Cancer Res. 2003 Nov15;9(15):5735-48.[PMID:14654559]
Functional Description
Regulates the organization of the actin cytoskeleton.
Sequence Annotation
Nucleotide-binding: 36 44 GTP.
Nucleotide-binding: 83 87 GTP.
Nucleotide-binding: 142 145 GTP.
Nucleotide-binding: 172 174 GTP.
Motif: 58 66 Effector region.
Modified residue: 215 215 Cysteine methyl ester.
Protein Length
218 AA.
Protein Sequence
(Canonical)
MSSGAASGTG RGRPRGGGPG PGDPPPSETH KLVVVGGGGV GKSALTIQFI QSYFVSDYDP  60
TIEDSYTKIC SVDGIPARLD ILDTAGQEEF GAMREQYMRA GHGFLLVFAI NDRQSFNEVG  120
KLFTQILRVK DRDDFPVVLV GNKADLESQR QVPRSEASAF GASHHVAYFE ASAKLRLNVD  180
EAFEQLVRAV RKYQEQELPP SPPSAPRKKG GGCPCVLL                          218
MSSGAASGTG RGRPRGGGPG PGDPPPSETH KLVVVGGGGV GKSALTIQFI QSYFVSDYDP  60
TIEDSYTKIC SVDGIPARLD ILDTAGQEEF GAMREQYMRA GHGFLLVFAI NDRQSFNEVG  120
KLFTQILRVK DRDDFPVVLV GNKADLESQR QVPRSEASAF GASHHVAYFE ASAKLRLNVD  180
EAFEQLVRAV RKYQEQELPP SPPSAPRKKG GGCPCVLL                          218
FASTA
(Canonical)
>LipidDB-9606-00692|P10301
MSSGAASGTGRGRPRGGGPGPGDPPPSETHKLVVVGGGGVGKSALTIQFIQSYFVSDYDP
TIEDSYTKICSVDGIPARLDILDTAGQEEFGAMREQYMRAGHGFLLVFAINDRQSFNEVG
KLFTQILRVKDRDDFPVVLVGNKADLESQRQVPRSEASAFGASHHVAYFEASAKLRLNVD
EAFEQLVRAVRKYQEQELPPSPPSAPRKKGGGCPCVLL
MSSGAASGTGRGRPRGGGPGPGDPPPSETHKLVVVGGGGVGKSALTIQFIQSYFVSDYDP
TIEDSYTKICSVDGIPARLDILDTAGQEEFGAMREQYMRAGHGFLLVFAINDRQSFNEVG
KLFTQILRVKDRDDFPVVLVGNKADLESQRQVPRSEASAFGASHHVAYFEASAKLRLNVD
EAFEQLVRAVRKYQEQELPPSPPSAPRKKGGGCPCVLL
Gene Ontology
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0019003; F:GDP binding; IDA:UniProtKB
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IDA:UniProtKB
GO:0032403; F:protein complex binding; IDA:MGI
GO:0007411; P:axon guidance; TAS:Reactome
GO:0030336; P:negative regulation of cell migration; IEA:Ensembl
GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB
GO:0007265; P:Ras protein signal transduction; TAS:ProtInc
GO:0007268; P:synaptic transmission; TAS:Reactome
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;