Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01459
Entry Name
UniProt Accession
Theoretical PI
5.74
Molecular Weight
23399.57
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Ras-related protein R-Ras2
Protein Synonyms/Alias
Ras-like protein TC21; Teratocarcinoma oncogene;
Gene Name
RRAS2
Gene Synonyms/Alias
TC21;
Created Date
21-JUN-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
199
Canonical
KEKDKKGCHCVIF**
[1]
S-Palmitoylation
201
Canonical
KDKKGCHCVIF****
[2]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
[2] Kho Y, Kim SC, Jiang C, Barma D, Kwon SW, Cheng J, Jaunbergs J, Weinbaum C,Tamanoi F, Falck J, Zhao Y. A tagging-via-substrate technology for detection and proteomics of farnesylated proteins. Proc Natl Acad Sci U S A. 2004 Aug24;101(34):12479-84. Epub 2004 Aug 12.[PMID:15308774]
Functional Description
It is a plasma membrane-associated GTP-binding protein with GTPase activity. Might transduce growth inhibitory signals across the cell membrane, exerting its effect through an effector shared with the Ras proteins but in an antagonistic fashion.
Sequence Annotation
Nucleotide-binding: 21 29 GTP.
Nucleotide-binding: 68 72 GTP.
Nucleotide-binding: 127 130 GTP.
Nucleotide-binding: 157 159 GTP.
Motif: 43 51 Effector region.
Modified residue: 2 2 N-acetylalanine.
Modified residue: 186 186 Phosphoserine.
Modified residue: 201 201 Cysteine methyl ester.
Protein Length
204 AA.
Protein Sequence
(Canonical)
MAAAGWRDGS GQEKYRLVVV GGGGVGKSAL TIQFIQSYFV TDYDPTIEDS YTKQCVIDDR  60
AARLDILDTA GQEEFGAMRE QYMRTGEGFL LVFSVTDRGS FEEIYKFQRQ ILRVKDRDEF  120
PMILIGNKAD LDHQRQVTQE EGQQLARQLK VTYMEASAKI RMNVDQAFHE LVRVIRKFQE  180
QECPPSPEPT RKEKDKKGCH CVIF                                         204
MAAAGWRDGS GQEKYRLVVV GGGGVGKSAL TIQFIQSYFV TDYDPTIEDS YTKQCVIDDR  60
AARLDILDTA GQEEFGAMRE QYMRTGEGFL LVFSVTDRGS FEEIYKFQRQ ILRVKDRDEF  120
PMILIGNKAD LDHQRQVTQE EGQQLARQLK VTYMEASAKI RMNVDQAFHE LVRVIRKFQE  180
QECPPSPEPT RKEKDKKGCH CVIF                                         204
FASTA
(Canonical)
>LipidDB-9606-01459|P62070
MAAAGWRDGSGQEKYRLVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCVIDDR
AARLDILDTAGQEEFGAMREQYMRTGEGFLLVFSVTDRGSFEEIYKFQRQILRVKDRDEF
PMILIGNKADLDHQRQVTQEEGQQLARQLKVTYMEASAKIRMNVDQAFHELVRVIRKFQE
QECPPSPEPTRKEKDKKGCHCVIF
MAAAGWRDGSGQEKYRLVVVGGGGVGKSALTIQFIQSYFVTDYDPTIEDSYTKQCVIDDR
AARLDILDTAGQEEFGAMREQYMRTGEGFLLVFSVTDRGSFEEIYKFQRQILRVKDRDEF
PMILIGNKADLDHQRQVTQEEGQQLARQLKVTYMEASAKIRMNVDQAFHELVRVIRKFQE
QECPPSPEPTRKEKDKKGCHCVIF
Gene Ontology
GO:0005783; C:endoplasmic reticulum; NAS:ProtInc
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0016020; C:membrane; IDA:UniProt
GO:0005886; C:plasma membrane; NAS:ProtInc
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; TAS:ProtInc
GO:0001649; P:osteoblast differentiation; IDA:UniProt
GO:0030335; P:positive regulation of cell migration; IEA:Ensembl
GO:0007265; P:Ras protein signal transduction; 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;