Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-00384
Entry Name
UniProt Accession
Theoretical PI
5.16
Molecular Weight
21298.13
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
GTPase HRas, N-terminally processed
Protein Synonyms/Alias
H-Ras-1; Transforming protein p21; c-H-ras; p21ras;
Gene Name
Hras
Gene Synonyms/Alias
Hras1;
Created Date
01-FEB-1991
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
181
Canonical
PDESGPGCMSCKCVL
[1]
S-Palmitoylation
184
Canonical
SGPGCMSCKCVLS**
[1]
S-Palmitoylation
186
Canonical
PGCMSCKCVLS****
[2]
S-Farnesylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Casey PJ, Solski PA, Der CJ, Buss JE. p21ras is modified by a farnesylisoprenoid. Proc Natl Acad Sci U S A. 1989 Nov;86(21):8323-7.[PMID:2682646]
[2] Clarke S, Vogel JP, Deschenes RJ, Stock J. Posttranslational modification ofthe Ha-ras oncogene protein: evidence for a third class of protein carboxylmethyltransferases. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4643-7. Erratum in:Proc Natl Acad Sci U S A 1988 Oct;85(20):7556.[PMID:3290900]
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 HRas, N-terminally processed.
Modified residue: 118 118 S-nitrosocysteine.
Modified residue: 186 186 Cysteine methyl ester.
Protein Length
189 AA.
Protein Sequence
(Canonical)
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG  60
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL  120
AARTVESRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGPG  180
CMSCKCVLS                                                          189
MTEYKLVVVG AGGVGKSALT IQLIQNHFVD EYDPTIEDSY RKQVVIDGET CLLDILDTAG  60
QEEYSAMRDQ YMRTGEGFLC VFAINNTKSF EDIHQYREQI KRVKDSDDVP MVLVGNKCDL  120
AARTVESRQA QDLARSYGIP YIETSAKTRQ GVEDAFYTLV REIRQHKLRK LNPPDESGPG  180
CMSCKCVLS                                                          189
FASTA
(Canonical)
>LipidDB-10116-00384|P20171
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
QEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPG
CMSCKCVLS
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
QEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPG
CMSCKCVLS
Gene Ontology
GO:0005794; C:Golgi apparatus; ISS:UniProtKB
GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0005525; F:GTP binding; ISS:UniProtKB
GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl
GO:0006915; P:apoptotic process; IMP:RGD
GO:0007050; P:cell cycle arrest; IEA:Ensembl
GO:0008283; P:cell proliferation; IEA:Ensembl
GO:0090398; P:cellular senescence; IEA:Ensembl
GO:0006897; P:endocytosis; IEA:Ensembl
GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl
GO:0006184; P:GTP catabolic process; IEA:InterPro
GO:0097193; P:intrinsic apoptotic signaling pathway; IEA:Ensembl
GO:0007093; P:mitotic cell cycle checkpoint; IEA:Ensembl
GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl
GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl
GO:0010629; P:negative regulation of gene expression; IEA:Ensembl
GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl
GO:0034259; P:negative regulation of Rho GTPase activity; IEA:Ensembl
GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IEA:Ensembl
GO:0030335; P:positive regulation of cell migration; IEA:Ensembl
GO:0045740; P:positive regulation of DNA replication; IMP:RGD
GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl
GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD
GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl
GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl
GO:2000630; P:positive regulation of miRNA metabolic process; IEA:Ensembl
GO:0032855; P:positive regulation of Rac GTPase activity; IEA:Ensembl
GO:0035022; P:positive regulation of Rac protein signal transduction; IEA:Ensembl
GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:MGI
GO:1900029; P:positive regulation of ruffle assembly; IEA:Ensembl
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl
GO:0090303; P:positive regulation of wound healing; IEA:Ensembl
GO:0051291; P:protein heterooligomerization; IPI:RGD
GO:0007265; P:Ras protein signal transduction; IMP:RGD
GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl
GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl
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;