Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00941
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; Ha-Ras; Transforming protein p21; c-H-ras; p21ras;
Gene Name
HRAS
Gene Synonyms/Alias
HRAS1;
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
181
Canonical
PDESGPGCMSCKCVL
[1][2]
S-Palmitoylation
184
Canonical
SGPGCMSCKCVLS**
[1][2]
S-Palmitoylation
186
Canonical
PGCMSCKCVLS****
[3]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Hancock JF, Magee AI, Childs JE, Marshall CJ. All ras proteins arepolyisoprenylated but only some are palmitoylated. Cell. 1989 Jun30;57(7):1167-77.[PMID:2661017]
[2] Forrester MT, Hess DT, Thompson JW, Hultman R, Moseley MA, Stamler JS, CaseyPJ. Site-specific analysis of protein S-acylation by resin-assisted capture. JLipid Res. 2011 Feb;52(2):393-8. doi: 10.1194/jlr.D011106. Epub 2010 Nov 2.[PMID:21044946]
[3] Dudler T, Gelb MH. Palmitoylation of Ha-Ras facilitates membrane binding,activation of downstream effectors, and meiotic maturation in Xenopus oocytes. J Biol Chem. 1996 May 10;271(19):11541-7.[PMID:8626715]
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; in GTPase HRas;alternate.
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-9606-00941|P01112
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
QEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPG
CMSCKCVLS
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
QEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPG
CMSCKCVLS
Gene Ontology
GO:0005737; C:cytoplasm; TAS:ProtInc
GO:0005829; C:cytosol; TAS:Reactome
GO:0005794; C:Golgi apparatus; IDA:UniProtKB
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0005525; F:GTP binding; IDA:UniProtKB
GO:0008022; F:protein C-terminus binding; IPI:UniProtKB
GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl
GO:0000186; P:activation of MAPKK activity; TAS:Reactome
GO:0007411; P:axon guidance; TAS:Reactome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0007050; P:cell cycle arrest; IDA:BHF-UCL
GO:0008283; P:cell proliferation; IEA:Ensembl
GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc
GO:0090398; P:cellular senescence; IDA:BHF-UCL
GO:0006935; P:chemotaxis; TAS:ProtInc
GO:0006897; P:endocytosis; IEA:Ensembl
GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome
GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl
GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome
GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome
GO:0006184; P:GTP catabolic process; IEA:InterPro
GO:0045087; P:innate immune response; TAS:Reactome
GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome
GO:0097193; P:intrinsic apoptotic signaling pathway; IEA:Ensembl
GO:0050900; P:leukocyte migration; TAS:Reactome
GO:0000165; P:MAPK cascade; TAS:Reactome
GO:0007093; P:mitotic cell cycle checkpoint; IDA:BHF-UCL
GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl
GO:0008285; P:negative regulation of cell proliferation; IDA:BHF-UCL
GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL
GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl
GO:0034259; P:negative regulation of Rho GTPase activity; IDA:BHF-UCL
GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome
GO:0009887; P:organ morphogenesis; TAS:ProtInc
GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IDA:BHF-UCL
GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL
GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL
GO:0045740; P:positive regulation of DNA replication; IDA:BHF-UCL
GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:BHF-UCL
GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL
GO:0046330; P:positive regulation of JNK cascade; IDA:BHF-UCL
GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL
GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL
GO:2000630; P:positive regulation of miRNA metabolic process; IDA:BHF-UCL
GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL
GO:0032855; P:positive regulation of Rac GTPase activity; IDA:BHF-UCL
GO:0035022; P:positive regulation of Rac protein signal transduction; IEA:Ensembl
GO:1900029; P:positive regulation of ruffle assembly; IDA:BHF-UCL
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL
GO:0090303; P:positive regulation of wound healing; IDA:BHF-UCL
GO:0051291; P:protein heterooligomerization; IEA:Ensembl
GO:0007265; P:Ras protein signal transduction; IDA:BHF-UCL
GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl
GO:0032228; P:regulation of synaptic transmission, GABAergic; IEA:Ensembl
GO:0007165; P:signal transduction; NAS:ProtInc
GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome
GO:0035176; P:social behavior; IEA:Ensembl
GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl
GO:0007268; P:synaptic transmission; TAS:Reactome
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;