Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9913-00104
Entry Name
UniProt Accession
Theoretical PI
5.83
Molecular Weight
21768.13
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Transforming protein RhoA
Protein Synonyms/Alias
Gb; p21;
Gene Name
RHOA
Gene Synonyms/Alias
ARHA; RHO12;
Created Date
01-JAN-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
190
Canonical
RGKKKSGCLVL****
[1]
S-Geranylgeranylation
Organism
Bos taurus (Bovine)
NCBI Taxa ID
9913
Reference
[1] Katayama M, Kawata M, Yoshida Y, Horiuchi H, Yamamoto T, Matsuura Y, Takai Y. The posttranslationally modified C-terminal structure of bovine aortic smoothmuscle rhoA p21. J Biol Chem. 1991 Jul 5;266(19):12639-45.[PMID:1905729]
Functional Description
Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion. May be an activator of PLCE1. Activated by ARHGEF2, which promotes the exchange of GDP for GTP. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity).
Sequence Annotation
Nucleotide-binding: 12 19 GTP.
Nucleotide-binding: 59 63 GTP.
Nucleotide-binding: 117 120 GTP.
Motif: 34 42 Effector region.
Modified residue: 41 41 ADP-ribosylasparagine; by botulinumtoxin.
Modified residue: 188 188 Phosphoserine; by PKG/PRKG1.
Modified residue: 190 190 Cysteine methyl ester.
Protein Length
193 AA.
Protein Sequence
(Canonical)
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT  60
AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD  120
LRNDEHTRRE LAKMKQEPVK PEEGRDMANR IGAFGYMECS AKTKDGVREV FEMATRAALQ  180
ARRGKKKSGC LVL                                                     193
FASTA
(Canonical)
>LipidDB-9913-00104|P61585
MAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDT
AGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKD
LRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQ
ARRGKKKSGCLVL
Gene Ontology
GO:0043296; C:apical junction complex; ISS:UniProtKB
GO:0005938; C:cell cortex; ISS:UniProtKB
GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW
GO:0005829; C:cytosol; IEA:Ensembl
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0030027; C:lamellipodium; ISS:UniProtKB
GO:0005739; C:mitochondrion; IEA:Ensembl
GO:0005634; C:nucleus; IEA:Ensembl
GO:0032587; C:ruffle membrane; IEA:Ensembl
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IEA:Ensembl
GO:0030521; P:androgen receptor signaling pathway; IEA:Ensembl
GO:0043297; P:apical junction assembly; ISS:UniProtKB
GO:0000902; P:cell morphogenesis; IEA:Ensembl
GO:0007160; P:cell-matrix adhesion; IEA:Ensembl
GO:0021795; P:cerebral cortex cell migration; IEA:Ensembl
GO:0036089; P:cleavage furrow formation; ISS:UniProtKB
GO:0021861; P:forebrain radial glial cell differentiation; IEA:Ensembl
GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; IEA:Ensembl
GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl
GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl
GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB
GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB
GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl
GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl
GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl
GO:0030334; P:regulation of cell migration; ISS:UniProtKB
GO:2000177; P:regulation of neural precursor cell proliferation; IEA:Ensembl
GO:0033688; P:regulation of osteoblast proliferation; IEA:Ensembl
GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Ensembl
GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl
GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro
GO:0090307; P:spindle assembly involved in mitosis; IEA:Ensembl
GO:0043149; P:stress fiber assembly; IEA:Ensembl
GO:0021762; P:substantia nigra development; IEA:Ensembl
GO:0061383; P:trabecula morphogenesis; IEA:Ensembl
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR003578; Small_GTPase_Rho
Pfam
Pfam; PF00071; Ras;
SMART
SMART; SM00174; RHO;
PROSITE
PROSITE; PS51420; RHO;
PRINTS
PRINTS; PR00449; RASTRNSFRMNG;