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Protein

Transforming protein RhoA

Gene

RHOA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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). Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis (By similarity).By similarity

Cofactori

Mg2+By similarity

Enzyme regulationi

GTP hydrolysis is stimulated by ARHGAP30.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198GTP
Nucleotide bindingi59 – 635GTPBy similarity
Nucleotide bindingi117 – 1204GTP

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-114604. GPVI-mediated activation cascade.
R-BTA-193634. Axonal growth inhibition (RHOA activation).
R-BTA-194840. Rho GTPase cycle.
R-BTA-198203. PI3K/AKT activation.
R-BTA-209563. Axonal growth stimulation.
R-BTA-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-BTA-392451. G beta:gamma signalling through PI3Kgamma.
R-BTA-3928662. EPHB-mediated forward signaling.
R-BTA-3928663. EPHA-mediated growth cone collapse.
R-BTA-4086400. PCP/CE pathway.
R-BTA-416482. G alpha (12/13) signalling events.
R-BTA-416550. Sema4D mediated inhibition of cell attachment and migration.
R-BTA-416572. Sema4D induced cell migration and growth-cone collapse.
R-BTA-4420097. VEGFA-VEGFR2 Pathway.
R-BTA-5625740. RHO GTPases activate PKNs.
R-BTA-5625900. RHO GTPases activate CIT.
R-BTA-5625970. RHO GTPases activate KTN1.
R-BTA-5627117. RHO GTPases Activate ROCKs.
R-BTA-5663220. RHO GTPases Activate Formins.
R-BTA-5666185. RHO GTPases Activate Rhotekin and Rhophilins.
R-BTA-6785631. ERBB2 Regulates Cell Motility.
R-BTA-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.

Names & Taxonomyi

Protein namesi
Recommended name:
Transforming protein RhoA
Alternative name(s):
Gb
p21
Gene namesi
Name:RHOA
Synonyms:ARHA, RHO12
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 22

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Transforming protein RhoAPRO_0000030407Add
BLAST
Propeptidei191 – 1933Removed in mature formPRO_0000030408

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411ADP-ribosylasparagine; by botulinum toxin2 Publications
Modified residuei188 – 1881Phosphoserine; by PKG/PRKG1By similarity
Modified residuei190 – 1901Cysteine methyl ester
Lipidationi190 – 1901S-geranylgeranyl cysteine1 Publication

Post-translational modificationi

Substrate for botulinum ADP-ribosyltransferase.By similarity
Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling (By similarity). Phosphorylation by SLK at Ser-188 in response to AGTR2 activation (By similarity).By similarity
Ubiquitinated by the BCR(BACURD1) and BCR(BACURD2) E3 ubiquitin ligase complexes, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration.By similarity

Keywords - PTMi

ADP-ribosylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

PaxDbiP61585.
PeptideAtlasiP61585.
PRIDEiP61585.

Interactioni

Subunit structurei

Binds PRKCL1, ROCK1 and ROCK2. Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN. Interacts with PLCE1 and AKAP13. Interacts with ARHGEF28. Interacts with DIAPH1. Interacts (in the constitutively activated, GTP-bound form) with DGKQ. Interacts with RACK1; enhances RHOA activation. Interacts with PKP4; the interaction is detected at the midbody. Interacts (GTP-bound form preferentially) with PKN2; the interaction stimulates autophosphorylation and phosphorylation of PKN2 (By similarity). Interacts with ARHGDIA; this interaction inactivates and stabilizes RHOA. Interacts with ARHGDIB (By similarity). Interacts (GTP-bound form) with KCNA2 (via cytoplasmic N-terminal domain) (By similarity).By similarity

Protein-protein interaction databases

IntActiP61585. 8 interactions.
MINTiMINT-139651.
STRINGi9913.ENSBTAP00000005600.

Structurei

3D structure databases

ProteinModelPortaliP61585.
SMRiP61585. Positions 2-181.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 429Effector regionSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi182 – 1876Arg/Lys-rich (basic)

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP61585.
KOiK04513.
OMAiAYKSLEC.
OrthoDBiEOG73FQPD.
TreeFamiTF300837.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61585-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG
60 70 80 90 100
KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT
110 120 130 140 150
PEVKHFCPNV PIILVGNKKD LRNDEHTRRE LAKMKQEPVK PEEGRDMANR
160 170 180 190
IGAFGYMECS AKTKDGVREV FEMATRAALQ ARRGKKKSGC LVL
Length:193
Mass (Da):21,768
Last modified:January 1, 1988 - v1
Checksum:iC4DA2DC31FF858BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27278 mRNA. Translation: AAA30409.1.
BC102880 mRNA. Translation: AAI02881.1.
PIRiA33518. TVBO12.
RefSeqiNP_788818.1. NM_176645.3.
UniGeneiBt.49678.

Genome annotation databases

EnsembliENSBTAT00000005600; ENSBTAP00000005600; ENSBTAG00000004279.
GeneIDi338049.
KEGGibta:338049.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27278 mRNA. Translation: AAA30409.1.
BC102880 mRNA. Translation: AAI02881.1.
PIRiA33518. TVBO12.
RefSeqiNP_788818.1. NM_176645.3.
UniGeneiBt.49678.

3D structure databases

ProteinModelPortaliP61585.
SMRiP61585. Positions 2-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP61585. 8 interactions.
MINTiMINT-139651.
STRINGi9913.ENSBTAP00000005600.

Proteomic databases

PaxDbiP61585.
PeptideAtlasiP61585.
PRIDEiP61585.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000005600; ENSBTAP00000005600; ENSBTAG00000004279.
GeneIDi338049.
KEGGibta:338049.

Organism-specific databases

CTDi387.

Phylogenomic databases

eggNOGiKOG0393. Eukaryota.
COG1100. LUCA.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP61585.
KOiK04513.
OMAiAYKSLEC.
OrthoDBiEOG73FQPD.
TreeFamiTF300837.

Enzyme and pathway databases

ReactomeiR-BTA-114604. GPVI-mediated activation cascade.
R-BTA-193634. Axonal growth inhibition (RHOA activation).
R-BTA-194840. Rho GTPase cycle.
R-BTA-198203. PI3K/AKT activation.
R-BTA-209563. Axonal growth stimulation.
R-BTA-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-BTA-392451. G beta:gamma signalling through PI3Kgamma.
R-BTA-3928662. EPHB-mediated forward signaling.
R-BTA-3928663. EPHA-mediated growth cone collapse.
R-BTA-4086400. PCP/CE pathway.
R-BTA-416482. G alpha (12/13) signalling events.
R-BTA-416550. Sema4D mediated inhibition of cell attachment and migration.
R-BTA-416572. Sema4D induced cell migration and growth-cone collapse.
R-BTA-4420097. VEGFA-VEGFR2 Pathway.
R-BTA-5625740. RHO GTPases activate PKNs.
R-BTA-5625900. RHO GTPases activate CIT.
R-BTA-5625970. RHO GTPases activate KTN1.
R-BTA-5627117. RHO GTPases Activate ROCKs.
R-BTA-5663220. RHO GTPases Activate Formins.
R-BTA-5666185. RHO GTPases Activate Rhotekin and Rhophilins.
R-BTA-6785631. ERBB2 Regulates Cell Motility.
R-BTA-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.

Miscellaneous databases

PROiP61585.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning of Gb, the substrate for botulinum ADP-ribosyltransferase from bovine adrenal gland and its identification as a rho gene product."
    Ogorochi T., Nemoto Y., Nakajima M., Nakamura E., Fujiwara M., Narumiya S.
    Biochem. Biophys. Res. Commun. 163:1175-1181(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  3. "Substrate for botulinum ADP-ribosyltransferase, Gb, has an amino acid sequence homologous to a putative rho gene product."
    Narumiya S., Sekine A., Fujiwara M.
    J. Biol. Chem. 263:17255-17257(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-25; 42-50; 52-57; 59-97; 99-104; 134-162 AND 169-176.
    Tissue: Adrenal gland.
  4. "Guanine nucleotide-dependent ADP-ribosylation of soluble rho catalyzed by Clostridium botulinum C3 ADP-ribosyltransferase. Isolation and characterization of a newly recognized form of rhoA."
    Williamson K.C., Smith L.A., Moss J., Vaughan M.
    J. Biol. Chem. 265:20807-20812(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 28-70 AND 99-194, ADP-RIBOSYLATION AT ASN-41.
  5. "Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase."
    Sekine A., Fujiwara M., Narumiya S.
    J. Biol. Chem. 264:8602-8605(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 37-47, ADP-RIBOSYLATION AT ASN-41.
  6. "The posttranslationally modified C-terminal structure of bovine aortic smooth muscle rhoA p21."
    Katayama M., Kawata M., Yoshida Y., Horiuchi H., Yamamoto T., Matsuura Y., Takai Y.
    J. Biol. Chem. 266:12639-12645(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISOPRENYLATION AT CYS-190.
    Tissue: Aortic smooth muscle.

Entry informationi

Entry nameiRHOA_BOVIN
AccessioniPrimary (citable) accession number: P61585
Secondary accession number(s): P06749, Q3ZC72, Q9UEJ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: July 6, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.