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Entry version 157 (02 Dec 2020)
Sequence version 1 (01 Jan 1988)
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Protein

Transforming protein RhoA

Gene

RHOA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state. Mainly associated with cytoskeleton organization, in active state binds to a variety of effector proteins to regulate cellular responses such as cytoskeletal dynamics, cell migration and cell cycle. 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. 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. Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis. Acts as an allosteric activator of guanine nucleotide exchange factor ECT2 by binding in its activated GTP-bound form to the PH domain of ECT2 which stimulates the release of PH inhibition and promotes the binding of substrate RHOA to the ECT2 catalytic center. May be an activator of PLCE1. In neurons, involved in the inhibiton of the initial spine growth. Upon activation by CaMKII, modulates dendritic spine structural plasticity by relaying CaMKII transient activation to synapse-specific, long-term signaling.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity and GDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase. Activated by GEFs such as ARHGEF2, ARHGEF3, ARHGEF28 and BCR. Inhibited by GAPs such as ARHGAP30. Inhibited by GDP dissociation inhibitors such as ARHGDIA.By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi12 – 19GTP8
Nucleotide bindingi59 – 63GTPBy similarity5
Nucleotide bindingi117 – 120GTP4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processCell cycle, Cell division
LigandGTP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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-5689896, Ovarian tumor domain proteases
R-BTA-6785631, ERBB2 Regulates Cell Motility
R-BTA-6798695, Neutrophil degranulation
R-BTA-8849471, PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-BTA-8985586, SLIT2:ROBO1 increases RHOA activity

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Transforming protein RhoA (EC:3.6.5.2By similarity)
Alternative name(s):
Gb
p21
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RHOA
Synonyms:ARHA, RHO12
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBos taurus (Bovine)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9913 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaRuminantiaPecoraBovidaeBovinaeBos
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000009136 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 22

Organism-specific databases

Vertebrate Gene Nomenclature Database

More...
VGNCi
VGNC:33943, RHOA

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000304071 – 190Transforming protein RhoAAdd BLAST190
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000030408191 – 193Removed in mature form3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei41ADP-ribosylasparagine; by botulinum toxin2 Publications1
Modified residuei188Phosphoserine; by PKG/PRKG1By similarity1
Modified residuei190Cysteine methyl ester1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi190S-geranylgeranyl cysteine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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(KCTD13) and BCR(TNFAIP1) E3 ubiquitin ligase complexes, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and synaptic transmission in neurons.By similarity

Keywords - PTMi

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

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P61585

PeptideAtlas

More...
PeptideAtlasi
P61585

PRoteomics IDEntifications database

More...
PRIDEi
P61585

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P61585

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSBTAG00000004279, Expressed in spermatocyte and 18 other tissues

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with ARHGEF28 (By similarity).

Interacts (via GTP-bound form) with RIPOR1 (via N-terminus); this interaction links RHOA to STK24 and STK26 kinases.

Interacts with RIPOR2 (via active GTP- or inactive GDP-bound forms) isoform 1 and isoform 2; these interactions are direct, block the loading of GTP to RHOA and decrease upon chemokine CCL19 stimulation in primary T lymphocytes. Binds PRKCL1, ROCK1 and ROCK2.

Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN.

Interacts with PLCE1 and AKAP13.

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.

Interacts with ARHGDIA; this interaction inactivates and stabilizes RHOA.

Interacts with ARHGDIB.

Interacts (GTP-bound form) with KCNA2 (via cytoplasmic N-terminal domain) (By similarity).

Interacts (GTP-bound form) with ECT2; the interaction results in allosteric activation of ECT2.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P61585

Protein interaction database and analysis system

More...
IntActi
P61585, 8 interactors

Molecular INTeraction database

More...
MINTi
P61585

STRING: functional protein association networks

More...
STRINGi
9913.ENSBTAP00000005600

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P61585

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P61585

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi34 – 42Effector regionSequence analysis9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi182 – 187Arg/Lys-rich (basic)6

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0393, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182945

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_041217_21_2_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P61585

Identification of Orthologs from Complete Genome Data

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OMAi
RWIPEIK

Database of Orthologous Groups

More...
OrthoDBi
1166960at2759

TreeFam database of animal gene trees

More...
TreeFami
TF300837

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027417, P-loop_NTPase
IPR005225, Small_GTP-bd_dom
IPR001806, Small_GTPase
IPR003578, Small_GTPase_Rho

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00071, Ras, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00231, small_GTP, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51420, RHO, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iC4DA2DC31FF858BC
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M27278 mRNA Translation: AAA30409.1
BC102880 mRNA Translation: AAI02881.1

Protein sequence database of the Protein Information Resource

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PIRi
A33518, TVBO12

NCBI Reference Sequences

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RefSeqi
NP_788818.1, NM_176645.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSBTAT00000005600; ENSBTAP00000005600; ENSBTAG00000004279

Database of genes from NCBI RefSeq genomes

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GeneIDi
338049

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bta:338049

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

BMRBiP61585
SMRiP61585
ModBaseiSearch...

Protein-protein interaction databases

CORUMiP61585
IntActiP61585, 8 interactors
MINTiP61585
STRINGi9913.ENSBTAP00000005600

PTM databases

iPTMnetiP61585

Proteomic databases

PaxDbiP61585
PeptideAtlasiP61585
PRIDEiP61585

Genome annotation databases

EnsembliENSBTAT00000005600; ENSBTAP00000005600; ENSBTAG00000004279
GeneIDi338049
KEGGibta:338049

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
387
VGNCiVGNC:33943, RHOA

Phylogenomic databases

eggNOGiKOG0393, Eukaryota
GeneTreeiENSGT00950000182945
HOGENOMiCLU_041217_21_2_1
InParanoidiP61585
OMAiRWIPEIK
OrthoDBi1166960at2759
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-5689896, Ovarian tumor domain proteases
R-BTA-6785631, ERBB2 Regulates Cell Motility
R-BTA-6798695, Neutrophil degranulation
R-BTA-8849471, PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-BTA-8985586, SLIT2:ROBO1 increases RHOA activity

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P61585

Gene expression databases

BgeeiENSBTAG00000004279, Expressed in spermatocyte and 18 other tissues

Family and domain databases

InterProiView protein in InterPro
IPR027417, P-loop_NTPase
IPR005225, Small_GTP-bd_dom
IPR001806, Small_GTPase
IPR003578, Small_GTPase_Rho
PfamiView protein in Pfam
PF00071, Ras, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
TIGRFAMsiTIGR00231, small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51420, RHO, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRHOA_BOVIN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P61585
Secondary accession number(s): P06749, Q3ZC72, Q9UEJ4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: December 2, 2020
This is version 157 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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