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Entry version 187 (03 Jul 2019)
Sequence version 1 (01 Jan 1988)
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Protein

Transforming protein RhoA

Gene

RHOA

Organism
Homo sapiens (Human)
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 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 (PubMed:8910519, PubMed:9121475). Involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis (PubMed:16236794, PubMed:12900402). Plays an essential role in cleavage furrow formation. Required for the apical junction formation of keratinocyte cell-cell adhesion (PubMed:20974804, PubMed:23940119). Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly (PubMed:19934221). 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 (PubMed:20937854). Regulates KCNA2 potassium channel activity by reducing its location at the cell surface in response to CHRM1 activation; promotes KCNA2 endocytosis (PubMed:9635436, PubMed:19403695). May be an activator of PLCE1 (PubMed:16103226). 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).By similarity11 Publications
(Microbial infection) Serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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+1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 (PubMed:23940119, PubMed:12221096). Inhibited by GAPs such as ARHGAP30 (PubMed:21565175). Inhibited by GDP dissociation inhibitors such as ARHGDIA (PubMed:20400958).4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 – 19GTP2 Publications8
Nucleotide bindingi59 – 63GTPBy similarity5
Nucleotide bindingi117 – 120GTP2 Publications4

<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, Host-virus interaction
LigandGTP-binding, Magnesium, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-114604 GPVI-mediated activation cascade
R-HSA-193634 Axonal growth inhibition (RHOA activation)
R-HSA-194840 Rho GTPase cycle
R-HSA-198203 PI3K/AKT activation
R-HSA-209563 Axonal growth stimulation
R-HSA-2173791 TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-HSA-392451 G beta:gamma signalling through PI3Kgamma
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-3928663 EPHA-mediated growth cone collapse
R-HSA-4086400 PCP/CE pathway
R-HSA-416482 G alpha (12/13) signalling events
R-HSA-416550 Sema4D mediated inhibition of cell attachment and migration
R-HSA-416572 Sema4D induced cell migration and growth-cone collapse
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-5625740 RHO GTPases activate PKNs
R-HSA-5625900 RHO GTPases activate CIT
R-HSA-5625970 RHO GTPases activate KTN1
R-HSA-5627117 RHO GTPases Activate ROCKs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-5666185 RHO GTPases Activate Rhotekin and Rhophilins
R-HSA-5689896 Ovarian tumor domain proteases
R-HSA-6785631 ERBB2 Regulates Cell Motility
R-HSA-6798695 Neutrophil degranulation
R-HSA-8849471 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-HSA-8985586 SLIT2:ROBO1 increases RHOA activity

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P61586

SIGNOR Signaling Network Open Resource

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SIGNORi
P61586

<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_and_taxonomy_section">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 RhoACurated (EC:3.6.5.22 Publications)
Alternative name(s):
Rho cDNA clone 12
Short name:
h12
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:RHOAImported
Synonyms:ARH12, ARHA, RHO12
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 3

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:667 RHOA

Online Mendelian Inheritance in Man (OMIM)

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MIMi
165390 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P61586

<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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi14G → V: Causes constitutive activation. 1 Publication1
Mutagenesisi34Y → A: Abolishes interaction with DGKQ. 2 Publications1
Mutagenesisi34Y → F: Abolishes AMPylation by Haemophilus IbpA. 2 Publications1
Mutagenesisi63Q → L: Causes constitutive activation. 1
Mutagenesisi193L → M: Converts geranyl-geranylation to farnesylation; does not prevent the cleavage by yopT. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
387

Open Targets

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OpenTargetsi
ENSG00000067560

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA134865095

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL6052

Drug and drug target database

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DrugBanki
DB04315 Guanosine-5'-Diphosphate

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RHOA

Domain mapping of disease mutations (DMDM)

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DMDMi
47606458

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000304111 – 190Transforming protein RhoAAdd BLAST190
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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_0000030412191 – 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 residuei34O-AMP-tyrosine; by Haemophilus IbpA; alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi34O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate1 Publication1
Modified residuei37O-AMP-threonine; by Vibrio VopS1 Publication1
Modified residuei41ADP-ribosylasparagine; by botulinum toxin1 Publication1
Modified residuei188Phosphoserine; by PKG/PRKG11 Publication1
Modified residuei190Cysteine methyl esterBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 cysteineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

(Microbial infection) Substrate for botulinum ADP-ribosyltransferase.1 Publication
(Microbial infection) Cleaved by yopT protease when the cell is infected by some Yersinia pathogens. This removes the lipid attachment, and leads to its displacement from plasma membrane and to subsequent cytoskeleton cleavage.2 Publications
(Microbial infection) AMPylation at Tyr-34 and Thr-37 are mediated by bacterial enzymes in case of infection by H.somnus and V.parahaemolyticus, respectively. AMPylation occurs in the effector region and leads to inactivation of the GTPase activity by preventing the interaction with downstream effectors, thereby inhibiting actin assembly in infected cells. It is unclear whether some human enzyme mediates AMPylation; FICD has such ability in vitro but additional experiments remain to be done to confirm results in vivo.2 Publications
(Microbial infection) Glycosylated at Tyr-34 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rho and leads to actin disassembly.1 Publication
Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling (PubMed:11162591). Phosphorylation by SLK at Ser-188 in response to AGTR2 activation (By similarity).By similarity1 Publication
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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei189 – 190Cleavage; by yopT2

Keywords - PTMi

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

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P61586

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P61586

MaxQB - The MaxQuant DataBase

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MaxQBi
P61586

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

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PaxDbi
P61586

PeptideAtlas

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PeptideAtlasi
P61586

PRoteomics IDEntifications database

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PRIDEi
P61586

ProteomicsDB human proteome resource

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ProteomicsDBi
57321

Consortium for Top Down Proteomics

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TopDownProteomicsi
P61586

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P61586

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P61586

SwissPalm database of S-palmitoylation events

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SwissPalmi
P61586

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P61586

<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

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Bgeei
ENSG00000067560 Expressed in 243 organ(s), highest expression level in metanephric glomerulus

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P61586 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P61586 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB005052

<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_section">'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_section">'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 (PubMed:27807006).

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 (PubMed:25588844). Binds PRKCL1, ROCK1 and ROCK2 (PubMed:10388627, PubMed:8617235, PubMed:8641286).

Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN (PubMed:10940294, PubMed:12221096, PubMed:9857026).

Interacts with PLCE1 and AKAP13 (PubMed:11696353, PubMed:12900402).

Interacts with DIAPH1 (PubMed:23325789).

Interacts (in the constitutively activated, GTP-bound form) with DGKQ (PubMed:10066731).

Interacts with RACK1; enhances RHOA activation (PubMed:20499158).

Interacts with PKP4; the interaction is detected at the midbody (PubMed:17115030).

Interacts (GTP-bound form preferentially) with PKN2; the interaction stimulates autophosphorylation and phosphorylation of PKN2 (PubMed:20974804, PubMed:9121475).

Interacts with ARHGDIA; this interaction inactivates and stabilizes RHOA (PubMed:20400958).

Interacts with ARHGDIB.

Interacts (GTP-bound form) with KCNA2 (via cytoplasmic N-terminal domain) (PubMed:9635436).

By similarity1 Publication16 Publications

(Microbial infection)

Interacts with yopT from Yersinia pestis.

2 Publications

(Microbial infection)

Interacts with human respiratory syncytial virus (HRSV) protein F; this interaction facilitates virus-induced syncytium formation.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106880, 189 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P61586

Database of interacting proteins

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DIPi
DIP-29642N

Protein interaction database and analysis system

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IntActi
P61586, 84 interactors

Molecular INTeraction database

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MINTi
P61586

STRING: functional protein association networks

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STRINGi
9606.ENSP00000400175

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P61586

<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

Secondary structure

1193
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P61586

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P61586

<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 general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The basic-rich region is essential for yopT recognition and cleavage.

<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

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eggNOGi
KOG0393 Eukaryota
COG1100 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000182945

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233974

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P61586

KEGG Orthology (KO)

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KOi
K04513

Identification of Orthologs from Complete Genome Data

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OMAi
DLRFDQK

Database of Orthologous Groups

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OrthoDBi
1166960at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P61586

TreeFam database of animal gene trees

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TreeFami
TF300837

Family and domain databases

Integrated resource of protein families, domains and functional sites

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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

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Pfami
View protein in Pfam
PF00071 Ras, 1 hit

Superfamily database of structural and functional annotation

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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

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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_length">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

P61586-1 [UniParc]FASTAAdd to basket
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        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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
C9JX21C9JX21_HUMAN
Transforming protein RhoA
RHOA
187Annotation score:

Annotation score:1 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>
C9JNR4C9JNR4_HUMAN
Transforming protein RhoA
RHOA
129Annotation score:

Annotation score:1 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>
C9JRM1C9JRM1_HUMAN
Transforming protein RhoA
RHOA
90Annotation score:

Annotation score:1 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti23I → T in BAD96276 (Ref. 5) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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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
X05026 mRNA Translation: CAA28690.1
L25080 mRNA Translation: AAC33178.1
AF498970 mRNA Translation: AAM21117.1
BT019870 mRNA Translation: AAV38673.1
AK222556 mRNA Translation: BAD96276.1
BX647063 mRNA Translation: CAE46190.1
AC104452 Genomic DNA No translation available.
AC121247 Genomic DNA No translation available.
AC137114 Genomic DNA No translation available.
BC001360 mRNA Translation: AAH01360.1
BC005976 mRNA Translation: AAH05976.1
L09159 mRNA Translation: AAA50612.1
M83094 Genomic DNA Translation: AAA67539.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS2795.1

Protein sequence database of the Protein Information Resource

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PIRi
A26675 TVHU12

NCBI Reference Sequences

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RefSeqi
NP_001300870.1, NM_001313941.1
NP_001655.1, NM_001664.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000418115; ENSP00000400175; ENSG00000067560

Database of genes from NCBI RefSeq genomes

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GeneIDi
387

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:387

UCSC genome browser

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UCSCi
uc003cwu.4 human

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05026 mRNA Translation: CAA28690.1
L25080 mRNA Translation: AAC33178.1
AF498970 mRNA Translation: AAM21117.1
BT019870 mRNA Translation: AAV38673.1
AK222556 mRNA Translation: BAD96276.1
BX647063 mRNA Translation: CAE46190.1
AC104452 Genomic DNA No translation available.
AC121247 Genomic DNA No translation available.
AC137114 Genomic DNA No translation available.
BC001360 mRNA Translation: AAH01360.1
BC005976 mRNA Translation: AAH05976.1
L09159 mRNA Translation: AAA50612.1
M83094 Genomic DNA Translation: AAA67539.1
CCDSiCCDS2795.1
PIRiA26675 TVHU12
RefSeqiNP_001300870.1, NM_001313941.1
NP_001655.1, NM_001664.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A2BX-ray2.40A1-181[»]
1CC0X-ray5.00A/C1-190[»]
1CXZX-ray2.20A1-181[»]
1DPFX-ray2.00A1-180[»]
1FTNX-ray2.10A1-193[»]
1KMQX-ray1.55A4-181[»]
1LB1X-ray2.81B/D/F/H1-190[»]
1OW3X-ray1.80B1-193[»]
1S1CX-ray2.60A/B1-181[»]
1TX4X-ray1.65B3-179[»]
1X86X-ray3.22B/D/F/H1-193[»]
1XCGX-ray2.50B/F3-180[»]
2RGNX-ray3.50C/F1-193[»]
3KZ1X-ray2.70E/F1-181[»]
3LW8X-ray1.85A/B/C/D2-181[»]
3LWNX-ray2.28A/B2-181[»]
3LXRX-ray1.68A2-181[»]
3MSXX-ray1.65A1-180[»]
3T06X-ray2.84B/F3-180[»]
4D0NX-ray2.10A1-184[»]
4XH9X-ray2.00B/E2-180[»]
4XOIX-ray2.09A/C1-180[»]
4XSGX-ray1.80A1-179[»]
4XSHX-ray2.50A1-179[»]
5A0FX-ray2.00A1-181[»]
5BWMX-ray2.50A1-179[»]
5C2KX-ray1.42A1-193[»]
5C4MX-ray1.30A1-193[»]
5EZ6X-ray1.80B1-181[»]
5FR1X-ray2.75A1-193[»]
5FR2X-ray3.35A1-193[»]
5HPYX-ray2.40B/F3-181[»]
5IRCX-ray1.72D/F2-181[»]
5JCPX-ray2.10A/B1-181[»]
5JHGX-ray2.50B/F1-181[»]
5JHHX-ray2.30B/F1-181[»]
5M6XX-ray2.40B/I2-193[»]
5M70X-ray2.20B/G2-193[»]
5ZHXX-ray3.50e/f/g/h1-193[»]
6BC0X-ray2.20F1-181[»]
6BCAX-ray2.00C/F1-181[»]
6BCBX-ray1.40F1-181[»]
6R3VX-ray1.75B1-193[»]
SMRiP61586
ModBaseiSearch...

Protein-protein interaction databases

BioGridi106880, 189 interactors
CORUMiP61586
DIPiDIP-29642N
IntActiP61586, 84 interactors
MINTiP61586
STRINGi9606.ENSP00000400175

Chemistry databases

BindingDBiP61586
ChEMBLiCHEMBL6052
DrugBankiDB04315 Guanosine-5'-Diphosphate

PTM databases

iPTMnetiP61586
PhosphoSitePlusiP61586
SwissPalmiP61586

Polymorphism and mutation databases

BioMutaiRHOA
DMDMi47606458

Proteomic databases

EPDiP61586
jPOSTiP61586
MaxQBiP61586
PaxDbiP61586
PeptideAtlasiP61586
PRIDEiP61586
ProteomicsDBi57321
TopDownProteomicsiP61586

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
387
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000418115; ENSP00000400175; ENSG00000067560
GeneIDi387
KEGGihsa:387
UCSCiuc003cwu.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
387
DisGeNETi387

GeneCards: human genes, protein and diseases

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GeneCardsi
RHOA
HGNCiHGNC:667 RHOA
HPAiCAB005052
MIMi165390 gene
neXtProtiNX_P61586
OpenTargetsiENSG00000067560
PharmGKBiPA134865095

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0393 Eukaryota
COG1100 LUCA
GeneTreeiENSGT00950000182945
HOGENOMiHOG000233974
InParanoidiP61586
KOiK04513
OMAiDLRFDQK
OrthoDBi1166960at2759
PhylomeDBiP61586
TreeFamiTF300837

Enzyme and pathway databases

ReactomeiR-HSA-114604 GPVI-mediated activation cascade
R-HSA-193634 Axonal growth inhibition (RHOA activation)
R-HSA-194840 Rho GTPase cycle
R-HSA-198203 PI3K/AKT activation
R-HSA-209563 Axonal growth stimulation
R-HSA-2173791 TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-HSA-392451 G beta:gamma signalling through PI3Kgamma
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-3928663 EPHA-mediated growth cone collapse
R-HSA-4086400 PCP/CE pathway
R-HSA-416482 G alpha (12/13) signalling events
R-HSA-416550 Sema4D mediated inhibition of cell attachment and migration
R-HSA-416572 Sema4D induced cell migration and growth-cone collapse
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-5625740 RHO GTPases activate PKNs
R-HSA-5625900 RHO GTPases activate CIT
R-HSA-5625970 RHO GTPases activate KTN1
R-HSA-5627117 RHO GTPases Activate ROCKs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-5666185 RHO GTPases Activate Rhotekin and Rhophilins
R-HSA-5689896 Ovarian tumor domain proteases
R-HSA-6785631 ERBB2 Regulates Cell Motility
R-HSA-6798695 Neutrophil degranulation
R-HSA-8849471 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-HSA-8985586 SLIT2:ROBO1 increases RHOA activity
SignaLinkiP61586
SIGNORiP61586

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
RHOA human
EvolutionaryTraceiP61586

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
RHOA

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
387
PMAP-CutDBiP61586

Protein Ontology

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PROi
PR:P61586

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000067560 Expressed in 243 organ(s), highest expression level in metanephric glomerulus
ExpressionAtlasiP61586 baseline and differential
GenevisibleiP61586 HS

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
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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_HUMAN
<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: P61586
Secondary accession number(s): P06749
, Q53HM4, Q5U024, Q9UDJ0, 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_and_isoforms">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: July 3, 2019
This is version 187 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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