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UniProtKB - Q9NRY4 (RHG35_HUMAN)

Entry version 205 (02 Jun 2021)
Sequence version 3 (03 Oct 2012)
Previous versions | rss
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Protein

Rho GTPase-activating protein 35

Gene

ARHGAP35

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

Rho GTPase-activating protein (GAP) (PubMed:19673492, PubMed:28894085).

Binds several acidic phospholipids which inhibits the Rho GAP activity to promote the Rac GAP activity (PubMed:19673492).

This binding is inhibited by phosphorylation by PRKCA (PubMed:19673492).

Involved in cell differentiation as well as cell adhesion and migration, plays an important role in retinal tissue morphogenesis, neural tube fusion, midline fusion of the cerebral hemispheres and mammary gland branching morphogenesis (By similarity).

Transduces signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP) (By similarity).

Transduces SRC-dependent signals from cell-surface adhesion molecules, such as laminin, to promote neurite outgrowth. Regulates axon outgrowth, guidance and fasciculation (By similarity).

Modulates Rho GTPase-dependent F-actin polymerization, organization and assembly, is involved in polarized cell migration and in the positive regulation of ciliogenesis and cilia elongation (By similarity).

During mammary gland development, is required in both the epithelial and stromal compartments for ductal outgrowth (By similarity).

Represses transcription of the glucocorticoid receptor by binding to the cis-acting regulatory sequence 5'-GAGAAAAGAAACTGGAGAAACTC-3'; this function is however unclear and would need additional experimental evidences (PubMed:1894621).

By similarity3 Publications

<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

Binding of acidic phospholipids inhibits the Rho GAP activity and promotes the Rac GAP activity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei28GTPCombined sources1 Publication1
Binding sitei52GTP; via carbonyl oxygenCombined sources1 Publication1
Binding sitei56GTPCombined sources1 Publication1

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 bindingi33 – 37GTPCombined sources1 Publication5
Nucleotide bindingi95 – 97GTPCombined sources1 Publication3
Nucleotide bindingi201 – 203GTPCombined sources1 Publication3
Nucleotide bindingi229 – 231GTPCombined sources1 Publication3

<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

  • DNA binding Source: UniProtKB-KW
  • GTPase activator activity Source: UniProtKB
  • GTPase activity Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • phospholipid binding Source: UniProtKB
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionDNA-binding, GTPase activation, Repressor
Biological processTranscription, Transcription regulation
LigandGTP-binding, Lipid-binding, Nucleotide-binding

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q9NRY4

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-194840, Rho GTPase cycle
R-HSA-416550, Sema4D mediated inhibition of cell attachment and migration
R-HSA-8849471, PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases

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

More...SignaLinki		Q9NRY4

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q9NRY4

<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:
Rho GTPase-activating protein 35Imported
Alternative name(s):
Glucocorticoid receptor DNA-binding factor 1
Glucocorticoid receptor repression factor 1
Short name:
GRF-1
Rho GAP p190A
Short name:
p190-A1 Publication
<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:ARHGAP35Imported
Synonyms:GRF11 Publication, GRLF11 Publication, KIAA1722, P190A1 Publication, p190ARHOGAP1 Publication
<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>OrganismiHomo sapiens (Human)Imported
<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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:4591, ARHGAP35

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		605277, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9NRY4

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000160007.17

<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

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi1221S → A: No effect on total phosphorylation levels. Abolishes inhibition of phospholipid binding by PRKCA phosphorylation. Decreases phosphorylation by PRKCA; when associated with A-1226. Abolishes phosphorylation by PRKCA; when associated with A-1126 and A-1236. 1 Publication1
Mutagenesisi1221S → D: Enhances Rac GAP activity. 1 Publication1
Mutagenesisi1226T → A: No effect on total phosphorylation levels. Abolishes inhibition of phospholipid binding by PRKCA phosphorylation. Decreases phosphorylation by PRKCA; when associated with A-1221. Abolishes phosphorylation by PRKCA; when associated with A-1121 and A-1236. 1 Publication1
Mutagenesisi1226T → D: Enhances Rac GAP activity. 1 Publication1
Mutagenesisi1236S → A: No effect on total phosphorylation levels. No effect on inhibition of phospholipid binding by PRKCA phosphorylation. Abolishes phosphorylation by PRKCA; when associated with A-1121 and A-1226. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		2909

Open Targets

More...OpenTargetsi		ENSG00000160007

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA28988

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9NRY4, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4523646

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		ARHGAP35

Domain mapping of disease mutations (DMDM)

More...DMDMi		408360250

<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_00000567301 – 1499Rho GTPase-activating protein 35Add BLAST1499

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 residuei308Phosphotyrosine1 Publication1
Modified residuei589PhosphoserineCombined sources1
Modified residuei770PhosphoserineCombined sources1
Modified residuei773PhosphoserineCombined sources1
Modified residuei970PhosphoserineCombined sources1
Modified residuei975PhosphoserineCombined sources1
Modified residuei985PhosphoserineBy similarity1
Modified residuei1001PhosphoserineCombined sources1
Modified residuei1072PhosphoserineCombined sources1
Modified residuei1087PhosphotyrosineCombined sources1
Modified residuei1105Phosphotyrosine; by ABL2 and PTK6Combined sources1 Publication1
Modified residuei1134PhosphoserineCombined sources1
Modified residuei1142PhosphoserineBy similarity1
Modified residuei1150PhosphoserineCombined sources1
Modified residuei1176PhosphoserineCombined sources1
Modified residuei1179PhosphoserineCombined sources1
Modified residuei1221Phosphoserine; by PKC/PRKCA1 Publication1
Modified residuei1226Phosphothreonine; by PKC/PRKCA1 Publication1
Modified residuei1236Phosphoserine; by PKC/PRKCA1 Publication1
Modified residuei1472PhosphoserineBy similarity1
Modified residuei1476PhosphoserineBy similarity1
Modified residuei1480PhosphothreonineBy similarity1
Modified residuei1483PhosphoserineBy similarity1

<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 of Tyr-1105 by PTK6 promotes the association with RASA1, inactivating RHOA while activating RAS. Phosphorylation at Tyr-308 by PDGFRA inhibits binding to GTF2I (PubMed:18829532, PubMed:19393245). Phosphorylated by PRKCA at Ser-1221 and Thr-1226, induces relocalization from the cytoplasm to regions of plasma membrane ruffling and prevents the binding and substrate specificity regulation by phospholipids (PubMed:19673492). In brain, phosphorylated by FYN and SRC (By similarity). During focal adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and Ser-1483. Phosphorylation by MAPK1 and MAPK3 inhibits GAP function and localizes ARGHAP35 away from newly forming focal adhesions and stress fibers in cells spreading on fibronectin (By similarity). Phosphorylation at Ser-1476 and Thr-1480 by GSK3B requires priming by MAPK and inhibits RhoGAP activity and modulates polarized cell migration (By similarity).By similarity3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q9NRY4

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9NRY4

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9NRY4

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

More...PaxDbi		Q9NRY4

PeptideAtlas

More...PeptideAtlasi		Q9NRY4

PRoteomics IDEntifications database

More...PRIDEi		Q9NRY4

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		82441

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9NRY4

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

More...PhosphoSitePlusi		Q9NRY4

<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

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in neutrophils (at protein level).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000160007, Expressed in frontal cortex and 242 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9NRY4, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000160007, Low tissue specificity

<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 RASA1 (By similarity).

Interacts with the general transcription factor GTF2I, the interaction sequesters GTF2I in the cytoplasm (PubMed:19393245).

By similarity1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		109166, 56 interactors

Database of interacting proteins

More...DIPi		DIP-34578N

Protein interaction database and analysis system

More...IntActi		Q9NRY4, 21 interactors

Molecular INTeraction database

More...MINTi		Q9NRY4

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000385720

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q9NRY4

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9NRY4, protein

<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

11499
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		Q9NRY4

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

More...SMRi		Q9NRY4

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9NRY4

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini270 – 327FF 1Add BLAST58
Domaini368 – 422FF 2Add BLAST55
Domaini429 – 483FF 3Add BLAST55
Domaini485 – 550FF 4Add BLAST66
Domaini592 – 767pG1 pseudoGTPasePROSITE-ProRule annotationAdd BLAST176
Domaini783 – 947pG2 pseudoGTPasePROSITE-ProRule annotationAdd BLAST165
Domaini1249 – 1436Rho-GAPPROSITE-ProRule annotationAdd BLAST188

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 266Has GTPase activity, required for proper localizationBy similarityAdd BLAST266
Regioni1058 – 1089DisorderedSequence analysisAdd BLAST32
Regioni1124 – 1146DisorderedSequence analysisAdd BLAST23
Regioni1177 – 1207DisorderedSequence analysisAdd BLAST31
Regioni1213 – 1236Required for phospholipid binding and regulation of the substrate preference1 PublicationAdd BLAST24
Regioni1446 – 1499DisorderedSequence analysisAdd BLAST54

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1124 – 1139Polar residuesSequence analysisAdd BLAST16
Compositional biasi1182 – 1196Basic and acidic residuesSequence analysisAdd BLAST15
Compositional biasi1451 – 1469Polar residuesSequence analysisAdd BLAST19
Compositional biasi1470 – 1486Pro residuesSequence analysisAdd BLAST17

<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

N-terminal part (1-266) has GTPase activity. Required for proper cellular localization.By similarity
The pG1 pseudoGTPase domain does not bind GTP.1 Publication

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4271, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT01030000234635

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_004268_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9NRY4

Identification of Orthologs from Complete Genome Data

More...OMAi		WAPGSDG

Database of Orthologous Groups

More...OrthoDBi		110157at2759

TreeFam database of animal gene trees

More...TreeFami		TF324451

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.10.440, 2 hits
1.10.555.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002713, FF_domain
IPR036517, FF_domain_sf
IPR027417, P-loop_NTPase
IPR039007, pG1
IPR008936, Rho_GTPase_activation_prot
IPR032835, RhoGAP-FF1
IPR000198, RhoGAP_dom
IPR039006, RhoGAP_pG2
IPR001806, Small_GTPase

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01846, FF, 1 hit
PF00071, Ras, 1 hit
PF00620, RhoGAP, 1 hit
PF16512, RhoGAP-FF1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00441, FF, 4 hits
SM00324, RhoGAP, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48350, SSF48350, 1 hit
SSF52540, SSF52540, 1 hit
SSF81698, SSF81698, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51676, FF, 4 hits
PS51852, PG1, 1 hit
PS51853, PG2, 1 hit
PS50238, RHOGAP, 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.

Q9NRY4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF 
        60         70         80         90        100
HLDHTSVLST SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI 
       110        120        130        140        150
DDQTFQPHRS TALQPYIKRA AATKLASAEK LMYFCTDQLG LEQDFEQKQM 
       160        170        180        190        200
PDGKLLVDGF LLGIDVSRGM NRNFDDQLKF VSNLYNQLAK TKKPIVVVLT 
       210        220        230        240        250
KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF STLVQLIDKS 
       260        270        280        290        300
RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKNHNE NWLSVSRKMQ 
       310        320        330        340        350
ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA 
       360        370        380        390        400
LIPNLDEIDH LSCIKAKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE 
       410        420        430        440        450
RIPFDLMDTV PAEQLYEAHL EKLRNERKRV EMRRAFKENL ETSPFITPGK 
       460        470        480        490        500
PWEEARSFIM NEDFYQWLEE SVYMDIYGKH QKQIIDKAKE EFQELLLEYS 
       510        520        530        540        550
ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER DALILKHIHF 
       560        570        580        590        600
VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDPNIDRINL 
       610        620        630        640        650
VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS 
       660        670        680        690        700
FQTPTFQPHG CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL 
       710        720        730        740        750
ILVNKRGDTS GETLHSLIQQ GQQIASKLQC VFLDPASAGI GYGRNINEKQ 
       760        770        780        790        800
ISQVLKGLLD SKRNLNLVSS TASIKDLADV DLRIVMCLMC GDPFSADDIL 
       810        820        830        840        850
FPVLQSQTCK SSHCGSNNSV LLELPIGLHK KRIELSVLSY HSSFSIRKSR 
       860        870        880        890        900
LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAVDVLDNDL 
       910        920        930        940        950
SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LEIFHPFFKD VVEKKNIIEA 
       960        970        980        990       1000
THMYDNAAEA CSTTEEVFNS PRAGSPLCNS NLQDSEEDIE PSYSLFREDT 
      1010       1020       1030       1040       1050
SLPSLSKDHS KLSMELEGND GLSFIMSNFE SKLNNKVPPP VKPKPPVHFE 
      1060       1070       1080       1090       1100
ITKGDLSYLD QGHRDGQRKS VSSSPWLPQD GFDPSDYAEP MDAVVKPRNE 
      1110       1120       1130       1140       1150
EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT SSLERGRKVS 
      1160       1170       1180       1190       1200
IVSKPVLYRT RCTRLGRFAS YRTSFSVGSD DELGPIRKKE EDQASQGYKG 
      1210       1220       1230       1240       1250
DNAVIPYETD EDPRRRNILR SLRRNTKKPK PKPRPSITKA TWESNYFGVP 
      1260       1270       1280       1290       1300
LTTVVTPEKP IPIFIERCIE YIEATGLSTE GIYRVSGNKS EMESLQRQFD 
      1310       1320       1330       1340       1350
QDHNLDLAEK DFTVNTVAGA MKSFFSELPD PLVPYNMQID LVEAHKINDR 
      1360       1370       1380       1390       1400
EQKLHALKEV LKKFPKENHE VFKYVISHLN KVSHNNKVNL MTSENLSICF 
      1410       1420       1430       1440       1450
WPTLMRPDFS TMDALTATRT YQTIIELFIQ QCPFFFYNRP ITEPPGARPS 
      1460       1470       1480       1490 
SPSAVASTVP FLTSTPVTSQ PSPPQSPPPT PQSPMQPLLP SQLQAEHTL
Length:1,499
Mass (Da):170,514
Last modified:October 3, 2012 - v3
<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:i8CCB493414A7E3E6
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAA58618 differs from that shown. Reason: Frameshift.Curated
The sequence AAF80386 differs from that shown. Unlikely isoform. Aberrant splice sites.Curated
The sequence AAF80386 differs from that shown. Reason: Frameshift.Curated

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 conflicti251R → P in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti309V → D in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti362S → G in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti414Q → A in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti414Q → A in AAA58618 (PubMed:1894621).Curated1
Sequence conflicti474M → T in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti474M → T in AAA58618 (PubMed:1894621).Curated1
Sequence conflicti978C → S in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti1292M → I in AAF80386 (PubMed:11054565).Curated1
Sequence conflicti1452 – 1453PS → RN in AAA58618 (PubMed:1894621).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AB051509 mRNA Translation: BAB21813.2
CH471126 Genomic DNA Translation: EAW57450.1
BC150257 mRNA Translation: AAI50258.1
AF159851 mRNA Translation: AAF80386.1 Sequence problems.
M73077 mRNA Translation: AAA58618.1 Frameshift.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS46127.1

NCBI Reference Sequences

More...RefSeqi		NP_004482.4, NM_004491.4
XP_016882203.1, XM_017026714.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000404338; ENSP00000385720; ENSG00000160007
ENST00000614079; ENSP00000483730; ENSG00000160007
ENST00000672722; ENSP00000500409; ENSG00000160007

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2909

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2909

UCSC genome browser

More...UCSCi		uc010ekv.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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB051509 mRNA Translation: BAB21813.2
CH471126 Genomic DNA Translation: EAW57450.1
BC150257 mRNA Translation: AAI50258.1
AF159851 mRNA Translation: AAF80386.1 Sequence problems.
M73077 mRNA Translation: AAA58618.1 Frameshift.
CCDSiCCDS46127.1
RefSeqiNP_004482.4, NM_004491.4
XP_016882203.1, XM_017026714.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K85NMR-A267-331[»]
3C5HX-ray1.80A13-249[»]
3FK2X-ray2.80A/B/C/D1212-1439[»]
6PXCX-ray1.60U1100-1112[»]
6WAYX-ray1.50V1086-1093[»]
BMRBiQ9NRY4
SMRiQ9NRY4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi109166, 56 interactors
DIPiDIP-34578N
IntActiQ9NRY4, 21 interactors
MINTiQ9NRY4
STRINGi9606.ENSP00000385720

Chemistry databases

BindingDBiQ9NRY4
ChEMBLiCHEMBL4523646

PTM databases

iPTMnetiQ9NRY4
PhosphoSitePlusiQ9NRY4

Genetic variation databases

BioMutaiARHGAP35
DMDMi408360250

Proteomic databases

EPDiQ9NRY4
jPOSTiQ9NRY4
MassIVEiQ9NRY4
PaxDbiQ9NRY4
PeptideAtlasiQ9NRY4
PRIDEiQ9NRY4
ProteomicsDBi82441

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		31509, 268 antibodies

The DNASU plasmid repository

More...DNASUi		2909

Genome annotation databases

EnsembliENST00000404338; ENSP00000385720; ENSG00000160007
ENST00000614079; ENSP00000483730; ENSG00000160007
ENST00000672722; ENSP00000500409; ENSG00000160007
GeneIDi2909
KEGGihsa:2909
UCSCiuc010ekv.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2909
DisGeNETi2909

GeneCards: human genes, protein and diseases

More...GeneCardsi		ARHGAP35
HGNCiHGNC:4591, ARHGAP35
HPAiENSG00000160007, Low tissue specificity
MIMi605277, gene
neXtProtiNX_Q9NRY4
OpenTargetsiENSG00000160007
PharmGKBiPA28988
VEuPathDBiHostDB:ENSG00000160007.17

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG4271, Eukaryota
GeneTreeiENSGT01030000234635
HOGENOMiCLU_004268_0_0_1
InParanoidiQ9NRY4
OMAiWAPGSDG
OrthoDBi110157at2759
TreeFamiTF324451

Enzyme and pathway databases

PathwayCommonsiQ9NRY4
ReactomeiR-HSA-194840, Rho GTPase cycle
R-HSA-416550, Sema4D mediated inhibition of cell attachment and migration
R-HSA-8849471, PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
SignaLinkiQ9NRY4
SIGNORiQ9NRY4

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		2909, 24 hits in 1003 CRISPR screens

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

More...ChiTaRSi		ARHGAP35, human
EvolutionaryTraceiQ9NRY4

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		GRLF1

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

More...GenomeRNAii		2909
PharosiQ9NRY4, Tbio

Protein Ontology

More...PROi		PR:Q9NRY4
RNActiQ9NRY4, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000160007, Expressed in frontal cortex and 242 other tissues
GenevisibleiQ9NRY4, HS

Family and domain databases

Gene3Di1.10.10.440, 2 hits
1.10.555.10, 1 hit
InterProiView protein in InterPro
IPR002713, FF_domain
IPR036517, FF_domain_sf
IPR027417, P-loop_NTPase
IPR039007, pG1
IPR008936, Rho_GTPase_activation_prot
IPR032835, RhoGAP-FF1
IPR000198, RhoGAP_dom
IPR039006, RhoGAP_pG2
IPR001806, Small_GTPase
PfamiView protein in Pfam
PF01846, FF, 1 hit
PF00071, Ras, 1 hit
PF00620, RhoGAP, 1 hit
PF16512, RhoGAP-FF1, 1 hit
SMARTiView protein in SMART
SM00441, FF, 4 hits
SM00324, RhoGAP, 1 hit
SUPFAMiSSF48350, SSF48350, 1 hit
SSF52540, SSF52540, 1 hit
SSF81698, SSF81698, 1 hit
PROSITEiView protein in PROSITE
PS51676, FF, 4 hits
PS51852, PG1, 1 hit
PS51853, PG2, 1 hit
PS50238, RHOGAP, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...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 nameiRHG35_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: Q9NRY4
Secondary accession number(s): A7E2A4, Q14452, Q9C0E1
<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: April 4, 2003
Last sequence update: October 3, 2012
Last modified: June 2, 2021
This is version 205 of the entry and version 3 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, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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