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Entry version 194 (16 Oct 2019)
Sequence version 3 (03 Oct 2012)
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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_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

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_section">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_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 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

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

Enzyme and pathway databases

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_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:
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_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:ARHGAP35Imported
Synonyms:GRF11 Publication, GRLF11 Publication, KIAA1722, P190A1 Publication, p190ARHOGAP1 Publication
<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)Imported
<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: Unplaced

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:4591 ARHGAP35

Online Mendelian Inheritance in Man (OMIM)

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MIMi
605277 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9NRY4

<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, 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_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>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

Polymorphism and mutation 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.<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_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

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

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EPDi
Q9NRY4

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9NRY4

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9NRY4

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

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PaxDbi
Q9NRY4

PeptideAtlas

More...
PeptideAtlasi
Q9NRY4

PRoteomics IDEntifications database

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PRIDEi
Q9NRY4

ProteomicsDB: a multi-organism proteome resource

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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 226 organ(s), highest expression level in frontal cortex

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9NRY4 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB037311
HPA055184
HPA056470

<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 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, 20 interactors

Database of interacting proteins

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DIPi
DIP-34578N

Protein interaction database and analysis system

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IntActi
Q9NRY4, 8 interactors

Molecular INTeraction database

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MINTi
Q9NRY4

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000385720

<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

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

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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_and_domains_section">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
Regioni1213 – 1236Required for phospholipid binding and regulation of the substrate preference1 PublicationAdd BLAST24

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 biasi1440 – 1490Pro-richAdd BLAST51

<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

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eggNOGi
KOG4271 Eukaryota
ENOG410XR4E LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000182819

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9NRY4

KEGG Orthology (KO)

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KOi
K05732

Identification of Orthologs from Complete Genome Data

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OMAi
WAPGSDG

Database of Orthologous Groups

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OrthoDBi
110157at2759

TreeFam database of animal gene trees

More...
TreeFami
TF324451

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.10.440, 2 hits
1.10.555.10, 1 hit

Integrated resource of protein families, domains and functional sites

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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

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

Superfamily database of structural and functional annotation

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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_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>Sequencei

<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.

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

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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
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

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CCDSi
CCDS46127.1

NCBI Reference Sequences

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

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
2909

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:2909

UCSC genome browser

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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

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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
2K85NMR-A267-331[»]
3C5HX-ray1.80A13-249[»]
3FK2X-ray2.80A/B/C/D1212-1439[»]
SMRiQ9NRY4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi109166, 20 interactors
DIPiDIP-34578N
IntActiQ9NRY4, 8 interactors
MINTiQ9NRY4
STRINGi9606.ENSP00000385720

PTM databases

iPTMnetiQ9NRY4
PhosphoSitePlusiQ9NRY4

Polymorphism and mutation databases

BioMutaiARHGAP35
DMDMi408360250

Proteomic databases

EPDiQ9NRY4
jPOSTiQ9NRY4
MassIVEiQ9NRY4
PaxDbiQ9NRY4
PeptideAtlasiQ9NRY4
PRIDEiQ9NRY4
ProteomicsDBi82441

Genome annotation databases

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
HPAiCAB037311
HPA055184
HPA056470
MIMi605277 gene
neXtProtiNX_Q9NRY4
OpenTargetsiENSG00000160007
PharmGKBiPA28988

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4271 Eukaryota
ENOG410XR4E LUCA
GeneTreeiENSGT00950000182819
InParanoidiQ9NRY4
KOiK05732
OMAiWAPGSDG
OrthoDBi110157at2759
TreeFamiTF324451

Enzyme and pathway databases

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

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

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GeneWikii
GRLF1

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

More...
GenomeRNAii
2909
PharosiQ9NRY4

Protein Ontology

More...
PROi
PR:Q9NRY4

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000160007 Expressed in 226 organ(s), highest expression level in frontal cortex
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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_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: April 4, 2003
Last sequence update: October 3, 2012
Last modified: October 16, 2019
This is version 194 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, Complete proteome, Reference proteome

Documents

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