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Entry version 169 (17 Jun 2020)
Sequence version 3 (09 Jan 2007)
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Protein

Rho GTPase-activating protein 35

Gene

Arhgap35

Organism
Mus musculus (Mouse)
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). Binds several acidic phospholipids which inhibits the Rho GAP activity to promote the Rac GAP activity (PubMed:16971514). This binding is inhibited by phosphorylation by PRKCA (By similarity). 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 (PubMed:11044403, PubMed:11283609, PubMed:18502760, PubMed:21945077). Transduces signals from p21-ras to the nucleus, acting via the ras GTPase-activating protein (GAP) (PubMed:16971514). Transduces SRC-dependent signals from cell-surface adhesion molecules, such as laminin, to promote neurite outgrowth. Regulates axon outgrowth, guidance and fasciculation (PubMed:11283609). 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 (PubMed:11044403, PubMed:26859289, PubMed:18502760). During mammary gland development, is required in both the epithelial and stromal compartments for ductal outgrowth (PubMed:21945077). 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 (By similarity).By similarity6 Publications

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 sitei28GTPBy similarity1
Binding sitei52GTP; via carbonyl oxygenBy similarity1
Binding sitei56GTPBy similarity1

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 – 37GTPBy similarity5
Nucleotide bindingi95 – 97GTPBy similarity3
Nucleotide bindingi201 – 203GTPBy similarity3
Nucleotide bindingi229 – 231GTPBy similarity3

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

<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
<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:Grlf1, 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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1929494 Arhgap35

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Deficiency leads to perinatal lethality and defective neural development. One third of the fetuses show exencephaly and spina bifida as well as defective kidney development.1 Publication

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>Mutagenesisi1396L → Q in ENU mutant Arhgap35-D34; mutant animals show hypodysplastic kidneys and neural tube closure defects; the number of ciliated cells and cilia average length are drastically reduced in the proximal tubules. Results in loss of activation of GTP hydrolysis. 1 Publication1
Mutagenesisi1472S → A: Reduces phosphorylation by GSK3B by 50%. No effect on polarized cell migration. 1 Publication1
Mutagenesisi1476S → A: Abolishes phosphorylation by GSK3B. Reduces phosphorylation by MAPK. Affects polarized cell migration. Increases RhoGAP catalytic activity. 1 Publication1
Mutagenesisi1480T → A: Abolishes phosphorylation by GSK3B. Reduces phosphorylation by MAPK. Affects polarized cell migration. Increases RhoGAP catalytic activity. 1 Publication1
Mutagenesisi1483S → A: Abolishes phosphorylation by GSK3B. Reduces phosphorylation by MAPK. No effect on polarized cell migration. 1 Publication1

<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_00000567311 – 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 residuei308PhosphotyrosineBy similarity1
Modified residuei589PhosphoserineCombined sources1
Modified residuei770PhosphoserineBy similarity1
Modified residuei773PhosphoserineCombined sources1
Modified residuei970PhosphoserineCombined sources1
Modified residuei975PhosphoserineCombined sources1
Modified residuei985PhosphoserineCombined sources1
Modified residuei1072PhosphoserineBy similarity1
Modified residuei1087PhosphotyrosineCombined sources1
Modified residuei1105Phosphotyrosine; by ABL2 and PTK6Combined sources1 Publication1
Modified residuei1134PhosphoserineCombined sources1
Modified residuei1142PhosphoserineCombined sources1
Modified residuei1150PhosphoserineBy similarity1
Modified residuei1176PhosphoserineBy similarity1
Modified residuei1179PhosphoserineCombined sources1
Modified residuei1221PhosphoserineBy similarity1
Modified residuei1226PhosphothreonineBy similarity1
Modified residuei1236PhosphoserineBy similarity1
Modified residuei1472Phosphoserine1 Publication1
Modified residuei1476Phosphoserine1 Publication1
Modified residuei1480Phosphothreonine1 Publication1
Modified residuei1483Phosphoserine1 Publication1

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

Phosphorylation 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 (By similarity). 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:11044403). In brain, phosphorylated by FYN and SRC (PubMed:11283609). 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 (PubMed:18502760).By similarity3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q91YM2

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q91YM2

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

More...
PaxDbi
Q91YM2

PRoteomics IDEntifications database

More...
PRIDEi
Q91YM2

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q91YM2

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

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PhosphoSitePlusi
Q91YM2

<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

Expressed in the developing kidneys (PubMed:26859289). Expressed in all regions of the mature nervous system (at protein level) (PubMed:11044403). Detected in neutrophils (at protein level) (PubMed:20675588).3 Publications

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

At 12.5 dpc, the highest level of expression is in the spinal cord and lower expression levels are seen in the developing brain. At 15.5 dpc, highly expressed in brain, spinal cord and eyes (PubMed:11044403). In developing kidney, at 17.5 dpc, low expression is observed in the glomerulus, while high expression levels are detected in the proximal tubule (PubMed:26859289). At 14.5 dpc, is expressed within the epithelial compartment of the embryonic mammary bud and at lower level in the surrounding stroma and skin. Also expressed at terminal end bunds (TEB) at comparable levels in body and cap cells as well as in fibroblasts and stroma surrounding the TEB (PubMed:21945077).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000058230 Expressed in ear vesicle and 284 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q91YM2 MM

<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 the general transcription factor GTF2I, the interaction sequesters GTF2I in the cytoplasm (By similarity).

Interacts with RASA1 (PubMed:16971514).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
231317, 1 interactor

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q91YM2

Protein interaction database and analysis system

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IntActi
Q91YM2, 2 interactors

Molecular INTeraction database

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MINTi
Q91YM2

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000075242

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q91YM2 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

3D structure databases

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

More...
SMRi
Q91YM2

Database of comparative protein structure models

More...
ModBasei
Search...

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

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 localization1 PublicationAdd BLAST266
Regioni1213 – 1236Required for phospholipid binding and regulation of the substrate preferenceBy similarityAdd 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 – 1487Pro-richAdd BLAST48

<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. Mutation of this region is a severely defective loss of function. Mutants have defective morphogenesis of neural retinal tissue, agenesis of the corpus callosum due to defectuous midline fusion of the cerebral hemispheres (PubMed:11044403). Mutants show defects in axon guidance and fasciculation (PubMed:11283609).2 Publications
The pG1 pseudoGTPase domain does not bind GTP.By similarity

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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_004268_0_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q91YM2

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

Database for complete collections of gene phylogenies

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PhylomeDBi
Q91YM2

TreeFam database of animal gene trees

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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

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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

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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.

Q91YM2-1 [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 NWPSVSRKMQ
310 320 330 340 350
ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA
360 370 380 390 400
LIPNLDEVDH LSCIKAKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE
410 420 430 440 450
RIPFDLMDTV PAEQLYETHL EKLRNERKRA EMRRAFKENL ETSPFITPGK
460 470 480 490 500
PWEEARSFIM NEDFYQWLEE SVYMDIYGKH QKQIIDRAKE EFQELLLEYS
510 520 530 540 550
ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER DALILKHIHF
560 570 580 590 600
VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDLNIDRINL
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 GDPFSADDVL
810 820 830 840 850
SPVLQSQTCK SSHCGSSNSV LLELPIGLHK KRIELSVLSY HSSFSIRKSR
860 870 880 890 900
LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAIDVLDNDL
910 920 930 940 950
SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LELFHPFFKD VVEKKNIIEA
960 970 980 990 1000
THMYDNVAEA CSTTEEVFNS PRAGSPLCNS NLQDSEEDVE PPSYHLFRED
1010 1020 1030 1040 1050
ATLPSLSKDH SKFSMELEGN DGLSFIMSNF ESKLNNKVPP PVKPKPPVHF
1060 1070 1080 1090 1100
DITKDLSYLD QGHREGQRKS MSSSPWMPQD GFDPSDYAEP MDAVVKPRNE
1110 1120 1130 1140 1150
EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT SSLERGRKVS
1160 1170 1180 1190 1200
AVSKPVLYRT 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 PLVPYSMQID LVEAHKINDR
1360 1370 1380 1390 1400
EQKLHALKEV LKKFPKENHE VFKYVISHLN KVSHNNKVNL MTSENLSICF
1410 1420 1430 1440 1450
WPTLMRPDFS SMDALTATRS YQTIIELFIQ QCPFFFYNRP ISEPPGAAPG
1460 1470 1480 1490
SPSAMAPTVP FLTSTPATSQ PSPPQSPPPT PQSPMQPLLS SQLQAEHTL
Length:1,499
Mass (Da):170,393
Last modified:January 9, 2007 - 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:i7E13EC38257CE950
GO

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
AK147326 mRNA Translation: BAE27848.1
AK147688 mRNA Translation: BAE28076.1
AK173242 Transcribed RNA Translation: BAD32520.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS20851.1

NCBI Reference Sequences

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RefSeqi
NP_766327.3, NM_172739.4
XP_006539872.1, XM_006539809.3
XP_011248814.1, XM_011250512.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000075845; ENSMUSP00000075242; ENSMUSG00000058230
ENSMUST00000171937; ENSMUSP00000127379; ENSMUSG00000058230

Database of genes from NCBI RefSeq genomes

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GeneIDi
232906

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:232906

UCSC genome browser

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UCSCi
uc009fhw.1 mouse

<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
AK147326 mRNA Translation: BAE27848.1
AK147688 mRNA Translation: BAE28076.1
AK173242 Transcribed RNA Translation: BAD32520.1
CCDSiCCDS20851.1
RefSeqiNP_766327.3, NM_172739.4
XP_006539872.1, XM_006539809.3
XP_011248814.1, XM_011250512.2

3D structure databases

SMRiQ91YM2
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi231317, 1 interactor
CORUMiQ91YM2
IntActiQ91YM2, 2 interactors
MINTiQ91YM2
STRINGi10090.ENSMUSP00000075242

PTM databases

iPTMnetiQ91YM2
PhosphoSitePlusiQ91YM2

Proteomic databases

jPOSTiQ91YM2
MaxQBiQ91YM2
PaxDbiQ91YM2
PRIDEiQ91YM2

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
31509 255 antibodies

Genome annotation databases

EnsembliENSMUST00000075845; ENSMUSP00000075242; ENSMUSG00000058230
ENSMUST00000171937; ENSMUSP00000127379; ENSMUSG00000058230
GeneIDi232906
KEGGimmu:232906
UCSCiuc009fhw.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2909
MGIiMGI:1929494 Arhgap35

Rodent Unidentified Gene-Encoded large proteins database

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Rougei
Search...

Phylogenomic databases

eggNOGiKOG4271 Eukaryota
ENOG410XR4E LUCA
GeneTreeiENSGT00950000182819
HOGENOMiCLU_004268_0_0_1
InParanoidiQ91YM2
KOiK05732
OMAiWAPGSDG
OrthoDBi110157at2759
PhylomeDBiQ91YM2
TreeFamiTF324451

Enzyme and pathway databases

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

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
232906 1 hit in 12 CRISPR screens

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

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ChiTaRSi
Arhgap35 mouse

Protein Ontology

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PROi
PR:Q91YM2
RNActiQ91YM2 protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000058230 Expressed in ear vesicle and 284 other tissues
GenevisibleiQ91YM2 MM

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

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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 nameiRHG35_MOUSE
<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: Q91YM2
Secondary accession number(s): Q3UGY1, Q69ZC4
<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: January 9, 2007
Last modified: June 17, 2020
This is version 169 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

<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

Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
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