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Protein

Rac GTPase-activating protein 1

Gene

RACGAP1

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

Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells.13 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri286 – 335Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST50

<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 functionDevelopmental protein, GTPase activation
Biological processCell cycle, Cell division, Differentiation, Ion transport, Spermatogenesis, Transport
LigandLipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-194840 Rho GTPase cycle
R-HSA-2132295 MHC class II antigen presentation
R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-983189 Kinesins

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q9H0H5

<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:
Rac GTPase-activating protein 1
Alternative name(s):
Male germ cell RacGap
Short name:
MgcRacGAP
Protein CYK4 homolog
Short name:
CYK4
Short name:
HsCYK-4
<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:RACGAP1Imported
Synonyms:KIAA1478Imported, MGCRACGAP
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000161800.12

Human Gene Nomenclature Database

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HGNCi
HGNC:9804 RACGAP1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
604980 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9H0H5

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Microtubule, 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>Mutagenesisi149S → A: Does not inhibit interaction with ECT2. Reduces strongly phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-170. 1 Publication1
Mutagenesisi157S → A: Does not inhibit interaction with ECT2. Reduces strongly phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-164 and A-170. Reduces strongly phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-164; A-170 and A-214. 2 Publications1
Mutagenesisi164S → A: Does not inhibit interaction with ECT2. Reduces strongly phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-157 and A-170. Reduces strongly phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-170 and A-214. 2 Publications1
Mutagenesisi170S → A: Does not inhibit interaction with ECT2. Reduces strongly phosphorylation, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-149; A-157 and A-164. Reduces strongly phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-214. 2 Publications1
Mutagenesisi214S → A: Reduces strongly phosphorylation by PLK1, inhibits interaction with ECT2 and cleavage furrow formation; when associated with A-157; A-164 and A-170. 1 Publication1
Mutagenesisi289F → G: Cytokinesis failure. 1 Publication1
Mutagenesisi292K → L: Cytokinesis failure. Abolishes localization at the cell membrane. 1 Publication1
Mutagenesisi306R → L: Cytokinesis failure. Abolishes localization at the cell membrane. 1 Publication1
Mutagenesisi309F → A: Cytokinesis failure. Abolishes localization at the cell membrane. 1 Publication1
Mutagenesisi316C → G: Cytokinesis failure. 1 Publication1
Mutagenesisi385R → A: Abolishes GAP activity towards RAC1. Abolishes GAP activity towards CDC42 in prometaphase. Induces multiple blebs during cytokinesis. 3 Publications1

Organism-specific databases

DisGeNET

More...
DisGeNETi
29127

Open Targets

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OpenTargetsi
ENSG00000161800

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34165

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2146306

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
RACGAP1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
74762727

<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_00002288081 – 632Rac GTPase-activating protein 1Add BLAST632

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 residuei1N-acetylmethionineCombined sources1
Modified residuei149Phosphoserine; by PLK11 Publication1
Modified residuei154PhosphoserineCombined sources1
Modified residuei157Phosphoserine; by PLK1Combined sources2 Publications1
Modified residuei161PhosphothreonineCombined sources1
Modified residuei164Phosphoserine; by PLK1Combined sources2 Publications1
Modified residuei170Phosphoserine; by PLK12 Publications1
Modified residuei203PhosphoserineCombined sources1
Modified residuei206PhosphoserineCombined sources1
Modified residuei214PhosphoserineCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei249PhosphothreonineCombined sources1
Modified residuei257PhosphoserineCombined sources1
Modified residuei260Phosphothreonine1 Publication1
Modified residuei342PhosphothreonineCombined sources1
Modified residuei387Phosphoserine; by AURKB1 Publication1
Cross-linki404Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei410Phosphoserine; by AURKB1 Publication1
Modified residuei567PhosphothreonineCombined sources1
Modified residuei580PhosphothreonineCombined sources1
Modified residuei588PhosphothreonineCombined sources1
Modified residuei600PhosphoserineCombined sources1
Modified residuei601PhosphothreonineCombined sources1
Modified residuei606PhosphothreonineCombined sources1
Modified residuei628PhosphoserineCombined sources1

<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

Phosphorylated at multiple sites in the midbody during cytokinesis. Phosphorylation by AURKB on Ser-387 at the midbody is, at least in part, responsible for exerting its latent GAP activity towards RhoA. Phosphorylation on multiple serine residues by PLK1 enhances its association with ECT2 and is critical for cleavage furrow formation.3 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9H0H5

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9H0H5

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

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PaxDbi
Q9H0H5

PeptideAtlas

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PeptideAtlasi
Q9H0H5

PRoteomics IDEntifications database

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PRIDEi
Q9H0H5

ProteomicsDB human proteome resource

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ProteomicsDBi
80279

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9H0H5

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

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PhosphoSitePlusi
Q9H0H5

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
Q9H0H5

<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

Highly expressed in testis, thymus and placenta. Expressed at lower levels in spleen and peripheral blood lymphocytes. In testis, expression is restricted to germ cells with the highest levels of expression found in spermatocytes. Expression is regulated in a cell cycle-dependent manner and peaks during G2/M phase.4 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is down-regulated during macrophage differention of HL-60 cells.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000161800 Expressed in 207 organ(s), highest expression level in female gonad

CleanEx database of gene expression profiles

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CleanExi
HS_RACGAP1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9H0H5 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9H0H5 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB025859
HPA039427
HPA043912

<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

Heterotetramer of two molecules each of RACGAP1 and KIF23. Found in the centralspindlin complex composed of RACGAP1 and KIF23. Associates with alpha-, beta- and gamma-tubulin and microtubules. Interacts via its Rho-GAP domain with RND2. Associates with AURKB during M phase. Interacts via its Rho-GAP domain and basic region with PRC1. The interaction with PRC1 inhibits its GAP activity towards CDC42 in vitro, which may be required for maintaining normal spindle morphology. Interacts with SLC26A8 via its N-terminus. Interacts with RAB11FIP3. Interacts with ECT2; the interaction is direct, occurs at anaphase and during cytokinesis in a microtubule-dependent manner and is enhanced by phosphorylation by PLK1. Interacts with KIF23; the interaction is direct.12 Publications

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
118892, 95 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9H0H5

Database of interacting proteins

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DIPi
DIP-33087N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q9H0H5

Protein interaction database and analysis system

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IntActi
Q9H0H5, 88 interactors

Molecular INTeraction database

More...
MINTi
Q9H0H5

STRING: functional protein association networks

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STRINGi
9606.ENSP00000309871

<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

1632
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q9H0H5

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

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SMRi
Q9H0H5

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q9H0H5

<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>Domaini349 – 539Rho-GAPPROSITE-ProRule annotationAdd BLAST191

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>Regioni106 – 285Interaction with SLC26A81 PublicationAdd BLAST180

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili53 – 110Sequence analysisAdd BLAST58

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

The coiled coil region is indispensible for localization to the midbody during cytokinesis.1 Publication
The phorbol-ester/DAG-type zinc finger domain mediates interaction with membranes enriched in phosphatidylinositol 3,4,5-trisphosphate and is required during mitotic cytokinesis for normal attachment of the midbody to the cell membrane.

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri286 – 335Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST50

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3564 Eukaryota
ENOG410XPK0 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154610

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230702

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG062009

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9H0H5

KEGG Orthology (KO)

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KOi
K16733

Identification of Orthologs from Complete Genome Data

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OMAi
HELGKYK

Database of Orthologous Groups

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OrthoDBi
EOG091G03O7

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9H0H5

TreeFam database of animal gene trees

More...
TreeFami
TF318102

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00029 C1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.555.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002219 PE/DAG-bd
IPR008936 Rho_GTPase_activation_prot
IPR000198 RhoGAP_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00130 C1_1, 1 hit
PF00620 RhoGAP, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00109 C1, 1 hit
SM00324 RhoGAP, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48350 SSF48350, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50238 RHOGAP, 1 hit
PS00479 ZF_DAG_PE_1, 1 hit
PS50081 ZF_DAG_PE_2, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

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

This entry has 1 described isoform and 21 potential isoforms that are computationally mapped.Show allAlign All

Q9H0H5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDTMMLNVRN LFEQLVRRVE ILSEGNEVQF IQLAKDFEDF RKKWQRTDHE
60 70 80 90 100
LGKYKDLLMK AETERSALDV KLKHARNQVD VEIKRRQRAE ADCEKLERQI
110 120 130 140 150
QLIREMLMCD TSGSIQLSEE QKSALAFLNR GQPSSSNAGN KRLSTIDESG
160 170 180 190 200
SILSDISFDK TDESLDWDSS LVKTFKLKKR EKRRSTSRQF VDGPPGPVKK
210 220 230 240 250
TRSIGSAVDQ GNESIVAKTT VTVPNDGGPI EAVSTIETVP YWTRSRRKTG
260 270 280 290 300
TLQPWNSDST LNSRQLEPRT ETDSVGTPQS NGGMRLHDFV SKTVIKPESC
310 320 330 340 350
VPCGKRIKFG KLSLKCRDCR VVSHPECRDR CPLPCIPTLI GTPVKIGEGM
360 370 380 390 400
LADFVSQTSP MIPSIVVHCV NEIEQRGLTE TGLYRISGCD RTVKELKEKF
410 420 430 440 450
LRVKTVPLLS KVDDIHAICS LLKDFLRNLK EPLLTFRLNR AFMEAAEITD
460 470 480 490 500
EDNSIAAMYQ AVGELPQANR DTLAFLMIHL QRVAQSPHTK MDVANLAKVF
510 520 530 540 550
GPTIVAHAVP NPDPVTMLQD IKRQPKVVER LLSLPLEYWS QFMMVEQENI
560 570 580 590 600
DPLHVIENSN AFSTPQTPDI KVSLLGPVTT PEHQLLKTPS SSSLSQRVRS
610 620 630
TLTKNTPRFG SKSKSATNLG RQGNFFASPM LK
Length:632
Mass (Da):71,027
Last modified:March 1, 2001 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i032B7DF9CEA8F39D
GO

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

There are 21 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8VS54F8VS54_HUMAN
Rac GTPase-activating protein 1
RACGAP1
129Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8W0L1F8W0L1_HUMAN
Rac GTPase-activating protein 1
RACGAP1
139Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8VWY4F8VWY4_HUMAN
Rac GTPase-activating protein 1
RACGAP1
174Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8VWX0F8VWX0_HUMAN
Rac GTPase-activating protein 1
RACGAP1
130Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8VVE5F8VVE5_HUMAN
Rac GTPase-activating protein 1
RACGAP1
177Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8VV47F8VV47_HUMAN
Rac GTPase-activating protein 1
RACGAP1
155Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8VUW9F8VUW9_HUMAN
Rac GTPase-activating protein 1
RACGAP1
107Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8VV39F8VV39_HUMAN
Rac GTPase-activating protein 1
RACGAP1
111Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8VZ66F8VZ66_HUMAN
Rac GTPase-activating protein 1
RACGAP1
150Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
F8VRD2F8VRD2_HUMAN
Rac GTPase-activating protein 1
RACGAP1
293Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
There are more potential isoformsShow all

<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 AAH24144 differs from that shown. Reason: Frameshift at positions 171, 205 and 437.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 conflicti155D → H in BAA91347 (PubMed:14702039).Curated1
Sequence conflicti518L → S in BAA90247 (PubMed:10979956).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AB030251 mRNA Translation: BAA90247.1
AL136794 mRNA Translation: CAB66728.1
AK000733 mRNA Translation: BAA91347.1
CR533565 mRNA Translation: CAG38596.1
BC024144 mRNA Translation: AAH24144.1 Frameshift.
BC032754 mRNA Translation: AAH32754.1
AB040911 mRNA Translation: BAA96002.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS8795.1

Protein sequence database of the Protein Information Resource

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PIRi
D59430

NCBI Reference Sequences

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RefSeqi
NP_001119575.1, NM_001126103.2
NP_001119576.1, NM_001126104.2
NP_001306928.1, NM_001319999.1
NP_001306929.1, NM_001320000.1
NP_001306930.1, NM_001320001.1
NP_001306931.1, NM_001320002.1
NP_001306932.1, NM_001320003.1
NP_001306933.1, NM_001320004.1
NP_001306934.1, NM_001320005.1
NP_001306935.1, NM_001320006.1
NP_001306936.1, NM_001320007.1
NP_037409.2, NM_013277.4
XP_006719422.1, XM_006719359.1
XP_011536540.1, XM_011538238.1
XP_016874709.1, XM_017019220.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.505469

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000312377; ENSP00000309871; ENSG00000161800
ENST00000427314; ENSP00000404190; ENSG00000161800
ENST00000454520; ENSP00000404808; ENSG00000161800
ENST00000547905; ENSP00000449370; ENSG00000161800
ENST00000551016; ENSP00000449374; ENSG00000161800

Database of genes from NCBI RefSeq genomes

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GeneIDi
29127

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:29127

UCSC genome browser

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UCSCi
uc001rvs.3 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
AB030251 mRNA Translation: BAA90247.1
AL136794 mRNA Translation: CAB66728.1
AK000733 mRNA Translation: BAA91347.1
CR533565 mRNA Translation: CAG38596.1
BC024144 mRNA Translation: AAH24144.1 Frameshift.
BC032754 mRNA Translation: AAH32754.1
AB040911 mRNA Translation: BAA96002.1
CCDSiCCDS8795.1
PIRiD59430
RefSeqiNP_001119575.1, NM_001126103.2
NP_001119576.1, NM_001126104.2
NP_001306928.1, NM_001319999.1
NP_001306929.1, NM_001320000.1
NP_001306930.1, NM_001320001.1
NP_001306931.1, NM_001320002.1
NP_001306932.1, NM_001320003.1
NP_001306933.1, NM_001320004.1
NP_001306934.1, NM_001320005.1
NP_001306935.1, NM_001320006.1
NP_001306936.1, NM_001320007.1
NP_037409.2, NM_013277.4
XP_006719422.1, XM_006719359.1
XP_011536540.1, XM_011538238.1
XP_016874709.1, XM_017019220.1
UniGeneiHs.505469

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
2OVJX-ray1.49A348-546[»]
3W6RX-ray1.90A348-546[»]
3WPQX-ray1.84A/B346-546[»]
3WPSX-ray2.70A/B346-546[»]
4B6DX-ray2.20A/B/C/D/E/F284-339[»]
5C2JX-ray2.50A346-546[»]
5C2KX-ray1.42A346-546[»]
ProteinModelPortaliQ9H0H5
SMRiQ9H0H5
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118892, 95 interactors
CORUMiQ9H0H5
DIPiDIP-33087N
ELMiQ9H0H5
IntActiQ9H0H5, 88 interactors
MINTiQ9H0H5
STRINGi9606.ENSP00000309871

Chemistry databases

ChEMBLiCHEMBL2146306

PTM databases

iPTMnetiQ9H0H5
PhosphoSitePlusiQ9H0H5

Polymorphism and mutation databases

BioMutaiRACGAP1
DMDMi74762727

Proteomic databases

EPDiQ9H0H5
MaxQBiQ9H0H5
PaxDbiQ9H0H5
PeptideAtlasiQ9H0H5
PRIDEiQ9H0H5
ProteomicsDBi80279

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
29127
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312377; ENSP00000309871; ENSG00000161800
ENST00000427314; ENSP00000404190; ENSG00000161800
ENST00000454520; ENSP00000404808; ENSG00000161800
ENST00000547905; ENSP00000449370; ENSG00000161800
ENST00000551016; ENSP00000449374; ENSG00000161800
GeneIDi29127
KEGGihsa:29127
UCSCiuc001rvs.3 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
29127
DisGeNETi29127
EuPathDBiHostDB:ENSG00000161800.12

GeneCards: human genes, protein and diseases

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GeneCardsi
RACGAP1

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0036723
HGNCiHGNC:9804 RACGAP1
HPAiCAB025859
HPA039427
HPA043912
MIMi604980 gene
neXtProtiNX_Q9H0H5
OpenTargetsiENSG00000161800
PharmGKBiPA34165

Human Unidentified Gene-Encoded large proteins database

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HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3564 Eukaryota
ENOG410XPK0 LUCA
GeneTreeiENSGT00940000154610
HOGENOMiHOG000230702
HOVERGENiHBG062009
InParanoidiQ9H0H5
KOiK16733
OMAiHELGKYK
OrthoDBiEOG091G03O7
PhylomeDBiQ9H0H5
TreeFamiTF318102

Enzyme and pathway databases

ReactomeiR-HSA-194840 Rho GTPase cycle
R-HSA-2132295 MHC class II antigen presentation
R-HSA-6811434 COPI-dependent Golgi-to-ER retrograde traffic
R-HSA-983189 Kinesins
SIGNORiQ9H0H5

Miscellaneous databases

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

More...
ChiTaRSi
RACGAP1 human
EvolutionaryTraceiQ9H0H5

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
RACGAP1

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

More...
GenomeRNAii
29127
PMAP-CutDBiQ9H0H5

Protein Ontology

More...
PROi
PR:Q9H0H5

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000161800 Expressed in 207 organ(s), highest expression level in female gonad
CleanExiHS_RACGAP1
ExpressionAtlasiQ9H0H5 baseline and differential
GenevisibleiQ9H0H5 HS

Family and domain databases

CDDicd00029 C1, 1 hit
Gene3Di1.10.555.10, 1 hit
InterProiView protein in InterPro
IPR002219 PE/DAG-bd
IPR008936 Rho_GTPase_activation_prot
IPR000198 RhoGAP_dom
PfamiView protein in Pfam
PF00130 C1_1, 1 hit
PF00620 RhoGAP, 1 hit
SMARTiView protein in SMART
SM00109 C1, 1 hit
SM00324 RhoGAP, 1 hit
SUPFAMiSSF48350 SSF48350, 1 hit
PROSITEiView protein in PROSITE
PS50238 RHOGAP, 1 hit
PS00479 ZF_DAG_PE_1, 1 hit
PS50081 ZF_DAG_PE_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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 nameiRGAP1_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: Q9H0H5
Secondary accession number(s): Q6PJ26
, Q9NWN2, Q9P250, Q9P2W2
<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: March 21, 2006
Last sequence update: March 1, 2001
Last modified: December 5, 2018
This is version 172 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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