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Entry version 178 (16 Oct 2019)
Sequence version 1 (31 Aug 2004)
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Protein

Ras-related C3 botulinum toxin substrate 1

Gene

Rac1

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

Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states (PubMed:24352656). In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization, neurons adhesion, migration and differentiation, and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In glioma cells, promotes cell migration and invasion. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. In neurons, is involved in dendritic spine formation and synaptic plasticity (PubMed:24352656, PubMed:26969129). In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3.By similarity4 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Regulated by guanine nucleotide exchange factors (GEFs) which promote the exchange of bound GDP for free GTP, GTPase activating proteins (GAPs) which increase the GTP hydrolysis activity, and GDP dissociation inhibitors which inhibit the dissociation of the nucleotide from the GTPase. GTP hydrolysis is stimulated by ARHGAP30 and ARHGAP44.2 Publications

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 sitei60GTP; via amide nitrogenBy similarity1

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 bindingi13 – 18GTPBy similarity6
Nucleotide bindingi30 – 35GTPBy similarity6
Nucleotide bindingi116 – 118GTPBy similarity3
Nucleotide bindingi159 – 160GTPBy similarity2

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-114604 GPVI-mediated activation cascade
R-MMU-1257604 PIP3 activates AKT signaling
R-MMU-1433557 Signaling by SCF-KIT
R-MMU-193648 NRAGE signals death through JNK
R-MMU-194840 Rho GTPase cycle
R-MMU-2029482 Regulation of actin dynamics for phagocytic cup formation
R-MMU-2424491 DAP12 signaling
R-MMU-2871796 FCERI mediated MAPK activation
R-MMU-376172 DSCAM interactions
R-MMU-389359 CD28 dependent Vav1 pathway
R-MMU-3928662 EPHB-mediated forward signaling
R-MMU-3928664 Ephrin signaling
R-MMU-3928665 EPH-ephrin mediated repulsion of cells
R-MMU-399954 Sema3A PAK dependent Axon repulsion
R-MMU-4086400 PCP/CE pathway
R-MMU-416550 Sema4D mediated inhibition of cell attachment and migration
R-MMU-418885 DCC mediated attractive signaling
R-MMU-4420097 VEGFA-VEGFR2 Pathway
R-MMU-445144 Signal transduction by L1
R-MMU-5218920 VEGFR2 mediated vascular permeability
R-MMU-5625740 RHO GTPases activate PKNs
R-MMU-5625900 RHO GTPases activate CIT
R-MMU-5625970 RHO GTPases activate KTN1
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-5627123 RHO GTPases activate PAKs
R-MMU-5663213 RHO GTPases Activate WASPs and WAVEs
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-5668599 RHO GTPases Activate NADPH Oxidases
R-MMU-5687128 MAPK6/MAPK4 signaling
R-MMU-6798695 Neutrophil degranulation
R-MMU-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-8849471 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-MMU-8875555 MET activates RAP1 and RAC1
R-MMU-9032759 NTRK2 activates RAC1
R-MMU-983231 Factors involved in megakaryocyte development and platelet production

<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:
Ras-related C3 botulinum toxin substrate 1Curated (EC:3.6.5.22 Publications)
Alternative name(s):
p21-Rac1
<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:Rac1Imported
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 5

Organism-specific databases

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

More...
MGIi
MGI:97845 Rac1

<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, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<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

Conditional knockout of Rac1 in the telencephalic ventricular zone of embryos leads to primary microcephaly. Self-renewal, survival, and differentiation of telencephalic neural progenitor cells is affected.1 Publication

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>Mutagenesisi12G → V: Constitutively active. Interacts with PARD6 proteins. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5628

<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_00000420381 – 189Ras-related C3 botulinum toxin substrate 1Add BLAST189
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000042039190 – 192Removed in mature formBy similarity3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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-linki147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
<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 residuei189Cysteine methyl esterBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi189S-geranylgeranyl cysteineBy similarity1

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

GTP-bound active form is ubiquitinated by HACE1, leading to its degradation by the proteasome.By similarity

Keywords - PTMi

Isopeptide bond, Lipoprotein, Methylation, Prenylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P63001

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P63001

MaxQB - The MaxQuant DataBase

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MaxQBi
P63001

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

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PaxDbi
P63001

PRoteomics IDEntifications database

More...
PRIDEi
P63001

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P63001

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

More...
PhosphoSitePlusi
P63001

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P63001

<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

Widely expressed.1 Publication

<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

Expressed in the neocortical neurons in the developing brain.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000001847 Expressed in 342 organ(s), highest expression level in CA1 field of hippocampus

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P63001 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P63001 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_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 the GEF proteins PREX1, FARP1, FARP2, DOCK1, DOCK2 and DOCK7, which promote the exchange between GDP and GTP, and therefore activate it.

Part of a quaternary complex containing PARD3, some PARD6 protein (PARD6A, PARD6B or PARD6G) and some atypical PKC protein (PRKCI or PRKCZ), which plays a central role in epithelial cell polarization.

Found in a trimeric complex composed of DOCK1 and ELMO1, which plays a central role in phagocytosis of apoptotic cells.

Interacts with RALBP1 via its effector domain.

Interacts with BAIAP2, BAIAP2L1, PLXNB1, CYFIP1/SRA-1 and DEF6. Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1.

Interacts with DSCAM; the interaction requires PAK1.

Interacts with TBC1D2.

Interacts with UNKL.

Interacts with USP6.

Interacts with SPATA13.

Interacts with ITGB4.

Interacts with the GTP-bound form of RAB7A.

Interacts with ARHGEF2.

Interacts with ARHGEF16; mediates activation of RAC1 by EPHA2.

Interacts with NOXA1.

Interacts with S100A8 and calprotectin (S100A8/9).

Interacts with ARHGDIA; the interaction is induced by SEMA5A, mediated through PLXNB3 and inactivates and stabilizes RAC1.

Interacts with PACSIN2.

Interacts with ITGB1BP1 (By similarity).

Interacts with the GEF protein RASGRF2, which promotes the exchange between GDP and GTP, and therefore activates it.

Interacts with PARD6A, PARD6B and PARD6G in a GTP-dependent manner.

Part of a complex with MAP2K3, MAP3K3 and CCM2.

Interacts with NISCH.

Interacts with PIP5K1A.

Interacts (GTP-bound form preferentially) with PKN2 (via the REM repeats); the interaction stimulates autophosphorylation and phosphorylation of PKN2.

Interacts with SRGAP2.

Interacts with PLXNB3.

Interacts (when active) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane.

Interacts with RAPH1 (via Ras associating and PH domains) (By similarity).

Interacts with MTSS2 (via IMD domain); this interaction may be important to potentiate PDGF-induced RAC1 activation.

Interacts (GTP-bound form) with SH3RF3.

Interacts with PAK2 (By similarity).

Interacts (GTP-bound form) with SH3RF1 (PubMed:22959435).

Found in a complex with SH3RF1, MAPK8IP1/JIP1, MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8/JNK1 (PubMed:23963642).

Interacts (both active GTP- or inactive GDP-bound forms) with SH3RF2 (By similarity).

By similarity12 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
202556, 36 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P63001

Database of interacting proteins

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DIPi
DIP-31545N

Protein interaction database and analysis system

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IntActi
P63001, 35 interactors

Molecular INTeraction database

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MINTi
P63001

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000079380

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P63001

<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

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SMRi
P63001

Database of comparative protein structure models

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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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi32 – 40Effector regionSequence analysis9

<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 effector region mediates interaction with DEF6.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0393 Eukaryota
COG1100 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153500

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000233974

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P63001

KEGG Orthology (KO)

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KOi
K04392

Database of Orthologous Groups

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OrthoDBi
1091615at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P63001

TreeFam database of animal gene trees

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TreeFami
TF101109

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
IPR001806 Small_GTPase
IPR003578 Small_GTPase_Rho

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00071 Ras, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00231 small_GTP, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51420 RHO, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

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

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P63001-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP
60 70 80 90 100
VNLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE
110 120 130 140 150
VRHHCPNTPI ILVGTKLDLR DDKDTIEKLK EKKLTPITYP QGLAMAKEIG
160 170 180 190
AVKYLECSAL TQRGLKTVFD EAIRAVLCPP PVKKRKRKCL LL
Length:192
Mass (Da):21,450
Last modified:August 31, 2004 - 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:iACEDF83A45E5EA67
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q3TLP8Q3TLP8_MOUSE
RAS-related C3 botulinum substrate ...
Rac1 mCG_23557
211Annotation 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>

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
X57277 mRNA Translation: CAA40545.1
AK009017 mRNA Translation: BAB26027.1
AK011072 mRNA Translation: BAB69451.1
AK034601 mRNA Translation: BAC28767.1
AK047969 mRNA Translation: BAC33203.1
AK088825 mRNA Translation: BAC40596.1
BC003828 mRNA Translation: AAH03828.1
BC051053 mRNA Translation: AAH51053.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS19843.1

Protein sequence database of the Protein Information Resource

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PIRi
A60347

NCBI Reference Sequences

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RefSeqi
NP_033033.1, NM_009007.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000080537; ENSMUSP00000079380; ENSMUSG00000001847

Database of genes from NCBI RefSeq genomes

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GeneIDi
19353

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:19353

UCSC genome browser

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UCSCi
uc009akk.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
X57277 mRNA Translation: CAA40545.1
AK009017 mRNA Translation: BAB26027.1
AK011072 mRNA Translation: BAB69451.1
AK034601 mRNA Translation: BAC28767.1
AK047969 mRNA Translation: BAC33203.1
AK088825 mRNA Translation: BAC40596.1
BC003828 mRNA Translation: AAH03828.1
BC051053 mRNA Translation: AAH51053.1
CCDSiCCDS19843.1
PIRiA60347
RefSeqiNP_033033.1, NM_009007.2

3D structure databases

SMRiP63001
ModBaseiSearch...

Protein-protein interaction databases

BioGridi202556, 36 interactors
CORUMiP63001
DIPiDIP-31545N
IntActiP63001, 35 interactors
MINTiP63001
STRINGi10090.ENSMUSP00000079380

Chemistry databases

BindingDBiP63001
ChEMBLiCHEMBL5628

PTM databases

iPTMnetiP63001
PhosphoSitePlusiP63001
SwissPalmiP63001

Proteomic databases

EPDiP63001
jPOSTiP63001
MaxQBiP63001
PaxDbiP63001
PRIDEiP63001

Genome annotation databases

EnsembliENSMUST00000080537; ENSMUSP00000079380; ENSMUSG00000001847
GeneIDi19353
KEGGimmu:19353
UCSCiuc009akk.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5879
MGIiMGI:97845 Rac1

Phylogenomic databases

eggNOGiKOG0393 Eukaryota
COG1100 LUCA
GeneTreeiENSGT00940000153500
HOGENOMiHOG000233974
InParanoidiP63001
KOiK04392
OrthoDBi1091615at2759
PhylomeDBiP63001
TreeFamiTF101109

Enzyme and pathway databases

ReactomeiR-MMU-114604 GPVI-mediated activation cascade
R-MMU-1257604 PIP3 activates AKT signaling
R-MMU-1433557 Signaling by SCF-KIT
R-MMU-193648 NRAGE signals death through JNK
R-MMU-194840 Rho GTPase cycle
R-MMU-2029482 Regulation of actin dynamics for phagocytic cup formation
R-MMU-2424491 DAP12 signaling
R-MMU-2871796 FCERI mediated MAPK activation
R-MMU-376172 DSCAM interactions
R-MMU-389359 CD28 dependent Vav1 pathway
R-MMU-3928662 EPHB-mediated forward signaling
R-MMU-3928664 Ephrin signaling
R-MMU-3928665 EPH-ephrin mediated repulsion of cells
R-MMU-399954 Sema3A PAK dependent Axon repulsion
R-MMU-4086400 PCP/CE pathway
R-MMU-416550 Sema4D mediated inhibition of cell attachment and migration
R-MMU-418885 DCC mediated attractive signaling
R-MMU-4420097 VEGFA-VEGFR2 Pathway
R-MMU-445144 Signal transduction by L1
R-MMU-5218920 VEGFR2 mediated vascular permeability
R-MMU-5625740 RHO GTPases activate PKNs
R-MMU-5625900 RHO GTPases activate CIT
R-MMU-5625970 RHO GTPases activate KTN1
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-5627123 RHO GTPases activate PAKs
R-MMU-5663213 RHO GTPases Activate WASPs and WAVEs
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-5668599 RHO GTPases Activate NADPH Oxidases
R-MMU-5687128 MAPK6/MAPK4 signaling
R-MMU-6798695 Neutrophil degranulation
R-MMU-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-8849471 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-MMU-8875555 MET activates RAP1 and RAC1
R-MMU-9032759 NTRK2 activates RAC1
R-MMU-983231 Factors involved in megakaryocyte development and platelet production

Miscellaneous databases

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

More...
ChiTaRSi
Rac1 mouse

Protein Ontology

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PROi
PR:P63001

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000001847 Expressed in 342 organ(s), highest expression level in CA1 field of hippocampus
ExpressionAtlasiP63001 baseline and differential
GenevisibleiP63001 MM

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR005225 Small_GTP-bd_dom
IPR001806 Small_GTPase
IPR003578 Small_GTPase_Rho
PfamiView protein in Pfam
PF00071 Ras, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00231 small_GTP, 1 hit
PROSITEiView protein in PROSITE
PS51420 RHO, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRAC1_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: P63001
Secondary accession number(s): O95501, P15154, Q9BTB4
<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: August 31, 2004
Last sequence update: August 31, 2004
Last modified: October 16, 2019
This is version 178 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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