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Entry version 186 (13 Feb 2019)
Sequence version 1 (31 Aug 2004)
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Protein

Ras-related C3 botulinum toxin substrate 1

Gene

RAC1

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

Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. 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 podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. 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 synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3.By similarity3 Publications
Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction.

<p>This subsection of the ‘Function’ 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 ARHGAP30.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 nitrogenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 – 18GTPCombined sources1 Publication6
Nucleotide bindingi30 – 35GTPCombined sources1 Publication6
Nucleotide bindingi116 – 118GTPCombined sources1 Publication3
Nucleotide bindingi159 – 160GTPCombined sources1 Publication2

<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

LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-114604 GPVI-mediated activation cascade
R-HSA-1257604 PIP3 activates AKT signaling
R-HSA-1433557 Signaling by SCF-KIT
R-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-164944 Nef and signal transduction
R-HSA-193648 NRAGE signals death through JNK
R-HSA-194840 Rho GTPase cycle
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-2424491 DAP12 signaling
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-376172 DSCAM interactions
R-HSA-389359 CD28 dependent Vav1 pathway
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-3928664 Ephrin signaling
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-399954 Sema3A PAK dependent Axon repulsion
R-HSA-399955 SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion
R-HSA-4086400 PCP/CE pathway
R-HSA-416550 Sema4D mediated inhibition of cell attachment and migration
R-HSA-418885 DCC mediated attractive signaling
R-HSA-428540 Activation of RAC1
R-HSA-428543 Inactivation of CDC42 and RAC1
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-445144 Signal transduction by L1
R-HSA-5218920 VEGFR2 mediated vascular permeability
R-HSA-5625740 RHO GTPases activate PKNs
R-HSA-5625900 RHO GTPases activate CIT
R-HSA-5625970 RHO GTPases activate KTN1
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5627123 RHO GTPases activate PAKs
R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-5668599 RHO GTPases Activate NADPH Oxidases
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-6798695 Neutrophil degranulation
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-8849471 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-HSA-8875555 MET activates RAP1 and RAC1
R-HSA-9032759 NTRK2 activates RAC1
R-HSA-9032845 Activated NTRK2 signals through CDK5
R-HSA-9619229 Activation of RAC1 downstream of NMDARs
R-HSA-983231 Factors involved in megakaryocyte development and platelet production

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

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SignaLinki
P63000

SIGNOR Signaling Network Open Resource

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SIGNORi
P63000

<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 1
Alternative name(s):
Cell migration-inducing gene 5 protein
Ras-like protein TC25
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:RAC1
Synonyms:TC25
ORF Names:MIG5
<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 7

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000136238.17

Human Gene Nomenclature Database

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HGNCi
HGNC:9801 RAC1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602048 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P63000

<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, 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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Mental retardation, autosomal dominant 48 (MRD48)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of mental retardation, a disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRD48 patients manifest global developmental delay and moderate to severe intellectual disability.
See also OMIM:617751
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_08045418C → Y in MRD48; decreased substrate adhesion-dependent cell spreading; dominant-negative effect; reduced neuronal proliferation. 1 Publication1
Natural variantiVAR_08045539N → S in MRD48; decreased substrate adhesion-dependent cell spreading; dominant-negative effect; reduced neuronal proliferation. 1 Publication1
Natural variantiVAR_08045651V → L in MRD48; unknown pathological significance. 1 Publication1
Natural variantiVAR_08045751V → M in MRD48; decreased substrate adhesion-dependent cell spreading; weak dominant-negative effect. 1 Publication1
Natural variantiVAR_08045864Y → D in MRD48; increased substrate adhesion-dependent cell spreading; constitutively active. 1 Publication1
Natural variantiVAR_08045973P → L in MRD48; decreased substrate adhesion-dependent cell spreading; weak dominant-negative effect. 1 Publication1
Natural variantiVAR_080460157C → Y in MRD48; decreased substrate adhesion-dependent cell spreading; weak dominant-negative effect. 1 Publication1

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. Increases nuclear localization and up-regulates transcriptional activity of NR3C2. 2 Publications1
Mutagenesisi17T → N: Constitutively inactivated. Abolishes interaction with PARD6 proteins. No effect on NR3C2 transcriptional activity. No interaction with PPP5C. Doesn't activate PPP5C phosphatase activity and translocate PPP5C to the plasma membrane. 3 Publications1
Mutagenesisi30G → V: No interaction with PPP5C; when associated with L-61. Translocates to the plasma membrane; also when associated with L-61. 1 Publication1
Mutagenesisi32Y → F: Abolishes AMPylation by Haemophilus IbpA. 1 Publication1
Mutagenesisi35T → A: Abolishes AMPylation by Vibrio VopS. 2 Publications1
Mutagenesisi35T → S: No interaction with PPP5C; when associated with L-61. Translocates to the plasma membrane; also when associated with L-61. 2 Publications1
Mutagenesisi37F → A: Strongly reduced interaction with PLCB2. 1 Publication1
Mutagenesisi56W → A: Strongly reduced interaction with PLCB2. 1 Publication1
Mutagenesisi61Q → L: Constitutively active. Interacts with PARD6 proteins. Interacts with PPP5C, activates its phosphatase activity and translocates PPP5C to the plasma membrane. No effect on interaction with RAPH1. No interaction with PPP5C; when associated with V-30 or S-35. Translocates to the plasma membrane; also when associated with V-30 or S-35. 3 Publications1
Mutagenesisi67L → A: Strongly reduced interaction with PLCB2. 1 Publication1
Mutagenesisi70L → A: Strongly reduced interaction with PLCB2. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

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DisGeNETi
5879

MalaCards human disease database

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MalaCardsi
RAC1
MIMi617751 phenotype

Open Targets

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OpenTargetsi
ENSG00000136238

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
500159 Microcephaly-corpus callosum and cerebellar vermis hypoplasia-facial dysmorphism-intellectual disability syndrom

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34162

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL6094

Drug and drug target database

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DrugBanki
DB00514 Dextromethorphan
DB04315 Guanosine-5'-Diphosphate

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RAC1

Domain mapping of disease mutations (DMDM)

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DMDMi
51702787

<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_00000420361 – 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_0000042037190 – 192Removed in mature formBy similarity3

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 residuei32O-AMP-tyrosine; by Haemophilus IbpA; alternate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi32O-linked (GlcNAc) tyrosine; by Photorhabdus PAU_02230; alternate1 Publication1
Modified residuei35O-AMP-threonine; by Vibrio VopS1 Publication1
Modified residuei39ADP-ribosylasparagine; by botulinum toxinBy similarity1
<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)1 Publication
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 cysteine1 Publication1
Isoform B (identifier: P63000-2)
Modified residuei71PhosphoserineCombined 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

(Microbial infection) AMPylation at Tyr-32 and Thr-35 are mediated by bacterial enzymes in case of infection by H.somnus and V.parahaemolyticus, respectively. AMPylation occurs in the effector region and leads to inactivation of the GTPase activity by preventing the interaction with downstream effectors, thereby inhibiting actin assembly in infected cells. It is unclear whether some human enzyme mediates AMPylation; FICD has such ability in vitro but additional experiments remain to be done to confirm results in vivo.2 Publications
GTP-bound active form is ubiquitinated by HACE1, leading to its degradation by the proteasome.2 Publications
(Microbial infection) Glycosylated at Tyr-32 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rac and leads to actin disassembly.1 Publication

Keywords - PTMi

ADP-ribosylation, Glycoprotein, Isopeptide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P63000

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P63000

MaxQB - The MaxQuant DataBase

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MaxQBi
P63000

PeptideAtlas

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PeptideAtlasi
P63000

PRoteomics IDEntifications database

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PRIDEi
P63000

ProteomicsDB human proteome resource

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ProteomicsDBi
57467
57468 [P63000-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P63000

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

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PhosphoSitePlusi
P63000

SwissPalm database of S-palmitoylation events

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SwissPalmi
P63000

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P63000

<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

Isoform B is predominantly identified in skin and epithelial tissues from the intestinal tract. Its expression is elevated in colorectal tumors at various stages of neoplastic progression, as compared to their respective adjacent tissues.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000136238 Expressed in 242 organ(s), highest expression level in esophagus squamous epithelium

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P63000 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P63000 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB035994
HPA047820

<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 NISCH. Interacts with PIP5K1A. Interacts with the GTP-bound form of RAB7A. Interacts with SRGAP2. Interacts with CYFIP1/SRA-1. Interacts with PLXNB3. Interacts with ARHGDIA; the interaction is induced by SEMA5A, mediated through PLXNB3 and inactivates and stabilizes RAC1. Interacts (GTP-bound form preferentially) with PKN2 (via the REM repeats); the interaction stimulates autophosphorylation and phosphorylation of PKN2. Interacts with the GEF proteins PREX1, RASGRF2, FARP1, FARP2, DOCK1, DOCK2 and DOCK7, which promote the exchange between GDP and GTP, and therefore activate it. Interacts with PARD6A, PARD6B and PARD6G in a GTP-dependent manner. 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 PLXNB1. Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1. Interacts with DSCAM; the interaction requires PAK1. Part of a complex with MAP2K3, MAP3K3, CCM2 and DEF6. Interacts with BAIAP2, BAIAP2L1 and DEF6. Interacts with Y.pseudotuberculosis YPKA and PLCB2. Interacts with NOXA1. Interacts with ARHGEF2. Interacts with TBC1D2. Interacts with UNKL. Interacts with USP6. Interacts with SPATA13. Interacts with ARHGEF16; mediates activation of RAC1 by EPHA2. Interacts with ITGB4. Interacts with S100A8 and calprotectin (S100A8/9). Interacts with PACSIN2. Interacts with ITGB1BP1. 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) (PubMed:18499456). Interacts with MTSS1L (via IMD domain); this interaction may be important to potentiate PDGF-induced RAC1 activation (PubMed:20875796). Interacts with PAK2 (PubMed:20696164). Interacts (GTP-bound form) with SH3RF1 and SH3RF3 (PubMed:20696164). Found in a complex with SH3RF1, MAPK8IP1/JIP1, MAP3K11/MLK3, MAP2K7/MKK7 and MAPK8/JNK1. Interacts (both active GTP- or inactive GDP-bound forms) with SH3RF2 (By similarity).By similarity41 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
111817, 197 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P63000

Database of interacting proteins

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DIPi
DIP-29260N

Protein interaction database and analysis system

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IntActi
P63000, 141 interactors

Molecular INTeraction database

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MINTi
P63000

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P63000

<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

1192
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1E96X-ray2.40A2-192[»]
1FOEX-ray2.80B/D/F/H1-177[»]
1G4UX-ray2.30R1-184[»]
1HE1X-ray2.00C/D2-176[»]
1HH4X-ray2.70A/B2-192[»]
1I4DX-ray2.50D1-192[»]
1I4LX-ray2.70D1-192[»]
1I4TX-ray2.60D1-192[»]
1MH1X-ray1.38A2-184[»]
1RYFX-ray1.75A/B1-182[»]
1RYHX-ray1.75A/B1-182[»]
2FJUX-ray2.20A1-177[»]
2H7VX-ray2.60A/B1-184[»]
2NZ8X-ray2.00A1-177[»]
2P2LX-ray1.90A/B/C1-184[»]
2RMKNMR-A1-192[»]
2VRWX-ray1.85A1-184[»]
2WKPX-ray1.90A4-180[»]
2WKQX-ray1.60A4-180[»]
2WKRX-ray2.20A4-180[»]
2YINX-ray2.70C/D1-177[»]
3B13X-ray3.01B/D1-177[»]
3BJIX-ray2.60C/D1-177[»]
3RYTX-ray3.58C1-177[»]
3SBDX-ray2.10A/B2-177[»]
3SBEX-ray2.60A2-177[»]
3SU8X-ray3.20A1-177[»]
3SUAX-ray4.39A/B/C1-177[»]
3TH5X-ray2.30A/B2-177[»]
4GZLX-ray2.00A/B2-177[»]
4GZMX-ray2.80A/B2-177[»]
4YONX-ray1.95B1-177[»]
5FI0X-ray3.28B/D/F/H1-192[»]
5HZHX-ray2.60A1-180[»]
5N6OX-ray2.59A/B2-177[»]
5O33X-ray1.64A1-177[»]
6BC1X-ray2.90A/B2-177[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P63000

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

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SMRi
P63000

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P63000

<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 DEF6.1 Publication

<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

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153500

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000233974

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG009351

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P63000

KEGG Orthology (KO)

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KOi
K04392

Identification of Orthologs from Complete Genome Data

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OMAi
KWHPEIS

Database of Orthologous Groups

More...
OrthoDBi
1091615at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P63000

TreeFam database of animal gene trees

More...
TreeFami
TF101109

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
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

More...
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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform A (identifier: P63000-1) [UniParc]FASTAAdd to basket
Also known as: Rac1A

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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
Isoform B (identifier: P63000-2) [UniParc] [UniParc]FASTAAdd to basket
Also known as: Rac1B, Rac1ins

The sequence of this isoform differs from the canonical sequence as follows:
     75-75: T → TVGETYGKDITSRGKDKPIA

Show »
Length:211
Mass (Da):23,467
Checksum:i93745E0CFBA5281F
GO

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

The sequence AAZ80485 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.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 conflicti192Missing in AAA36544 (PubMed:2108320).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_08045418C → Y in MRD48; decreased substrate adhesion-dependent cell spreading; dominant-negative effect; reduced neuronal proliferation. 1 Publication1
Natural variantiVAR_01454026N → D. Corresponds to variant dbSNP:rs5830Ensembl.1
Natural variantiVAR_01454128F → L. Corresponds to variant dbSNP:rs5832Ensembl.1
Natural variantiVAR_08045539N → S in MRD48; decreased substrate adhesion-dependent cell spreading; dominant-negative effect; reduced neuronal proliferation. 1 Publication1
Natural variantiVAR_08045651V → L in MRD48; unknown pathological significance. 1 Publication1
Natural variantiVAR_08045751V → M in MRD48; decreased substrate adhesion-dependent cell spreading; weak dominant-negative effect. 1 Publication1
Natural variantiVAR_01454259A → T. Corresponds to variant dbSNP:rs5837Ensembl.1
Natural variantiVAR_01454363D → G. Corresponds to variant dbSNP:rs5831Ensembl.1
Natural variantiVAR_08045864Y → D in MRD48; increased substrate adhesion-dependent cell spreading; constitutively active. 1 Publication1
Natural variantiVAR_08045973P → L in MRD48; decreased substrate adhesion-dependent cell spreading; weak dominant-negative effect. 1 Publication1
Natural variantiVAR_01454593V → G. Corresponds to variant dbSNP:rs5826Ensembl.1
Natural variantiVAR_01454493V → I. Corresponds to variant dbSNP:rs5825Ensembl.1
Natural variantiVAR_014546108T → I. Corresponds to variant dbSNP:rs5838Ensembl.1
Natural variantiVAR_014547130K → R. Corresponds to variant dbSNP:rs5828Ensembl.1
Natural variantiVAR_014548133K → E. Corresponds to variant dbSNP:rs5835Ensembl.1
Natural variantiVAR_033303135T → I1 PublicationCorresponds to variant dbSNP:rs11540455Ensembl.1
Natural variantiVAR_080460157C → Y in MRD48; decreased substrate adhesion-dependent cell spreading; weak dominant-negative effect. 1 Publication1
Natural variantiVAR_014549180P → S. Corresponds to variant dbSNP:rs16063Ensembl.1
Natural variantiVAR_014550182V → E. Corresponds to variant dbSNP:rs5836Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_00571075T → TVGETYGKDITSRGKDKPIA in isoform B. 3 Publications1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M29870 mRNA Translation: AAA36537.1
M31467 mRNA Translation: AAA36544.1
AJ132694 mRNA Translation: CAA10732.1
AJ132695 Genomic DNA Translation: CAB53579.5
AJ132695 Genomic DNA Translation: CAA10733.6
AF136373 mRNA Translation: AAD30547.1
AY279384 mRNA Translation: AAQ16632.1
AF498964 mRNA Translation: AAM21111.1
BT007121 mRNA Translation: AAP35785.1
DQ165078 Genomic DNA Translation: AAZ80485.1 Different initiation.
AC009412 Genomic DNA Translation: AAS07511.1
AC009412 Genomic DNA Translation: AAS07512.1
BC004247 mRNA Translation: AAH04247.1
BC050687 mRNA Translation: AAH50687.1
BC107748 mRNA Translation: AAI07749.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS5348.1
CCDS5349.1 [P63000-2]

Protein sequence database of the Protein Information Resource

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PIRi
A34788 TVHUC1

NCBI Reference Sequences

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RefSeqi
NP_008839.2, NM_006908.4 [P63000-1]
NP_061485.1, NM_018890.3 [P63000-2]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.413812

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000348035; ENSP00000258737; ENSG00000136238 [P63000-1]
ENST00000356142; ENSP00000348461; ENSG00000136238 [P63000-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
5879

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:5879

UCSC genome browser

More...
UCSCi
uc003spw.4 human

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29870 mRNA Translation: AAA36537.1
M31467 mRNA Translation: AAA36544.1
AJ132694 mRNA Translation: CAA10732.1
AJ132695 Genomic DNA Translation: CAB53579.5
AJ132695 Genomic DNA Translation: CAA10733.6
AF136373 mRNA Translation: AAD30547.1
AY279384 mRNA Translation: AAQ16632.1
AF498964 mRNA Translation: AAM21111.1
BT007121 mRNA Translation: AAP35785.1
DQ165078 Genomic DNA Translation: AAZ80485.1 Different initiation.
AC009412 Genomic DNA Translation: AAS07511.1
AC009412 Genomic DNA Translation: AAS07512.1
BC004247 mRNA Translation: AAH04247.1
BC050687 mRNA Translation: AAH50687.1
BC107748 mRNA Translation: AAI07749.1
CCDSiCCDS5348.1
CCDS5349.1 [P63000-2]
PIRiA34788 TVHUC1
RefSeqiNP_008839.2, NM_006908.4 [P63000-1]
NP_061485.1, NM_018890.3 [P63000-2]
UniGeneiHs.413812

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E96X-ray2.40A2-192[»]
1FOEX-ray2.80B/D/F/H1-177[»]
1G4UX-ray2.30R1-184[»]
1HE1X-ray2.00C/D2-176[»]
1HH4X-ray2.70A/B2-192[»]
1I4DX-ray2.50D1-192[»]
1I4LX-ray2.70D1-192[»]
1I4TX-ray2.60D1-192[»]
1MH1X-ray1.38A2-184[»]
1RYFX-ray1.75A/B1-182[»]
1RYHX-ray1.75A/B1-182[»]
2FJUX-ray2.20A1-177[»]
2H7VX-ray2.60A/B1-184[»]
2NZ8X-ray2.00A1-177[»]
2P2LX-ray1.90A/B/C1-184[»]
2RMKNMR-A1-192[»]
2VRWX-ray1.85A1-184[»]
2WKPX-ray1.90A4-180[»]
2WKQX-ray1.60A4-180[»]
2WKRX-ray2.20A4-180[»]
2YINX-ray2.70C/D1-177[»]
3B13X-ray3.01B/D1-177[»]
3BJIX-ray2.60C/D1-177[»]
3RYTX-ray3.58C1-177[»]
3SBDX-ray2.10A/B2-177[»]
3SBEX-ray2.60A2-177[»]
3SU8X-ray3.20A1-177[»]
3SUAX-ray4.39A/B/C1-177[»]
3TH5X-ray2.30A/B2-177[»]
4GZLX-ray2.00A/B2-177[»]
4GZMX-ray2.80A/B2-177[»]
4YONX-ray1.95B1-177[»]
5FI0X-ray3.28B/D/F/H1-192[»]
5HZHX-ray2.60A1-180[»]
5N6OX-ray2.59A/B2-177[»]
5O33X-ray1.64A1-177[»]
6BC1X-ray2.90A/B2-177[»]
ProteinModelPortaliP63000
SMRiP63000
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111817, 197 interactors
CORUMiP63000
DIPiDIP-29260N
IntActiP63000, 141 interactors
MINTiP63000

Chemistry databases

BindingDBiP63000
ChEMBLiCHEMBL6094
DrugBankiDB00514 Dextromethorphan
DB04315 Guanosine-5'-Diphosphate

PTM databases

iPTMnetiP63000
PhosphoSitePlusiP63000
SwissPalmiP63000

Polymorphism and mutation databases

BioMutaiRAC1
DMDMi51702787

Proteomic databases

EPDiP63000
jPOSTiP63000
MaxQBiP63000
PeptideAtlasiP63000
PRIDEiP63000
ProteomicsDBi57467
57468 [P63000-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5879
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000348035; ENSP00000258737; ENSG00000136238 [P63000-1]
ENST00000356142; ENSP00000348461; ENSG00000136238 [P63000-2]
GeneIDi5879
KEGGihsa:5879
UCSCiuc003spw.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5879
DisGeNETi5879
EuPathDBiHostDB:ENSG00000136238.17

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RAC1

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0031500
HGNCiHGNC:9801 RAC1
HPAiCAB035994
HPA047820
MalaCardsiRAC1
MIMi602048 gene
617751 phenotype
neXtProtiNX_P63000
OpenTargetsiENSG00000136238
Orphaneti500159 Microcephaly-corpus callosum and cerebellar vermis hypoplasia-facial dysmorphism-intellectual disability syndrom
PharmGKBiPA34162

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

GeneTreeiENSGT00940000153500
HOGENOMiHOG000233974
HOVERGENiHBG009351
InParanoidiP63000
KOiK04392
OMAiKWHPEIS
OrthoDBi1091615at2759
PhylomeDBiP63000
TreeFamiTF101109

Enzyme and pathway databases

ReactomeiR-HSA-114604 GPVI-mediated activation cascade
R-HSA-1257604 PIP3 activates AKT signaling
R-HSA-1433557 Signaling by SCF-KIT
R-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
R-HSA-164944 Nef and signal transduction
R-HSA-193648 NRAGE signals death through JNK
R-HSA-194840 Rho GTPase cycle
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-2424491 DAP12 signaling
R-HSA-2871796 FCERI mediated MAPK activation
R-HSA-376172 DSCAM interactions
R-HSA-389359 CD28 dependent Vav1 pathway
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-3928664 Ephrin signaling
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-399954 Sema3A PAK dependent Axon repulsion
R-HSA-399955 SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion
R-HSA-4086400 PCP/CE pathway
R-HSA-416550 Sema4D mediated inhibition of cell attachment and migration
R-HSA-418885 DCC mediated attractive signaling
R-HSA-428540 Activation of RAC1
R-HSA-428543 Inactivation of CDC42 and RAC1
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-445144 Signal transduction by L1
R-HSA-5218920 VEGFR2 mediated vascular permeability
R-HSA-5625740 RHO GTPases activate PKNs
R-HSA-5625900 RHO GTPases activate CIT
R-HSA-5625970 RHO GTPases activate KTN1
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5627123 RHO GTPases activate PAKs
R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-5668599 RHO GTPases Activate NADPH Oxidases
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-6798695 Neutrophil degranulation
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-8849471 PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases
R-HSA-8875555 MET activates RAP1 and RAC1
R-HSA-9032759 NTRK2 activates RAC1
R-HSA-9032845 Activated NTRK2 signals through CDK5
R-HSA-9619229 Activation of RAC1 downstream of NMDARs
R-HSA-983231 Factors involved in megakaryocyte development and platelet production
SignaLinkiP63000
SIGNORiP63000

Miscellaneous databases

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

More...
ChiTaRSi
RAC1 human
EvolutionaryTraceiP63000

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
RAC1

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

More...
GenomeRNAii
5879
PMAP-CutDBiP63000

Protein Ontology

More...
PROi
PR:P63000

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000136238 Expressed in 242 organ(s), highest expression level in esophagus squamous epithelium
ExpressionAtlasiP63000 baseline and differential
GenevisibleiP63000 HS

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

More...
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 nameiRAC1_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: P63000
Secondary accession number(s): O95501
, P15154, Q3Y4D3, Q5JAA8, 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: February 13, 2019
This is version 186 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. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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