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P63000 (RAC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related C3 botulinum toxin substrate 1
Alternative name(s):
Cell migration-inducing gene 5 protein
Ras-like protein TC25
p21-Rac1
Gene names
Name:RAC1
Synonyms:TC25
ORF Names:MIG5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 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. 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. Ref.13 Ref.15 Ref.35 Ref.37 Ref.39 Ref.43 Ref.44 Ref.49 Ref.53

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. Ref.13 Ref.15 Ref.35 Ref.37 Ref.39 Ref.43 Ref.44 Ref.49 Ref.53

Enzyme regulation

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. Ref.47

Subunit structure

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. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.30 Ref.31 Ref.32 Ref.33 Ref.38 Ref.39 Ref.42 Ref.44 Ref.45 Ref.49 Ref.50 Ref.51 Ref.52 Ref.54

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Melanosome. Cytoplasm By similarity. Note: Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine By similarity. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts By similarity. Ref.29 Ref.44 Ref.49

Tissue specificity

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.

Domain

The effector region mediates interaction with DEF6. Ref.31

Post-translational modification

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.

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

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Sequence caution

The sequence AAZ80485.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandGTP-binding
Nucleotide-binding
   PTMADP-ribosylation
Isopeptide bond
Lipoprotein
Methylation
Phosphoprotein
Prenylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

T cell costimulation

Traceable author statement. Source: Reactome

Wnt signaling pathway, planar cell polarity pathway

Inferred from electronic annotation. Source: Ensembl

actin cytoskeleton organization

Inferred from genetic interaction PubMed 19890013. Source: MGI

actin filament polymerization

Traceable author statement PubMed 9312003. Source: UniProtKB

anatomical structure arrangement

Inferred from electronic annotation. Source: Ensembl

anatomical structure morphogenesis

Traceable author statement PubMed 9572733. Source: ProtInc

apoptotic signaling pathway

Traceable author statement. Source: Reactome

auditory receptor cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

bone resorption

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Traceable author statement PubMed 9572733. Source: ProtInc

cell motility

Inferred from direct assay Ref.39. Source: UniProtKB

cell proliferation

Inferred from electronic annotation. Source: Ensembl

cell-cell junction organization

Inferred from electronic annotation. Source: Ensembl

cell-matrix adhesion

Non-traceable author statement PubMed 18156211. Source: BHF-UCL

cellular component movement

Traceable author statement PubMed 9572733. Source: ProtInc

cerebral cortex radially oriented cell migration

Inferred from electronic annotation. Source: Ensembl

cochlea morphogenesis

Inferred from electronic annotation. Source: Ensembl

dendrite morphogenesis

Inferred from electronic annotation. Source: Ensembl

dopaminergic neuron differentiation

Inferred from electronic annotation. Source: Ensembl

embryonic olfactory bulb interneuron precursor migration

Inferred from electronic annotation. Source: Ensembl

engulfment of apoptotic cell

Inferred from electronic annotation. Source: Ensembl

epithelial cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

hyperosmotic response

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Traceable author statement PubMed 9572733. Source: ProtInc

innate immune response

Traceable author statement. Source: Reactome

intracellular signal transduction

Traceable author statement PubMed 9572733. Source: ProtInc

lamellipodium assembly

Inferred from mutant phenotype PubMed 9312003. Source: UniProtKB

localization within membrane

Inferred from mutant phenotype PubMed 16636067. Source: BHF-UCL

mast cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-23 production

Inferred from direct assay PubMed 16982892. Source: BHF-UCL

negative regulation of receptor-mediated endocytosis

Traceable author statement PubMed 9312003. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of Rho protein signal transduction

Traceable author statement PubMed 9312003. Source: UniProtKB

positive regulation of actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of lamellipodium assembly

Inferred from direct assay PubMed 15467718. Source: MGI

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from mutant phenotype Ref.53. Source: UniProtKB

regulation of cell migration

Inferred from mutant phenotype Ref.37Ref.48. Source: UniProtKB

regulation of defense response to virus by virus

Traceable author statement. Source: Reactome

regulation of hydrogen peroxide metabolic process

Traceable author statement PubMed 16636067. Source: BHF-UCL

regulation of respiratory burst

Inferred from direct assay PubMed 16636067. Source: BHF-UCL

response to wounding

Traceable author statement PubMed 9572733. Source: ProtInc

ruffle assembly

Inferred from electronic annotation. Source: Ensembl

ruffle organization

Traceable author statement PubMed 9312003. Source: UniProtKB

semaphorin-plexin signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: Ensembl

substrate adhesion-dependent cell spreading

Inferred from electronic annotation. Source: Ensembl

viral process

Traceable author statement. Source: Reactome

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

extrinsic component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

lamellipodium

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

phagocytic cup

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

ruffle membrane

Inferred from electronic annotation. Source: Ensembl

trans-Golgi network

Inferred from direct assay PubMed 12915445. Source: FlyBase

   Molecular_functionGTP binding

Inferred from direct assay Ref.48. Source: UniProtKB

GTPase activity

Traceable author statement PubMed 9312003. Source: UniProtKB

Rho GDP-dissociation inhibitor binding

Inferred from sequence or structural similarity. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 16636067. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.23PubMed 15048733Ref.33Ref.39PubMed 19843518PubMed 20660631Ref.45Ref.50Ref.48Ref.51Ref.14. Source: UniProtKB

thioesterase binding

Inferred from physical interaction Ref.26. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: P63000-1)

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.
Isoform B (identifier: P63000-2)

Also known as: Rac1B; Rac1ins;

The sequence of this isoform differs from the canonical sequence as follows:
     75-75: T → TVGETYGKDITSRGKDKPIA
Note: Contains a phosphoserine at position 71.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 189189Ras-related C3 botulinum toxin substrate 1
PRO_0000042036
Propeptide190 – 1923Removed in mature form By similarity
PRO_0000042037

Regions

Nucleotide binding10 – 178GTP By similarity
Nucleotide binding57 – 615GTP By similarity
Nucleotide binding115 – 1184GTP By similarity
Motif32 – 409Effector region Potential

Amino acid modifications

Modified residue321O-AMP-tyrosine; by Haemophilus IbpA
Modified residue351O-AMP-threonine; by Vibrio VopS
Modified residue391ADP-ribosylasparagine; by botulinum toxin By similarity
Modified residue1891Cysteine methyl ester By similarity
Lipidation1891S-geranylgeranyl cysteine Ref.12
Cross-link147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.34

Natural variations

Alternative sequence751T → TVGETYGKDITSRGKDKPIA in isoform B.
VSP_005710
Natural variant261N → D.
Corresponds to variant rs5830 [ dbSNP | Ensembl ].
VAR_014540
Natural variant281F → L.
Corresponds to variant rs5832 [ dbSNP | Ensembl ].
VAR_014541
Natural variant591A → T.
Corresponds to variant rs5837 [ dbSNP | Ensembl ].
VAR_014542
Natural variant631D → G.
Corresponds to variant rs5831 [ dbSNP | Ensembl ].
VAR_014543
Natural variant931V → G.
Corresponds to variant rs5826 [ dbSNP | Ensembl ].
VAR_014545
Natural variant931V → I.
Corresponds to variant rs5825 [ dbSNP | Ensembl ].
VAR_014544
Natural variant1081T → I.
Corresponds to variant rs5838 [ dbSNP | Ensembl ].
VAR_014546
Natural variant1301K → R.
Corresponds to variant rs5828 [ dbSNP | Ensembl ].
VAR_014547
Natural variant1331K → E.
Corresponds to variant rs5835 [ dbSNP | Ensembl ].
VAR_014548
Natural variant1351T → I. Ref.7
Corresponds to variant rs11540455 [ dbSNP | Ensembl ].
VAR_033303
Natural variant1801P → S.
Corresponds to variant rs16063 [ dbSNP | Ensembl ].
VAR_014549
Natural variant1821V → E.
Corresponds to variant rs5836 [ dbSNP | Ensembl ].
VAR_014550

Experimental info

Mutagenesis121G → V: Constitutively active. Interacts with PARD6 proteins. Increases nuclear localization and up-regulates transcriptional activity of NR3C2. Ref.21 Ref.35
Mutagenesis171T → 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. Ref.21 Ref.35 Ref.44
Mutagenesis301G → V: No interaction with PPP5C; when associated with L-61. Translocates to the plasma membrane; also when associated with L-61. Ref.44
Mutagenesis321Y → F: Abolishes AMPylation by Haemophilus IbpA. Ref.40
Mutagenesis351T → A: Abolishes AMPylation by Vibrio VopS. Ref.41 Ref.44
Mutagenesis351T → S: No interaction with PPP5C; when associated with L-61. Translocates to the plasma membrane; also when associated with L-61. Ref.41 Ref.44
Mutagenesis371F → A: Strongly reduced interaction with PLCB2. Ref.64
Mutagenesis561W → A: Strongly reduced interaction with PLCB2. Ref.64
Mutagenesis611Q → L: Constitutively active. Interacts with PARD6 proteins. Interacts with PPP5C, activates its phosphatase activity and translocates PPP5C to the plasma membrane. 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. Ref.18 Ref.44
Mutagenesis671L → A: Strongly reduced interaction with PLCB2. Ref.64
Mutagenesis701L → A: Strongly reduced interaction with PLCB2. Ref.64
Sequence conflict1921Missing in AAA36544. Ref.2

Secondary structure

....................................... 192
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A (Rac1A) [UniParc].

Last modified August 31, 2004. Version 1.
Checksum: ACEDF83A45E5EA67

FASTA19221,450
        10         20         30         40         50         60 
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG 

        70         80         90        100        110        120 
QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPNTPI ILVGTKLDLR 

       130        140        150        160        170        180 
DDKDTIEKLK EKKLTPITYP QGLAMAKEIG AVKYLECSAL TQRGLKTVFD EAIRAVLCPP 

       190 
PVKKRKRKCL LL 

« Hide

Isoform B (Rac1B) (Rac1ins) [UniParc] [UniParc].

Checksum: 93745E0CFBA5281F
Show »

FASTA21123,467

References

« Hide 'large scale' references
[1]"Rac, a novel ras-related family of proteins that are botulinum toxin substrates."
Didsbury J., Weber R.F., Bokoch G.M., Evans T., Snyderman R.
J. Biol. Chem. 264:16378-16382(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[2]"Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line."
Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P.
Mol. Cell. Biol. 10:1793-1798(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[3]"Small GTPase Rac1: structure, localization, and expression of the human gene."
Matos P., Skaug J., Marques B., Beck S., Verissimo F., Gespach C., Boavida M.G., Scherer S.W., Jordan P.
Biochem. Biophys. Res. Commun. 277:741-751(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B).
[4]"Cloning of a novel human Rac1b splice variant with increased expression in colorectal tumors."
Jordan P., Brazao R., Boavida M.G., Gespach C., Chastre E.
Oncogene 18:6835-6839(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
Tissue: Colon and Skin.
[5]"Mutations and altered expression of Rac1 in human breast cancer --characterization of a new Rac1 isoform, Rac1ins."
Schnelzer A., Knaus U., Prechtel D., Dehne K., Harbeck N., Gerhard M., Schmitt M., Lengyel E.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
[6]"Identification of a human migration-inducing gene."
Kim J.W.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
[7]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Puhl H.L. III, Ikeda S.R., Aronstam R.S.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), VARIANT ILE-135.
[8]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
[9]NIEHS SNPs program
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Tissue: Pancreas and Skin.
[12]"Carboxyl-terminal isoprenylation of ras-related GTP-binding proteins encoded by rac1, rac2, and ralA."
Kinsella B.T., Erdman R.A., Maltese W.A.
J. Biol. Chem. 266:9786-9794(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: ISOPRENYLATION AT CYS-189.
[13]"The small GTP-binding protein rac regulates growth factor-induced membrane ruffling."
Ridley A.J., Paterson H.F., Johnston C.L., Diekmann D., Hall A.
Cell 70:401-410(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity."
Jullien-Flores V., Dorseuil O., Romero F., Letourneur F., Saragosti S., Berger R., Tavitian A., Gacon G., Camonis J.H.
J. Biol. Chem. 270:22473-22477(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RALBP1.
[15]"The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization."
Vincent S., Settleman J.
Mol. Cell. Biol. 17:2247-2256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PKN2.
[16]"Cloning and characterization of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases."
Ren Y., Li R., Zheng Y., Busch H.
J. Biol. Chem. 273:34954-34960(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGEF2.
[17]"Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins."
Nishihara H., Kobayashi S., Hashimoto Y., Ohba F., Mochizuki N., Kurata T., Nagashima K., Matsuda M.
Biochim. Biophys. Acta 1452:179-187(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DOCK2.
[18]"The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1."
Johansson A.-S., Driessens M., Aspenstroem P.
J. Cell Sci. 113:3267-3275(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARD6A, MUTAGENESIS OF GLN-61.
[19]"IRSp53 is an essential intermediate between Rac and WAVE in the regulation of membrane ruffling."
Miki H., Yamaguchi H., Suetsugu S., Takenawa T.
Nature 408:732-735(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAIAP2.
[20]"The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner."
Vikis H.G., Li W., He Z., Guan K.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:12457-12462(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLXNB1.
[21]"Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C."
Noda Y., Takeya R., Ohno S., Naito S., Ito T., Sumimoto H.
Genes Cells 6:107-119(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARD6A; PARD6B AND PARD6G; PRKCI AND PRKCZ, MUTAGENESIS OF GLY-12 AND THR-17.
[22]"P-Rex1, a PtdIns(3,4,5)P3- and Gbetagamma-regulated guanine-nucleotide exchange factor for Rac."
Welch H.C.E., Coadwell W.J., Ellson C.D., Ferguson G.J., Andrews S.R., Erdjument-Bromage H., Tempst P., Hawkins P.T., Stephens L.R.
Cell 108:809-821(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVATION BY PREX1.
[23]"The integrin cytoplasmic domain-associated protein ICAP-1 binds and regulates Rho family GTPases during cell spreading."
Degani S., Balzac F., Brancaccio M., Guazzone S., Retta S.F., Silengo L., Eva A., Tarone G.
J. Cell Biol. 156:377-387(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITGB1BP1.
[24]"Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex."
Brugnera E., Haney L., Grimsley C., Lu M., Walk S.F., Tosello-Trampont A.-C., Macara I.G., Madhani H., Fink G.R., Ravichandran K.S.
Nat. Cell Biol. 4:574-582(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT OF A COMPLEX CONTAINING ELMO1 AND DOCK1.
[25]"Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases."
Takeya R., Ueno N., Kami K., Taura M., Kohjima M., Izaki T., Nunoi H., Sumimoto H.
J. Biol. Chem. 278:25234-25246(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOXA1.
[26]"The TRE17 oncogene encodes a component of a novel effector pathway for Rho GTPases Cdc42 and Rac1 and stimulates actin remodeling."
Masuda-Robens J.M., Kutney S.N., Qi H., Chou M.M.
Mol. Cell. Biol. 23:2151-2161(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH USP6.
[27]"The Down syndrome cell adhesion molecule (DSCAM) interacts with and activates Pak."
Li W., Guan K.L.
J. Biol. Chem. 279:32824-32831(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DSCAM.
[28]"The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67phox and Rac-2."
Kerkhoff C., Nacken W., Benedyk M., Dagher M.C., Sopalla C., Doussiere J.
FASEB J. 19:467-469(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH S100A8 AND CALPROTECTIN.
[29]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[30]"The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18."
Watabe-Uchida M., John K.A., Janas J.A., Newey S.E., Van Aelst L.
Neuron 51:727-739(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DOCK7.
[31]"Cooperation of DEF6 with activated Rac in regulating cell morphology."
Oka T., Ihara S., Fukui Y.
J. Biol. Chem. 282:2011-2018(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DEF6, DOMAIN.
[32]"Characterisation of IRTKS, a novel IRSp53/MIM family actin regulator with distinct filament bundling properties."
Millard T.H., Dawson J., Machesky L.M.
J. Cell Sci. 120:1663-1672(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAIAP2L1.
[33]"Asef2 functions as a Cdc42 exchange factor and is stimulated by the release of an autoinhibitory module from a concealed C-terminal activation element."
Hamann M.J., Lubking C.M., Luchini D.N., Billadeau D.D.
Mol. Cell. Biol. 27:1380-1393(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPATA13.
[34]"Activated Rac1, but not the tumorigenic variant Rac1b, is ubiquitinated on Lys 147 through a JNK-regulated process."
Visvikis O., Lores P., Boyer L., Chardin P., Lemichez E., Gacon G.
FEBS J. 275:386-396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-147.
[35]"Modification of mineralocorticoid receptor function by Rac1 GTPase: implication in proteinuric kidney disease."
Shibata S., Nagase M., Yoshida S., Kawarazaki W., Kurihara H., Tanaka H., Miyoshi J., Takai Y., Fujita T.
Nat. Med. 14:1370-1376(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-12 AND THR-17.
[36]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 (ISOFORM B), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[37]"The Rho-family GEF Asef2 activates Rac to modulate adhesion and actin dynamics and thereby regulate cell migration."
Bristow J.M., Sellers M.H., Majumdar D., Anderson B., Hu L., Webb D.J.
J. Cell Sci. 122:4535-4546(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[38]"The SWI/SNF protein BAF60b is ubiquitinated through a signalling process involving Rac GTPase and the RING finger protein Unkempt."
Lores P., Visvikis O., Luna R., Lemichez E., Gacon G.
FEBS J. 277:1453-1464(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UNKL.
[39]"BPAG1e maintains keratinocyte polarity through beta4 integrin-mediated modulation of Rac1 and cofilin activities."
Hamill K.J., Hopkinson S.B., DeBiase P., Jones J.C.
Mol. Biol. Cell 20:2954-2962(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ITGB4.
[40]"The fic domain: regulation of cell signaling by adenylylation."
Worby C.A., Mattoo S., Kruger R.P., Corbeil L.B., Koller A., Mendez J.C., Zekarias B., Lazar C., Dixon J.E.
Mol. Cell 34:93-103(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: AMPYLATION AT TYR-32, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF TYR-32.
[41]"AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling."
Yarbrough M.L., Li Y., Kinch L.N., Grishin N.V., Ball H.L., Orth K.
Science 323:269-272(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: AMPYLATION AT THR-35, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF THR-35.
[42]"Armus is a Rac1 effector that inactivates Rab7 and regulates E-cadherin degradation."
Frasa M.A., Maximiano F.C., Smolarczyk K., Francis R.E., Betson M.E., Lozano E., Goldenring J., Seabra M.C., Rak A., Ahmadian M.R., Braga V.M.
Curr. Biol. 20:198-208(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TBC1D2.
[43]"Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through RhoGDIalpha-mediated inactivation of Rac1 GTPase."
Li X., Lee A.Y.
J. Biol. Chem. 285:32436-32445(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[44]"Activated Rac1 GTPase translocates protein phosphatase 5 to the cell membrane and stimulates phosphatase activity in vitro."
Chatterjee A., Wang L., Armstrong D.L., Rossie S.
J. Biol. Chem. 285:3872-3882(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PPP5C, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-17; GLY-30; THR-35 AND GLN-61.
[45]"Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent mechanism."
Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S., Negishi M., Katoh H.
J. Cell Biol. 190:461-477(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGEF16.
[46]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[47]"ARHGAP30 is a Wrch-1-interacting protein involved in actin dynamics and cell adhesion."
Naji L., Pacholsky D., Aspenstrom P.
Biochem. Biophys. Res. Commun. 409:96-102(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[48]"The E3 ubiquitin-ligase HACE1 catalyzes the ubiquitylation of active Rac1."
Torrino S., Visvikis O., Doye A., Boyer L., Stefani C., Munro P., Bertoglio J., Gacon G., Mettouchi A., Lemichez E.
Dev. Cell 21:959-965(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION.
[49]"The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration."
de Kreuk B.J., Nethe M., Fernandez-Borja M., Anthony E.C., Hensbergen P.J., Deelder A.M., Plomann M., Hordijk P.L.
J. Cell Sci. 124:2375-2388(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PACSIN2.
[50]"The Rho target PRK2 regulates apical junction formation in human bronchial epithelial cells."
Wallace S.W., Magalhaes A., Hall A.
Mol. Cell. Biol. 31:81-91(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PKN2.
[51]"The novel synaptogenic protein Farp1 links postsynaptic cytoskeletal dynamics and transsynaptic organization."
Cheadle L., Biederer T.
J. Cell Biol. 199:985-1001(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FARP1.
[52]"ARHGDIA: a novel gene implicated in nephrotic syndrome."
Gupta I.R., Baldwin C., Auguste D., Ha K.C., El Andalousi J., Fahiminiya S., Bitzan M., Bernard C., Akbari M.R., Narod S.A., Rosenblatt D.S., Majewski J., Takano T.
J. Med. Genet. 50:330-338(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARHGDIA.
[53]"Beta-arrestin-dependent activation of the cofilin pathway is required for the scavenging activity of the atypical chemokine receptor D6."
Borroni E.M., Cancellieri C., Vacchini A., Benureau Y., Lagane B., Bachelerie F., Arenzana-Seisdedos F., Mizuno K., Mantovani A., Bonecchi R., Locati M.
Sci. Signal. 6:RA30-RA30(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[54]"Structural basis for autoinhibition of the guanine nucleotide exchange factor FARP2."
He X., Kuo Y.C., Rosche T.J., Zhang X.
Structure 21:355-364(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FARP2.
[55]"The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue."
Hirshberg M., Stockley R.W., Dodson G., Webb M.R.
Nat. Struct. Biol. 4:147-152(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 1-184 IN COMPLEX WITH GTP ANALOG.
[56]"Structure of the TPR domain of p67phox in complex with Rac.GTP."
Lapouge K., Smith S.J., Walker P.A., Gamblin S.J., Smerdon S.J., Rittinger K.
Mol. Cell 6:899-907(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT LEU-61 IN COMPLEX WITH GTP AND NCF2.
[57]"Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1."
Worthylake D.K., Rossman K.L., Sondek J.
Nature 408:682-688(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-177 IN COMPLEX WITH TIAM1.
[58]"Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1."
Stebbins C.E., Galan J.E.
Mol. Cell 6:1449-1460(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-184 IN COMPLEX WITH SALMONELLA SPTP.
[59]"How the Pseudomonas aeruginosa ExoS toxin downregulates Rac."
Wuertele M., Wolf E., Pederson K.J., Buchwald G., Ahmadian M.R., Barbieri J.T., Wittinghofer A.
Nat. Struct. Biol. 8:23-26(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-176 IN COMPLEX WITH GTP ANALOG AND P.AERUGINOSA EXOS.
[60]"Crystal structure of the Rac1-RhoGDI complex involved in NADPH oxidase activation."
Grizot S., Faure J., Fieschi F., Vignais P.V., Dagher M.-C., Pebay-Peyroula E.
Biochemistry 40:10007-10013(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ARHGDIA.
[61]"The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways."
Tarricone C., Xiao B., Justin N., Walker P.A., Rittinger K., Gamblin S.J., Smerdon S.J.
Nature 411:215-219(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GTP ANALOG AND ARFIP2.
[62]"Alternative splicing of Rac1 generates Rac1b, a self-activating GTPase."
Fiegen D., Haeusler L.C., Blumenstein L., Herbrand U., Dvorsky R., Vetter I.R., Ahmadian M.R.
J. Biol. Chem. 279:4743-4749(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF ISOFORM B, CHARACTERIZATION (ISOFORM B).
[63]"Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors."
Prehna G., Ivanov M.I., Bliska J.B., Stebbins C.E.
Cell 126:869-880(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-184 IN COMPLEX WITH Y.PSEUDOTUBERCULOSIS YPKA.
[64]"Crystal structure of Rac1 bound to its effector phospholipase C-beta2."
Jezyk M.R., Snyder J.T., Gershberg S., Worthylake D.K., Harden T.K., Sondek J.
Nat. Struct. Mol. Biol. 13:1135-1140(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-177 IN COMPLEX WITH GTP ANALOG AND PLCB2, MUTAGENESIS OF PHE-37; TRP-56; LEU-67 AND LEU-70.
[65]"Multiple factors confer specific Cdc42 and Rac protein activation by dedicator of cytokinesis (DOCK) nucleotide exchange factors."
Kulkarni K., Yang J., Zhang Z., Barford D.
J. Biol. Chem. 286:25341-25351(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-177 IN COMPLEX WITH DOCK2.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS5348.1.
CCDS5349.1. [P63000-2]
PIRTVHUC1. A34788.
RefSeqNP_008839.2. NM_006908.4. [P63000-1]
NP_061485.1. NM_018890.3. [P63000-2]
UniGeneHs.413812.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
DisProtDP00408.
ProteinModelPortalP63000.
SMRP63000. Positions 1-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111817. 127 interactions.
DIPDIP-29260N.
IntActP63000. 94 interactions.
MINTMINT-4999291.
STRING9606.ENSP00000348461.

Chemistry

BindingDBP63000.
ChEMBLCHEMBL6094.
DrugBankDB00175. Pravastatin.
DB00641. Simvastatin.

PTM databases

PhosphoSiteP63000.

Polymorphism databases

DMDM51702787.

Proteomic databases

MaxQBP63000.
PaxDbP63000.
PRIDEP63000.

Protocols and materials databases

DNASU5879.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000348035; ENSP00000258737; ENSG00000136238. [P63000-1]
ENST00000356142; ENSP00000348461; ENSG00000136238. [P63000-2]
GeneID5879.
KEGGhsa:5879.
UCSCuc003spx.3. human.

Organism-specific databases

CTD5879.
GeneCardsGC07P006380.
H-InvDBHIX0031500.
HGNCHGNC:9801. RAC1.
HPACAB035994.
MIM602048. gene.
neXtProtNX_P63000.
PharmGKBPA34162.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233974.
HOVERGENHBG009351.
KOK04392.
OMAYPQTVAE.
OrthoDBEOG764747.
PhylomeDBP63000.
TreeFamTF101109.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP63000.

Gene expression databases

ArrayExpressP63000.
BgeeP63000.
CleanExHS_RAC1.
GenevestigatorP63000.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAC1. human.
EvolutionaryTraceP63000.
GeneWikiRAC1.
GenomeRNAi5879.
NextBio22846.
PMAP-CutDBP63000.
PROP63000.
SOURCESearch...

Entry information

Entry nameRAC1_HUMAN
AccessionPrimary (citable) accession number: P63000
Secondary accession number(s): O95501 expand/collapse secondary AC list , P15154, Q3Y4D3, Q5JAA8, Q9BTB4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: July 9, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM