P63000 (RAC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity. 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. Ref.13 Ref.15 Ref.35 Ref.37 Ref.41 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.41
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.44
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 and mediated through PLXNB3 By similarity. 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, 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). 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.29 Ref.30 Ref.31 Ref.32 Ref.36 Ref.37 Ref.40 Ref.42 Ref.46
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.28
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.30
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 component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	GTP-binding Nucleotide-binding
PTM	ADP-ribosylation Isopeptide bond Lipoprotein Methylation Phosphoprotein Prenylation Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell costimulation Traceable author statement. Source: Reactome Wnt receptor signaling pathway, planar cell polarity pathway Inferred from electronic annotation. Source: Compara actin filament polymerization Traceable author statement PubMed 9312003. Source: UniProtKB anatomical structure arrangement Inferred from electronic annotation. Source: Compara apoptotic process Traceable author statement. Source: Reactome auditory receptor cell morphogenesis Inferred from electronic annotation. Source: Compara axon guidance Traceable author statement. Source: Reactome bone resorption Inferred from electronic annotation. Source: Compara cell motility Inferred from direct assay Ref.37. Source: UniProtKB cell proliferation Inferred from electronic annotation. Source: Compara cell-cell junction organization Inferred from electronic annotation. Source: Compara cell-matrix adhesion Non-traceable author statement PubMed 18156211. Source: BHF-UCL cerebral cortex radially oriented cell migration Inferred from electronic annotation. Source: Compara cochlea morphogenesis Inferred from electronic annotation. Source: Compara dendrite morphogenesis Inferred from electronic annotation. Source: Compara dopaminergic neuron differentiation Inferred from electronic annotation. Source: Compara embryonic olfactory bulb interneuron precursor migration Inferred from electronic annotation. Source: Compara engulfment of apoptotic cell Inferred from electronic annotation. Source: Compara epithelial cell morphogenesis Inferred from electronic annotation. Source: Compara hyperosmotic response Inferred from electronic annotation. Source: Compara inflammatory response 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: Compara 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 nerve growth factor 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: Compara 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: Compara 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: Compara regulation of cell migration Inferred from mutant phenotype Ref.35Ref.45. 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 ruffle assembly Inferred from electronic annotation. Source: Compara ruffle organization Traceable author statement PubMed 9312003. Source: UniProtKB small GTPase mediated signal transduction Traceable author statement. Source: Reactome substrate adhesion-dependent cell spreading Inferred from electronic annotation. Source: Compara viral reproduction Traceable author statement. Source: Reactome
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome extrinsic to plasma membrane Inferred from electronic annotation. Source: Compara lamellipodium Inferred from electronic annotation. Source: Compara melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell phagocytic cup Inferred from electronic annotation. Source: Compara plasma membrane Traceable author statement. Source: Reactome ruffle membrane Inferred from electronic annotation. Source: Compara trans-Golgi network Inferred from direct assay PubMed 12915445. Source: FlyBase
Molecular_function	GTP binding Inferred from direct assay Ref.45. Source: UniProtKB GTPase activity Traceable author statement PubMed 9312003. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARFIP2	P53365	9	EBI-413628,EBI-638194
BAIAP2	Q9UQB8	4	EBI-413628,EBI-525456
DOCK1	Q14185	8	EBI-413628,EBI-446740
LRRK2	Q5S007	5	EBI-413628,EBI-5323863
NCF2	P19878	2	EBI-413628,EBI-489611
PAK1	Q13153	8	EBI-413628,EBI-1307
PAK3	O75914	2	EBI-413628,EBI-3389553
PARD6A	Q9NPB6	2	EBI-413628,EBI-81876
PARD6B	Q9BYG5	3	EBI-413628,EBI-295391
PARD6G	Q9BYG4	2	EBI-413628,EBI-295417
PRKCI	P41743	3	EBI-413628,EBI-286199

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 189

189

Ras-related C3 botulinum toxin substrate 1

PRO_0000042036

Propeptide

190 – 192

3

Removed in mature form By similarity

PRO_0000042037

Regions

Nucleotide binding

10 – 17

8

GTP By similarity

Nucleotide binding

57 – 61

5

GTP By similarity

Nucleotide binding

115 – 118

4

GTP By similarity

Motif

32 – 40

9

Effector region Potential

Amino acid modifications

Modified residue

32

1

O-AMP-tyrosine; by Haemophilus IbpA

Modified residue

35

1

O-AMP-threonine; by Vibrio VopS

Modified residue

39

1

ADP-ribosylasparagine; by botulinum toxin By similarity

Modified residue

189

1

Cysteine methyl ester

Lipidation

189

1

S-geranylgeranyl cysteine Ref.12

Cross-link

147

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.33

Natural variations

Alternative sequence

75

1

T → TVGETYGKDITSRGKDKPIA in isoform B.

VSP_005710

Natural variant

26

1

N → D.
Corresponds to variant rs5830 [ dbSNP | Ensembl ].

VAR_014540

Natural variant

28

1

F → L.
Corresponds to variant rs5832 [ dbSNP | Ensembl ].

VAR_014541

Natural variant

59

1

A → T.
Corresponds to variant rs5837 [ dbSNP | Ensembl ].

VAR_014542

Natural variant

63

1

D → G.
Corresponds to variant rs5831 [ dbSNP | Ensembl ].

VAR_014543

Natural variant

93

1

V → G.
Corresponds to variant rs5826 [ dbSNP | Ensembl ].

VAR_014545

Natural variant

93

1

V → I.
Corresponds to variant rs5825 [ dbSNP | Ensembl ].

VAR_014544

Natural variant

108

1

T → I.
Corresponds to variant rs5838 [ dbSNP | Ensembl ].

VAR_014546

Natural variant

130

1

K → R.
Corresponds to variant rs5828 [ dbSNP | Ensembl ].

VAR_014547

Natural variant

133

1

K → E.
Corresponds to variant rs5835 [ dbSNP | Ensembl ].

VAR_014548

Natural variant

135

1

T → I. Ref.7
Corresponds to variant rs11540455 [ dbSNP | Ensembl ].

VAR_033303

Natural variant

180

1

P → S.
Corresponds to variant rs16063 [ dbSNP | Ensembl ].

VAR_014549

Natural variant

182

1

V → E.
Corresponds to variant rs5836 [ dbSNP | Ensembl ].

VAR_014550

Experimental info

Mutagenesis

12

1

G → V: Constitutively active. Interacts with PARD6 proteins. Ref.21

Mutagenesis

17

1

T → N: Constitutively inactivated. Abolishes interaction with PARD6 proteins. Ref.21

Mutagenesis

32

1

Y → F: Abolishes AMPylation by Haemophilus IbpA. Ref.38

Mutagenesis

35

1

T → A: Abolishes AMPylation by Vibrio VopS. Ref.39

Mutagenesis

37

1

F → A: Strongly reduced interaction with PLCB2. Ref.56

Mutagenesis

56

1

W → A: Strongly reduced interaction with PLCB2. Ref.56

Mutagenesis

61

1

Q → L: Constitutively active. Interacts with PARD6 proteins. Ref.18

Mutagenesis

67

1

L → A: Strongly reduced interaction with PLCB2. Ref.56

Mutagenesis

70

1

L → A: Strongly reduced interaction with PLCB2. Ref.56

Sequence conflict

192

1

Missing in AAA36544. Ref.2

Secondary structure

1

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192

Helix Strand Turn

Details...

Beta strand

2 – 9

8

Helix

12 – 14

3

Helix

16 – 25

10

Beta strand

31 – 36

6

Beta strand

39 – 46

8

Beta strand

49 – 56

8

Helix

62 – 64

3

Turn

65 – 67

3

Helix

68 – 71

4

Beta strand

76 – 83

8

Helix

87 – 95

9

Helix

97 – 104

8

Beta strand

106 – 108

3

Beta strand

110 – 115

6

Helix

117 – 120

4

Helix

123 – 131

9

Helix

139 – 148

10

Beta strand

152 – 156

5

Turn

159 – 161

3

Helix

165 – 176

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (Rac1A) [UniParc]. Last modified August 31, 2004. Version 1. Checksum: ACEDF83A45E5EA67	FASTA	192	21,450
	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
	Isoform B (Rac1B) (Rac1ins) [UniParc] [UniParc]. Checksum: 93745E0CFBA5281F	FASTA	211	23,467
	10 20 30 40 50 60 MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG 70 80 90 100 110 120 QEDYDRLRPL SYPQTVGETY GKDITSRGKD KPIADVFLIC FSLVSPASFE NVRAKWYPEV 130 140 150 160 170 180 RHHCPNTPII LVGTKLDLRD DKDTIEKLKE KKLTPITYPQ GLAMAKEIGA VKYLECSALT 190 200 210 QRGLKTVFDE AIRAVLCPPP VKKRKRKCLL L

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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.
[28]	"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], MASS SPECTROMETRY. Tissue: Melanoma.
[29]	"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.
[30]	"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.
[31]	"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.
[32]	"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.
[33]	"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.
[34]	"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), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[35]	"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.
[36]	"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.
[37]	"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.
[38]	"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, MASS SPECTROMETRY, MUTAGENESIS OF TYR-32.
[39]	"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, MASS SPECTROMETRY, MUTAGENESIS OF THR-35.
[40]	"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.
[41]	"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.
[42]	"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.
[43]	"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].
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"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.
[48]	"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.
[49]	"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.
[50]	"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.
[51]	"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.
[52]	"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.
[53]	"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.
[54]	"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).
[55]	"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.
[56]	"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.
[57]	"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

NIEHS-SNPs

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.

IPI

IPI00010271.
IPI00219675.

PIR

TVHUC1. A34788.

RefSeq

NP_008839.2. NM_006908.4.
NP_061485.1. NM_018890.3.

UniGene

Hs.413812.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E96	X-ray	2.40	A	2-192	[»]
1FOE	X-ray	2.80	B/D/F/H	1-177	[»]
1G4U	X-ray	2.30	R	1-184	[»]
1HE1	X-ray	2.00	C/D	2-176	[»]
1HH4	X-ray	2.70	A/B	2-192	[»]
1I4D	X-ray	2.50	D	1-192	[»]
1I4L	X-ray	2.70	D	1-192	[»]
1I4T	X-ray	2.60	D	1-192	[»]
1MH1	X-ray	1.38	A	2-184	[»]
1RYF	X-ray	1.75	A/B	1-182	[»]
1RYH	X-ray	1.75	A/B	1-182	[»]
2FJU	X-ray	2.20	A	1-177	[»]
2H7V	X-ray	2.60	A/B	1-184	[»]
2NZ8	X-ray	2.00	A	1-177	[»]
2P2L	X-ray	1.90	A/B/C	1-184	[»]
2RMK	NMR	-	A	1-192	[»]
2VRW	X-ray	1.85	A	1-184	[»]
2WKP	X-ray	1.90	A	4-180	[»]
2WKQ	X-ray	1.60	A	4-180	[»]
2WKR	X-ray	2.20	A	4-180	[»]
2YIN	X-ray	2.70	C/D	1-177	[»]
3B13	X-ray	3.01	B/D	1-177	[»]
3BJI	X-ray	2.60	C/D	1-177	[»]
3RYT	X-ray	3.58	C	1-177	[»]
3SBD	X-ray	2.10	A/B	2-177	[»]
3SBE	X-ray	2.60	A	2-177	[»]
3SU8	X-ray	3.20	A	1-177	[»]
3SUA	X-ray	4.39	A/B/C	1-177	[»]
3TH5	X-ray	2.30	A/B	2-177	[»]
4GZL	X-ray	2.00	A/B	2-177	[»]
4GZM	X-ray	2.80	A/B	2-177	[»]

DisProt

DP00408.

ProteinModelPortal

P63000.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29260N.

IntAct

P63000. 65 interactions.

MINT

MINT-4999291.

STRING

9606.ENSP00000348461.

PTM databases

PhosphoSite

P63000.

Polymorphism databases

DMDM

51702787.

Proteomic databases

PaxDb

P63000.

PRIDE

P63000.

Protocols and materials databases

DNASU

5879.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000348035; ENSP00000258737; ENSG00000136238.
ENST00000356142; ENSP00000348461; ENSG00000136238.

GeneID

5879.

KEGG

hsa:5879.

UCSC

uc003spx.3. human.

Organism-specific databases

CTD

5879.

GeneCards

GC07P006380.

H-InvDB

HIX0031500.

HGNC

HGNC:9801. RAC1.

HPA

CAB035994.

MIM

602048. gene.

neXtProt

NX_P63000.

PharmGKB

PA34162.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233974.

HOVERGEN

HBG009351.

KO

K04392.

OMA

DTCGKDR.

OrthoDB

EOG466VN1.

Enzyme and pathway databases

Pathway_Interaction_DB

a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling.
angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
arf_3pathway. Arf1 pathway.
arf6downstreampathway. Arf6 downstream pathway.
bcr_5pathway. BCR signaling pathway.
pi3kcipathway. Class I PI3K signaling events.
endothelinpathway. Endothelins.
epha2_fwdpathway. EPHA2 forward signaling.
ephbfwdpathway. EPHB forward signaling.
ephrinbrevpathway. Ephrin B reverse signaling.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
il6_7pathway. IL6-mediated signaling events.
avb3_integrin_pathway. Integrins in angiogenesis.
lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development.
lysophospholipid_pathway. LPA receptor mediated events.
trkrpathway. Neurotrophic factor-mediated Trk receptor signaling.
avb3_opn_pathway. Osteopontin-mediated events.
p38_mkk3_6pathway. p38 MAPK signaling pathway.
p75ntrpathway. p75(NTR)-mediated signaling.
a4b1_paxdep_pathway. Paxillin-dependent events mediated by a4b1.
a4b1_paxindep_pathway. Paxillin-independent events mediated by a4b1 and a4b7.
pdgfrbpathway. PDGFR-beta signaling pathway.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.
s1p_s1p1_pathway. S1P1 pathway.
s1p_s1p2_pathway. S1P2 pathway.
s1p_s1p3_pathway. S1P3 pathway.
prlsignalingeventspathway. Signaling events mediated by PRL.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
ret_pathway. Signaling events regulated by Ret tyrosine kinase.
syndecan_4_pathway. Syndecan-4-mediated signaling events.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P63000.

Bgee

P63000.

CleanEx

HS_RAC1.

Genevestigator

P63000.

GermOnline

ENSG00000136238. Homo sapiens.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00174. RHO. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51420. RHO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P63000.

ChEMBL

CHEMBL6094.

ChiTaRS

RAC1. human.

DrugBank

DB00175. Pravastatin.
DB00641. Simvastatin.

EvolutionaryTrace

P63000.

GenomeRNAi

5879.

NextBio

22846.

PMAP-CutDB

P63000.

SOURCE

Search...

Entry information

Entry name

RAC1_HUMAN

Accession

Primary (citable) accession number: P63000
Secondary accession number(s): O95501 , P15154, Q3Y4D3, Q5JAA8, Q9BTB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	August 31, 2004
Last modified:	May 1, 2013
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.