Reviewed, UniProtKB/Swiss-Prot P63000 (RAC1_HUMAN)

Names and origin

Protein names

Recommended name:
    Ras-related C3 botulinum toxin substrate 1
Alternative name(s):
    p21-Rac1
    Ras-like protein TC25
    Cell migration-inducing gene 5 protein

Gene names

Name:	RAC1
ORF Names:	MIG5

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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. Ref.13 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
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.
Subunit structure	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. Part of a complex with MAP2K3, MAP3K3, CCM2 and DEF6. Interacts with BAIAP2, BAIAP2L1, CYFIP1/SRA-1 and DEF6. Interacts with Y.pseudotuberculosis YPKA and PLCB2. Interacts with NOXA1. Interacts with ARHGEF2. Interacts with NISCH By similarity.
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side By similarity. Melanosome. 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.
Tissue specificity	Isoform B is predominantly identified in skin and epithelial tissues from the intestinal tract. The expression of isoform B 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.26
Sequence similarities	Belongs to the small GTPase superfamily. Rho family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	GTP-binding Nucleotide-binding
PTM	ADP-ribosylation Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	actin filament polymerization Traceable author statement. Source: UniProtKB anatomical structure morphogenesis Traceable author statement. Source: ProtInc cell adhesion Traceable author statement. Source: ProtInc cell motion Traceable author statement. Source: ProtInc inflammatory response Traceable author statement. Source: ProtInc lamellipodium assembly Inferred from mutant phenotype. Source: UniProtKB localization within membrane Inferred from mutant phenotype. Source: UniProtKB negative regulation of receptor-mediated endocytosis Traceable author statement. Source: UniProtKB positive regulation of Rho protein signal transduction Traceable author statement. Source: UniProtKB positive regulation of lamellipodium assembly Inferred from direct assay. Source: MGI regulation of hydrogen peroxide metabolic process Traceable author statement. Source: UniProtKB regulation of respiratory burst Inferred from direct assay. Source: UniProtKB ruffle organization Traceable author statement. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from Experiment. Source: Reactome melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from direct assay. Source: MGI GTP-dependent protein binding Ref.17 Inferred from physical interaction. Source: ProtInc GTPase activity Ref.1 Traceable author statement. Source: UniProtKB enzyme binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q06409	1	EBI-413628,EBI-35964	From a different organism.
ARFIP2	P53365	4	EBI-413628,EBI-638194
ARHGDIA	P52565	1	EBI-413628,EBI-712693
DOCK1	Q14185	3	EBI-413628,EBI-446740
DOCK2	Q92608	1	EBI-413628,EBI-448771
limE	O60952	1	EBI-413628,EBI-1808840	From a different organism.
NCF2	P19878	2	EBI-413628,EBI-489611
PAK1	Q13153	3	EBI-413628,EBI-1307
Pak1	O88643	1	EBI-413628,EBI-457240	From a different organism.
Pak3	Q61036	1	EBI-413628,EBI-457317	From a different organism.
PARD6A	Q9NPB6	1	EBI-413628,EBI-81876
PARD6B	Q9BYG5	1	EBI-413628,EBI-295391
PARD6G	Q9BYG4	1	EBI-413628,EBI-295417
sptP	P74873	1	EBI-413628,EBI-1030433	From a different organism.

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

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

39

1

ADP-ribosylasparagine; by botulinum toxin By similarity

Modified residue

71

1

Phosphoserine Ref.28

Modified residue

189

1

Cysteine methyl ester

Lipidation

189

1

S-geranylgeranyl cysteine

Natural variations

Alternative sequence

75

1

T → TVGETYGKDITSRGKDKPIA in isoform B.

VSP_005710

Natural variant

26

1

N → D: dbSNP rs5830.

VAR_014540

Natural variant

28

1

F → L: dbSNP rs5832.

VAR_014541

Natural variant

59

1

A → T: dbSNP rs5837.

VAR_014542

Natural variant

63

1

D → G: dbSNP rs5831.

VAR_014543

Natural variant

93

1

V → G: dbSNP rs5826.

VAR_014545

Natural variant

93

1

V → I: dbSNP rs5825.

VAR_014544

Natural variant

108

1

T → I: dbSNP rs5838.

VAR_014546

Natural variant

130

1

K → R: dbSNP rs5828.

VAR_014547

Natural variant

133

1

K → E: dbSNP rs5835.

VAR_014548

Natural variant

135

1

T → I: dbSNP rs11540455. Ref.7

VAR_033303

Natural variant

180

1

P → S: dbSNP rs16063.

VAR_014549

Natural variant

182

1

V → E: dbSNP rs5836.

VAR_014550

Experimental info

Mutagenesis

12

1

G → V: Constitutively active. Interacts with PARD6 proteins. Ref.20

Mutagenesis

17

1

T → N: Constitutively inactivated. Abolishes interaction with PARD6 proteins. Ref.20

Mutagenesis

37

1

F → A: Strongly reduced interaction with PLCB2. Ref.39

Mutagenesis

56

1

W → A: Strongly reduced interaction with PLCB2. Ref.39

Mutagenesis

61

1

Q → L: Constitutively active. Interacts with PARD6 proteins. Ref.17

Mutagenesis

67

1

L → A: Strongly reduced interaction with PLCB2. Ref.39

Mutagenesis

70

1

L → A: Strongly reduced interaction with PLCB2. Ref.39

Sequence conflict

192

1

Missing in AAA36544. Ref.2

Secondary structure

1

.

.

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192

Helix Strand Turn

Details...

Beta strand

4 – 9

6

Helix

16 – 25

10

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

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: 2674130] [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: 2108320] [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: 11062023] [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: 10597294] [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: 12853948] [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: 15489334] [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: 1903399] [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: 1643658] [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: 7673236] [Abstract] Cited for: INTERACTION WITH RALBP1.
[15]	"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: 9857026] [Abstract] Cited for: INTERACTION WITH ARHGEF2.
[16]	"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: 10559471] [Abstract] Cited for: INTERACTION WITH DOCK2.
[17]	"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: 10954424] [Abstract] Cited for: INTERACTION WITH PARD6A, MUTAGENESIS OF GLN-61.
[18]	"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: 11130076] [Abstract] Cited for: INTERACTION WITH BAIAP2.
[19]	"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: 11035813] [Abstract] Cited for: INTERACTION WITH PLXNB1.
[20]	"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: 11260256] [Abstract] Cited for: INTERACTION WITH PARD6A; PARD6B AND PARD6G; PRKCI AND PRKCZ, MUTAGENESIS OF GLY-12 AND THR-17.
[21]	"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: 11955434] [Abstract] Cited for: ACTIVATION BY PREX1.
[22]	"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: 12134158] [Abstract] Cited for: SUBUNIT OF A COMPLEX CONTAINING ELMO1 AND DOCK1.
[23]	"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: 12716910] [Abstract] Cited for: INTERACTION WITH NOXA1.
[24]	"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: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[25]	"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: 16982419] [Abstract] Cited for: INTERACTION WITH DOCK7.
[26]	"Cooperation of DEF6 with activated Rac in regulating cell morphology." Oka T., Ihara S., Fukui Y. J. Biol. Chem. 282:2011-2018(2007) [PubMed: 17121847] [Abstract] Cited for: INTERACTION WITH DEF6, DOMAIN.
[27]	"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: 17430976] [Abstract] Cited for: INTERACTION WITH BAIAP2L1.
[28]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, MASS SPECTROMETRY.
[29]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[30]	"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: 9033596] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.38 ANGSTROMS) OF 1-184 IN COMPLEX WITH GTP ANALOG.
[31]	"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: 11090627] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT LEU-61 IN COMPLEX WITH GTP AND NCF2.
[32]	"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: 11130063] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-177 IN COMPLEX WITH TIAM1.
[33]	"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: 11163217] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-184 IN COMPLEX WITH SALMONELLA SPTP.
[34]	"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: 11135665] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-176 IN COMPLEX WITH GTP ANALOG AND P.AERUGINOSA EXOS.
[35]	"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: 11513578] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH ARHGDIA.
[36]	"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: 11346801] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GTP ANALOG AND ARFIP2.
[37]	"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: 14625275] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF ISOFORM B, CHARACTERIZATION OF ISOFORM B.
[38]	"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: 16959567] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-184 IN COMPLEX WITH Y.PSEUDOTUBERCULOSIS YPKA.
[39]	"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: 17115053] [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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

UniGene

Hs.413812

3D structure databases

PDBPDBe

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	[»]
3BJI	X-ray	2.60	C/D	1-177	[»]

DisProt

DP00408.

ModBase

Search...

Protein-protein interaction databases

IntAct

P63000. 27 interactions.

PTM databases

PhosphoSite

P63000.

Proteomic databases

PRIDE

P63000.

Genome annotation databases

Ensembl

ENSG00000136238. Homo sapiens. [Contig view]

GeneID

5879.

KEGG

hsa:5879.

Organism-specific databases

GeneCards

GC07P006380.

H-InvDB

HIX0006465.
HIX0056506.

HGNC

HGNC:9801. RAC1.

HPA

CAB002002.

MIM

602048. gene.

PharmGKB

PA26481.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P63000.

OMA

P63000. DTYGKDI.

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_11044. Signaling by Rho GTPases.
REACT_11061. Signalling by NGF.
REACT_604. Hemostasis.
REACT_6185. HIV Infection.

Gene expression databases

ArrayExpress

P63000.

Bgee

P63000.

CleanEx

HS_RAC1.

GermOnline

ENSG00000136238. Homo sapiens.

Family and domain databases

InterPro

IPR003578. GTPase_Rho.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
[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 Resources

DrugBank

DB00175. Pravastatin.
DB00641. Simvastatin.

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:	June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)