UniProt Accession

 RAC1_HUMAN; P63000; O95501; P15154; Q3Y4D3; Q5JAA8; Q9BTB4 

Genbank Protein ID

 M29870; M31467; AJ132694; AJ132695; AJ132695; AF136373; AY279384; AF498964; BT007121; DQ165078; AC009412; AC009412; BC004247; BC050687; BC107748 

Genbank Nucleotide ID

 AAA36537.1; AAA36544.1; CAA10732.1; CAB53579.5; CAA10733.6; AAD30547.1; AAQ16632.1; AAM21111.1; AAP35785.1; AAZ80485.1; AAS07511.1; AAS07512.1; AAH04247.1; AAH50687.1; AAI07749.1 

Protein Name

 Ras-related C3 botulinum toxin substrate 1 

Protein Synonyms/Alias

 Cell migration-inducing gene 5 protein; Ras-like protein TC25; p21-Rac1 

Gene Name

 RAC1 

Gene Synonyms/Alias

 TC25; MIG5 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
96	SFENVRAKWYPEVRH	ubiquitination	[1]
116	PIILVGTKLDLRDDK	ubiquitination	[1, 2, 3, 4]
123	KLDLRDDKDTIEKLK	ubiquitination	[2, 3]
133	IEKLKEKKLTPITYP	ubiquitination	[1, 2, 3, 5, 6]
147	PQGLAMAKEIGAVKY	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9]
153	AKEIGAVKYLECSAL	ubiquitination	[1, 3, 8]
166	ALTQRGLKTVFDEAI	ubiquitination	[1, 2, 5]
183	VLCPPPVKKRKRKCL	sumoylation	[10]
183	VLCPPPVKKRKRKCL	ubiquitination	[1, 2, 3, 5]
184	LCPPPVKKRKRKCLL	sumoylation	[10]
186	PPPVKKRKRKCLLL*	sumoylation	[10]
188	PVKKRKRKCLLL***	sumoylation	[10]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [8] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [9] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [10] SUMOylation of the GTPase Rac1 is required for optimal cell migration.
 Castillo-Lluva S, Tatham MH, Jones RC, Jaffray EG, Edmondson RD, Hay RT, Malliri A.
 Nat Cell Biol. 2010 Nov;12(11):1078-85. [PMID: 20935639] 

Functional Description

 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. 

Sequence Annotation

 NP_BIND 10 17 GTP (By similarity).
 NP_BIND 57 61 GTP (By similarity).
 NP_BIND 115 118 GTP (By similarity).
 MOTIF 32 40 Effector region (Potential).
 MOD_RES 32 32 O-AMP-tyrosine; by Haemophilus IbpA.
 MOD_RES 35 35 O-AMP-threonine; by Vibrio VopS.
 MOD_RES 39 39 ADP-ribosylasparagine; by botulinum toxin
 MOD_RES 189 189 Cysteine methyl ester.
 LIPID 189 189 S-geranylgeranyl cysteine.
 CROSSLNK 147 147 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 3D-structure; ADP-ribosylation; Alternative splicing; Cell membrane; Complete proteome; Cytoplasm; GTP-binding; Isopeptide bond; Lipoprotein; Membrane; Methylation; Nucleotide-binding; Phosphoprotein; Polymorphism; Prenylation; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 192 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0019897; C:extrinsic to plasma membrane; IEA:Compara.
 GO:0000139; C:Golgi membrane; IEA:Compara.
 GO:0030027; C:lamellipodium; IEA:Compara.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0001891; C:phagocytic cup; IEA:Compara.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0032587; C:ruffle membrane; IEA:Compara.
 GO:0005802; C:trans-Golgi network; IDA:FlyBase.
 GO:0005525; F:GTP binding; IDA:UniProtKB.
 GO:0003924; F:GTPase activity; TAS:UniProtKB.
 GO:0030041; P:actin filament polymerization; TAS:UniProtKB.
 GO:0048532; P:anatomical structure arrangement; IEA:Compara.
 GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
 GO:0002093; P:auditory receptor cell morphogenesis; IEA:Compara.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0045453; P:bone resorption; IEA:Compara.
 GO:0048870; P:cell motility; IDA:UniProtKB.
 GO:0008283; P:cell proliferation; IEA:Compara.
 GO:0045216; P:cell-cell junction organization; IEA:Compara.
 GO:0007160; P:cell-matrix adhesion; NAS:BHF-UCL.
 GO:0021799; P:cerebral cortex radially oriented cell migration; IEA:Compara.
 GO:0090103; P:cochlea morphogenesis; IEA:Compara.
 GO:0048813; P:dendrite morphogenesis; IEA:Compara.
 GO:0071542; P:dopaminergic neuron differentiation; IEA:Compara.
 GO:0021831; P:embryonic olfactory bulb interneuron precursor migration; IEA:Compara.
 GO:0043652; P:engulfment of apoptotic cell; IEA:Compara.
 GO:0003382; P:epithelial cell morphogenesis; IEA:Compara.
 GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
 GO:0006972; P:hyperosmotic response; IEA:Compara.
 GO:0006954; P:inflammatory response; TAS:ProtInc.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
 GO:0030032; P:lamellipodium assembly; IMP:UniProtKB.
 GO:0051668; P:localization within membrane; IMP:BHF-UCL.
 GO:0002551; P:mast cell chemotaxis; IEA:Compara.
 GO:0032707; P:negative regulation of interleukin-23 production; IDA:BHF-UCL.
 GO:0048261; P:negative regulation of receptor-mediated endocytosis; TAS:UniProtKB.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0030838; P:positive regulation of actin filament polymerization; IEA:Compara.
 GO:0045740; P:positive regulation of DNA replication; IEA:Compara.
 GO:0010592; P:positive regulation of lamellipodium assembly; IDA:MGI.
 GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Compara.
 GO:0035025; P:positive regulation of Rho protein signal transduction; TAS:UniProtKB.
 GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
 GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
 GO:0010310; P:regulation of hydrogen peroxide metabolic process; TAS:BHF-UCL.
 GO:0060263; P:regulation of respiratory burst; IDA:BHF-UCL.
 GO:0097178; P:ruffle assembly; IEA:Compara.
 GO:0031529; P:ruffle organization; TAS:UniProtKB.
 GO:0007264; P:small GTPase mediated signal transduction; IEA:Compara.
 GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Compara.
 GO:0031295; P:T cell costimulation; TAS:Reactome.
 GO:0016032; P:viral reproduction; TAS:Reactome.
 GO:0060071; P:Wnt receptor signaling pathway, planar cell polarity pathway; IEA:Compara. 

Interpro

 IPR027417; P-loop_NTPase.
 IPR005225; Small_GTP-bd_dom.
 IPR001806; Small_GTPase.
 IPR003578; Small_GTPase_Rho. 

Pfam

 PF00071; Ras 

SMART

 SM00174; RHO 

PROSITE

 PS51420; RHO 

PRINTS

 PR00449; RASTRNSFRMNG.