Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00630
Entry Name
UniProt Accession
Theoretical PI
8.77
Molecular Weight
21450.11
Genbank Protein ID
Genbank Nucleotide ID
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
31-AUG-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
178
Canonical
EAIRAVLCPPPVKKR
[1]
S-Palmitoylation
189
Canonical
VKKRKRKCLLL****
[2]
S-Geranylgeranylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Navarro-Lérida I, Sánchez-Perales S, Calvo M, Rentero C, Zheng Y, Enrich C,Del Pozo MA. A palmitoylation switch mechanism regulates Rac1 function andmembrane organization. EMBO J. 2012 Feb 1;31(3):534-51. doi:10.1038/emboj.2011.446. Epub 2011 Dec 9.[PMID:22157745]
[2] Kinsella BT, Erdman RA, Maltese WA. Carboxyl-terminal isoprenylation ofras-related GTP-binding proteins encoded by rac1, rac2, and ralA. J Biol Chem.1991 May 25;266(15):9786-94.[PMID:1903399]
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. 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.
Sequence Annotation
Nucleotide-binding: 10 17 GTP.
Nucleotide-binding: 57 61 GTP.
Nucleotide-binding: 115 118 GTP.
Motif: 32 40 Effector region.
Modified residue: 32 32 O-AMP-tyrosine; by Haemophilus IbpA.
Modified residue: 35 35 O-AMP-threonine; by Vibrio VopS.
Modified residue: 39 39 ADP-ribosylasparagine; by botulinumtoxin.
Modified residue: 189 189 Cysteine methyl ester.
Protein Length
192 AA.
Protein Sequence
(Canonical)
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG  60
QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPNTPI ILVGTKLDLR  120
DDKDTIEKLK EKKLTPITYP QGLAMAKEIG AVKYLECSAL TQRGLKTVFD EAIRAVLCPP  180
PVKKRKRKCL LL                                                      192
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG  60
QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPNTPI ILVGTKLDLR  120
DDKDTIEKLK EKKLTPITYP QGLAMAKEIG AVKYLECSAL TQRGLKTVFD EAIRAVLCPP  180
PVKKRKRKCL LL                                                      192
FASTA
(Canonical)
>LipidDB-9606-00630|P63000
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR
DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPP
PVKKRKRKCLLL
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLR
DDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPP
PVKKRKRKCLLL
Gene Ontology
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:Ensembl
GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL
GO:0005829; C:cytosol; ISS:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0019897; C:extrinsic component of plasma membrane; IEA:Ensembl
GO:0005925; C:focal adhesion; IDA:UniProtKB
GO:0000139; C:Golgi membrane; IEA:Ensembl
GO:0030027; C:lamellipodium; IDA:UniProtKB
GO:0016020; C:membrane; ISS:UniProtKB
GO:0001891; C:phagocytic cup; IEA:Ensembl
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0032587; C:ruffle membrane; IEA:Ensembl
GO:0005802; C:trans-Golgi network; IDA:FlyBase
GO:0019899; F:enzyme binding; IPI:BHF-UCL
GO:0005525; F:GTP binding; IDA:UniProtKB
GO:0003924; F:GTPase activity; TAS:UniProtKB
GO:0051022; F:Rho GDP-dissociation inhibitor binding; ISS:UniProtKB
GO:0031996; F:thioesterase binding; IPI:UniProtKB
GO:0030036; P:actin cytoskeleton organization; IGI:MGI
GO:0030041; P:actin filament polymerization; TAS:UniProtKB
GO:0048532; P:anatomical structure arrangement; IEA:Ensembl
GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc
GO:0097190; P:apoptotic signaling pathway; TAS:Reactome
GO:0002093; P:auditory receptor cell morphogenesis; IEA:Ensembl
GO:0007411; P:axon guidance; TAS:Reactome
GO:0007596; P:blood coagulation; TAS:Reactome
GO:0045453; P:bone resorption; IEA:Ensembl
GO:0007155; P:cell adhesion; TAS:ProtInc
GO:0048870; P:cell motility; IDA:UniProtKB
GO:0008283; P:cell proliferation; IEA:Ensembl
GO:0045216; P:cell-cell junction organization; IEA:Ensembl
GO:0007160; P:cell-matrix adhesion; NAS:BHF-UCL
GO:0006928; P:cellular component movement; TAS:ProtInc
GO:0021799; P:cerebral cortex radially oriented cell migration; IEA:Ensembl
GO:0090103; P:cochlea morphogenesis; IEA:Ensembl
GO:0048813; P:dendrite morphogenesis; IEA:Ensembl
GO:0071542; P:dopaminergic neuron differentiation; IEA:Ensembl
GO:0021831; P:embryonic olfactory bulb interneuron precursor migration; IEA:Ensembl
GO:0043652; P:engulfment of apoptotic cell; IEA:Ensembl
GO:0003382; P:epithelial cell morphogenesis; IEA:Ensembl
GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome
GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome
GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:Ensembl
GO:0006972; P:hyperosmotic response; IEA:Ensembl
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:Ensembl
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:Ensembl
GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome
GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl
GO:0051894; P:positive regulation of focal adhesion assembly; IDA:UniProtKB
GO:0010592; P:positive regulation of lamellipodium assembly; IMP:UniProtKB
GO:0090023; P:positive regulation of neutrophil chemotaxis; IMP:UniProtKB
GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Ensembl
GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB
GO:0035025; P:positive regulation of Rho protein signal transduction; TAS:UniProtKB
GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB
GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB
GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl
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:0009611; P:response to wounding; TAS:ProtInc
GO:0097178; P:ruffle assembly; IEA:Ensembl
GO:0031529; P:ruffle organization; TAS:UniProtKB
GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB
GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl
GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB
GO:0031295; P:T cell costimulation; TAS:Reactome
GO:0016032; P:viral process; TAS:Reactome
GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; IEA:Ensembl
Interpro
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR005225; Small_GTP-bd_dom
InterPro; IPR001806; Small_GTPase
InterPro; IPR003578; Small_GTPase_Rho
Pfam
Pfam; PF00071; Ras;
SMART
SMART; SM00174; RHO;
PROSITE
PROSITE; PS51420; RHO;
PRINTS
PRINTS; PR00449; RASTRNSFRMNG;