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Protein

Ras-related C3 botulinum toxin substrate 1

Gene

RAC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.
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.

Enzyme regulationi

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 ARHGAP30.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 178GTPBy similarity
Nucleotide bindingi57 – 615GTPBy similarity
Nucleotide bindingi115 – 1184GTPBy similarity

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • Rho GDP-dissociation inhibitor binding Source: UniProtKB
  • thioesterase binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: MGI
  • actin filament polymerization Source: UniProtKB
  • anatomical structure arrangement Source: Ensembl
  • anatomical structure morphogenesis Source: ProtInc
  • apoptotic signaling pathway Source: Reactome
  • auditory receptor cell morphogenesis Source: Ensembl
  • axon guidance Source: Reactome
  • blood coagulation Source: Reactome
  • cell adhesion Source: ProtInc
  • cell-cell junction organization Source: Ensembl
  • cell-matrix adhesion Source: BHF-UCL
  • cell motility Source: UniProtKB
  • cerebral cortex GABAergic interneuron development Source: Ensembl
  • cerebral cortex radially oriented cell migration Source: Ensembl
  • cochlea morphogenesis Source: Ensembl
  • dendrite morphogenesis Source: Ensembl
  • dopaminergic neuron differentiation Source: Ensembl
  • embryonic olfactory bulb interneuron precursor migration Source: Ensembl
  • engulfment of apoptotic cell Source: Ensembl
  • ephrin receptor signaling pathway Source: Reactome
  • epithelial cell morphogenesis Source: Ensembl
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  • G-protein coupled receptor signaling pathway Source: Ensembl
  • homeostasis of number of cells within a tissue Source: Ensembl
  • hyperosmotic response Source: Ensembl
  • inflammatory response Source: ProtInc
  • innate immune response Source: Reactome
  • intracellular signal transduction Source: ProtInc
  • lamellipodium assembly Source: UniProtKB
  • localization within membrane Source: BHF-UCL
  • movement of cell or subcellular component Source: ProtInc
  • negative regulation of interleukin-23 production Source: BHF-UCL
  • negative regulation of receptor-mediated endocytosis Source: UniProtKB
  • neurotrophin TRK receptor signaling pathway Source: Reactome
  • platelet activation Source: Reactome
  • positive regulation of actin filament polymerization Source: Ensembl
  • positive regulation of apoptotic process Source: Reactome
  • positive regulation of cell-substrate adhesion Source: UniProtKB
  • positive regulation of focal adhesion assembly Source: UniProtKB
  • positive regulation of lamellipodium assembly Source: UniProtKB
  • positive regulation of neutrophil chemotaxis Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase activity Source: Ensembl
  • positive regulation of protein phosphorylation Source: UniProtKB
  • positive regulation of Rho protein signal transduction Source: UniProtKB
  • positive regulation of stress fiber assembly Source: UniProtKB
  • positive regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • protein localization to plasma membrane Source: Ensembl
  • regulation of cell migration Source: UniProtKB
  • regulation of defense response to virus by virus Source: Reactome
  • regulation of fibroblast migration Source: Ensembl
  • regulation of hydrogen peroxide metabolic process Source: BHF-UCL
  • regulation of neuron maturation Source: Ensembl
  • regulation of respiratory burst Source: BHF-UCL
  • regulation of small GTPase mediated signal transduction Source: Reactome
  • response to wounding Source: ProtInc
  • ruffle assembly Source: Ensembl
  • ruffle organization Source: UniProtKB
  • semaphorin-plexin signaling pathway Source: UniProtKB
  • small GTPase mediated signal transduction Source: Reactome
  • substrate adhesion-dependent cell spreading Source: UniProtKB
  • synaptic transmission, GABAergic Source: Ensembl
  • T cell costimulation Source: Reactome
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome
  • viral process Source: Reactome
  • Wnt signaling pathway, planar cell polarity pathway Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_11068. Nef and signal transduction.
REACT_111040. Signaling by SCF-KIT.
REACT_13638. NRAGE signals death through JNK.
REACT_147814. DAP12 signaling.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_163701. FCERI mediated MAPK activation.
REACT_1695. GPVI-mediated activation cascade.
REACT_18407. G alpha (12/13) signalling events.
REACT_19226. Activation of Rac.
REACT_19236. Sema3A PAK dependent Axon repulsion.
REACT_19238. CD28 dependent Vav1 pathway.
REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_19342. Inactivation of Cdc42 and Rac.
REACT_22272. Signal transduction by L1.
REACT_22351. DCC mediated attractive signaling.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_25299. DSCAM interactions.
REACT_263952. EPHB-mediated forward signaling.
REACT_263991. VEGFR2 mediated vascular permeability.
REACT_264047. Ephrin signaling.
REACT_264198. EPH-ephrin mediated repulsion of cells.
REACT_264199. PCP/CE pathway.
REACT_264464. VEGFA-VEGFR2 Pathway.
REACT_355141. RHO GTPases Activate NADPH Oxidases.
REACT_355252. RHO GTPases Activate Formins.
REACT_355303. RHO GTPases activate CIT.
REACT_355321. RHO GTPases activate KTN1.
REACT_355347. RHO GTPases activate PAKs.
REACT_355372. RHO GTPases Activate WASPs and WAVEs.
REACT_355469. RHO GTPases activate IQGAPs.
REACT_355542. RHO GTPases activate PKNs.
SignaLinkiP63000.

Names & Taxonomyi

Protein namesi
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 namesi
Name:RAC1
Synonyms:TC25
ORF Names:MIG5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:9801. RAC1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  • cytosol Source: UniProtKB
  • early endosome membrane Source: Ensembl
  • endoplasmic reticulum membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extrinsic component of plasma membrane Source: Ensembl
  • focal adhesion Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • nucleus Source: Ensembl
  • phagocytic cup Source: Ensembl
  • plasma membrane Source: Reactome
  • ruffle membrane Source: Ensembl
  • trans-Golgi network Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121G → V: Constitutively active. Interacts with PARD6 proteins. Increases nuclear localization and up-regulates transcriptional activity of NR3C2. 2 Publications
Mutagenesisi17 – 171T → 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. 3 Publications
Mutagenesisi30 – 301G → V: No interaction with PPP5C; when associated with L-61. Translocates to the plasma membrane; also when associated with L-61. 1 Publication
Mutagenesisi32 – 321Y → F: Abolishes AMPylation by Haemophilus IbpA. 1 Publication
Mutagenesisi35 – 351T → A: Abolishes AMPylation by Vibrio VopS. 2 Publications
Mutagenesisi35 – 351T → S: No interaction with PPP5C; when associated with L-61. Translocates to the plasma membrane; also when associated with L-61. 2 Publications
Mutagenesisi37 – 371F → A: Strongly reduced interaction with PLCB2. 1 Publication
Mutagenesisi56 – 561W → A: Strongly reduced interaction with PLCB2. 1 Publication
Mutagenesisi61 – 611Q → L: Constitutively active. Interacts with PARD6 proteins. Interacts with PPP5C, activates its phosphatase activity and translocates PPP5C to the plasma membrane. No effect on interaction with RAPH1. 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. 3 Publications
Mutagenesisi67 – 671L → A: Strongly reduced interaction with PLCB2. 1 Publication
Mutagenesisi70 – 701L → A: Strongly reduced interaction with PLCB2. 1 Publication

Organism-specific databases

PharmGKBiPA34162.

Chemistry

DrugBankiDB00514. Dextromethorphan.

Polymorphism and mutation databases

BioMutaiRAC1.
DMDMi51702787.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 189189Ras-related C3 botulinum toxin substrate 1PRO_0000042036Add
BLAST
Propeptidei190 – 1923Removed in mature formBy similarityPRO_0000042037

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321O-AMP-tyrosine; by Haemophilus IbpA1 Publication
Modified residuei35 – 351O-AMP-threonine; by Vibrio VopS1 Publication
Modified residuei39 – 391ADP-ribosylasparagine; by botulinum toxinBy similarity
Cross-linki147 – 147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei189 – 1891Cysteine methyl esterBy similarity
Lipidationi189 – 1891S-geranylgeranyl cysteine1 Publication
Isoform B (identifier: P63000-2)
Modified residuei71 – 711Phosphoserine1 Publication

Post-translational modificationi

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.2 Publications
GTP-bound active form is ubiquitinated by HACE1, leading to its degradation by the proteasome.2 Publications

Keywords - PTMi

ADP-ribosylation, Isopeptide bond, Lipoprotein, Methylation, Phosphoprotein, Prenylation, Ubl conjugation

Proteomic databases

MaxQBiP63000.
PaxDbiP63000.
PRIDEiP63000.

PTM databases

PhosphoSiteiP63000.

Miscellaneous databases

PMAP-CutDBP63000.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiP63000.
CleanExiHS_RAC1.
ExpressionAtlasiP63000. baseline and differential.
GenevisibleiP63000. HS.

Organism-specific databases

HPAiCAB035994.
HPA047820.

Interactioni

Subunit structurei

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. Interacts with RAPH1 (via Ras associating and PH domains) (PubMed:18499456).39 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARFIP2P533659EBI-413628,EBI-638194
ARHGDIAP525656EBI-413628,EBI-712693
ARHGEF7Q141558EBI-413628,EBI-717515
BAIAP2Q9UQB84EBI-413628,EBI-525456
BIRC2Q134902EBI-413628,EBI-514538
CAV1Q031353EBI-413628,EBI-603614
CDC23Q9UJX23EBI-413628,EBI-396137
CHN2P527574EBI-413628,EBI-714925
DOCK1Q1418510EBI-413628,EBI-446740
DOCK2Q926083EBI-413628,EBI-448771
FLNBO753692EBI-413628,EBI-352089
HMHA1Q926193EBI-413628,EBI-2825900
KRT40Q6A1623EBI-413628,EBI-10171697
LRRK2Q5S0075EBI-413628,EBI-5323863
LZTS2Q9BRK43EBI-413628,EBI-741037
OCRLQ019683EBI-413628,EBI-6148898
PAK1Q1315319EBI-413628,EBI-1307
PAK2Q131774EBI-413628,EBI-1045887
PAK3O759142EBI-413628,EBI-3389553
PARD6AQ9NPB62EBI-413628,EBI-81876
PARD6BQ9BYG53EBI-413628,EBI-295391
PARD6GQ9BYG42EBI-413628,EBI-295417
PLCG1P191747EBI-413628,EBI-79387
PRKCIP417433EBI-413628,EBI-286199
SETQ011058EBI-413628,EBI-1053182
SH3RF1Q7Z6J02EBI-413628,EBI-311339
SH3RF3Q8TEJ36EBI-413628,EBI-7975674
TNFAIP8L2Q6P5892EBI-413628,EBI-9073209
UNKLQ9H9P52EBI-413628,EBI-7797561
USH1CQ9Y6N93EBI-413628,EBI-954308
VAV1P154982EBI-413628,EBI-625518
XIAPP981703EBI-413628,EBI-517127

Protein-protein interaction databases

BioGridi111817. 144 interactions.
DIPiDIP-29260N.
IntActiP63000. 104 interactions.
MINTiMINT-4999291.

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Helixi12 – 143Combined sources
Helixi16 – 2510Combined sources
Beta strandi31 – 366Combined sources
Beta strandi39 – 468Combined sources
Beta strandi49 – 568Combined sources
Helixi62 – 643Combined sources
Turni65 – 673Combined sources
Helixi68 – 714Combined sources
Beta strandi76 – 838Combined sources
Helixi87 – 959Combined sources
Helixi97 – 1048Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi110 – 1156Combined sources
Helixi117 – 1204Combined sources
Helixi123 – 1319Combined sources
Helixi139 – 14810Combined sources
Beta strandi152 – 1565Combined sources
Turni159 – 1613Combined sources
Helixi165 – 17612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
DisProtiDP00408.
ProteinModelPortaliP63000.
SMRiP63000. Positions 1-177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63000.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi32 – 409Effector regionSequence Analysis

Domaini

The effector region mediates interaction with DEF6.1 Publication

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rho family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP63000.
KOiK04392.
OMAiNPIIYPQ.
OrthoDBiEOG764747.
PhylomeDBiP63000.
TreeFamiTF101109.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P63000-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP
60 70 80 90 100
VNLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE
110 120 130 140 150
VRHHCPNTPI ILVGTKLDLR DDKDTIEKLK EKKLTPITYP QGLAMAKEIG
160 170 180 190
AVKYLECSAL TQRGLKTVFD EAIRAVLCPP PVKKRKRKCL LL
Length:192
Mass (Da):21,450
Last modified:August 31, 2004 - v1
Checksum:iACEDF83A45E5EA67
GO
Isoform B (identifier: P63000-2) [UniParc] [UniParc]FASTAAdd to basket

Also known as: Rac1B, Rac1ins

The sequence of this isoform differs from the canonical sequence as follows:
     75-75: T → TVGETYGKDITSRGKDKPIA

Show »
Length:211
Mass (Da):23,467
Checksum:i93745E0CFBA5281F
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1921Missing in AAA36544 (PubMed:2108320).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 261N → D.
Corresponds to variant rs5830 [ dbSNP | Ensembl ].
VAR_014540
Natural varianti28 – 281F → L.
Corresponds to variant rs5832 [ dbSNP | Ensembl ].
VAR_014541
Natural varianti59 – 591A → T.
Corresponds to variant rs5837 [ dbSNP | Ensembl ].
VAR_014542
Natural varianti63 – 631D → G.
Corresponds to variant rs5831 [ dbSNP | Ensembl ].
VAR_014543
Natural varianti93 – 931V → G.
Corresponds to variant rs5826 [ dbSNP | Ensembl ].
VAR_014545
Natural varianti93 – 931V → I.
Corresponds to variant rs5825 [ dbSNP | Ensembl ].
VAR_014544
Natural varianti108 – 1081T → I.
Corresponds to variant rs5838 [ dbSNP | Ensembl ].
VAR_014546
Natural varianti130 – 1301K → R.
Corresponds to variant rs5828 [ dbSNP | Ensembl ].
VAR_014547
Natural varianti133 – 1331K → E.
Corresponds to variant rs5835 [ dbSNP | Ensembl ].
VAR_014548
Natural varianti135 – 1351T → I.1 Publication
Corresponds to variant rs11540455 [ dbSNP | Ensembl ].
VAR_033303
Natural varianti180 – 1801P → S.
Corresponds to variant rs16063 [ dbSNP | Ensembl ].
VAR_014549
Natural varianti182 – 1821V → E.
Corresponds to variant rs5836 [ dbSNP | Ensembl ].
VAR_014550

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei75 – 751T → TVGETYGKDITSRGKDKPIA in isoform B. 3 PublicationsVSP_005710

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5348.1.
CCDS5349.1. [P63000-2]
PIRiA34788. TVHUC1.
RefSeqiNP_008839.2. NM_006908.4. [P63000-1]
NP_061485.1. NM_018890.3. [P63000-2]
UniGeneiHs.413812.

Genome annotation databases

EnsembliENST00000348035; ENSP00000258737; ENSG00000136238.
GeneIDi5879.
KEGGihsa:5879.
UCSCiuc003spx.3. human.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS5348.1.
CCDS5349.1. [P63000-2]
PIRiA34788. TVHUC1.
RefSeqiNP_008839.2. NM_006908.4. [P63000-1]
NP_061485.1. NM_018890.3. [P63000-2]
UniGeneiHs.413812.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
DisProtiDP00408.
ProteinModelPortaliP63000.
SMRiP63000. Positions 1-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111817. 144 interactions.
DIPiDIP-29260N.
IntActiP63000. 104 interactions.
MINTiMINT-4999291.

Chemistry

BindingDBiP63000.
ChEMBLiCHEMBL3301397.
DrugBankiDB00514. Dextromethorphan.

PTM databases

PhosphoSiteiP63000.

Polymorphism and mutation databases

BioMutaiRAC1.
DMDMi51702787.

Proteomic databases

MaxQBiP63000.
PaxDbiP63000.
PRIDEiP63000.

Protocols and materials databases

DNASUi5879.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000348035; ENSP00000258737; ENSG00000136238.
GeneIDi5879.
KEGGihsa:5879.
UCSCiuc003spx.3. human.

Organism-specific databases

CTDi5879.
GeneCardsiGC07P006380.
H-InvDBHIX0031500.
HGNCiHGNC:9801. RAC1.
HPAiCAB035994.
HPA047820.
MIMi602048. gene.
neXtProtiNX_P63000.
PharmGKBiPA34162.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP63000.
KOiK04392.
OMAiNPIIYPQ.
OrthoDBiEOG764747.
PhylomeDBiP63000.
TreeFamiTF101109.

Enzyme and pathway databases

ReactomeiREACT_11051. Rho GTPase cycle.
REACT_11068. Nef and signal transduction.
REACT_111040. Signaling by SCF-KIT.
REACT_13638. NRAGE signals death through JNK.
REACT_147814. DAP12 signaling.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_163701. FCERI mediated MAPK activation.
REACT_1695. GPVI-mediated activation cascade.
REACT_18407. G alpha (12/13) signalling events.
REACT_19226. Activation of Rac.
REACT_19236. Sema3A PAK dependent Axon repulsion.
REACT_19238. CD28 dependent Vav1 pathway.
REACT_19266. Sema4D mediated inhibition of cell attachment and migration.
REACT_19277. Sema4D induced cell migration and growth-cone collapse.
REACT_19279. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_19342. Inactivation of Cdc42 and Rac.
REACT_22272. Signal transduction by L1.
REACT_22351. DCC mediated attractive signaling.
REACT_24970. Factors involved in megakaryocyte development and platelet production.
REACT_25299. DSCAM interactions.
REACT_263952. EPHB-mediated forward signaling.
REACT_263991. VEGFR2 mediated vascular permeability.
REACT_264047. Ephrin signaling.
REACT_264198. EPH-ephrin mediated repulsion of cells.
REACT_264199. PCP/CE pathway.
REACT_264464. VEGFA-VEGFR2 Pathway.
REACT_355141. RHO GTPases Activate NADPH Oxidases.
REACT_355252. RHO GTPases Activate Formins.
REACT_355303. RHO GTPases activate CIT.
REACT_355321. RHO GTPases activate KTN1.
REACT_355347. RHO GTPases activate PAKs.
REACT_355372. RHO GTPases Activate WASPs and WAVEs.
REACT_355469. RHO GTPases activate IQGAPs.
REACT_355542. RHO GTPases activate PKNs.
SignaLinkiP63000.

Miscellaneous databases

ChiTaRSiRAC1. human.
EvolutionaryTraceiP63000.
GeneWikiiRAC1.
GenomeRNAii5879.
NextBioi22846.
PMAP-CutDBP63000.
PROiP63000.
SOURCEiSearch...

Gene expression databases

BgeeiP63000.
CleanExiHS_RAC1.
ExpressionAtlasiP63000. baseline and differential.
GenevisibleiP63000. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. "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. 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. 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. "CED-10/Rac1 mediates axon guidance by regulating the asymmetric distribution of MIG-10/lamellipodin."
    Quinn C.C., Pfeil D.S., Wadsworth W.G.
    Curr. Biol. 18:808-813(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAPH1, MUTAGENESIS OF GLN-61.
  35. "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.
  36. "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.
  37. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 (ISOFORM B), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  38. "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.
  39. "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.
  40. "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.
  41. Cited for: AMPYLATION AT TYR-32, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF TYR-32.
  42. "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.
  43. Cited for: INTERACTION WITH TBC1D2.
  44. "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.
  45. "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.
  46. "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.
  47. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  48. "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.
  49. "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.
  50. "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.
  51. "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.
  52. "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.
  53. Cited for: INTERACTION WITH ARHGDIA.
  54. "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.
  55. "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.
  56. "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.
  57. "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.
  58. "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.
  59. "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.
  60. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-176 IN COMPLEX WITH GTP ANALOG AND P.AERUGINOSA EXOS.
  61. "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.
  62. "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.
  63. "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).
  64. "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.
  65. "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.
  66. "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.

Entry informationi

Entry nameiRAC1_HUMAN
AccessioniPrimary (citable) accession number: P63000
Secondary accession number(s): O95501
, P15154, Q3Y4D3, Q5JAA8, Q9BTB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: July 22, 2015
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.