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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
  • auditory receptor cell morphogenesis Source: Ensembl
  • axon guidance Source: Ensembl
  • blood coagulation Source: Reactome
  • bone resorption Source: Ensembl
  • cell adhesion Source: ProtInc
  • cell-cell junction organization Source: Ensembl
  • cell-matrix adhesion Source: BHF-UCL
  • cell motility Source: UniProtKB
  • cell proliferation Source: Ensembl
  • cellular response to mechanical stimulus Source: Ensembl
  • 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
  • intracellular signal transduction Source: ProtInc
  • lamellipodium assembly Source: UniProtKB
  • localization within membrane Source: BHF-UCL
  • mast cell chemotaxis Source: Ensembl
  • 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
  • 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 DNA replication Source: Ensembl
  • 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 cell size 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: Ensembl
  • 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
  • Wnt signaling pathway, planar cell polarity pathway Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-164944. Nef and signal transduction.
R-HSA-193648. NRAGE signals death through JNK.
R-HSA-194840. Rho GTPase cycle.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2424491. DAP12 signaling.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-376172. DSCAM interactions.
R-HSA-389359. CD28 dependent Vav1 pathway.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928664. Ephrin signaling.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-399954. Sema3A PAK dependent Axon repulsion.
R-HSA-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-HSA-4086400. PCP/CE pathway.
R-HSA-416482. G alpha (12/13) signalling events.
R-HSA-416550. Sema4D mediated inhibition of cell attachment and migration.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
R-HSA-418885. DCC mediated attractive signaling.
R-HSA-428540. Activation of Rac.
R-HSA-428543. Inactivation of Cdc42 and Rac.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-445144. Signal transduction by L1.
R-HSA-5218920. VEGFR2 mediated vascular permeability.
R-HSA-5625740. RHO GTPases activate PKNs.
R-HSA-5625900. RHO GTPases activate CIT.
R-HSA-5625970. RHO GTPases activate KTN1.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5627123. RHO GTPases activate PAKs.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5668599. RHO GTPases Activate NADPH Oxidases.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP63000.
SIGNORiP63000.

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
Proteomesi
  • UP000005640 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
  • extracellular matrix Source: BHF-UCL
  • extrinsic component of plasma membrane Source: Ensembl
  • focal adhesion Source: UniProtKB
  • Golgi membrane Source: Ensembl
  • 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

ChEMBLiCHEMBL3301397.
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 IbpA; alternate1 Publication
Glycosylationi32 – 321O-linked (GlcNAc); by Photorhabdus PAU_02230; alternate1 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 – 711PhosphoserineCombined sources

Post-translational modificationi

(Microbial infection) 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
(Microbial infection) Glycosylated at Tyr-32 by Photorhabdus asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230 inhibits downstream signaling by an impaired interaction with diverse regulator and effector proteins of Rac and leads to actin disassembly.1 Publication

Keywords - PTMi

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

Proteomic databases

EPDiP63000.
MaxQBiP63000.
PeptideAtlasiP63000.
PRIDEiP63000.

PTM databases

iPTMnetiP63000.
PhosphoSiteiP63000.
SwissPalmiP63000.

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

BgeeiENSG00000136238.
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
CAV1Q031352EBI-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
PAK1Q1315322EBI-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

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi111817. 165 interactions.
DIPiDIP-29260N.
IntActiP63000. 112 interactions.
MINTiMINT-4999291.

Chemistry

BindingDBiP63000.

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[»]
4YONX-ray1.95B1-177[»]
5FI0X-ray3.28B/D/F/H1-192[»]
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

GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP63000.
KOiK04392.
OMAiSPRRHKC.
PhylomeDBiP63000.
TreeFamiTF101109.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 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 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. [P63000-1]
ENST00000356142; ENSP00000348461; ENSG00000136238. [P63000-2]
GeneIDi5879.
KEGGihsa:5879.
UCSCiuc003spw.4. 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[»]
4YONX-ray1.95B1-177[»]
5FI0X-ray3.28B/D/F/H1-192[»]
DisProtiDP00408.
ProteinModelPortaliP63000.
SMRiP63000. Positions 1-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111817. 165 interactions.
DIPiDIP-29260N.
IntActiP63000. 112 interactions.
MINTiMINT-4999291.

Chemistry

BindingDBiP63000.
ChEMBLiCHEMBL3301397.
DrugBankiDB00514. Dextromethorphan.

PTM databases

iPTMnetiP63000.
PhosphoSiteiP63000.
SwissPalmiP63000.

Polymorphism and mutation databases

BioMutaiRAC1.
DMDMi51702787.

Proteomic databases

EPDiP63000.
MaxQBiP63000.
PeptideAtlasiP63000.
PRIDEiP63000.

Protocols and materials databases

DNASUi5879.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000348035; ENSP00000258737; ENSG00000136238. [P63000-1]
ENST00000356142; ENSP00000348461; ENSG00000136238. [P63000-2]
GeneIDi5879.
KEGGihsa:5879.
UCSCiuc003spw.4. human.

Organism-specific databases

CTDi5879.
GeneCardsiRAC1.
H-InvDBHIX0031500.
HGNCiHGNC:9801. RAC1.
HPAiCAB035994.
HPA047820.
MIMi602048. gene.
neXtProtiNX_P63000.
PharmGKBiPA34162.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP63000.
KOiK04392.
OMAiSPRRHKC.
PhylomeDBiP63000.
TreeFamiTF101109.

Enzyme and pathway databases

ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-1433557. Signaling by SCF-KIT.
R-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-164944. Nef and signal transduction.
R-HSA-193648. NRAGE signals death through JNK.
R-HSA-194840. Rho GTPase cycle.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-2424491. DAP12 signaling.
R-HSA-2871796. FCERI mediated MAPK activation.
R-HSA-376172. DSCAM interactions.
R-HSA-389359. CD28 dependent Vav1 pathway.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928664. Ephrin signaling.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-399954. Sema3A PAK dependent Axon repulsion.
R-HSA-399955. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
R-HSA-4086400. PCP/CE pathway.
R-HSA-416482. G alpha (12/13) signalling events.
R-HSA-416550. Sema4D mediated inhibition of cell attachment and migration.
R-HSA-416572. Sema4D induced cell migration and growth-cone collapse.
R-HSA-418885. DCC mediated attractive signaling.
R-HSA-428540. Activation of Rac.
R-HSA-428543. Inactivation of Cdc42 and Rac.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-445144. Signal transduction by L1.
R-HSA-5218920. VEGFR2 mediated vascular permeability.
R-HSA-5625740. RHO GTPases activate PKNs.
R-HSA-5625900. RHO GTPases activate CIT.
R-HSA-5625970. RHO GTPases activate KTN1.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5627123. RHO GTPases activate PAKs.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5668599. RHO GTPases Activate NADPH Oxidases.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-8849471. PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP63000.
SIGNORiP63000.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000136238.
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.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: September 7, 2016
This is version 160 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

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 one 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.