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P63000

- RAC1_HUMAN

UniProt

P63000 - RAC1_HUMAN

Protein

Ras-related C3 botulinum toxin substrate 1

Gene

RAC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (31 Aug 2004)
      Previous versions | rss
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    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

    1. enzyme binding Source: BHF-UCL
    2. GTPase activity Source: UniProtKB
    3. GTP binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. Rho GDP-dissociation inhibitor binding Source: UniProtKB
    6. thioesterase binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: MGI
    2. actin filament polymerization Source: UniProtKB
    3. anatomical structure arrangement Source: Ensembl
    4. anatomical structure morphogenesis Source: ProtInc
    5. apoptotic signaling pathway Source: Reactome
    6. auditory receptor cell morphogenesis Source: Ensembl
    7. axon guidance Source: Reactome
    8. blood coagulation Source: Reactome
    9. bone resorption Source: Ensembl
    10. cell adhesion Source: ProtInc
    11. cell-cell junction organization Source: Ensembl
    12. cell-matrix adhesion Source: BHF-UCL
    13. cell motility Source: UniProtKB
    14. cell proliferation Source: Ensembl
    15. cellular component movement Source: ProtInc
    16. cerebral cortex radially oriented cell migration Source: Ensembl
    17. cochlea morphogenesis Source: Ensembl
    18. dendrite morphogenesis Source: Ensembl
    19. dopaminergic neuron differentiation Source: Ensembl
    20. embryonic olfactory bulb interneuron precursor migration Source: Ensembl
    21. engulfment of apoptotic cell Source: Ensembl
    22. epithelial cell morphogenesis Source: Ensembl
    23. Fc-epsilon receptor signaling pathway Source: Reactome
    24. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    25. hyperosmotic response Source: Ensembl
    26. inflammatory response Source: ProtInc
    27. innate immune response Source: Reactome
    28. intracellular signal transduction Source: ProtInc
    29. lamellipodium assembly Source: UniProtKB
    30. localization within membrane Source: BHF-UCL
    31. mast cell chemotaxis Source: Ensembl
    32. negative regulation of interleukin-23 production Source: BHF-UCL
    33. negative regulation of receptor-mediated endocytosis Source: UniProtKB
    34. neurotrophin TRK receptor signaling pathway Source: Reactome
    35. platelet activation Source: Reactome
    36. positive regulation of actin filament polymerization Source: Ensembl
    37. positive regulation of apoptotic process Source: Reactome
    38. positive regulation of DNA replication Source: Ensembl
    39. positive regulation of lamellipodium assembly Source: MGI
    40. positive regulation of phosphatidylinositol 3-kinase activity Source: Ensembl
    41. positive regulation of protein phosphorylation Source: UniProtKB
    42. positive regulation of Rho protein signal transduction Source: UniProtKB
    43. regulation of cell migration Source: UniProtKB
    44. regulation of defense response to virus by virus Source: Reactome
    45. regulation of hydrogen peroxide metabolic process Source: BHF-UCL
    46. regulation of respiratory burst Source: BHF-UCL
    47. response to wounding Source: ProtInc
    48. ruffle assembly Source: Ensembl
    49. ruffle organization Source: UniProtKB
    50. semaphorin-plexin signaling pathway Source: UniProtKB
    51. small GTPase mediated signal transduction Source: Ensembl
    52. substrate adhesion-dependent cell spreading Source: Ensembl
    53. T cell costimulation Source: Reactome
    54. viral process Source: Reactome
    55. Wnt signaling pathway, planar cell polarity pathway Source: Ensembl

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_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_172581. PCP/CE pathway.
    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.
    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: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:9801. RAC1.

    Subcellular locationi

    Cell membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Melanosome 3 Publications. Cytoplasm By similarity
    Note: Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine By similarity. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Found in the ruffled border (a late endosomal-like compartment in the plasma membrane) of bone-resorbing osteoclasts By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    2. cytosol Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. extrinsic component of plasma membrane Source: Ensembl
    5. Golgi membrane Source: Ensembl
    6. lamellipodium Source: Ensembl
    7. melanosome Source: UniProtKB-SubCell
    8. membrane Source: UniProtKB
    9. phagocytic cup Source: Ensembl
    10. plasma membrane Source: Reactome
    11. ruffle membrane Source: Ensembl
    12. trans-Golgi network Source: FlyBase

    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 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. 2 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.

    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)2 Publications
    Modified residuei189 – 1891Cysteine methyl esterBy similarity
    Lipidationi189 – 1891S-geranylgeranyl cysteine1 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

    ArrayExpressiP63000.
    BgeeiP63000.
    CleanExiHS_RAC1.
    GenevestigatoriP63000.

    Organism-specific databases

    HPAiCAB035994.

    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.38 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
    CHN2P527574EBI-413628,EBI-714925
    DOCK1Q1418510EBI-413628,EBI-446740
    DOCK2Q926083EBI-413628,EBI-448771
    FLNBO753692EBI-413628,EBI-352089
    LRRK2Q5S0075EBI-413628,EBI-5323863
    OCRLQ019683EBI-413628,EBI-6148898
    PAK1Q1315316EBI-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
    VAV1P154982EBI-413628,EBI-625518
    XIAPP981703EBI-413628,EBI-517127

    Protein-protein interaction databases

    BioGridi111817. 128 interactions.
    DIPiDIP-29260N.
    IntActiP63000. 94 interactions.
    MINTiMINT-4999291.
    STRINGi9606.ENSP00000348461.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000233974.
    HOVERGENiHBG009351.
    KOiK04392.
    OMAiYPQTVAE.
    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. Align

    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

    MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP    50
    VNLGLWDTAG QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE 100
    VRHHCPNTPI ILVGTKLDLR DDKDTIEKLK EKKLTPITYP QGLAMAKEIG 150
    AVKYLECSAL TQRGLKTVFD EAIRAVLCPP PVKKRKRKCL LL 192
    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

    Note: Contains a phosphoserine at position 71.

    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.

    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:
    EMBL
    GenBank
    DDBJ
    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.
    UCSCiuc003spx.3. human.

    Polymorphism databases

    DMDMi51702787.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS5348.1.
    CCDS5349.1. [P63000-2 ]
    PIRi A34788. TVHUC1.
    RefSeqi NP_008839.2. NM_006908.4. [P63000-1 ]
    NP_061485.1. NM_018890.3. [P63000-2 ]
    UniGenei Hs.413812.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E96 X-ray 2.40 A 2-192 [» ]
    1FOE X-ray 2.80 B/D/F/H 1-177 [» ]
    1G4U X-ray 2.30 R 1-184 [» ]
    1HE1 X-ray 2.00 C/D 2-176 [» ]
    1HH4 X-ray 2.70 A/B 2-192 [» ]
    1I4D X-ray 2.50 D 1-192 [» ]
    1I4L X-ray 2.70 D 1-192 [» ]
    1I4T X-ray 2.60 D 1-192 [» ]
    1MH1 X-ray 1.38 A 2-184 [» ]
    1RYF X-ray 1.75 A/B 1-182 [» ]
    1RYH X-ray 1.75 A/B 1-182 [» ]
    2FJU X-ray 2.20 A 1-177 [» ]
    2H7V X-ray 2.60 A/B 1-184 [» ]
    2NZ8 X-ray 2.00 A 1-177 [» ]
    2P2L X-ray 1.90 A/B/C 1-184 [» ]
    2RMK NMR - A 1-192 [» ]
    2VRW X-ray 1.85 A 1-184 [» ]
    2WKP X-ray 1.90 A 4-180 [» ]
    2WKQ X-ray 1.60 A 4-180 [» ]
    2WKR X-ray 2.20 A 4-180 [» ]
    2YIN X-ray 2.70 C/D 1-177 [» ]
    3B13 X-ray 3.01 B/D 1-177 [» ]
    3BJI X-ray 2.60 C/D 1-177 [» ]
    3RYT X-ray 3.58 C 1-177 [» ]
    3SBD X-ray 2.10 A/B 2-177 [» ]
    3SBE X-ray 2.60 A 2-177 [» ]
    3SU8 X-ray 3.20 A 1-177 [» ]
    3SUA X-ray 4.39 A/B/C 1-177 [» ]
    3TH5 X-ray 2.30 A/B 2-177 [» ]
    4GZL X-ray 2.00 A/B 2-177 [» ]
    4GZM X-ray 2.80 A/B 2-177 [» ]
    DisProti DP00408.
    ProteinModelPortali P63000.
    SMRi P63000. Positions 1-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111817. 128 interactions.
    DIPi DIP-29260N.
    IntActi P63000. 94 interactions.
    MINTi MINT-4999291.
    STRINGi 9606.ENSP00000348461.

    Chemistry

    BindingDBi P63000.
    ChEMBLi CHEMBL6094.
    DrugBanki DB00175. Pravastatin.
    DB00641. Simvastatin.

    PTM databases

    PhosphoSitei P63000.

    Polymorphism databases

    DMDMi 51702787.

    Proteomic databases

    MaxQBi P63000.
    PaxDbi P63000.
    PRIDEi P63000.

    Protocols and materials databases

    DNASUi 5879.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000348035 ; ENSP00000258737 ; ENSG00000136238 . [P63000-1 ]
    ENST00000356142 ; ENSP00000348461 ; ENSG00000136238 . [P63000-2 ]
    GeneIDi 5879.
    KEGGi hsa:5879.
    UCSCi uc003spx.3. human.

    Organism-specific databases

    CTDi 5879.
    GeneCardsi GC07P006380.
    H-InvDB HIX0031500.
    HGNCi HGNC:9801. RAC1.
    HPAi CAB035994.
    MIMi 602048. gene.
    neXtProti NX_P63000.
    PharmGKBi PA34162.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233974.
    HOVERGENi HBG009351.
    KOi K04392.
    OMAi YPQTVAE.
    OrthoDBi EOG764747.
    PhylomeDBi P63000.
    TreeFami TF101109.

    Enzyme and pathway databases

    Reactomei 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_172581. PCP/CE pathway.
    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.
    SignaLinki P63000.

    Miscellaneous databases

    ChiTaRSi RAC1. human.
    EvolutionaryTracei P63000.
    GeneWikii RAC1.
    GenomeRNAii 5879.
    NextBioi 22846.
    PMAP-CutDB P63000.
    PROi P63000.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63000.
    Bgeei P63000.
    CleanExi HS_RAC1.
    Genevestigatori P63000.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR005225. Small_GTP-bd_dom.
    IPR001806. Small_GTPase.
    IPR003578. Small_GTPase_Rho.
    [Graphical view ]
    Pfami PF00071. Ras. 1 hit.
    [Graphical view ]
    PRINTSi PR00449. RASTRNSFRMNG.
    SMARTi SM00174. RHO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00231. small_GTP. 1 hit.
    PROSITEi PS51420. RHO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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.
    35. "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.
    36. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 (ISOFORM B), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    37. "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.
    38. "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.
    39. "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.
    40. Cited for: AMPYLATION AT TYR-32, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF TYR-32.
    41. "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.
    42. Cited for: INTERACTION WITH TBC1D2.
    43. "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.
    44. "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.
    45. "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.
    46. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    47. "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.
    48. "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.
    49. "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.
    50. "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.
    51. "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.
    52. Cited for: INTERACTION WITH ARHGDIA.
    53. "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.
    54. "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.
    55. "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.
    56. "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.
    57. "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.
    58. "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.
    59. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-176 IN COMPLEX WITH GTP ANALOG AND P.AERUGINOSA EXOS.
    60. "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.
    61. "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.
    62. "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).
    63. "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.
    64. "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.
    65. "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: October 1, 2014
    This is version 138 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