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P63001

- RAC1_MOUSE

UniProt

P63001 - RAC1_MOUSE

Protein

Ras-related C3 botulinum toxin substrate 1

Gene

Rac1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (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. 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 podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3.1 Publication

    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 By similarity.By similarity

    Regions

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

    GO - Molecular functioni

    1. GTPase activity Source: MGI
    2. GTP binding Source: MGI
    3. GTP-dependent protein binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. Rho GDP-dissociation inhibitor binding Source: UniProtKB

    GO - Biological processi

    1. actin filament polymerization Source: MGI
    2. anatomical structure arrangement Source: MGI
    3. auditory receptor cell morphogenesis Source: MGI
    4. axon guidance Source: MGI
    5. bone resorption Source: Ensembl
    6. cell adhesion Source: MGI
    7. cell-cell junction organization Source: MGI
    8. cell migration Source: MGI
    9. cell motility Source: UniProtKB
    10. cell proliferation Source: Ensembl
    11. cerebral cortex radially oriented cell migration Source: MGI
    12. cochlea morphogenesis Source: MGI
    13. cytoskeleton organization Source: MGI
    14. dendrite development Source: MGI
    15. dendrite morphogenesis Source: MGI
    16. dopaminergic neuron differentiation Source: MGI
    17. embryonic olfactory bulb interneuron precursor migration Source: MGI
    18. endocytosis Source: MGI
    19. engulfment of apoptotic cell Source: BHF-UCL
    20. epithelial cell morphogenesis Source: MGI
    21. G-protein coupled receptor signaling pathway Source: MGI
    22. hyperosmotic response Source: MGI
    23. lamellipodium assembly Source: MGI
    24. localization within membrane Source: Ensembl
    25. mast cell chemotaxis Source: Ensembl
    26. negative regulation of interleukin-23 production Source: Ensembl
    27. phagocytosis, engulfment Source: UniProtKB
    28. positive regulation of actin filament polymerization Source: MGI
    29. positive regulation of DNA replication Source: Ensembl
    30. positive regulation of lamellipodium assembly Source: MGI
    31. positive regulation of phosphatidylinositol 3-kinase activity Source: MGI
    32. positive regulation of protein phosphorylation Source: UniProtKB
    33. protein localization to plasma membrane Source: MGI
    34. regulation of cell migration Source: MGI
    35. regulation of respiratory burst Source: Ensembl
    36. ruffle assembly Source: UniProtKB
    37. ruffle organization Source: MGI
    38. semaphorin-plexin signaling pathway Source: UniProtKB
    39. small GTPase mediated signal transduction Source: MGI
    40. substrate adhesion-dependent cell spreading Source: MGI
    41. Wnt signaling pathway, planar cell polarity pathway Source: MGI

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_188185. DAP12 signaling.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_188578. Signaling by SCF-KIT.
    REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_204733. G alpha (12/13) signalling events.
    REACT_209641. NRAGE signals death through JNK.
    REACT_214043. PCP/CE pathway.
    REACT_215461. Signal transduction by L1.
    REACT_220092. GPVI-mediated activation cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ras-related C3 botulinum toxin substrate 1
    Alternative name(s):
    p21-Rac1
    Gene namesi
    Name:Rac1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:97845. Rac1.

    Subcellular locationi

    Cell membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Melanosome By similarity. Cytoplasm By similarity
    Note: Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine. 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. cell projection Source: MGI
    2. cytoplasm Source: MGI
    3. cytoplasmic membrane-bounded vesicle Source: MGI
    4. cytosol Source: UniProtKB
    5. extrinsic component of plasma membrane Source: MGI
    6. Golgi membrane Source: Ensembl
    7. lamellipodium Source: MGI
    8. melanosome Source: UniProtKB-SubCell
    9. membrane Source: MGI
    10. phagocytic cup Source: UniProtKB
    11. ruffle membrane Source: UniProtKB
    12. trans-Golgi network Source: Ensembl

    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. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 189189Ras-related C3 botulinum toxin substrate 1PRO_0000042038Add
    BLAST
    Propeptidei190 – 1923Removed in mature formBy similarityPRO_0000042039

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki147 – 147Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei189 – 1891Cysteine methyl esterBy similarity
    Lipidationi189 – 1891S-geranylgeranyl cysteineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Isopeptide bond, Lipoprotein, Methylation, Prenylation, Ubl conjugation

    Proteomic databases

    MaxQBiP63001.
    PaxDbiP63001.
    PRIDEiP63001.

    PTM databases

    PhosphoSiteiP63001.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiP63001.
    BgeeiP63001.
    CleanExiMM_RAC1.
    GenevestigatoriP63001.

    Interactioni

    Subunit structurei

    Interacts with the GEF proteins PREX1, FARP1, FARP2, DOCK1, DOCK2 and DOCK7, which promote the exchange between GDP and GTP, and therefore activate it. 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 BAIAP2, BAIAP2L1, PLXNB1, CYFIP1/SRA-1 and DEF6. Probably found in a ternary complex composed of DSCAM, PAK1 and RAC1. Interacts with DSCAM; the interaction requires PAK1. Interacts with TBC1D2. Interacts with UNKL. Interacts with USP6. Interacts with SPATA13. Interacts with ITGB4. Interacts with the GTP-bound form of RAB7A. Interacts with ARHGEF2. Interacts with ARHGEF16; mediates activation of RAC1 by EPHA2. Interacts with NOXA1. Interacts with S100A8 and calprotectin (S100A8/9). Interacts with ARHGDIA; the interaction is induced by SEMA5A, mediated through PLXNB3 and inactivates and stabilizes RAC1. Interacts with PACSIN2. Interacts with ITGB1BP1 By similarity. Interacts with the GEF protein RASGRF2, which promotes the exchange between GDP and GTP, and therefore activates it. Interacts with PARD6A, PARD6B and PARD6G in a GTP-dependent manner. Part of a complex with MAP2K3, MAP3K3 and CCM2. Interacts with NISCH. Interacts with PIP5K1A. Interacts (GTP-bound form preferentially) with PKN2 (via the REM repeats); the interaction stimulates autophosphorylation and phosphorylation of PKN2. Interacts with SRGAP2. Interacts with PLXNB3. Interacts (when active) with PPP5C (via TPR repeats); activates PPP5C phosphatase activity and translocates PPP5C to the cell membrane.By similarity10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Dlg4Q621082EBI-413646,EBI-300895
    PAK1Q131533EBI-413646,EBI-1307From a different organism.
    Sod1P082284EBI-413646,EBI-1635090

    Protein-protein interaction databases

    BioGridi202556. 20 interactions.
    IntActiP63001. 28 interactions.
    MINTiMINT-1602774.

    Structurei

    3D structure databases

    ProteinModelPortaliP63001.
    SMRiP63001. Positions 1-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

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

    Domaini

    The effector region mediates interaction with DEF6.By similarity

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rho family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    GeneTreeiENSGT00640000091266.
    HOGENOMiHOG000233974.
    HOVERGENiHBG009351.
    KOiK04392.
    OrthoDBiEOG764747.
    PhylomeDBiP63001.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P63001-1 [UniParc]FASTAAdd to Basket

    « 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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57277 mRNA. Translation: CAA40545.1.
    AK009017 mRNA. Translation: BAB26027.1.
    AK011072 mRNA. Translation: BAB69451.1.
    AK034601 mRNA. Translation: BAC28767.1.
    AK047969 mRNA. Translation: BAC33203.1.
    AK088825 mRNA. Translation: BAC40596.1.
    BC003828 mRNA. Translation: AAH03828.1.
    BC051053 mRNA. Translation: AAH51053.1.
    CCDSiCCDS19843.1.
    PIRiA60347.
    RefSeqiNP_033033.1. NM_009007.2.
    UniGeneiMm.292510.
    Mm.469963.
    Mm.475073.

    Genome annotation databases

    EnsembliENSMUST00000080537; ENSMUSP00000079380; ENSMUSG00000001847.
    GeneIDi19353.
    KEGGimmu:19353.
    UCSCiuc009akk.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57277 mRNA. Translation: CAA40545.1 .
    AK009017 mRNA. Translation: BAB26027.1 .
    AK011072 mRNA. Translation: BAB69451.1 .
    AK034601 mRNA. Translation: BAC28767.1 .
    AK047969 mRNA. Translation: BAC33203.1 .
    AK088825 mRNA. Translation: BAC40596.1 .
    BC003828 mRNA. Translation: AAH03828.1 .
    BC051053 mRNA. Translation: AAH51053.1 .
    CCDSi CCDS19843.1.
    PIRi A60347.
    RefSeqi NP_033033.1. NM_009007.2.
    UniGenei Mm.292510.
    Mm.469963.
    Mm.475073.

    3D structure databases

    ProteinModelPortali P63001.
    SMRi P63001. Positions 1-177.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202556. 20 interactions.
    IntActi P63001. 28 interactions.
    MINTi MINT-1602774.

    Chemistry

    BindingDBi P63001.
    ChEMBLi CHEMBL5628.

    PTM databases

    PhosphoSitei P63001.

    Proteomic databases

    MaxQBi P63001.
    PaxDbi P63001.
    PRIDEi P63001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000080537 ; ENSMUSP00000079380 ; ENSMUSG00000001847 .
    GeneIDi 19353.
    KEGGi mmu:19353.
    UCSCi uc009akk.1. mouse.

    Organism-specific databases

    CTDi 5879.
    MGIi MGI:97845. Rac1.

    Phylogenomic databases

    eggNOGi COG1100.
    GeneTreei ENSGT00640000091266.
    HOGENOMi HOG000233974.
    HOVERGENi HBG009351.
    KOi K04392.
    OrthoDBi EOG764747.
    PhylomeDBi P63001.
    TreeFami TF101109.

    Enzyme and pathway databases

    Reactomei REACT_188185. DAP12 signaling.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_188578. Signaling by SCF-KIT.
    REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_204733. G alpha (12/13) signalling events.
    REACT_209641. NRAGE signals death through JNK.
    REACT_214043. PCP/CE pathway.
    REACT_215461. Signal transduction by L1.
    REACT_220092. GPVI-mediated activation cascade.

    Miscellaneous databases

    ChiTaRSi RAC1. mouse.
    NextBioi 296387.
    PROi P63001.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P63001.
    Bgeei P63001.
    CleanExi MM_RAC1.
    Genevestigatori P63001.

    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. "The murine rac1 gene: cDNA cloning, tissue distribution and regulated expression of rac1 mRNA by disassembly of actin microfilaments."
      Moll J., Sansig G., Fattori E., van der Putten H.
      Oncogene 6:863-866(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
      Tissue: Thymus.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Head, Liver, Thymus and Tongue.
    3. "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].
      Strain: Czech II and FVB/N.
      Tissue: Mammary tumor.
    4. "The exchange factor Ras-GRF2 activates Ras-dependent and Rac-dependent mitogen-activated protein kinase pathways."
      Fan W.-T., Koch C.A., de Hoog C.L., Fam N.P., Moran M.F.
      Curr. Biol. 8:935-938(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RASGRF2.
    5. "The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42."
      Joberty G., Petersen C., Gao L., Macara I.G.
      Nat. Cell Biol. 2:531-539(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARD6A, MUTAGENESIS OF GLY-12.
    6. "A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity."
      Lin D., Edwards A.S., Fawcett J.P., Mbamalu G., Scott J.D., Pawson T.
      Nat. Cell Biol. 2:540-547(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARD6B.
    7. "Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-dependent actin assembly."
      Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C., Carpenter C.L.
      Curr. Biol. 10:153-156(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIP5K1A.
    8. Cited for: INTERACTION WITH MAP3K3; MAP2K3 AND CCM2.
    9. "Regulation of p21-activated kinase-independent Rac1 signal transduction by Nischarin."
      Reddig P.J., Xu D., Juliano R.L.
      J. Biol. Chem. 280:30994-31002(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NISCH.
    10. "Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma kinase activation leading to cytoskeleton function and cell migration in astrocytes."
      Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.
      J. Neurochem. 101:1002-1017(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PKN2.
    11. "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.
    12. "The F-BAR domain of srGAP2 induces membrane protrusions required for neuronal migration and morphogenesis."
      Guerrier S., Coutinho-Budd J., Sassa T., Gresset A., Jordan N.V., Chen K., Jin W.L., Frost A., Polleux F.
      Cell 138:990-1004(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRGAP2, ENZYME REGULATION.
    13. "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: INTERACTION WITH PLXNB3.
    14. "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.

    Entry informationi

    Entry nameiRAC1_MOUSE
    AccessioniPrimary (citable) accession number: P63001
    Secondary accession number(s): O95501, P15154, 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 123 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3