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Protein

Ras-related C3 botulinum toxin substrate 1

Gene

Rac1

Organism
Mus musculus (Mouse)
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. 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. enzyme binding Source: MGI
  2. GTPase activity Source: MGI
  3. GTP binding Source: MGI
  4. GTP-dependent protein binding Source: UniProtKB
  5. Rho GDP-dissociation inhibitor binding Source: UniProtKB
  6. thioesterase binding Source: MGI

GO - Biological processi

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

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_271763. DSCAM interactions.
REACT_277280. Activation of Rac.
REACT_278281. Ephrin signaling.
REACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_289095. NRAGE signals death through JNK.
REACT_295273. Sema4D mediated inhibition of cell attachment and migration.
REACT_295531. DCC mediated attractive signaling.
REACT_299052. G alpha (12/13) signalling events.
REACT_300885. Inactivation of Cdc42 and Rac.
REACT_301936. DAP12 signaling.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_307441. Sema3A PAK dependent Axon repulsion.
REACT_313804. EPHB-mediated forward signaling.
REACT_314186. FCERI mediated MAPK activation.
REACT_314615. EPH-ephrin mediated repulsion of cells.
REACT_314817. CD28 dependent Vav1 pathway.
REACT_315885. VEGFA-VEGFR2 Pathway.
REACT_321965. VEGFR2 mediated vascular permeability.
REACT_327841. Signaling by SCF-KIT.
REACT_333985. PCP/CE pathway.
REACT_337915. GPVI-mediated activation cascade.
REACT_340782. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_344463. Regulation of actin dynamics for phagocytic cup formation.
REACT_348121. Sema4D induced cell migration and growth-cone collapse.
REACT_353319. Signal transduction by L1.

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 Componenti: 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. actin filament Source: Ensembl
  2. cell projection Source: MGI
  3. cytoplasm Source: MGI
  4. cytoplasmic membrane-bounded vesicle Source: MGI
  5. cytoplasmic ribonucleoprotein granule Source: MGI
  6. cytosol Source: UniProtKB
  7. extracellular vesicular exosome Source: MGI
  8. extrinsic component of plasma membrane Source: MGI
  9. focal adhesion Source: MGI
  10. Golgi membrane Source: Ensembl
  11. lamellipodium Source: MGI
  12. melanosome Source: UniProtKB-SubCell
  13. membrane Source: MGI
  14. phagocytic cup Source: UniProtKB
  15. ruffle membrane Source: UniProtKB
  16. trans-Golgi network Source: MGI
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. 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

BgeeiP63001.
CleanExiMM_RAC1.
ExpressionAtlasiP63001. baseline and differential.
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.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP63001.
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

        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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry

BindingDBiP63001.
ChEMBLiCHEMBL5628.

PTM databases

PhosphoSiteiP63001.

Proteomic databases

MaxQBiP63001.
PaxDbiP63001.
PRIDEiP63001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5879.
MGIiMGI:97845. Rac1.

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000118978.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP63001.
KOiK04392.
OrthoDBiEOG764747.
PhylomeDBiP63001.
TreeFamiTF101109.

Enzyme and pathway databases

ReactomeiREACT_271763. DSCAM interactions.
REACT_277280. Activation of Rac.
REACT_278281. Ephrin signaling.
REACT_280010. Factors involved in megakaryocyte development and platelet production.
REACT_289095. NRAGE signals death through JNK.
REACT_295273. Sema4D mediated inhibition of cell attachment and migration.
REACT_295531. DCC mediated attractive signaling.
REACT_299052. G alpha (12/13) signalling events.
REACT_300885. Inactivation of Cdc42 and Rac.
REACT_301936. DAP12 signaling.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_307441. Sema3A PAK dependent Axon repulsion.
REACT_313804. EPHB-mediated forward signaling.
REACT_314186. FCERI mediated MAPK activation.
REACT_314615. EPH-ephrin mediated repulsion of cells.
REACT_314817. CD28 dependent Vav1 pathway.
REACT_315885. VEGFA-VEGFR2 Pathway.
REACT_321965. VEGFR2 mediated vascular permeability.
REACT_327841. Signaling by SCF-KIT.
REACT_333985. PCP/CE pathway.
REACT_337915. GPVI-mediated activation cascade.
REACT_340782. SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion.
REACT_344463. Regulation of actin dynamics for phagocytic cup formation.
REACT_348121. Sema4D induced cell migration and growth-cone collapse.
REACT_353319. Signal transduction by L1.

Miscellaneous databases

ChiTaRSiRac1. mouse.
NextBioi296387.
PROiP63001.
SOURCEiSearch...

Gene expression databases

BgeeiP63001.
CleanExiMM_RAC1.
ExpressionAtlasiP63001. baseline and differential.
GenevestigatoriP63001.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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(1990) [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(2004) [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(2003) [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(1997) [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(1999) [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(1999) [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(1999) [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(2004) [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(2006) [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(2007) [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(2008) [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(2009) [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(2010) [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: April 1, 2015
This is version 129 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

Similar proteinsi

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