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Q62159

- RHOC_MOUSE

UniProt

Q62159 - RHOC_MOUSE

Protein

Rho-related GTP-binding protein RhoC

Gene

Rhoc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (13 Apr 2004)
      Previous versions | rss
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    Functioni

    Regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Serves as a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis. Regulates apical junction formation in bronchial epithelial cells.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 198GTPBy similarity
    Nucleotide bindingi59 – 635GTPBy similarity
    Nucleotide bindingi117 – 1204GTPBy similarity

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. protein binding Source: MGI
    3. signal transducer activity Source: Ensembl

    GO - Biological processi

    1. apical junction assembly Source: UniProtKB
    2. cytokinesis Source: UniProtKB
    3. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
    4. small GTPase mediated signal transduction Source: InterPro

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_204733. G alpha (12/13) signalling events.
    REACT_210090. Rho GTPase cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho-related GTP-binding protein RhoC
    Alternative name(s):
    Silica-induced gene 61 protein
    Short name:
    SIG-61
    Gene namesi
    Name:Rhoc
    Synonyms:Arhc
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:106028. Rhoc.

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. Cleavage furrow By similarity
    Note: Translocates to the equatorial region before furrow formation in a ECT2-dependent manner.By similarity

    GO - Cellular componenti

    1. cleavage furrow Source: UniProtKB
    2. cytosol Source: Ensembl
    3. nucleus Source: MGI
    4. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 190190Rho-related GTP-binding protein RhoCPRO_0000042024Add
    BLAST
    Propeptidei191 – 1933Removed in mature formBy similarityPRO_0000042025

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei190 – 1901Cysteine methyl esterBy similarity
    Lipidationi190 – 1901S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiQ62159.
    PaxDbiQ62159.
    PRIDEiQ62159.

    PTM databases

    PhosphoSiteiQ62159.

    Expressioni

    Inductioni

    Up-regulated in silica-treated macrophages.1 Publication

    Gene expression databases

    ArrayExpressiQ62159.
    BgeeiQ62159.
    CleanExiMM_RHOC.
    GenevestigatoriQ62159.

    Interactioni

    Subunit structurei

    Interacts with AKAP13, DIAPH1, ROCK1 and ROCK2 By similarity. Interacts with ARHGDIA By similarity. Interacts with PKN2 and RTKN.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi198197. 1 interaction.
    IntActiQ62159. 2 interactions.
    MINTiMINT-4132345.

    Structurei

    3D structure databases

    ProteinModelPortaliQ62159.
    SMRiQ62159. Positions 3-179.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi34 – 429Effector regionSequence Analysis

    Sequence similaritiesi

    Belongs to the small GTPase superfamily. Rho family.Curated

    Phylogenomic databases

    eggNOGiCOG1100.
    GeneTreeiENSGT00700000104143.
    HOGENOMiHOG000233974.
    HOVERGENiHBG009351.
    InParanoidiQ62159.
    KOiK07857.
    OMAiGKKHHCV.
    OrthoDBiEOG73FQPD.
    PhylomeDBiQ62159.
    TreeFamiTF300837.

    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.

    Q62159-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYIADIEVDG    50
    KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT 100
    PEVKHFCPNV PIILVGNKKD LRQDEHTRRE LAKMKQEPVR SEEGRDMANR 150
    ISAFGYLECS AKTKEGVREV FEMATRAGLQ VRKNKRRRGC PIL 193
    Length:193
    Mass (Da):22,006
    Last modified:April 13, 2004 - v2
    Checksum:iA193DA581560F131
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti102 – 1021E → Q in CAA56682. (PubMed:7868905)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80638 mRNA. Translation: CAA56682.1.
    AK011599 mRNA. Translation: BAB27724.1.
    AK152802 mRNA. Translation: BAE31507.1.
    AK160650 mRNA. Translation: BAE35941.1.
    BC004627 mRNA. Translation: AAH04627.1.
    CCDSiCCDS17704.1.
    RefSeqiNP_001278788.1. NM_001291859.1.
    NP_031510.2. NM_007484.2.
    UniGeneiMm.262.

    Genome annotation databases

    EnsembliENSMUST00000002303; ENSMUSP00000002303; ENSMUSG00000002233.
    ENSMUST00000106787; ENSMUSP00000102399; ENSMUSG00000002233.
    GeneIDi11853.
    KEGGimmu:11853.
    UCSCiuc008qul.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X80638 mRNA. Translation: CAA56682.1 .
    AK011599 mRNA. Translation: BAB27724.1 .
    AK152802 mRNA. Translation: BAE31507.1 .
    AK160650 mRNA. Translation: BAE35941.1 .
    BC004627 mRNA. Translation: AAH04627.1 .
    CCDSi CCDS17704.1.
    RefSeqi NP_001278788.1. NM_001291859.1.
    NP_031510.2. NM_007484.2.
    UniGenei Mm.262.

    3D structure databases

    ProteinModelPortali Q62159.
    SMRi Q62159. Positions 3-179.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198197. 1 interaction.
    IntActi Q62159. 2 interactions.
    MINTi MINT-4132345.

    PTM databases

    PhosphoSitei Q62159.

    Proteomic databases

    MaxQBi Q62159.
    PaxDbi Q62159.
    PRIDEi Q62159.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000002303 ; ENSMUSP00000002303 ; ENSMUSG00000002233 .
    ENSMUST00000106787 ; ENSMUSP00000102399 ; ENSMUSG00000002233 .
    GeneIDi 11853.
    KEGGi mmu:11853.
    UCSCi uc008qul.2. mouse.

    Organism-specific databases

    CTDi 389.
    MGIi MGI:106028. Rhoc.

    Phylogenomic databases

    eggNOGi COG1100.
    GeneTreei ENSGT00700000104143.
    HOGENOMi HOG000233974.
    HOVERGENi HBG009351.
    InParanoidi Q62159.
    KOi K07857.
    OMAi GKKHHCV.
    OrthoDBi EOG73FQPD.
    PhylomeDBi Q62159.
    TreeFami TF300837.

    Enzyme and pathway databases

    Reactomei REACT_204733. G alpha (12/13) signalling events.
    REACT_210090. Rho GTPase cycle.

    Miscellaneous databases

    NextBioi 279829.
    PROi Q62159.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q62159.
    Bgeei Q62159.
    CleanExi MM_RHOC.
    Genevestigatori Q62159.

    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. "Isolation of nine gene sequences induced by silica in murine macrophages."
      Segade F., Claudio E., Wrobel K., Ramos S., Lazo P.S.
      J. Immunol. 154:2384-2392(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
      Tissue: Macrophage.
    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.
      Tissue: Bone marrow.
    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: FVB/N.
      Tissue: Mammary tumor.
    4. "Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain."
      Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N., Fujisawa K., Morii N., Madaule P., Narumiya S.
      J. Biol. Chem. 271:13556-13560(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RTKN.
    5. "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: FUNCTION, INTERACTION WITH PKN2.

    Entry informationi

    Entry nameiRHOC_MOUSE
    AccessioniPrimary (citable) accession number: Q62159
    Secondary accession number(s): Q3TUN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 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