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P08134

- RHOC_HUMAN

UniProt

P08134 - RHOC_HUMAN

Protein

Rho-related GTP-binding protein RhoC

Gene

RHOC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 1 (01 Aug 1988)
      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.2 Publications

    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: UniProtKB
    3. signal transducer activity Source: UniProtKB

    GO - Biological processi

    1. apical junction assembly Source: UniProtKB
    2. axon guidance Source: Reactome
    3. cytokinesis Source: UniProtKB
    4. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    5. regulation of small GTPase mediated signal transduction Source: Reactome
    6. small GTPase mediated signal transduction Source: Reactome

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.
    SignaLinkiP08134.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho-related GTP-binding protein RhoC
    Alternative name(s):
    Rho cDNA clone 9
    Short name:
    h9
    Gene namesi
    Name:RHOC
    Synonyms:ARH9, ARHC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:669. RHOC.

    Subcellular locationi

    Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated. Cleavage furrow 1 Publication
    Note: Translocates to the equatorial region before furrow formation in a ECT2-dependent manner.

    GO - Cellular componenti

    1. cleavage furrow Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: Ensembl
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24951.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 190190Rho-related GTP-binding protein RhoCPRO_0000042022Add
    BLAST
    Propeptidei191 – 1933Removed in mature formBy similarityPRO_0000042023

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei41 – 411ADP-ribosylasparagine; by botulinum toxinBy similarity
    Modified residuei190 – 1901Cysteine methyl esterBy similarity
    Lipidationi190 – 1901S-geranylgeranyl cysteineBy similarity

    Keywords - PTMi

    ADP-ribosylation, Lipoprotein, Methylation, Prenylation

    Proteomic databases

    MaxQBiP08134.
    PaxDbiP08134.
    PRIDEiP08134.

    PTM databases

    PhosphoSiteiP08134.

    Expressioni

    Gene expression databases

    ArrayExpressiP08134.
    BgeeiP08134.
    CleanExiHS_RHOC.
    GenevestigatoriP08134.

    Organism-specific databases

    HPAiCAB010821.

    Interactioni

    Subunit structurei

    Interacts with RTKN By similarity. Interacts with AKAP13, DIAPH1, PKN2, ROCK1 and ROCK2. Interacts with ARHGDIA.By similarity5 Publications

    Protein-protein interaction databases

    BioGridi106882. 11 interactions.
    IntActiP08134. 6 interactions.
    MINTiMINT-1216716.
    STRINGi9606.ENSP00000285735.

    Structurei

    Secondary structure

    1
    193
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1310
    Helixi18 – 2710
    Beta strandi43 – 486
    Beta strandi51 – 588
    Helixi64 – 663
    Turni67 – 693
    Helixi70 – 734
    Beta strandi78 – 858
    Helixi89 – 979
    Helixi99 – 1068
    Beta strandi112 – 1176
    Helixi119 – 1213
    Helixi125 – 1328
    Turni133 – 1353
    Helixi141 – 15010
    Beta strandi154 – 1585
    Turni161 – 1633
    Helixi167 – 17913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Z2CX-ray3.00A/C1-193[»]
    2GCNX-ray1.85A1-181[»]
    2GCOX-ray1.40A/B1-181[»]
    2GCPX-ray2.15A1-181[»]
    ProteinModelPortaliP08134.
    SMRiP08134. Positions 3-179.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08134.

    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.
    HOGENOMiHOG000233974.
    HOVERGENiHBG009351.
    KOiK07857.
    OrthoDBiEOG73FQPD.
    PhylomeDBiP08134.
    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.

    P08134-1 [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:August 1, 1988 - v1
    Checksum:iA193DA581560F131
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti120 – 1201D → H.
    Corresponds to variant rs11538959 [ dbSNP | Ensembl ].
    VAR_051974

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06821 mRNA. Translation: CAA29969.1.
    L25081 mRNA. Translation: AAC33179.1.
    AF498972 mRNA. Translation: AAM21119.1.
    CR450360 mRNA. Translation: CAG29356.1.
    BT019448 mRNA. Translation: AAV38255.1.
    AK094474 mRNA. Translation: BAG52873.1.
    AL603832 Genomic DNA. Translation: CAI14058.1.
    CH471122 Genomic DNA. Translation: EAW56534.1.
    BC007245 mRNA. Translation: AAH07245.1.
    BC009177 mRNA. Translation: AAH09177.1.
    BC052808 mRNA. Translation: AAH52808.1.
    CCDSiCCDS854.1.
    PIRiS01029. TVHURC.
    RefSeqiNP_001036143.1. NM_001042678.1.
    NP_001036144.1. NM_001042679.1.
    NP_786886.1. NM_175744.4.
    UniGeneiHs.502659.
    Hs.658289.

    Genome annotation databases

    EnsembliENST00000285735; ENSP00000285735; ENSG00000155366.
    ENST00000339083; ENSP00000345236; ENSG00000155366.
    ENST00000369632; ENSP00000358646; ENSG00000155366.
    ENST00000369633; ENSP00000358647; ENSG00000155366.
    ENST00000369637; ENSP00000358651; ENSG00000155366.
    ENST00000369638; ENSP00000358652; ENSG00000155366.
    ENST00000369642; ENSP00000358656; ENSG00000155366.
    GeneIDi389.
    KEGGihsa:389.
    UCSCiuc001ecp.1. human.

    Polymorphism databases

    DMDMi132543.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06821 mRNA. Translation: CAA29969.1 .
    L25081 mRNA. Translation: AAC33179.1 .
    AF498972 mRNA. Translation: AAM21119.1 .
    CR450360 mRNA. Translation: CAG29356.1 .
    BT019448 mRNA. Translation: AAV38255.1 .
    AK094474 mRNA. Translation: BAG52873.1 .
    AL603832 Genomic DNA. Translation: CAI14058.1 .
    CH471122 Genomic DNA. Translation: EAW56534.1 .
    BC007245 mRNA. Translation: AAH07245.1 .
    BC009177 mRNA. Translation: AAH09177.1 .
    BC052808 mRNA. Translation: AAH52808.1 .
    CCDSi CCDS854.1.
    PIRi S01029. TVHURC.
    RefSeqi NP_001036143.1. NM_001042678.1.
    NP_001036144.1. NM_001042679.1.
    NP_786886.1. NM_175744.4.
    UniGenei Hs.502659.
    Hs.658289.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Z2C X-ray 3.00 A/C 1-193 [» ]
    2GCN X-ray 1.85 A 1-181 [» ]
    2GCO X-ray 1.40 A/B 1-181 [» ]
    2GCP X-ray 2.15 A 1-181 [» ]
    ProteinModelPortali P08134.
    SMRi P08134. Positions 3-179.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106882. 11 interactions.
    IntActi P08134. 6 interactions.
    MINTi MINT-1216716.
    STRINGi 9606.ENSP00000285735.

    PTM databases

    PhosphoSitei P08134.

    Polymorphism databases

    DMDMi 132543.

    Proteomic databases

    MaxQBi P08134.
    PaxDbi P08134.
    PRIDEi P08134.

    Protocols and materials databases

    DNASUi 389.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000285735 ; ENSP00000285735 ; ENSG00000155366 .
    ENST00000339083 ; ENSP00000345236 ; ENSG00000155366 .
    ENST00000369632 ; ENSP00000358646 ; ENSG00000155366 .
    ENST00000369633 ; ENSP00000358647 ; ENSG00000155366 .
    ENST00000369637 ; ENSP00000358651 ; ENSG00000155366 .
    ENST00000369638 ; ENSP00000358652 ; ENSG00000155366 .
    ENST00000369642 ; ENSP00000358656 ; ENSG00000155366 .
    GeneIDi 389.
    KEGGi hsa:389.
    UCSCi uc001ecp.1. human.

    Organism-specific databases

    CTDi 389.
    GeneCardsi GC01M113243.
    HGNCi HGNC:669. RHOC.
    HPAi CAB010821.
    MIMi 165380. gene.
    neXtProti NX_P08134.
    PharmGKBi PA24951.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1100.
    HOGENOMi HOG000233974.
    HOVERGENi HBG009351.
    KOi K07857.
    OrthoDBi EOG73FQPD.
    PhylomeDBi P08134.
    TreeFami TF300837.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.
    SignaLinki P08134.

    Miscellaneous databases

    EvolutionaryTracei P08134.
    GeneWikii RhoC.
    GenomeRNAii 389.
    NextBioi 1619.
    PROi P08134.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08134.
    Bgeei P08134.
    CleanExi HS_RHOC.
    Genevestigatori P08134.

    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. "Coding sequence of human rho cDNAs clone 6 and clone 9."
      Chardin P., Madaule P., Tavitian A.
      Nucleic Acids Res. 16:2717-2717(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Fagan K.P., Oliveira L., Pittler S.J.
      Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Retina.
    3. "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].
      Tissue: Brain.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Cerebellum.
    7. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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].
      Tissue: Skin.
    10. "The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton."
      Leung T., Chen X.-Q., Manser E., Lim L.
      Mol. Cell. Biol. 16:5313-5327(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROCK1 AND ROCK2.
    11. "AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation."
      Diviani D., Soderling J., Scott J.D.
      J. Biol. Chem. 276:44247-44257(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AKAP13.
    12. "Dissecting the role of Rho-mediated signaling in contractile ring formation."
      Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S., Miki T.
      Mol. Biol. Cell 17:43-55(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Regulation of Rho GTPase crosstalk, degradation and activity by RhoGDI1."
      Boulter E., Garcia-Mata R., Guilluy C., Dubash A., Rossi G., Brennwald P.J., Burridge K.
      Nat. Cell Biol. 12:477-483(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGDIA.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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.
    16. "Structural and mechanistic insights into the interaction between Rho and mammalian Dia."
      Rose R., Weyand M., Lammers M., Ishizaki T., Ahmadian M.R., Wittinghofer A.
      Nature 435:513-518(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH DIAPH1.

    Entry informationi

    Entry nameiRHOC_HUMAN
    AccessioniPrimary (citable) accession number: P08134
    Secondary accession number(s): B3KSW1, Q6ICN3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: October 1, 2014
    This is version 168 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 1
      Human chromosome 1: 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