SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q62159

- RHOC_MOUSE

UniProt

Q62159 - RHOC_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Rho-related GTP-binding protein RhoC

Gene
Rhoc, Arhc
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 198GTP By similarity
Nucleotide bindingi59 – 635GTP By similarity
Nucleotide bindingi117 – 1204GTP By 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
Complete GO annotation...

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; Lipid-anchor; Cytoplasmic side Reviewed prediction. 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
Complete GO annotation...

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 form By similarityPRO_0000042025

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei190 – 1901Cysteine methyl ester By similarity
Lipidationi190 – 1901S-geranylgeranyl cysteine By 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.2 Publications

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ62159.
SMRiQ62159. Positions 3-179.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi34 – 429Effector region Reviewed prediction

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti102 – 1021E → Q in CAA56682. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 136 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

Similar proteinsi