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P08134 (RHOC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 166. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rho-related GTP-binding protein RhoC
Alternative name(s):
Rho cDNA clone 9
Short name=h9
Gene names
Name:RHOC
Synonyms:ARH9, ARHC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length193 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12 Ref.15

Subunit structure

Interacts with RTKN By similarity. Interacts with AKAP13, DIAPH1, PKN2, ROCK1 and ROCK2. Interacts with ARHGDIA. Ref.10 Ref.11 Ref.13 Ref.15

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Cleavage furrow. Note: Translocates to the equatorial region before furrow formation in a ECT2-dependent manner. Ref.12

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 190190Rho-related GTP-binding protein RhoC
PRO_0000042022
Propeptide191 – 1933Removed in mature form By similarity
PRO_0000042023

Regions

Nucleotide binding12 – 198GTP By similarity
Nucleotide binding59 – 635GTP By similarity
Nucleotide binding117 – 1204GTP By similarity
Motif34 – 429Effector region Potential

Amino acid modifications

Modified residue411ADP-ribosylasparagine; by botulinum toxin By similarity
Modified residue1901Cysteine methyl ester By similarity
Lipidation1901S-geranylgeranyl cysteine By similarity

Natural variations

Natural variant1201D → H.
Corresponds to variant rs11538959 [ dbSNP | Ensembl ].
VAR_051974

Secondary structure

.................................. 193
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08134 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: A193DA581560F131

FASTA19322,006
        10         20         30         40         50         60 
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYIADIEVDG KQVELALWDT 

        70         80         90        100        110        120 
AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD 

       130        140        150        160        170        180 
LRQDEHTRRE LAKMKQEPVR SEEGRDMANR ISAFGYLECS AKTKEGVREV FEMATRAGLQ 

       190 
VRKNKRRRGC PIL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS854.1.
PIRTVHURC. S01029.
RefSeqNP_001036143.1. NM_001042678.1.
NP_001036144.1. NM_001042679.1.
NP_786886.1. NM_175744.4.
UniGeneHs.502659.
Hs.658289.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z2CX-ray3.00A/C1-193[»]
2GCNX-ray1.85A1-181[»]
2GCOX-ray1.40A/B1-181[»]
2GCPX-ray2.15A1-181[»]
ProteinModelPortalP08134.
SMRP08134. Positions 3-179.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106882. 11 interactions.
IntActP08134. 6 interactions.
MINTMINT-1216716.
STRING9606.ENSP00000285735.

PTM databases

PhosphoSiteP08134.

Polymorphism databases

DMDM132543.

Proteomic databases

MaxQBP08134.
PaxDbP08134.
PRIDEP08134.

Protocols and materials databases

DNASU389.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285735; ENSP00000285735; ENSG00000155366.
ENST00000339083; ENSP00000345236; ENSG00000155366.
ENST00000369632; ENSP00000358646; ENSG00000155366.
ENST00000369633; ENSP00000358647; ENSG00000155366.
ENST00000369637; ENSP00000358651; ENSG00000155366.
ENST00000369638; ENSP00000358652; ENSG00000155366.
ENST00000369642; ENSP00000358656; ENSG00000155366.
GeneID389.
KEGGhsa:389.
UCSCuc001ecp.1. human.

Organism-specific databases

CTD389.
GeneCardsGC01M113243.
HGNCHGNC:669. RHOC.
HPACAB010821.
MIM165380. gene.
neXtProtNX_P08134.
PharmGKBPA24951.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1100.
HOGENOMHOG000233974.
HOVERGENHBG009351.
KOK07857.
OrthoDBEOG73FQPD.
PhylomeDBP08134.
TreeFamTF300837.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
SignaLinkP08134.

Gene expression databases

ArrayExpressP08134.
BgeeP08134.
CleanExHS_RHOC.
GenevestigatorP08134.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00174. RHO. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51420. RHO. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08134.
GeneWikiRhoC.
GenomeRNAi389.
NextBio1619.
PROP08134.
SOURCESearch...

Entry information

Entry nameRHOC_HUMAN
AccessionPrimary (citable) accession number: P08134
Secondary accession number(s): B3KSW1, Q6ICN3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 9, 2014
This is version 166 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM