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Protein

Rho-related GTP-binding protein RhoC

Gene

RHOC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.2 Publications

Regions

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

GO - Molecular functioni

  • GTP binding Source: UniProtKB-KW
  • signal transducer activity Source: UniProtKB

GO - Biological processi

  • apical junction assembly Source: UniProtKB
  • axon guidance Source: Reactome
  • cytokinesis Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of lipase activity Source: AgBase
  • regulation of small GTPase mediated signal transduction Source: Reactome
  • skeletal muscle satellite cell migration Source: AgBase
  • small GTPase mediated signal transduction Source: Reactome
  • wound healing, spreading of cells Source: AgBase
Complete GO annotation...

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.
REACT_355021. RHO GTPases Activate Rhotekin and Rhophilins.
REACT_355192. RHO GTPases Activate ROCKs.
REACT_355252. RHO GTPases Activate Formins.
REACT_355303. RHO GTPases activate CIT.
REACT_355542. RHO GTPases activate PKNs.
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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:669. RHOC.

Subcellular locationi

GO - Cellular componenti

  • cleavage furrow Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleus Source: Ensembl
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24951.

Polymorphism and mutation databases

BioMutaiRHOC.
DMDMi132543.

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

BgeeiP08134.
CleanExiHS_RHOC.
ExpressionAtlasiP08134. baseline and differential.
GenevestigatoriP08134.

Organism-specific databases

HPAiHPA062346.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM65BQ9Y4F95EBI-747589,EBI-2798942

Protein-protein interaction databases

BioGridi106882. 12 interactions.
IntActiP08134. 8 interactions.
MINTiMINT-1216716.
STRINGi9606.ENSP00000285735.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP08134.
KOiK07857.
OMAiNILEKWH.
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

        10         20         30         40         50
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYIADIEVDG
60 70 80 90 100
KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT
110 120 130 140 150
PEVKHFCPNV PIILVGNKKD LRQDEHTRRE LAKMKQEPVR SEEGRDMANR
160 170 180 190
ISAFGYLECS AKTKEGVREV FEMATRAGLQ VRKNKRRRGC PIL
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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi106882. 12 interactions.
IntActiP08134. 8 interactions.
MINTiMINT-1216716.
STRINGi9606.ENSP00000285735.

PTM databases

PhosphoSiteiP08134.

Polymorphism and mutation databases

BioMutaiRHOC.
DMDMi132543.

Proteomic databases

MaxQBiP08134.
PaxDbiP08134.
PRIDEiP08134.

Protocols and materials databases

DNASUi389.
Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

CTDi389.
GeneCardsiGC01M113243.
HGNCiHGNC:669. RHOC.
HPAiHPA062346.
MIMi165380. gene.
neXtProtiNX_P08134.
PharmGKBiPA24951.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119020.
HOGENOMiHOG000233974.
HOVERGENiHBG009351.
InParanoidiP08134.
KOiK07857.
OMAiNILEKWH.
OrthoDBiEOG73FQPD.
PhylomeDBiP08134.
TreeFamiTF300837.

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.
REACT_355021. RHO GTPases Activate Rhotekin and Rhophilins.
REACT_355192. RHO GTPases Activate ROCKs.
REACT_355252. RHO GTPases Activate Formins.
REACT_355303. RHO GTPases activate CIT.
REACT_355542. RHO GTPases activate PKNs.
SignaLinkiP08134.

Miscellaneous databases

ChiTaRSiRHOC. human.
EvolutionaryTraceiP08134.
GeneWikiiRhoC.
GenomeRNAii389.
NextBioi1619.
PROiP08134.
SOURCEiSearch...

Gene expression databases

BgeeiP08134.
CleanExiHS_RHOC.
ExpressionAtlasiP08134. baseline and differential.
GenevestigatoriP08134.

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. "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: May 27, 2015
This is version 175 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

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.