P08134 (RHOC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho-related GTP-binding protein RhoC

Alternative name(s):
Rho cDNA clone 9
Short name=h9

Gene names

Name:	RHOC
Synonyms:	ARH9, ARHC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	193 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.14
Subunit structure	Interacts with RTKN By similarity. Interacts with AKAP13, DIAPH1, PKN2, ROCK1 and ROCK2. Ref.10 Ref.11 Ref.14
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.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Ligand	GTP-binding Nucleotide-binding
PTM	ADP-ribosylation Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apical junction assembly Inferred from direct assay Ref.14. Source: UniProtKB axon guidance Traceable author statement. Source: Reactome cell cycle cytokinesis Inferred from direct assay Ref.12. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular_component	cleavage furrow Inferred from direct assay Ref.12. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: Compara plasma membrane Traceable author statement. Source: Reactome
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW signal transducer activity Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 190

190

Rho-related GTP-binding protein RhoC

PRO_0000042022

Propeptide

191 – 193

3

Removed in mature form By similarity

PRO_0000042023

Regions

Nucleotide binding

12 – 19

8

GTP By similarity

Nucleotide binding

59 – 63

5

GTP By similarity

Nucleotide binding

117 – 120

4

GTP By similarity

Motif

34 – 42

9

Effector region Potential

Amino acid modifications

Modified residue

19

1

Phosphothreonine By similarity

Modified residue

26

1

Phosphoserine By similarity

Modified residue

41

1

ADP-ribosylasparagine; by botulinum toxin By similarity

Modified residue

190

1

Cysteine methyl ester By similarity

Lipidation

190

1

S-geranylgeranyl cysteine By similarity

Natural variations

Natural variant

120

1

D → H.
Corresponds to variant rs11538959 [ dbSNP | Ensembl ].

VAR_051974

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

193

Helix Strand Turn

Details...

Beta strand

4 – 13

10

Helix

18 – 27

10

Beta strand

43 – 48

6

Beta strand

51 – 58

8

Helix

64 – 66

3

Turn

67 – 69

3

Helix

70 – 73

4

Beta strand

78 – 85

8

Helix

89 – 97

9

Helix

99 – 106

8

Beta strand

112 – 117

6

Helix

119 – 121

3

Helix

125 – 132

8

Turn

133 – 135

3

Helix

141 – 150

10

Beta strand

154 – 158

5

Turn

161 – 163

3

Helix

167 – 179

13

Sequences

	Sequence		Length	Mass (Da)
	P08134 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: A193DA581560F131	FASTA	193	22,006
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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]	"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].
[14]	"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.
[15]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00027434.

PIR

TVHURC. S01029.

RefSeq

NP_001036143.1. NM_001042678.1.
NP_001036144.1. NM_001042679.1.
NP_786886.1. NM_175744.4.

UniGene

Hs.502659.
Hs.658289.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P08134.

ModBase

Search...

Protein-protein interaction databases

IntAct

P08134. 7 interactions.

MINT

MINT-1216716.

STRING

9606.ENSP00000285735.

PTM databases

PhosphoSite

P08134.

Polymorphism databases

DMDM

132543.

Proteomic databases

PaxDb

P08134.

PRIDE

P08134.

Protocols and materials databases

DNASU

389.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000285735; ENSP00000285735; ENSG00000155366.
ENST00000339083; ENSP00000345236; ENSG00000155366.
ENST00000369632; ENSP00000358646; ENSG00000155366.
ENST00000369633; ENSP00000358647; ENSG00000155366.
ENST00000369637; ENSP00000358651; ENSG00000155366.
ENST00000369638; ENSP00000358652; ENSG00000155366.
ENST00000369642; ENSP00000358656; ENSG00000155366.

GeneID

389.

KEGG

hsa:389.

UCSC

uc001ecp.1. human.

Organism-specific databases

CTD

389.

GeneCards

GC01M113243.

HGNC

HGNC:669. RHOC.

HPA

CAB010821.

MIM

165380. gene.

neXtProt

NX_P08134.

PharmGKB

PA24951.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233974.

HOVERGEN

HBG009351.

KO

K07857.

OrthoDB

EOG4G4GRD.

PhylomeDB

P08134.

Enzyme and pathway databases

Pathway_Interaction_DB

p75ntrpathway. p75(NTR)-mediated signaling.
prlsignalingeventspathway. Signaling events mediated by PRL.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

P08134.

Bgee

P08134.

CleanEx

HS_RHOC.

Genevestigator

P08134.

GermOnline

ENSG00000155366. Homo sapiens.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003578. Small_GTPase_Rho.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00174. RHO. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51420. RHO. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P08134.

GenomeRNAi

389.

NextBio

1619.

SOURCE

Search...

Entry information

Entry name

RHOC_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 153 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.