Reviewed, UniProtKB/Swiss-Prot P08134 (RHOC_HUMAN)

Names and origin

Protein names

Recommended name:
    Rho-related GTP-binding protein RhoC
Alternative name(s):
    H9

Gene names

Name:	RHOC
Synonyms:	ARH9, ARHC

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
Subunit structure	Interacts with DIAPH1, ROCK1, ROCK2 and RTKN. Interacts with AKAP13. Ref.8 Ref.9
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential.
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
Gene Ontology (GO)
Biological process	positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from mutant phenotype. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct signal transducer activity Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARHGDIA	P52565	1	EBI-747589,EBI-712693
CNKSR1	Q969H4	1	EBI-747589,EBI-741671
VHL	P40337	1	EBI-747589,EBI-301246

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: dbSNP rs11538959.

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)
	P08134-1 [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: 3283705] [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]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[8]	"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: 8816443] [Abstract] Cited for: INTERACTION WITH ROCK1 AND ROCK2.
[9]	"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: 11546812] [Abstract] Cited for: INTERACTION WITH AKAP13.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"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: 15864301] [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

EMBLGenBankDDBJ

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.
AL603832 Genomic DNA. Translation: CAI14058.1.
BC007245 mRNA. Translation: AAH07245.1.
BC009177 mRNA. Translation: AAH09177.1.
BC052808 mRNA. Translation: AAH52808.1.

IPI

IPI00027434.

PIR

TVHURC. S01029.

RefSeq

NP_001036143.1.
NP_001036144.1.
NP_786886.1.

UniGene

Hs.502659
Hs.658289

3D structure databases

PDBPDBe

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	1-181	[»]
			B	1-181	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P08134. 10 interactions.

PTM databases

PhosphoSite

P08134.

Proteomic databases

PRIDE

P08134.

Genome annotation databases

Ensembl

ENSG00000155366. Homo sapiens. [Contig view]

GeneID

389.

KEGG

hsa:389.

Organism-specific databases

GeneCards

GC01M112955.

H-InvDB

HIX0000895.

HGNC

HGNC:669. RHOC.

HPA

CAB010821.

MIM

165380. gene.

PharmGKB

PA24951.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P08134.

OMA

P08134. LRNDEST.

Enzyme and pathway databases

Pathway_Interaction_DB

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

Reactome

REACT_11044. Signaling by Rho GTPases.

Gene expression databases

Bgee

P08134.

CleanEx

HS_RHOC.

GermOnline

ENSG00000155366. Homo sapiens.

Family and domain databases

InterPro

IPR003578. GTPase_Rho.
IPR013753. Ras.
IPR001806. Ras_GTPase.
IPR005225. Small_GTP_bd.
[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 Resources

NextBio

1619.

SOURCE

Search...

Entry information

Entry name

RHOC_HUMAN

Accession

Primary (citable) accession number: P08134
Secondary accession number(s): Q6ICN3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	June 16, 2009
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)