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Rho-related GTP-binding protein RhoC (Rho cDNA clone 9) (h9)

 RHOC_HUMAN              Reviewed;         193 AA.
P08134; B3KSW1; Q6ICN3;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
25-OCT-2017, entry version 199.
RecName: Full=Rho-related GTP-binding protein RhoC;
AltName: Full=Rho cDNA clone 9;
Short=h9;
Flags: Precursor;
Name=RHOC; Synonyms=ARH9, ARHC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3283705; DOI=10.1093/nar/16.6.2717;
Chardin P., Madaule P., Tavitian A.;
"Coding sequence of human rho cDNAs clone 6 and clone 9.";
Nucleic Acids Res. 16:2717-2717(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Retina;
Fagan K.P., Oliveira L., Pittler S.J.;
Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
"cDNA clones of human proteins involved in signal transduction
sequenced by the Guthrie cDNA resource center (www.cdna.org).";
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
INTERACTION WITH ROCK1 AND ROCK2.
PubMed=8816443; DOI=10.1128/MCB.16.10.5313;
Leung T., Chen X.-Q., Manser E., Lim L.;
"The p160 RhoA-binding kinase ROK alpha is a member of a kinase family
and is involved in the reorganization of the cytoskeleton.";
Mol. Cell. Biol. 16:5313-5327(1996).
[11]
INTERACTION WITH AKAP13.
PubMed=11546812; DOI=10.1074/jbc.M106629200;
Diviani D., Soderling J., Scott J.D.;
"AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective
Rho-mediated stress fiber formation.";
J. Biol. Chem. 276:44247-44257(2001).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16236794; DOI=10.1091/mbc.E05-06-0569;
Kamijo K., Ohara N., Abe M., Uchimura T., Hosoya H., Lee J.S.,
Miki T.;
"Dissecting the role of Rho-mediated signaling in contractile ring
formation.";
Mol. Biol. Cell 17:43-55(2006).
[13]
INTERACTION WITH ARHGDIA.
PubMed=20400958; DOI=10.1038/ncb2049;
Boulter E., Garcia-Mata R., Guilluy C., Dubash A., Rossi G.,
Brennwald P.J., Burridge K.;
"Regulation of Rho GTPase crosstalk, degradation and activity by
RhoGDI1.";
Nat. Cell Biol. 12:477-483(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
FUNCTION, AND INTERACTION WITH PKN2.
PubMed=20974804; DOI=10.1128/MCB.01001-10;
Wallace S.W., Magalhaes A., Hall A.;
"The Rho target PRK2 regulates apical junction formation in human
bronchial epithelial cells.";
Mol. Cell. Biol. 31:81-91(2011).
[16]
GLYCOSYLATION AT TYR-34 (MICROBIAL INFECTION).
PubMed=24141704; DOI=10.1038/nsmb.2688;
Jank T., Bogdanovic X., Wirth C., Haaf E., Spoerner M., Boehmer K.E.,
Steinemann M., Orth J.H., Kalbitzer H.R., Warscheid B., Hunte C.,
Aktories K.;
"A bacterial toxin catalyzing tyrosine glycosylation of Rho and
deamidation of Gq and Gi proteins.";
Nat. Struct. Mol. Biol. 20:1273-1280(2013).
[17]
INTERACTION WITH RIPOR1.
PubMed=27807006; DOI=10.1242/jcs.198614;
Mardakheh F.K., Self A., Marshall C.J.;
"RHO binding to FAM65A regulates Golgi reorientation during cell
migration.";
J. Cell Sci. 129:4466-4479(2016).
[18]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH DIAPH1.
PubMed=15864301; DOI=10.1038/nature03604;
Rose R., Weyand M., Lammers M., Ishizaki T., Ahmadian M.R.,
Wittinghofer A.;
"Structural and mechanistic insights into the interaction between Rho
and mammalian Dia.";
Nature 435:513-518(2005).
-!- 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. {ECO:0000269|PubMed:16236794,
ECO:0000269|PubMed:20974804}.
-!- SUBUNIT: Interacts with RTKN (By similarity). Interacts with
AKAP13 (PubMed:11546812). Interacts with DIAPH1 (PubMed:15864301).
Interacts with PKN2 (PubMed:20974804). Interacts with ROCK1 and
ROCK2 (PubMed:8816443). Interacts with ARHGDIA (PubMed:20400958).
Interacts with RIPOR1 (PubMed:27807006). {ECO:0000250,
ECO:0000250|UniProtKB:Q62159, ECO:0000269|PubMed:11546812,
ECO:0000269|PubMed:15864301, ECO:0000269|PubMed:20400958,
ECO:0000269|PubMed:20974804, ECO:0000269|PubMed:27807006,
ECO:0000269|PubMed:8816443}.
-!- INTERACTION:
Q9Y4F9:RIPOR2; NbExp=5; IntAct=EBI-747589, EBI-2798942;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cleavage furrow
{ECO:0000269|PubMed:16236794}. Note=Translocates to the equatorial
region before furrow formation in a ECT2-dependent manner.
-!- PTM: (Microbial infection) Glycosylated at Tyr-34 by Photorhabdus
asymbiotica toxin PAU_02230. Mono-O-GlcNAcylation by PAU_02230
inhibits downstream signaling by an impaired interaction with
diverse regulator and effector proteins of Rho and leads to actin
disassembly. {ECO:0000269|PubMed:24141704}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RHOCID42110ch1p13.html";
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EMBL; X06821; CAA29969.1; -; mRNA.
EMBL; L25081; AAC33179.1; -; mRNA.
EMBL; AF498972; AAM21119.1; -; mRNA.
EMBL; CR450360; CAG29356.1; -; mRNA.
EMBL; BT019448; AAV38255.1; -; mRNA.
EMBL; AK094474; BAG52873.1; -; mRNA.
EMBL; AL603832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471122; EAW56534.1; -; Genomic_DNA.
EMBL; BC007245; AAH07245.1; -; mRNA.
EMBL; BC009177; AAH09177.1; -; mRNA.
EMBL; BC052808; AAH52808.1; -; mRNA.
CCDS; CCDS854.1; -.
PIR; S01029; TVHURC.
RefSeq; NP_001036143.1; NM_001042678.1.
RefSeq; NP_001036144.1; NM_001042679.1.
RefSeq; NP_786886.1; NM_175744.4.
UniGene; Hs.502659; -.
UniGene; Hs.658289; -.
PDB; 1Z2C; X-ray; 3.00 A; A/C=1-193.
PDB; 2GCN; X-ray; 1.85 A; A=1-181.
PDB; 2GCO; X-ray; 1.40 A; A/B=1-181.
PDB; 2GCP; X-ray; 2.15 A; A=1-181.
PDBsum; 1Z2C; -.
PDBsum; 2GCN; -.
PDBsum; 2GCO; -.
PDBsum; 2GCP; -.
ProteinModelPortal; P08134; -.
SMR; P08134; -.
BioGrid; 106882; 31.
IntAct; P08134; 10.
MINT; MINT-1216716; -.
STRING; 9606.ENSP00000285735; -.
iPTMnet; P08134; -.
PhosphoSitePlus; P08134; -.
SwissPalm; P08134; -.
BioMuta; RHOC; -.
DMDM; 132543; -.
EPD; P08134; -.
MaxQB; P08134; -.
PaxDb; P08134; -.
PeptideAtlas; P08134; -.
PRIDE; P08134; -.
TopDownProteomics; P08134; -.
DNASU; 389; -.
Ensembl; ENST00000285735; ENSP00000285735; ENSG00000155366.
Ensembl; ENST00000339083; ENSP00000345236; ENSG00000155366.
Ensembl; ENST00000369632; ENSP00000358646; ENSG00000155366.
Ensembl; ENST00000369633; ENSP00000358647; ENSG00000155366.
Ensembl; ENST00000369637; ENSP00000358651; ENSG00000155366.
Ensembl; ENST00000369638; ENSP00000358652; ENSG00000155366.
Ensembl; ENST00000369642; ENSP00000358656; ENSG00000155366.
GeneID; 389; -.
KEGG; hsa:389; -.
UCSC; uc001ecp.1; human.
CTD; 389; -.
DisGeNET; 389; -.
EuPathDB; HostDB:ENSG00000155366.16; -.
GeneCards; RHOC; -.
HGNC; HGNC:669; RHOC.
MIM; 165380; gene.
neXtProt; NX_P08134; -.
OpenTargets; ENSG00000155366; -.
PharmGKB; PA24951; -.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00760000119020; -.
HOGENOM; HOG000233974; -.
HOVERGEN; HBG009351; -.
InParanoid; P08134; -.
KO; K07857; -.
OMA; WISEVVH; -.
PhylomeDB; P08134; -.
TreeFam; TF300837; -.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-5625900; RHO GTPases activate CIT.
Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
SignaLink; P08134; -.
SIGNOR; P08134; -.
ChiTaRS; RHOC; human.
EvolutionaryTrace; P08134; -.
GeneWiki; RhoC; -.
GenomeRNAi; 389; -.
PRO; PR:P08134; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000155366; -.
CleanEx; HS_RHOC; -.
ExpressionAtlas; P08134; baseline and differential.
Genevisible; P08134; HS.
GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0032420; C:stereocilium; ISS:UniProtKB.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IEA:InterPro.
GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
GO; GO:0043297; P:apical junction assembly; IDA:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0060193; P:positive regulation of lipase activity; IDA:AgBase.
GO; GO:0032464; P:positive regulation of protein homooligomerization; ISS:UniProtKB.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:1902766; P:skeletal muscle satellite cell migration; ISS:AgBase.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
GO; GO:0044319; P:wound healing, spreading of cells; ISS:AgBase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR003578; Small_GTPase_Rho.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51420; RHO; 1.
1: Evidence at protein level;
3D-structure; ADP-ribosylation; Cell membrane; Complete proteome;
Glycoprotein; GTP-binding; Lipoprotein; Membrane; Methylation;
Nucleotide-binding; Polymorphism; Prenylation; Reference proteome.
CHAIN 1 190 Rho-related GTP-binding protein RhoC.
/FTId=PRO_0000042022.
PROPEP 191 193 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000042023.
NP_BIND 12 19 GTP. {ECO:0000250}.
NP_BIND 59 63 GTP. {ECO:0000250}.
NP_BIND 117 120 GTP. {ECO:0000250}.
MOTIF 34 42 Effector region. {ECO:0000255}.
MOD_RES 41 41 ADP-ribosylasparagine; by botulinum
toxin. {ECO:0000250}.
MOD_RES 190 190 Cysteine methyl ester.
{ECO:0000250|UniProtKB:P62745}.
LIPID 190 190 S-geranylgeranyl cysteine.
{ECO:0000250|UniProtKB:P62745}.
CARBOHYD 34 34 O-linked (GlcNAc) tyrosine; by
Photorhabdus PAU_02230.
{ECO:0000269|PubMed:24141704}.
VARIANT 120 120 D -> H (in dbSNP:rs11538959).
/FTId=VAR_051974.
STRAND 4 13 {ECO:0000244|PDB:2GCO}.
HELIX 18 27 {ECO:0000244|PDB:2GCO}.
STRAND 43 48 {ECO:0000244|PDB:2GCO}.
STRAND 51 58 {ECO:0000244|PDB:2GCO}.
HELIX 64 66 {ECO:0000244|PDB:2GCO}.
TURN 67 69 {ECO:0000244|PDB:2GCO}.
HELIX 70 73 {ECO:0000244|PDB:2GCO}.
STRAND 78 85 {ECO:0000244|PDB:2GCO}.
HELIX 89 97 {ECO:0000244|PDB:2GCO}.
HELIX 99 106 {ECO:0000244|PDB:2GCO}.
STRAND 112 117 {ECO:0000244|PDB:2GCO}.
HELIX 119 121 {ECO:0000244|PDB:2GCO}.
HELIX 125 132 {ECO:0000244|PDB:2GCO}.
TURN 133 135 {ECO:0000244|PDB:2GCO}.
HELIX 141 150 {ECO:0000244|PDB:2GCO}.
STRAND 154 158 {ECO:0000244|PDB:2GCO}.
TURN 161 163 {ECO:0000244|PDB:2GCO}.
HELIX 167 179 {ECO:0000244|PDB:2GCO}.
SEQUENCE 193 AA; 22006 MW; A193DA581560F131 CRC64;
MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYIADIEVDG KQVELALWDT
AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD
LRQDEHTRRE LAKMKQEPVR SEEGRDMANR ISAFGYLECS AKTKEGVREV FEMATRAGLQ
VRKNKRRRGC PIL


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EIAAB34750 ARHC,Chicken,Gallus gallus,RHOC,Rho-related GTP-binding protein RhoC
EH1236 Rho-related GTP-binding protein RhoC Elisa Kit 96T
DC02112 Human RHOC cDNA Clone
DC02112 Human RHOC cDNA Clone, Vector pcDNA4_TO_myc-His A 10 ug
EIAAB34747 ARH6,ARHB,h6,Homo sapiens,Human,Rho cDNA clone 6,RHOB,Rho-related GTP-binding protein RhoB
A1062 RHOC Primary Antibody, RHOC, Species: Human Recombinant Protein Source: Rabbit Polyclonal 50ug
PR-198 RhoC Ras-like GTP-binding protein human, recombinant, E. coli 50
EIAAB29238 Homo sapiens,Human,KIAA1534,OBPH1,ORP5,ORP-5,OSBPL5,OSBP-related protein 5,Oxysterol-binding protein homolog 1;,Oxysterol-binding protein-related protein 5
18-003-43154 SWI_SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related - SMARCE1-related protein; HMG domain protein HMG20B; Structural DNA-binding protein BRAF35; BRCA2 0.05 mg Aff Pur


 

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