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Rho-associated protein kinase 1 (EC 2.7.11.1) (Renal carcinoma antigen NY-REN-35) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p160 ROCK-1) (p160ROCK)

 ROCK1_HUMAN             Reviewed;        1354 AA.
Q13464; B0YJ91; Q2KHM4; Q59GZ4;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-OCT-2018, entry version 195.
RecName: Full=Rho-associated protein kinase 1;
EC=2.7.11.1;
AltName: Full=Renal carcinoma antigen NY-REN-35;
AltName: Full=Rho-associated, coiled-coil-containing protein kinase 1;
AltName: Full=Rho-associated, coiled-coil-containing protein kinase I;
Short=ROCK-I;
AltName: Full=p160 ROCK-1;
Short=p160ROCK;
Name=ROCK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 187-195; 281-288;
465-473; 818-828; 885-893 AND 934-945, FUNCTION, PHOSPHORYLATION,
INTERACTION WITH RHOA, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Leukemia;
PubMed=8617235;
Ishizaki T., Maekawa M., Fujisawa K., Okawa K., Iwamatsu A.,
Fujita A., Watanabe N., Saito Y., Kakizuka A., Morii N., Narumiya S.;
"The small GTP-binding protein Rho binds to and activates a 160 kDa
Ser/Thr protein kinase homologous to myotonic dystrophy kinase.";
EMBO J. 15:1885-1893(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[4]
PROTEIN SEQUENCE OF 2-13; 85-94; 327-334; 405-415 AND 546-563,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Embryonic kidney;
Bienvenut W.V., Ramsay A., Leung H.Y.;
Submitted (MAR-2009) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 323-1027.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
ROLE IN SMOOTH MUSCLE CONTRACTION.
PubMed=9722579; DOI=10.1074/jbc.273.36.23433;
Van Eyk J.E., Arrell D.K., Foster D.B., Strauss J.D., Heinonen T.Y.,
Furmaniak-Kazmierczak E., Cote G.P., Mak A.S.;
"Different molecular mechanisms for Rho family GTPase-dependent, Ca2+-
independent contraction of smooth muscle.";
J. Biol. Chem. 273:23433-23439(1998).
[7]
IDENTIFICATION AS A RENAL CANCER ANTIGEN.
TISSUE=Renal cell carcinoma;
PubMed=10508479;
DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5;
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
Old L.J.;
"Antigens recognized by autologous antibody in patients with renal-
cell carcinoma.";
Int. J. Cancer 83:456-464(1999).
[8]
FUNCTION, INTERACTION WITH LIMK1 AND LIMK2, AND INHIBITION BY Y-27632.
PubMed=10436159; DOI=10.1126/science.285.5429.895;
Maekawa M., Ishizaki T., Boku S., Watanabe N., Fujita A., Iwamatsu A.,
Obinata T., Ohashi K., Mizuno K., Narumiya S.;
"Signaling from Rho to the actin cytoskeleton through protein kinases
ROCK and LIM-kinase.";
Science 285:895-898(1999).
[9]
FUNCTION, AND INTERACTION WITH LIMK1.
PubMed=10652353; DOI=10.1074/jbc.275.5.3577;
Ohashi K., Nagata K., Maekawa M., Ishizaki T., Narumiya S., Mizuno K.;
"Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation
at threonine 508 within the activation loop.";
J. Biol. Chem. 275:3577-3582(2000).
[10]
FUNCTION, AND INTERACTION WITH LIMK2.
PubMed=11018042; DOI=10.1074/jbc.M007074200;
Sumi T., Matsumoto K., Nakamura T.;
"Specific activation of LIM kinase 2 via phosphorylation of threonine
505 by ROCK, a Rho-dependent protein kinase.";
J. Biol. Chem. 276:670-676(2001).
[11]
CLEAVAGE BY CASPASE-3, MUTAGENESIS OF ASP-1113, INTERACTION WITH
PPP1R12A, AND FUNCTION.
PubMed=11283607; DOI=10.1038/35070019;
Sebbagh M., Renvoize C., Hamelin J., Riche N., Bertoglio J.,
Breard J.;
"Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and
apoptotic membrane blebbing.";
Nat. Cell Biol. 3:346-352(2001).
[12]
INTERACTION WITH GEM.
PubMed=11956230; DOI=10.1083/jcb.200111026;
Ward Y., Yap S.-F., Ravichandran V., Matsumura F., Ito M.,
Spinelli B., Kelly K.;
"The GTP binding proteins Gem and Rad are negative regulators of the
Rho-Rho kinase pathway.";
J. Cell Biol. 157:291-302(2002).
[13]
INTERACTION WITH RHOE AND PPP1R12A, AND SUBCELLULAR LOCATION.
PubMed=12773565; DOI=10.1128/MCB.23.12.4219-4229.2003;
Riento K., Guasch R.M., Garg R., Jin B., Ridley A.J.;
"RhoE binds to ROCK I and inhibits downstream signaling.";
Mol. Cell. Biol. 23:4219-4229(2003).
[14]
REVIEW.
PubMed=12778124; DOI=10.1038/nrm1128;
Riento K., Ridley A.J.;
"Rocks: multifunctional kinases in cell behaviour.";
Nat. Rev. Mol. Cell Biol. 4:446-456(2003).
[15]
INTERACTION WITH TSG101.
PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P.,
Rodesch C.K., Sundquist W.I.;
"Human ESCRT and ALIX proteins interact with proteins of the midbody
and function in cytokinesis.";
EMBO J. 26:4215-4227(2007).
[16]
FUNCTION, AND INTERACTION WITH DAPK3.
PubMed=17158456; DOI=10.1074/jbc.M609990200;
Hagerty L., Weitzel D.H., Chambers J., Fortner C.N., Brush M.H.,
Loiselle D., Hosoya H., Haystead T.A.;
"ROCK1 phosphorylates and activates zipper-interacting protein
kinase.";
J. Biol. Chem. 282:4884-4893(2007).
[17]
FUNCTION, INTERACTION WITH FHOD1, AND SUBCELLULAR LOCATION.
PubMed=18694941; DOI=10.1074/jbc.M801800200;
Hannemann S., Madrid R., Stastna J., Kitzing T., Gasteier J.,
Schoenichen A., Bouchet J., Jimenez A., Geyer M., Grosse R.,
Benichou S., Fackler O.T.;
"The diaphanous-related formin FHOD1 associates with ROCK1 and
promotes Src-dependent plasma membrane blebbing.";
J. Biol. Chem. 283:27891-27903(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1105, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[19]
FUNCTION, AND INTERACTION WITH PFN1.
PubMed=18573880; DOI=10.1128/MCB.00079-08;
Shao J., Welch W.J., Diprospero N.A., Diamond M.I.;
"Phosphorylation of profilin by ROCK1 regulates polyglutamine
aggregation.";
Mol. Cell. Biol. 28:5196-5208(2008).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
FUNCTION, AND INTERACTION WITH JIP3.
PubMed=19036714; DOI=10.1126/scisignal.1161938;
Ongusaha P.P., Qi H.H., Raj L., Kim Y.B., Aaronson S.A., Davis R.J.,
Shi Y., Liao J.K., Lee S.W.;
"Identification of ROCK1 as an upstream activator of the JIP-3 to JNK
signaling axis in response to UVB damage.";
Sci. Signal. 1:RA14-RA14(2008).
[22]
FUNCTION.
PubMed=19181962; DOI=10.1152/ajpheart.01038.2008;
Kroll J., Epting D., Kern K., Dietz C.T., Feng Y., Hammes H.P.,
Wieland T., Augustin H.G.;
"Inhibition of Rho-dependent kinases ROCK I/II activates VEGF-driven
retinal neovascularization and sprouting angiogenesis.";
Am. J. Physiol. 296:H893-H899(2009).
[23]
FUNCTION, AND INTERACTION WITH PPP1R12A.
PubMed=19131646; DOI=10.1161/CIRCRESAHA.108.188524;
Wang Y., Zheng X.R., Riddick N., Bryden M., Baur W., Zhang X.,
Surks H.K.;
"ROCK isoform regulation of myosin phosphatase and contractility in
vascular smooth muscle cells.";
Circ. Res. 104:531-540(2009).
[24]
FUNCTION.
PubMed=19997641; DOI=10.1371/journal.pone.0008190;
Lock F.E., Hotchin N.A.;
"Distinct roles for ROCK1 and ROCK2 in the regulation of keratinocyte
differentiation.";
PLoS ONE 4:E8190-E8190(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1105, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-647, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[27]
INTERACTION WITH CHORDC1.
PubMed=20230755; DOI=10.1016/j.devcel.2009.12.020;
Ferretti R., Palumbo V., Di Savino A., Velasco S., Sbroggio M.,
Sportoletti P., Micale L., Turco E., Silengo L., Palumbo G.,
Hirsch E., Teruya-Feldstein J., Bonaccorsi S., Pandolfi P.P.,
Gatti M., Tarone G., Brancaccio M.;
"Morgana/chp-1, a ROCK inhibitor involved in centrosome duplication
and tumorigenesis.";
Dev. Cell 18:486-495(2010).
[28]
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).
[29]
FUNCTION, AND CLEAVAGE BY CASPASE-3.
PubMed=21072057; DOI=10.1038/cdd.2010.140;
Gabet A.S., Coulon S., Fricot A., Vandekerckhove J., Chang Y.,
Ribeil J.A., Lordier L., Zermati Y., Asnafi V., Belaid Z., Debili N.,
Vainchenker W., Varet B., Hermine O., Courtois G.;
"Caspase-activated ROCK-1 allows erythroblast terminal maturation
independently of cytokine-induced Rho signaling.";
Cell Death Differ. 18:678-689(2011).
[30]
REVIEW.
PubMed=20803696; DOI=10.1002/cm.20472;
Amano M., Nakayama M., Kaibuchi K.;
"Rho-kinase/ROCK: A key regulator of the cytoskeleton and cell
polarity.";
Cytoskeleton 67:545-554(2010).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1328, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 947-1015 IN COMPLEX WITH
RHOA.
PubMed=14660612; DOI=10.1074/jbc.M311911200;
Dvorsky R., Blumenstein L., Vetter I.R., Ahmadian M.R.;
"Structural insights into the interaction of ROCKI with the switch
regions of RhoA.";
J. Biol. Chem. 279:7098-7104(2004).
[36]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 6-415, AND SUBUNIT.
PubMed=16249185; DOI=10.1074/jbc.M508847200;
Jacobs M., Hayakawa K., Swenson L., Bellon S., Fleming M., Taslimi P.,
Doran J.;
"The structure of dimeric ROCK I reveals the mechanism for ligand
selectivity.";
J. Biol. Chem. 281:260-268(2006).
[37]
VARIANTS [LARGE SCALE ANALYSIS] ASN-108; SER-773; PRO-1112; SER-1193;
GLU-1217; GLN-1262 AND ARG-1264.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Protein kinase which is a key regulator of actin
cytoskeleton and cell polarity. Involved in regulation of smooth
muscle contraction, actin cytoskeleton organization, stress fiber
and focal adhesion formation, neurite retraction, cell adhesion
and motility via phosphorylation of DAPK3, GFAP, LIMK1, LIMK2,
MYL9/MLC2, PFN1 and PPP1R12A. Phosphorylates FHOD1 and acts
synergistically with it to promote SRC-dependent non-apoptotic
plasma membrane blebbing. Phosphorylates JIP3 and regulates the
recruitment of JNK to JIP3 upon UVB-induced stress. Acts as a
suppressor of inflammatory cell migration by regulating PTEN
phosphorylation and stability. Acts as a negative regulator of
VEGF-induced angiogenic endothelial cell activation. Required for
centrosome positioning and centrosome-dependent exit from mitosis.
Plays a role in terminal erythroid differentiation. May regulate
closure of the eyelids and ventral body wall by inducing the
assembly of actomyosin bundles. Promotes keratinocyte terminal
differentiation. Involved in osteoblast compaction through the
fibronectin fibrillogenesis cell-mediated matrix assembly process,
essential for osteoblast mineralization.
{ECO:0000269|PubMed:10436159, ECO:0000269|PubMed:10652353,
ECO:0000269|PubMed:11018042, ECO:0000269|PubMed:11283607,
ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18573880,
ECO:0000269|PubMed:18694941, ECO:0000269|PubMed:19036714,
ECO:0000269|PubMed:19131646, ECO:0000269|PubMed:19181962,
ECO:0000269|PubMed:19997641, ECO:0000269|PubMed:21072057,
ECO:0000269|PubMed:8617235, ECO:0000269|PubMed:9722579}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y-
27632.
-!- SUBUNIT: Homodimer. Interacts with RHOB, RHOC, MYLC2B and PTEN.
Interacts with ITGB1BP1 (via N-terminus and PTB domain) (By
similarity). Interacts with RHOA (activated by GTP), CHORDC1,
DAPK3, GEM, JIP3, RHOE, PPP1R12A, PFN1, LIMK1, LIMK2 and TSG101.
Interacts with FHOD1 in a Src-dependent manner. {ECO:0000250,
ECO:0000269|PubMed:10436159, ECO:0000269|PubMed:10652353,
ECO:0000269|PubMed:11018042, ECO:0000269|PubMed:11283607,
ECO:0000269|PubMed:11956230, ECO:0000269|PubMed:12773565,
ECO:0000269|PubMed:14660612, ECO:0000269|PubMed:16249185,
ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:17853893,
ECO:0000269|PubMed:18573880, ECO:0000269|PubMed:18694941,
ECO:0000269|PubMed:19036714, ECO:0000269|PubMed:19131646,
ECO:0000269|PubMed:20230755, ECO:0000269|PubMed:8617235}.
-!- INTERACTION:
Q8IYR0:CFAP206; NbExp=3; IntAct=EBI-876651, EBI-749051;
Q86V42:FAM124A; NbExp=3; IntAct=EBI-876651, EBI-744506;
Q7Z6J6:FRMD5; NbExp=4; IntAct=EBI-876651, EBI-727282;
P25791:LMO2; NbExp=3; IntAct=EBI-876651, EBI-739696;
O15481:MAGEB4; NbExp=3; IntAct=EBI-876651, EBI-751857;
Q13203:MYBPH; NbExp=2; IntAct=EBI-876651, EBI-5655165;
Q9BUI4:POLR3C; NbExp=3; IntAct=EBI-876651, EBI-5452779;
P61586:RHOA; NbExp=4; IntAct=EBI-876651, EBI-446668;
Q99816:TSG101; NbExp=4; IntAct=EBI-876651, EBI-346882;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome, centriole
{ECO:0000250}. Golgi apparatus membrane; Peripheral membrane
protein. Cell projection, bleb. Cytoplasm, cytoskeleton
{ECO:0000250}. Cell membrane {ECO:0000250}. Cell projection,
lamellipodium {ECO:0000250}. Cell projection, ruffle
{ECO:0000250}. Note=Associated with the mother centriole and an
intercentriolar linker. Colocalizes with ITGB1BP1 and ITGB1 at the
cell membrane predominantly in lamellipodia and membrane ruffles,
but also in retraction fibers. Localizes at the cell membrane in
an ITGB1BP1-dependent manner (By similarity). A small proportion
is associated with Golgi membranes. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in blood platelets.
{ECO:0000269|PubMed:8617235}.
-!- DOMAIN: The C-terminal auto-inhibitory domain interferes with
kinase activity. RHOA binding leads to a conformation change and
activation of the kinase. Truncated ROCK1 is constitutively
activated.
-!- PTM: Autophosphorylated on serine and threonine residues.
{ECO:0000269|PubMed:8617235}.
-!- PTM: Cleaved by caspase-3 during apoptosis. This leads to
constitutive activation of the kinase and membrane blebbing.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. {ECO:0000305}.
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EMBL; U43195; AAB02814.1; -; mRNA.
EMBL; EF445027; ACA06069.1; -; Genomic_DNA.
EMBL; BC113114; AAI13115.1; -; mRNA.
EMBL; AB208965; BAD92202.1; -; mRNA.
CCDS; CCDS11870.2; -.
PIR; S69211; S69211.
RefSeq; NP_005397.1; NM_005406.2.
UniGene; Hs.306307; -.
PDB; 1S1C; X-ray; 2.60 A; X/Y=947-1015.
PDB; 2ESM; X-ray; 3.20 A; A/B=6-415.
PDB; 2ETK; X-ray; 2.96 A; A/B=6-415.
PDB; 2ETR; X-ray; 2.60 A; A/B=6-415.
PDB; 2V55; X-ray; 3.70 A; A/C=1-406.
PDB; 3D9V; X-ray; 3.30 A; A/B=6-415.
PDB; 3NCZ; X-ray; 3.00 A; A/B/C/D=6-415.
PDB; 3NDM; X-ray; 3.30 A; A/B/C/D=6-415.
PDB; 3O0Z; X-ray; 2.33 A; A/B/C/D=535-700.
PDB; 3TV7; X-ray; 2.75 A; A/B/C/D=6-415.
PDB; 3TWJ; X-ray; 2.90 A; A/B/C/D=6-415.
PDB; 3V8S; X-ray; 2.29 A; A/B/C/D=6-415.
PDB; 4L2W; X-ray; 2.49 A; A/B/C/D=834-914.
PDB; 4W7P; X-ray; 2.80 A; A/B/C/D=2-410.
PDB; 4YVC; X-ray; 3.20 A; A/B=6-415.
PDB; 4YVE; X-ray; 3.40 A; A/B=6-415.
PDB; 5BML; X-ray; 2.95 A; A/B=6-415.
PDB; 5F5P; X-ray; 3.57 A; C/D/E/F=834-913.
PDB; 5HVU; X-ray; 2.80 A; A/B=6-415.
PDB; 5KKS; X-ray; 3.30 A; A/B=6-415.
PDB; 5KKT; X-ray; 2.80 A; A/B=6-415.
PDB; 5UZJ; X-ray; 3.30 A; A/B=6-415.
PDB; 5WNE; X-ray; 2.60 A; A/B/C/D=6-415.
PDB; 5WNF; X-ray; 2.45 A; A/B/C/D=6-415.
PDB; 5WNG; X-ray; 2.90 A; A/B/C/D=6-415.
PDB; 5WNH; X-ray; 3.10 A; A/B/C/D=6-415.
PDBsum; 1S1C; -.
PDBsum; 2ESM; -.
PDBsum; 2ETK; -.
PDBsum; 2ETR; -.
PDBsum; 2V55; -.
PDBsum; 3D9V; -.
PDBsum; 3NCZ; -.
PDBsum; 3NDM; -.
PDBsum; 3O0Z; -.
PDBsum; 3TV7; -.
PDBsum; 3TWJ; -.
PDBsum; 3V8S; -.
PDBsum; 4L2W; -.
PDBsum; 4W7P; -.
PDBsum; 4YVC; -.
PDBsum; 4YVE; -.
PDBsum; 5BML; -.
PDBsum; 5F5P; -.
PDBsum; 5HVU; -.
PDBsum; 5KKS; -.
PDBsum; 5KKT; -.
PDBsum; 5UZJ; -.
PDBsum; 5WNE; -.
PDBsum; 5WNF; -.
PDBsum; 5WNG; -.
PDBsum; 5WNH; -.
ProteinModelPortal; Q13464; -.
SMR; Q13464; -.
BioGrid; 112020; 46.
DIP; DIP-35645N; -.
ELM; Q13464; -.
IntAct; Q13464; 24.
MINT; Q13464; -.
STRING; 9606.ENSP00000382697; -.
BindingDB; Q13464; -.
ChEMBL; CHEMBL3231; -.
DrugBank; DB08756; (R)-TRANS-4-(1-AMINOETHYL)-N-(4-PYRIDYL) CYCLOHEXANECARBOXAMIDE.
DrugBank; DB07876; (S)-2-METHYL-1-[(4-METHYL-5-ISOQUINOLINE)SULFONYL]-HOMOPIPERAZINE.
DrugBank; DB04707; HYDROXYFASUDIL.
GuidetoPHARMACOLOGY; 1503; -.
iPTMnet; Q13464; -.
PhosphoSitePlus; Q13464; -.
SwissPalm; Q13464; -.
BioMuta; ROCK1; -.
DMDM; 47605999; -.
EPD; Q13464; -.
MaxQB; Q13464; -.
PaxDb; Q13464; -.
PeptideAtlas; Q13464; -.
PRIDE; Q13464; -.
ProteomicsDB; 59461; -.
Ensembl; ENST00000399799; ENSP00000382697; ENSG00000067900.
GeneID; 6093; -.
KEGG; hsa:6093; -.
UCSC; uc002kte.4; human.
CTD; 6093; -.
DisGeNET; 6093; -.
EuPathDB; HostDB:ENSG00000067900.7; -.
GeneCards; ROCK1; -.
HGNC; HGNC:10251; ROCK1.
HPA; CAB004562; -.
HPA; HPA007567; -.
HPA; HPA045639; -.
MIM; 601702; gene.
neXtProt; NX_Q13464; -.
OpenTargets; ENSG00000067900; -.
PharmGKB; PA34623; -.
eggNOG; KOG0612; Eukaryota.
eggNOG; ENOG410XR1Q; LUCA.
GeneTree; ENSGT00760000118994; -.
HOGENOM; HOG000017259; -.
HOVERGEN; HBG053111; -.
InParanoid; Q13464; -.
KO; K04514; -.
OMA; SMLDVDL; -.
OrthoDB; EOG091G0BOR; -.
PhylomeDB; Q13464; -.
TreeFam; TF313551; -.
Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
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-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; Q13464; -.
SignaLink; Q13464; -.
SIGNOR; Q13464; -.
ChiTaRS; ROCK1; human.
EvolutionaryTrace; Q13464; -.
GeneWiki; ROCK1; -.
GenomeRNAi; 6093; -.
PRO; PR:Q13464; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000067900; Expressed in 100 organ(s), highest expression level in popliteal artery.
CleanEx; HS_ROCK1; -.
ExpressionAtlas; Q13464; baseline and differential.
Genevisible; Q13464; HS.
GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0010494; C:cytoplasmic stress granule; ISS:ARUK-UCL.
GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0001726; C:ruffle; ISS:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0017049; F:GTP-Rho binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
GO; GO:0003383; P:apical constriction; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0032060; P:bleb assembly; IEA:Ensembl.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0007159; P:leukocyte cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0050900; P:leukocyte migration; IDA:BHF-UCL.
GO; GO:0050901; P:leukocyte tethering or rolling; IDA:BHF-UCL.
GO; GO:0022614; P:membrane to membrane docking; IDA:BHF-UCL.
GO; GO:0051451; P:myoblast migration; ISS:UniProtKB.
GO; GO:1902992; P:negative regulation of amyloid precursor protein catabolic process; IMP:ARUK-UCL.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; IMP:ARUK-UCL.
GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; IGI:UniProtKB.
GO; GO:0070168; P:negative regulation of biomineral tissue development; ISS:BHF-UCL.
GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; TAS:ARUK-UCL.
GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; IMP:UniProtKB.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO; GO:0140058; P:neuron projection arborization; IGI:ARUK-UCL.
GO; GO:0031175; P:neuron projection development; IGI:ARUK-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:1900223; P:positive regulation of amyloid-beta clearance; IGI:ARUK-UCL.
GO; GO:0010508; P:positive regulation of autophagy; IGI:ARUK-UCL.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:ARUK-UCL.
GO; GO:1905205; P:positive regulation of connective tissue replacement; IMP:ARUK-UCL.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:ARUK-UCL.
GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:1902003; P:regulation of amyloid-beta formation; TAS:ARUK-UCL.
GO; GO:0110061; P:regulation of angiotensin-activated signaling pathway; IMP:ARUK-UCL.
GO; GO:0010506; P:regulation of autophagy; TAS:ARUK-UCL.
GO; GO:0030155; P:regulation of cell adhesion; TAS:UniProtKB.
GO; GO:2000145; P:regulation of cell motility; TAS:UniProtKB.
GO; GO:2000114; P:regulation of establishment of cell polarity; TAS:UniProtKB.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; IMP:UniProtKB.
GO; GO:0051893; P:regulation of focal adhesion assembly; TAS:UniProtKB.
GO; GO:0045616; P:regulation of keratinocyte differentiation; IMP:UniProtKB.
GO; GO:0045664; P:regulation of neuron differentiation; IGI:ARUK-UCL.
GO; GO:0051492; P:regulation of stress fiber assembly; TAS:UniProtKB.
GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IGI:ARUK-UCL.
GO; GO:1990776; P:response to angiotensin; ISS:ARUK-UCL.
GO; GO:0071559; P:response to transforming growth factor beta; ISS:ARUK-UCL.
GO; GO:0007266; P:Rho protein signal transduction; IGI:ARUK-UCL.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0006939; P:smooth muscle contraction; TAS:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
CDD; cd00029; C1; 1.
CDD; cd11639; HR1_ROCK1; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR015008; Rho-bd_dom.
InterPro; IPR029876; ROCK1.
InterPro; IPR020684; ROCK1/ROCK2.
InterPro; IPR037310; ROCK1_HR1.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR22988:SF33; PTHR22988:SF33; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF08912; Rho_Binding; 1.
PIRSF; PIRSF037568; Rho_kinase; 1.
SMART; SM00109; C1; 1.
SMART; SM00233; PH; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS51860; REM_1; 1.
PROSITE; PS51859; RHO_BD; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Apoptosis; ATP-binding; Cell membrane;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Golgi apparatus; Kinase;
Magnesium; Membrane; Metal-binding; Nucleotide-binding;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.4}.
CHAIN 2 1354 Rho-associated protein kinase 1.
/FTId=PRO_0000086619.
DOMAIN 76 338 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 341 409 AGC-kinase C-terminal.
DOMAIN 479 556 REM-1. {ECO:0000255|PROSITE-
ProRule:PRU01207}.
DOMAIN 949 1015 RhoBD. {ECO:0000255|PROSITE-
ProRule:PRU01206}.
DOMAIN 1118 1317 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
NP_BIND 82 90 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 1228 1281 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
REGION 368 727 Interaction with FHOD1.
{ECO:0000269|PubMed:18694941}.
REGION 998 1010 RHOA binding.
REGION 1115 1354 Auto-inhibitory.
COILED 422 692 {ECO:0000255}.
COILED 1011 1102 {ECO:0000255}.
COMPBIAS 636 980 Glu-rich.
ACT_SITE 198 198 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 105 105 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 1113 1114 Cleavage; by caspase-3.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.4}.
MOD_RES 647 647 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 1105 1105 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332}.
MOD_RES 1108 1108 Phosphoserine.
{ECO:0000250|UniProtKB:P70335}.
MOD_RES 1328 1328 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 108 108 S -> N (in dbSNP:rs55811609).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041055.
VARIANT 773 773 T -> S (in dbSNP:rs45562542).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041056.
VARIANT 1112 1112 T -> P (in dbSNP:rs35881519).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041057.
VARIANT 1193 1193 P -> S (in a lung neuroendocrine
carcinoma sample; somatic mutation;
dbSNP:rs1057520015).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041058.
VARIANT 1217 1217 Q -> E (in dbSNP:rs2847092).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041059.
VARIANT 1262 1262 R -> Q (in dbSNP:rs1045142).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041060.
VARIANT 1264 1264 C -> R (in dbSNP:rs2663698).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041061.
MUTAGEN 1113 1113 D->A: Abolishes cleavage by caspase-3.
{ECO:0000269|PubMed:11283607}.
CONFLICT 170 170 V -> A (in Ref. 3; AAI13115).
{ECO:0000305}.
CONFLICT 197 197 R -> G (in Ref. 3; AAI13115).
{ECO:0000305}.
CONFLICT 220 220 C -> R (in Ref. 3; AAI13115).
{ECO:0000305}.
CONFLICT 323 325 RLG -> GTR (in Ref. 5; BAD92202).
{ECO:0000305}.
CONFLICT 521 521 D -> N (in Ref. 3; AAI13115).
{ECO:0000305}.
CONFLICT 965 965 K -> R (in Ref. 3; AAI13115).
{ECO:0000305}.
CONFLICT 1354 1354 S -> R (in Ref. 2; ACA06069).
{ECO:0000305}.
HELIX 9 19 {ECO:0000244|PDB:3V8S}.
HELIX 27 41 {ECO:0000244|PDB:3V8S}.
HELIX 44 47 {ECO:0000244|PDB:3V8S}.
HELIX 50 69 {ECO:0000244|PDB:3V8S}.
HELIX 73 75 {ECO:0000244|PDB:3V8S}.
STRAND 76 84 {ECO:0000244|PDB:3V8S}.
STRAND 86 95 {ECO:0000244|PDB:3V8S}.
TURN 96 98 {ECO:0000244|PDB:3V8S}.
STRAND 101 108 {ECO:0000244|PDB:3V8S}.
HELIX 109 114 {ECO:0000244|PDB:3V8S}.
HELIX 121 130 {ECO:0000244|PDB:3V8S}.
STRAND 139 144 {ECO:0000244|PDB:3V8S}.
STRAND 146 153 {ECO:0000244|PDB:3V8S}.
STRAND 157 160 {ECO:0000244|PDB:3NDM}.
HELIX 161 167 {ECO:0000244|PDB:3V8S}.
HELIX 172 191 {ECO:0000244|PDB:3V8S}.
HELIX 201 203 {ECO:0000244|PDB:3V8S}.
STRAND 204 206 {ECO:0000244|PDB:3V8S}.
STRAND 212 214 {ECO:0000244|PDB:3V8S}.
HELIX 217 219 {ECO:0000244|PDB:5KKS}.
STRAND 227 230 {ECO:0000244|PDB:3V8S}.
HELIX 238 240 {ECO:0000244|PDB:3V8S}.
HELIX 243 247 {ECO:0000244|PDB:3V8S}.
TURN 248 252 {ECO:0000244|PDB:3V8S}.
STRAND 254 256 {ECO:0000244|PDB:3V8S}.
HELIX 258 273 {ECO:0000244|PDB:3V8S}.
HELIX 283 291 {ECO:0000244|PDB:3V8S}.
HELIX 293 296 {ECO:0000244|PDB:3V8S}.
HELIX 307 316 {ECO:0000244|PDB:3V8S}.
HELIX 320 322 {ECO:0000244|PDB:3V8S}.
TURN 324 327 {ECO:0000244|PDB:2ETR}.
HELIX 329 333 {ECO:0000244|PDB:3V8S}.
HELIX 336 338 {ECO:0000244|PDB:3V8S}.
TURN 345 347 {ECO:0000244|PDB:3TV7}.
HELIX 348 350 {ECO:0000244|PDB:3V8S}.
HELIX 365 367 {ECO:0000244|PDB:3NCZ}.
HELIX 392 394 {ECO:0000244|PDB:3V8S}.
STRAND 399 402 {ECO:0000244|PDB:2ETR}.
HELIX 535 540 {ECO:0000244|PDB:3O0Z}.
HELIX 544 691 {ECO:0000244|PDB:3O0Z}.
HELIX 840 902 {ECO:0000244|PDB:4L2W}.
HELIX 947 982 {ECO:0000244|PDB:1S1C}.
HELIX 984 1011 {ECO:0000244|PDB:1S1C}.
SEQUENCE 1354 AA; 158175 MW; 93078CBB009A6F27 CRC64;
MSTGDSFETR FEKMDNLLRD PKSEVNSDCL LDGLDALVYD LDFPALRKNK NIDNFLSRYK
DTINKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSTRK VYAMKLLSKF EMIKRSDSAF
FWEERDIMAF ANSPWVVQLF YAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA
EVVLALDAIH SMGFIHRDVK PDNMLLDKSG HLKLADFGTC MKMNKEGMVR CDTAVGTPDY
ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNSLTFP
DDNDISKEAK NLICAFLTDR EVRLGRNGVE EIKRHLFFKN DQWAWETLRD TVAPVVPDLS
SDIDTSNFDD LEEDKGEEET FPIPKAFVGN QLPFVGFTYY SNRRYLSSAN PNDNRTSSNA
DKSLQESLQK TIYKLEEQLH NEMQLKDEME QKCRTSNIKL DKIMKELDEE GNQRRNLEST
VSQIEKEKML LQHRINEYQR KAEQENEKRR NVENEVSTLK DQLEDLKKVS QNSQLANEKL
SQLQKQLEEA NDLLRTESDT AVRLRKSHTE MSKSISQLES LNRELQERNR ILENSKSQTD
KDYYQLQAIL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLEKVEG ERKEAQDMLN
HSEKEKNNLE IDLNYKLKSL QQRLEQEVNE HKVTKARLTD KHQSIEEAKS VAMCEMEKKL
KEEREAREKA ENRVVQIEKQ CSMLDVDLKQ SQQKLEHLTG NKERMEDEVK NLTLQLEQES
NKRLLLQNEL KTQAFEADNL KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR
ELQDQLEAEQ YFSTLYKTQV KELKEEIEEK NRENLKKIQE LQNEKETLAT QLDLAETKAE
SEQLARGLLE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEEANSMLTK DIEILRRENE
ELTEKMKKAE EEYKLEKEEE ISNLKAAFEK NINTERTLKT QAVNKLAEIM NRKDFKIDRK
KANTQDLRKK EKENRKLQLE LNQEREKFNQ MVVKHQKELN DMQAQLVEEC AHRNELQMQL
ASKESDIEQL RAKLLDLSDS TSVASFPSAD ETDGNLPESR IEGWLSVPNR GNIKRYGWKK
QYVVVSSKKI LFYNDEQDKE QSNPSMVLDI DKLFHVRPVT QGDVYRAETE EIPKIFQILY
ANEGECRKDV EMEPVQQAEK TNFQNHKGHE FIPTLYHFPA NCDACAKPLW HVFKPPPALE
CRRCHVKCHR DHLDKKEDLI CPCKVSYDVT SARDMLLLAC SQDEQKKWVT HLVKKIPKNP
PSGFVRASPR TLSTRSTANQ SFRKVVKNTS GKTS


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E1852h ELISA Homo sapiens,Human,KIAA0619,p164 ROCK-2,Rho kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 96T
U1852h CLIA Homo sapiens,Human,KIAA0619,p164 ROCK-2,Rho kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 96T
U1852r CLIA p150 ROK-alpha,p164 ROCK-2,Rat,Rattus norvegicus,RhoA-binding kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containi 96T
E1852r ELISA kit p150 ROK-alpha,p164 ROCK-2,Rat,Rattus norvegicus,RhoA-binding kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-co 96T
U1852r CLIA kit p150 ROK-alpha,p164 ROCK-2,Rat,Rattus norvegicus,RhoA-binding kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-con 96T
E1852r ELISA p150 ROK-alpha,p164 ROCK-2,Rat,Rattus norvegicus,RhoA-binding kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-contain 96T
U1852h CLIA kit Homo sapiens,Human,KIAA0619,p164 ROCK-2,Rho kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein ki 96T
E1852h ELISA kit Homo sapiens,Human,KIAA0619,p164 ROCK-2,Rho kinase 2,Rho-associated protein kinase 2,Rho-associated, coiled-coil-containing protein kinase 2,Rho-associated, coiled-coil-containing protein k 96T
EIAAB35682 cAMP-dependent protein kinase ROCK-I,CePKA,Corneal epithelial Rho-associated-Ser_Thr kinase 1,HEBM1,Oryctolagus cuniculus,p160 ROCK-1,p160ROCK,Rabbit,Rho-associated protein kinase 1,Rho-associated, co
18-272-195137 ROCK1 Cleavage Site ( 1113 _ 1114 ) - Rabbit polyclonal to ROCK1 Cleavage Site ( 1113 _ 1114 ); EC 2.7.11.1; Rho-associated. coiled-coil-containing protein kinase 1; p160 ROCK-1; p160ROCK; Renal carci 0.05 ml
G8446 Rock-2 (Rho Associated Coiled Coil Containing Protein Kinase 2), Pig, ELISA Kit 96T
201-12-0681 Human Rho-associated coiled-coil containing protein kinase 2,Rock-2 ELISA Kit 48T
YHB2600Hu Human Rho-associated coiled-coil containing protein kinase 2,Rock-2 ELISA Kit 48T


 

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