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Rho-associated protein kinase 2 (EC 2.7.11.1) (Rho kinase 2) (Rho-associated, coiled-coil-containing protein kinase 2) (Rho-associated, coiled-coil-containing protein kinase II) (ROCK-II) (p164 ROCK-2)

 ROCK2_HUMAN             Reviewed;        1388 AA.
O75116; Q53QZ0; Q53SJ7; Q9UQN5;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 4.
30-AUG-2017, entry version 178.
RecName: Full=Rho-associated protein kinase 2;
EC=2.7.11.1;
AltName: Full=Rho kinase 2;
AltName: Full=Rho-associated, coiled-coil-containing protein kinase 2;
AltName: Full=Rho-associated, coiled-coil-containing protein kinase II;
Short=ROCK-II;
AltName: Full=p164 ROCK-2;
Name=ROCK2; Synonyms=KIAA0619;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-431.
TISSUE=Brain;
PubMed=9933571; DOI=10.1006/geno.1998.5344;
Takahashi N., Tuiki H., Saya H., Kaibuchi K.;
"Localization of the gene coding for ROCK II/Rho kinase on human
chromosome 2p24.";
Genomics 55:235-237(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-431.
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
FUNCTION, AND INTERACTION WITH PPP1R12A.
PubMed=10579722; DOI=10.1083/jcb.147.5.1023;
Kawano Y., Fukata Y., Oshiro N., Amano M., Nakamura T., Ito M.,
Matsumura F., Inagaki M., Kaibuchi K.;
"Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase
by Rho-kinase in vivo.";
J. Cell Biol. 147:1023-1038(1999).
[5]
CLEAVAGE BY GRANZYME B, MUTAGENESIS OF ASP-1131, AND FUNCTION.
PubMed=15699075; DOI=10.1084/jem.20031877;
Sebbagh M., Hamelin J., Bertoglio J., Solary E., Breard J.;
"Direct cleavage of ROCK II by granzyme B induces target cell membrane
blebbing in a caspase-independent manner.";
J. Exp. Med. 201:465-471(2005).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EP300.
PubMed=16574662; DOI=10.1074/jbc.M510954200;
Tanaka T., Nishimura D., Wu R.C., Amano M., Iso T., Kedes L.,
Nishida H., Kaibuchi K., Hamamori Y.;
"Nuclear Rho kinase, ROCK2, targets p300 acetyltransferase.";
J. Biol. Chem. 281:15320-15329(2006).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NPM1.
PubMed=17015463; DOI=10.1128/MCB.01383-06;
Ma Z., Kanai M., Kawamura K., Kaibuchi K., Ye K., Fukasawa K.;
"Interaction between ROCK II and nucleophosmin/B23 in the regulation
of centrosome duplication.";
Mol. Cell. Biol. 26:9016-9034(2006).
[8]
PHOSPHORYLATION AT TYR-722, AND DEPHOSPHORYLATION.
PubMed=18559669; DOI=10.1083/jcb.200710187;
Lee H.H., Chang Z.F.;
"Regulation of RhoA-dependent ROCKII activation by Shp2.";
J. Cell Biol. 181:999-1012(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, 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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, AND 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).
[11]
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).
[12]
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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, 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).
[14]
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).
[15]
PHOSPHORYLATION AT TYR-722.
PubMed=20826462; DOI=10.1242/jcs.071555;
Lee H.H., Tien S.C., Jou T.S., Chang Y.C., Jhong J.G., Chang Z.F.;
"Src-dependent phosphorylation of ROCK participates in regulation of
focal adhesion dynamics.";
J. Cell Sci. 123:3368-3377(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
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).
[18]
FUNCTION, AND INTERACTION WITH BRCA2.
PubMed=21084279; DOI=10.1158/0008-5472.CAN-10-0030;
Wang H.F., Takenaka K., Nakanishi A., Miki Y.;
"BRCA2 and nucleophosmin coregulate centrosome amplification and form
a complex with the Rho effector kinase ROCK2.";
Cancer Res. 71:68-77(2011).
[19]
FUNCTION, AND INTERACTION WITH SORL1.
PubMed=21147781; DOI=10.1074/jbc.M110.167239;
Herskowitz J.H., Seyfried N.T., Gearing M., Kahn R.A., Peng J.,
Levey A.I., Lah J.J.;
"Rho kinase II phosphorylation of the lipoprotein receptor LR11/SORLA
alters amyloid-beta production.";
J. Biol. Chem. 286:6117-6127(2011).
[20]
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).
[21]
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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, AND 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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1212; SER-1362 AND
SER-1374, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[24]
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).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
VARIANTS [LARGE SCALE ANALYSIS] ASN-431; VAL-601 AND PRO-1194.
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 ADD1, BRCA2, CNN1, EZR,
DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM.
Phosphorylates SORL1 and IRF4. Acts as a negative regulator of
VEGF-induced angiogenic endothelial cell activation. Positively
regulates the activation of p42/MAPK1-p44/MAPK3 and of
p90RSK/RPS6KA1 during myogenic differentiation. Plays an important
role in the timely initiation of centrosome duplication. Inhibits
keratinocyte terminal differentiation. May regulate closure of the
eyelids and ventral body wall through organization of actomyosin
bundles. Plays a critical role in the regulation of spine and
synaptic properties in the hippocampus. Plays an important role in
generating the circadian rhythm of the aortic myofilament Ca(2+)
sensitivity and vascular contractility by modulating the myosin
light chain phosphorylation. {ECO:0000269|PubMed:10579722,
ECO:0000269|PubMed:15699075, ECO:0000269|PubMed:16574662,
ECO:0000269|PubMed:17015463, ECO:0000269|PubMed:19131646,
ECO:0000269|PubMed:19997641, ECO:0000269|PubMed:21084279,
ECO:0000269|PubMed:21147781}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Activated by RHOA binding. Inhibited by Y-27632
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with IRS1, RHOB and RHOC (By
similarity). Interacts with RHOA (activated by GTP), PPP1R12A,
CHORDC1, SORL1, EP300 and BRCA2. Interacts with NPM1 and this
interaction enhances its activity. Interacts with RAF1 (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250};
Peripheral membrane protein {ECO:0000250}. Nucleus. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome.
Note=Cytoplasmic, and associated with actin microfilaments and the
plasma membrane. {ECO:0000250}.
-!- DOMAIN: An interaction between Thr-414 and Asp-48 is essential for
kinase activity and dimerization. {ECO:0000250}.
-!- PTM: Phosphorylation at Tyr-722 reduces its binding to RHOA and is
crucial for focal adhesion dynamics. Dephosphorylation by PTPN11
stimulates its RHOA binding activity.
{ECO:0000269|PubMed:18559669, ECO:0000269|PubMed:20826462}.
-!- PTM: Cleaved by granzyme B 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}.
-!- SEQUENCE CAUTION:
Sequence=AAX93049.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=BAA31594.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ROCK2ID43474ch2p25.html";
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EMBL; D87931; BAA75636.1; -; mRNA.
EMBL; AB014519; BAA31594.2; ALT_INIT; mRNA.
EMBL; AC018463; AAX93049.1; ALT_SEQ; Genomic_DNA.
EMBL; AC099344; AAY14825.1; -; Genomic_DNA.
CCDS; CCDS42654.1; -.
RefSeq; NP_001308572.1; NM_001321643.1.
RefSeq; NP_004841.2; NM_004850.4.
UniGene; Hs.681743; -.
PDB; 4L6Q; X-ray; 2.79 A; A/B=19-417.
PDB; 4WOT; X-ray; 2.93 A; A/B/C/D=22-417.
PDB; 5U7Q; X-ray; 3.15 A; A/B/C/D=23-417.
PDB; 5U7R; X-ray; 3.33 A; A/B/C/D=23-417.
PDBsum; 4L6Q; -.
PDBsum; 4WOT; -.
PDBsum; 5U7Q; -.
PDBsum; 5U7R; -.
ProteinModelPortal; O75116; -.
SMR; O75116; -.
BioGrid; 114860; 25.
IntAct; O75116; 11.
MINT; MINT-4299744; -.
STRING; 9606.ENSP00000317985; -.
BindingDB; O75116; -.
ChEMBL; CHEMBL2973; -.
DrugBank; DB08756; (R)-TRANS-4-(1-AMINOETHYL)-N-(4-PYRIDYL) CYCLOHEXANECARBOXAMIDE.
GuidetoPHARMACOLOGY; 1504; -.
iPTMnet; O75116; -.
PhosphoSitePlus; O75116; -.
SwissPalm; O75116; -.
BioMuta; ROCK2; -.
EPD; O75116; -.
MaxQB; O75116; -.
PaxDb; O75116; -.
PeptideAtlas; O75116; -.
PRIDE; O75116; -.
Ensembl; ENST00000315872; ENSP00000317985; ENSG00000134318.
GeneID; 9475; -.
KEGG; hsa:9475; -.
UCSC; uc002rbd.2; human.
CTD; 9475; -.
DisGeNET; 9475; -.
GeneCards; ROCK2; -.
H-InvDB; HIX0001828; -.
HGNC; HGNC:10252; ROCK2.
HPA; CAB008666; -.
HPA; HPA007459; -.
HPA; HPA044109; -.
MIM; 604002; gene.
neXtProt; NX_O75116; -.
OpenTargets; ENSG00000134318; -.
PharmGKB; PA34624; -.
eggNOG; KOG0612; Eukaryota.
eggNOG; ENOG410XR1Q; LUCA.
GeneTree; ENSGT00760000118994; -.
HOGENOM; HOG000017259; -.
HOVERGEN; HBG053111; -.
InParanoid; O75116; -.
KO; K17388; -.
OMA; PNQSIRR; -.
OrthoDB; EOG091G0BOR; -.
PhylomeDB; O75116; -.
TreeFam; TF313551; -.
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.
SignaLink; O75116; -.
SIGNOR; O75116; -.
ChiTaRS; ROCK2; human.
GenomeRNAi; 9475; -.
PRO; PR:O75116; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000134318; -.
CleanEx; HS_ROCK2; -.
ExpressionAtlas; O75116; baseline and differential.
Genevisible; O75116; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0017048; F:Rho GTPase binding; IEA:InterPro.
GO; GO:0072518; F:Rho-dependent protein serine/threonine kinase activity; IMP:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
GO; GO:0071394; P:cellular response to testosterone stimulus; IMP:UniProtKB.
GO; GO:0051298; P:centrosome duplication; IMP:UniProtKB.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
GO; GO:0000910; P:cytokinesis; NAS:ProtInc.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0090002; P:establishment of protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
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:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; IMP:UniProtKB.
GO; GO:0010825; P:positive regulation of centrosome duplication; IEA:InterPro.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; TAS:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; TAS:UniProtKB.
GO; GO:2000145; P:regulation of cell motility; TAS:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; ISS: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:0051492; P:regulation of stress fiber assembly; TAS:UniProtKB.
GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0006939; P:smooth muscle contraction; TAS:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0039694; P:viral RNA genome replication; IMP:ParkinsonsUK-UCL.
CDD; cd00029; C1; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR015008; Rho-bd_dom.
InterPro; IPR020684; ROCK1/ROCK2.
InterPro; IPR029878; ROCK2.
InterPro; IPR008271; Ser/Thr_kinase_AS.
PANTHER; PTHR22988:SF40; PTHR22988:SF40; 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; SSF50729; SSF50729; 2.
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; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Biological rhythms; Cell membrane;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Kinase;
Magnesium; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
CHAIN 1 1388 Rho-associated protein kinase 2.
/FTId=PRO_0000086625.
DOMAIN 92 354 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 357 425 AGC-kinase C-terminal.
REPEAT 475 559 REM.
DOMAIN 1150 1349 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
NP_BIND 98 106 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ZN_FING 1260 1315 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
REGION 363 784 Interaction with PPP1R12A.
REGION 373 420 Interaction with NPM1.
{ECO:0000269|PubMed:17015463}.
REGION 979 1047 RHOA binding. {ECO:0000250}.
COILED 429 1024 {ECO:0000255}.
COILED 1053 1131 {ECO:0000255}.
ACT_SITE 214 214 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 121 121 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 1131 1132 Cleavage; by granzyme B.
MOD_RES 414 414 Phosphothreonine; by ROCK2.
{ECO:0000250|UniProtKB:Q62868}.
MOD_RES 722 722 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:18559669,
ECO:0000269|PubMed:20826462}.
MOD_RES 1137 1137 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1212 1212 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1362 1362 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1374 1374 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VARIANT 431 431 T -> N (in dbSNP:rs2230774).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:9734811,
ECO:0000269|PubMed:9933571}.
/FTId=VAR_041062.
VARIANT 601 601 D -> V (in dbSNP:rs35768389).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041063.
VARIANT 1083 1083 K -> M (in dbSNP:rs34945852).
/FTId=VAR_057110.
VARIANT 1194 1194 S -> P (in a metastatic melanoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041064.
MUTAGEN 1131 1131 D->A: Abolishes cleavage by granzyme B.
{ECO:0000269|PubMed:15699075}.
CONFLICT 83 83 R -> K (in Ref. 1; BAA75636).
{ECO:0000305}.
HELIX 29 35 {ECO:0000244|PDB:4L6Q}.
HELIX 43 57 {ECO:0000244|PDB:4L6Q}.
HELIX 60 63 {ECO:0000244|PDB:4L6Q}.
HELIX 66 85 {ECO:0000244|PDB:4L6Q}.
HELIX 89 91 {ECO:0000244|PDB:4L6Q}.
STRAND 92 100 {ECO:0000244|PDB:4L6Q}.
STRAND 102 111 {ECO:0000244|PDB:4L6Q}.
TURN 112 114 {ECO:0000244|PDB:4L6Q}.
STRAND 117 124 {ECO:0000244|PDB:4L6Q}.
HELIX 125 130 {ECO:0000244|PDB:4L6Q}.
HELIX 138 146 {ECO:0000244|PDB:4L6Q}.
STRAND 155 160 {ECO:0000244|PDB:4L6Q}.
STRAND 162 169 {ECO:0000244|PDB:4L6Q}.
HELIX 177 183 {ECO:0000244|PDB:4L6Q}.
HELIX 188 207 {ECO:0000244|PDB:4L6Q}.
HELIX 217 219 {ECO:0000244|PDB:4L6Q}.
STRAND 220 222 {ECO:0000244|PDB:4L6Q}.
STRAND 228 230 {ECO:0000244|PDB:4L6Q}.
STRAND 241 246 {ECO:0000244|PDB:4L6Q}.
HELIX 254 256 {ECO:0000244|PDB:4L6Q}.
HELIX 259 264 {ECO:0000244|PDB:4L6Q}.
STRAND 270 272 {ECO:0000244|PDB:4L6Q}.
HELIX 274 289 {ECO:0000244|PDB:4L6Q}.
HELIX 299 307 {ECO:0000244|PDB:4L6Q}.
HELIX 309 312 {ECO:0000244|PDB:4L6Q}.
STRAND 317 319 {ECO:0000244|PDB:5U7Q}.
HELIX 323 332 {ECO:0000244|PDB:4L6Q}.
HELIX 336 338 {ECO:0000244|PDB:4L6Q}.
TURN 340 343 {ECO:0000244|PDB:4L6Q}.
HELIX 346 349 {ECO:0000244|PDB:4L6Q}.
HELIX 352 354 {ECO:0000244|PDB:4L6Q}.
TURN 361 363 {ECO:0000244|PDB:4L6Q}.
HELIX 364 366 {ECO:0000244|PDB:4L6Q}.
HELIX 408 410 {ECO:0000244|PDB:4L6Q}.
SEQUENCE 1388 AA; 160900 MW; 876240F410C2487E CRC64;
MSRPPPTGKM PGAPETAPGD GAGASRQRKL EALIRDPRSP INVESLLDGL NSLVLDLDFP
ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR GAFGEVQLVR HKASQKVYAM
KLLSKFEMIK RSDSAFFWEE RDIMAFANSP WVVQLFYAFQ DDRYLYMVME YMPGGDLVNL
MSNYDVPEKW AKFYTAEVVL ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD
ETGMVHCDTA VGTPDYISPE VLKSQGGDGF YGRECDWWSV GVFLYEMLVG DTPFYADSLV
GTYSKIMDHK NSLCFPEDAE ISKHAKNLIC AFLTDREVRL GRNGVEEIRQ HPFFKNDQWH
WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP KAFVGNQLPF IGFTYYRENL
LLSDSPSCRE TDSIQSRKNE ESQEIQKKLY TLEEHLSNEM QAKEELEQKC KSVNTRLEKT
AKELEEEITL RKSVESALRQ LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL
EDLKKRNQNS QISTEKVNQL QRQLDETNAL LRTESDTAAR LRKTQAESSK QIQQLESNNR
DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRICG LEEDLKNGKI
LLAKVELEKR QLQERFTDLE KEKSNMEIDM TYQLKVIQQS LEQEEAEHKA TKARLADKNK
IYESIEEAKS EAMKEMEKKL LEERTLKQKV ENLLLEAEKR CSLLDCDLKQ SQQKINELLK
QKDVLNEDVR NLTLKIEQET QKRCLTQNDL KMQTQQVNTL KMSEKQLKQE NNHLMEMKMN
LEKQNAELRK ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEECEEK TKLGKELQQK
KQELQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI KEMMARHKQE
LTEKDATIAS LEETNRTLTS DVANLANEKE ELNNKLKDVQ EQLSRLKDEE ISAAAIKAQF
EKQLLTERTL KTQAVNKLAE IMNRKEPVKR GNDTDVRRKE KENRKLHMEL KSEREKLTQQ
MIKYQKELNE MQAQIAEESQ IRIELQMTLD SKDSDIEQLR SQLQALHIGL DSSSIGSGPG
DAEADDGFPE SRLEGWLSLP VRNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL
DIDKLFHVRP VTQTDVYRAD AKEIPRIFQI LYANEGESKK EQEFPVEPVG EKSNYICHKG
HEFIPTLYHF PTNCEACMKP LWHMFKPPPA LECRRCHIKC HKDHMDKKEE IIAPCKVYYD
ISTAKNLLLL ANSTEEQQKW VSRLVKKIPK KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR
QLAPNKPS


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