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Rho-associated protein kinase 1 (EC 2.7.11.1) (Rho-associated, coiled-coil-containing protein kinase 1) (Rho-associated, coiled-coil-containing protein kinase I) (ROCK-I) (p160 ROCK-1) (p160ROCK)

 ROCK1_MOUSE             Reviewed;        1354 AA.
P70335; Q8C3G4; Q8C7H0;
24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
05-DEC-2018, entry version 184.
RecName: Full=Rho-associated protein kinase 1;
EC=2.7.11.1;
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Embryo, and Heart;
PubMed=8772201; DOI=10.1016/0014-5793(96)00811-3;
Nakagawa O., Fujisawa K., Ishizaki T., Saito Y., Nakao K.,
Narumiya S.;
"ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil
forming protein serine/threonine kinase in mice.";
FEBS Lett. 392:189-193(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-506 (ISOFORM 2).
STRAIN=FVB/N; TISSUE=Mammary gland;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 472-1354.
STRAIN=C57BL/6J; TISSUE=Heart, and Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15753128; DOI=10.1083/jcb.200411179;
Shimizu Y., Thumkeo D., Keel J., Ishizaki T., Oshima H., Oshima M.,
Noda Y., Matsumura F., Taketo M.M., Narumiya S.;
"ROCK-I regulates closure of the eyelids and ventral body wall by
inducing assembly of actomyosin bundles.";
J. Cell Biol. 168:941-953(2005).
[5]
INTERACTION WITH ITGB1BP1, AND SUBCELLULAR LOCATION.
PubMed=16741948; DOI=10.1002/jcp.20699;
Stroeken P.J., Alvarez B., Van Rheenen J., Wijnands Y.M., Geerts D.,
Jalink K., Roos E.;
"Integrin cytoplasmic domain-associated protein-1 (ICAP-1) interacts
with the ROCK-I kinase at the plasma membrane.";
J. Cell. Physiol. 208:620-628(2006).
[6]
INTERACTION WITH ITGB1BP1.
PubMed=17654484; DOI=10.1002/jcp.21215;
Alvarez B., Stroeken P.J., Edel M.J., Roos E.;
"Integrin Cytoplasmic domain-Associated Protein-1 (ICAP-1) promotes
migration of myoblasts and affects focal adhesions.";
J. Cell. Physiol. 214:474-482(2008).
[7]
FUNCTION.
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).
[8]
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).
[9]
FUNCTION, AND INTERACTION WITH PTEN.
PubMed=20008297; DOI=10.1182/blood-2009-08-237222;
Vemula S., Shi J., Hanneman P., Wei L., Kapur R.;
"ROCK1 functions as a suppressor of inflammatory cell migration by
regulating PTEN phosphorylation and stability.";
Blood 115:1785-1796(2010).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1105 AND SER-1108, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
FUNCTION.
PubMed=21768292; DOI=10.1083/jcb.201007108;
Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A.,
Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.;
"Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
fibronectin deposition.";
J. Cell Biol. 194:307-322(2011).
-!- 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. Required for centrosome positioning and
centrosome-dependent exit from mitosis. Plays a role in terminal
erythroid differentiation. Promotes keratinocyte terminal
differentiation (By similarity). 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. Involved in
osteoblast compaction through the fibronectin fibrillogenesis
cell-mediated matrix assembly process, essential for osteoblast
mineralization. May regulate closure of the eyelids and ventral
body wall by inducing the assembly of actomyosin bundles.
{ECO:0000250, ECO:0000269|PubMed:15753128,
ECO:0000269|PubMed:19036714, ECO:0000269|PubMed:19181962,
ECO:0000269|PubMed:20008297, ECO:0000269|PubMed:21768292}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.1;
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y-
27632 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homodimer (By similarity). Interacts with RHOA (activated
by GTP), RHOB, RHOC, GEM, MYLC2B, RHOE, PPP1R12A, LIMK1, LIMK2,
TSG101, CHORDC1, DAPK3, PFN1 and JIP3 (By similarity). Interacts
with FHOD1 in a Src-dependent manner (By similarity). Interacts
with PTEN. Interacts with ITGB1BP1 (via N-terminus and PTB
domain). {ECO:0000250, ECO:0000269|PubMed:16741948,
ECO:0000269|PubMed:17654484, ECO:0000269|PubMed:20008297}.
-!- INTERACTION:
P61588:Rnd3; NbExp=7; IntAct=EBI-989293, EBI-6930266;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16741948}.
Cytoplasm, cytoskeleton, microtubule organizing center,
centrosome, centriole {ECO:0000269|PubMed:16741948}. Golgi
apparatus membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}. Cell projection, bleb {ECO:0000250}. Cytoplasm,
cytoskeleton {ECO:0000269|PubMed:16741948}. Cell membrane
{ECO:0000269|PubMed:16741948}. Cell projection, lamellipodium
{ECO:0000269|PubMed:16741948}. Cell projection, ruffle
{ECO:0000269|PubMed:16741948}. Note=Associated with the mother
centriole and an intercentriolar linker. A small proportion is
associated with Golgi membranes (By similarity). 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.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P70335-1; Sequence=Displayed;
Name=2;
IsoId=P70335-2; Sequence=VSP_010448;
Note=May be due to a competing donor splice site. No
experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in brain, heart, lung, liver,
stomach, spleen, kidney, testis, muscle, embryo and placenta.
{ECO:0000269|PubMed:8772201}.
-!- 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.
-!- PTM: Cleaved by caspase-3 during apoptosis. This leads to
constitutive activation of the kinase and membrane blebbing (By
similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice exhibit both EOB (eyes open at birth)
and omphalocele phenotypes as a result of disorganization of
actomyosin cables in the eyelid epithelium and defective actin
assembly in the umbilical ring. {ECO:0000269|PubMed:15753128}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH57154.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAC34154.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; U58512; AAC53132.1; -; mRNA.
EMBL; AK050269; BAC34154.1; ALT_INIT; mRNA.
EMBL; AK085974; BAC39581.1; -; mRNA.
EMBL; BC057154; AAH57154.1; ALT_SEQ; mRNA.
CCDS; CCDS29053.2; -. [P70335-1]
PIR; S74244; S74244.
RefSeq; NP_033097.1; NM_009071.2. [P70335-1]
RefSeq; XP_006525788.1; XM_006525725.1. [P70335-2]
UniGene; Mm.6710; -.
ProteinModelPortal; P70335; -.
SMR; P70335; -.
BioGrid; 202950; 30.
DIP; DIP-35521N; -.
IntAct; P70335; 30.
MINT; P70335; -.
STRING; 10090.ENSMUSP00000069549; -.
iPTMnet; P70335; -.
PhosphoSitePlus; P70335; -.
EPD; P70335; -.
MaxQB; P70335; -.
PaxDb; P70335; -.
PeptideAtlas; P70335; -.
PRIDE; P70335; -.
Ensembl; ENSMUST00000067947; ENSMUSP00000069549; ENSMUSG00000024290. [P70335-1]
GeneID; 19877; -.
KEGG; mmu:19877; -.
UCSC; uc008eaq.1; mouse. [P70335-1]
CTD; 6093; -.
MGI; MGI:107927; Rock1.
eggNOG; KOG0612; Eukaryota.
eggNOG; ENOG410XR1Q; LUCA.
GeneTree; ENSGT00940000153442; -.
HOGENOM; HOG000017259; -.
HOVERGEN; HBG053111; -.
InParanoid; P70335; -.
KO; K04514; -.
OMA; EQEQTEH; -.
OrthoDB; EOG091G0BOR; -.
PhylomeDB; P70335; -.
TreeFam; TF313551; -.
Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
Reactome; R-MMU-416482; G alpha (12/13) signalling events.
Reactome; R-MMU-416572; Sema4D induced cell migration and growth-cone collapse.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-5627117; RHO GTPases Activate ROCKs.
Reactome; R-MMU-6798695; Neutrophil degranulation.
ChiTaRS; Rock1; mouse.
PRO; PR:P70335; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024290; Expressed in 294 organ(s), highest expression level in aorta.
Genevisible; P70335; MM.
GO; GO:0106003; C:amyloid-beta complex; IEA:Ensembl.
GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:ARUK-UCL.
GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0017049; F:GTP-Rho binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0072518; F:Rho-dependent protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
GO; GO:0003383; P:apical constriction; IGI:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0032060; P:bleb assembly; IMP:MGI.
GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:MGI.
GO; GO:0007010; P:cytoskeleton organization; ISO:MGI.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
GO; GO:0050900; P:leukocyte migration; ISO:MGI.
GO; GO:0050901; P:leukocyte tethering or rolling; ISO:MGI.
GO; GO:0022614; P:membrane to membrane docking; ISO:MGI.
GO; GO:0051451; P:myoblast migration; IMP:UniProtKB.
GO; GO:1902992; P:negative regulation of amyloid precursor protein catabolic process; ISO:MGI.
GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISO:MGI.
GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; ISO:MGI.
GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; ISO:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
GO; GO:0140058; P:neuron projection arborization; ISO:MGI.
GO; GO:0031175; P:neuron projection development; ISO:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISO:MGI.
GO; GO:0010508; P:positive regulation of autophagy; ISO:MGI.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:MGI.
GO; GO:1905205; P:positive regulation of connective tissue replacement; ISO:MGI.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
GO; GO:0032970; P:regulation of actin filament-based process; IGI:MGI.
GO; GO:0110061; P:regulation of angiotensin-activated signaling pathway; ISO:MGI.
GO; GO:2000114; P:regulation of establishment of cell polarity; IEA:InterPro.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:MGI.
GO; GO:0045616; P:regulation of keratinocyte differentiation; ISO:MGI.
GO; GO:0045664; P:regulation of neuron differentiation; ISO:MGI.
GO; GO:0051492; P:regulation of stress fiber assembly; IEA:InterPro.
GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:MGI.
GO; GO:1990776; P:response to angiotensin; IGI:ARUK-UCL.
GO; GO:0071559; P:response to transforming growth factor beta; IGI:ARUK-UCL.
GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI.
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;
Acetylation; Alternative splicing; Apoptosis; ATP-binding;
Cell membrane; Cell projection; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Golgi apparatus; Kinase; Magnesium; Membrane;
Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q13464}.
CHAIN 2 1354 Rho-associated protein kinase 1.
/FTId=PRO_0000086620.
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 1283 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
REGION 368 727 Interaction with FHOD1. {ECO:0000250}.
REGION 998 1010 RHOA binding. {ECO:0000250}.
REGION 1115 1354 Auto-inhibitory. {ECO:0000250}.
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. {ECO:0000250}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:Q13464}.
MOD_RES 1105 1105 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1108 1108 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1328 1328 Phosphoserine.
{ECO:0000250|UniProtKB:Q13464}.
VAR_SEQ 425 425 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010448.
SEQUENCE 1354 AA; 158171 MW; A1CBD543B831CF96 CRC64;
MSTGDSFETR FEKIDNLLRD 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 LEEDKGDEET FPIPKAFVGN QLPFVGFTYY SNRRYLPSAN ASENRSSSNV
DKSLQESLQK TIYKLEEQLH NEMQLKDEME QKCRTSNLKL DKIMKELDEE GNQRRNLESA
VSQIEKEKML LQHRINEYQR KVEQENEKRR NIENEVSTLK DQLEDLRKAS QTSQLANEKL
TQLQKQLEEA NDLLRTESDT AVRLRKSHTE MSKSISQLES LNRELQERNR ILENSKSQAD
KDYYQLQAVL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLERVEG ERKEAQDMLN
HSEKEKNNLE IDLNYKLKSI QQRLEQEVNE HKVTKARLTD KHQSIEEAKS VAMCEMEKKL
KEEREAREKA ENRVVETEKQ CSMLDVDLKQ SQQKLEHLTE NKERMEDEVK NLALQLEQES
NKRLLLQNEL KTQAFEADNL KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR
ELQDQLEAEQ YFSTLYKTQV KELKEEIEEK NRENLRKIQE LQSEKETLST QLDLAETKAE
SEQLARGILE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEETNSVLTK DIEMLRKENE
ELNERMRTAE EEYKLKKEEE INNLKAAFEK NISTERTLKT QAVNKLAEIM NRKDFKIDRK
KANTQDLRKK EKENRKLQLE LNQEREKFNQ MVVKHQKELN DMQAQLVEEC THRNELQMQL
ASKESDIEQL RAKLLDLSDS TSVASFPSAD ETDGNLPESR IEGWLSVPNR GNIKRYGWKK
QYVVVSSKKI LFYNDEQDKE QSSPSMVLDI DKLFHVRPVT QGDVYRAETE EIPKIFQILY
ANEGECRKDI EVEPVQQGEK TNFQNHKGHE FIPTLYHFPA NCEACAKPLW HVFKPPPALE
CRRCHVKCHR DHLDKKEDLI SPCKVSYDVT SARDMLLLAC SQDEQKKWVT HLVKKIPKNP
PSGFVRASPR TLSTRSTANQ SFRKVVKNTS GKTS


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