ROCK1_MOUSE
ID ROCK1_MOUSE Reviewed; 1354 AA.
AC P70335; Q8C3G4; Q8C7H0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Rho-associated protein kinase 1;
DE EC=2.7.11.1;
DE AltName: Full=Rho-associated, coiled-coil-containing protein kinase 1;
DE AltName: Full=Rho-associated, coiled-coil-containing protein kinase I;
DE Short=ROCK-I;
DE AltName: Full=p160 ROCK-1;
DE Short=p160ROCK;
GN Name=Rock1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Embryo, and Heart;
RX PubMed=8772201; DOI=10.1016/0014-5793(96)00811-3;
RA Nakagawa O., Fujisawa K., Ishizaki T., Saito Y., Nakao K., Narumiya S.;
RT "ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming
RT protein serine/threonine kinase in mice.";
RL FEBS Lett. 392:189-193(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-506 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 472-1354.
RC STRAIN=C57BL/6J; TISSUE=Heart, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15753128; DOI=10.1083/jcb.200411179;
RA Shimizu Y., Thumkeo D., Keel J., Ishizaki T., Oshima H., Oshima M.,
RA Noda Y., Matsumura F., Taketo M.M., Narumiya S.;
RT "ROCK-I regulates closure of the eyelids and ventral body wall by inducing
RT assembly of actomyosin bundles.";
RL J. Cell Biol. 168:941-953(2005).
RN [5]
RP INTERACTION WITH ITGB1BP1, AND SUBCELLULAR LOCATION.
RX PubMed=16741948; DOI=10.1002/jcp.20699;
RA Stroeken P.J., Alvarez B., Van Rheenen J., Wijnands Y.M., Geerts D.,
RA Jalink K., Roos E.;
RT "Integrin cytoplasmic domain-associated protein-1 (ICAP-1) interacts with
RT the ROCK-I kinase at the plasma membrane.";
RL J. Cell. Physiol. 208:620-628(2006).
RN [6]
RP INTERACTION WITH ITGB1BP1.
RX PubMed=17654484; DOI=10.1002/jcp.21215;
RA Alvarez B., Stroeken P.J., Edel M.J., Roos E.;
RT "Integrin Cytoplasmic domain-Associated Protein-1 (ICAP-1) promotes
RT migration of myoblasts and affects focal adhesions.";
RL J. Cell. Physiol. 214:474-482(2008).
RN [7]
RP FUNCTION.
RX PubMed=19036714; DOI=10.1126/scisignal.1161938;
RA Ongusaha P.P., Qi H.H., Raj L., Kim Y.B., Aaronson S.A., Davis R.J.,
RA Shi Y., Liao J.K., Lee S.W.;
RT "Identification of ROCK1 as an upstream activator of the JIP-3 to JNK
RT signaling axis in response to UVB damage.";
RL Sci. Signal. 1:RA14-RA14(2008).
RN [8]
RP FUNCTION.
RX PubMed=19181962; DOI=10.1152/ajpheart.01038.2008;
RA Kroll J., Epting D., Kern K., Dietz C.T., Feng Y., Hammes H.P., Wieland T.,
RA Augustin H.G.;
RT "Inhibition of Rho-dependent kinases ROCK I/II activates VEGF-driven
RT retinal neovascularization and sprouting angiogenesis.";
RL Am. J. Physiol. 296:H893-H899(2009).
RN [9]
RP FUNCTION, AND INTERACTION WITH PTEN.
RX PubMed=20008297; DOI=10.1182/blood-2009-08-237222;
RA Vemula S., Shi J., Hanneman P., Wei L., Kapur R.;
RT "ROCK1 functions as a suppressor of inflammatory cell migration by
RT regulating PTEN phosphorylation and stability.";
RL Blood 115:1785-1796(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1105 AND SER-1108, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION.
RX PubMed=21768292; DOI=10.1083/jcb.201007108;
RA Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D.,
RA Block M.R., Albiges-Rizo C., Bouvard D.;
RT "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent
RT fibronectin deposition.";
RL J. Cell Biol. 194:307-322(2011).
RN [12]
RP INTERACTION WITH SHROOM3.
RX PubMed=22493320; DOI=10.1091/mbc.e11-11-0937;
RA Mohan S., Rizaldy R., Das D., Bauer R.J., Heroux A., Trakselis M.A.,
RA Hildebrand J.D., VanDemark A.P.;
RT "Structure of Shroom domain 2 reveals a three-segmented coiled-coil
RT required for dimerization, Rock binding, and apical constriction.";
RL Mol. Biol. Cell 23:2131-2142(2012).
RN [13]
RP FUNCTION.
RX PubMed=30115939; DOI=10.1038/s41598-018-30115-3;
RA Wang L., Buckley A.F., Spurney R.F.;
RT "Regulation of cofilin phosphorylation in glomerular podocytes by testis
RT specific kinase 1 (TESK1).";
RL Sci. Rep. 8:12286-12286(2018).
CC -!- FUNCTION: Protein kinase which is a key regulator of the actin
CC cytoskeleton and cell polarity (PubMed:19036714, PubMed:19181962).
CC Involved in regulation of smooth muscle contraction, actin cytoskeleton
CC organization, stress fiber and focal adhesion formation, neurite
CC retraction, cell adhesion and motility via phosphorylation of DAPK3,
CC GFAP, LIMK1, LIMK2, MYL9/MLC2, TPPP, PFN1 and PPP1R12A
CC (PubMed:19036714, PubMed:19181962). Phosphorylates FHOD1 and acts
CC synergistically with it to promote SRC-dependent non-apoptotic plasma
CC membrane blebbing. Phosphorylates JIP3 and regulates the recruitment of
CC JNK to JIP3 upon UVB-induced stress (By similarity). Acts as a
CC suppressor of inflammatory cell migration by regulating PTEN
CC phosphorylation and stability (PubMed:20008297). Acts as a negative
CC regulator of VEGF-induced angiogenic endothelial cell activation.
CC Required for centrosome positioning and centrosome-dependent exit from
CC mitosis (By similarity). Plays a role in terminal erythroid
CC differentiation (By similarity). Inhibits podocyte motility via
CC regulation of actin cytoskeletal dynamics and phosphorylation of CFL1
CC (PubMed:30115939). Promotes keratinocyte terminal differentiation (By
CC similarity). Involved in osteoblast compaction through the fibronectin
CC fibrillogenesis cell-mediated matrix assembly process, essential for
CC osteoblast mineralization (PubMed:21768292). May regulate closure of
CC the eyelids and ventral body wall by inducing the assembly of
CC actomyosin bundles (PubMed:15753128). {ECO:0000250|UniProtKB:Q13464,
CC ECO:0000250|UniProtKB:Q8MIT6, ECO:0000269|PubMed:15753128,
CC ECO:0000269|PubMed:19036714, ECO:0000269|PubMed:19181962,
CC ECO:0000269|PubMed:20008297, ECO:0000269|PubMed:21768292,
CC ECO:0000269|PubMed:30115939}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:Q13464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000250|UniProtKB:Q13464};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:Q13464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000250|UniProtKB:Q13464};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by RHOA binding. Inhibited by Y-27632
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with RHOA (activated by
CC GTP), RHOB, RHOC, GEM, MYLC2B, RHOE, PPP1R12A, LIMK1, LIMK2, TSG101,
CC CHORDC1, DAPK3, PFN1 and JIP3 (By similarity). Interacts with FHOD1 in
CC a Src-dependent manner (By similarity). Interacts with PTEN. Interacts
CC with ITGB1BP1 (via N-terminus and PTB domain). Interacts with SHROOM3
CC (PubMed:22493320). {ECO:0000250, ECO:0000269|PubMed:16741948,
CC ECO:0000269|PubMed:17654484, ECO:0000269|PubMed:20008297,
CC ECO:0000269|PubMed:22493320}.
CC -!- INTERACTION:
CC P70335; P61588: Rnd3; NbExp=7; IntAct=EBI-989293, EBI-6930266;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16741948}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000269|PubMed:16741948}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q13464}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q13464}. Cell projection, bleb
CC {ECO:0000250|UniProtKB:Q13464}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16741948}. Cell membrane
CC {ECO:0000269|PubMed:16741948}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:16741948}. Cell projection, ruffle
CC {ECO:0000269|PubMed:16741948}. Note=A small proportion is associated
CC with Golgi membranes (By similarity). Associated with the mother
CC centriole and an intercentriolar linker (PubMed:16741948). Colocalizes
CC with ITGB1BP1 and ITGB1 at the cell membrane predominantly in
CC lamellipodia and membrane ruffles, but also in retraction fibers
CC (PubMed:16741948). Localizes at the cell membrane in an ITGB1BP1-
CC dependent manner (PubMed:16741948). {ECO:0000250|UniProtKB:Q13464,
CC ECO:0000269|PubMed:16741948}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P70335-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P70335-2; Sequence=VSP_010448;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, lung, liver,
CC stomach, spleen, kidney, testis, muscle, embryo and placenta.
CC {ECO:0000269|PubMed:8772201}.
CC -!- DOMAIN: The C-terminal auto-inhibitory domain interferes with kinase
CC activity. RHOA binding leads to a conformation change and activation of
CC the kinase. Truncated ROCK1 is constitutively activated.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC -!- PTM: Cleaved by caspase-3 during apoptosis. This leads to constitutive
CC activation of the kinase and membrane blebbing (By similarity).
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit both EOB (eyes open at birth) and
CC omphalocele phenotypes as a result of disorganization of actomyosin
CC cables in the eyelid epithelium and defective actin assembly in the
CC umbilical ring. {ECO:0000269|PubMed:15753128}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH57154.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAC34154.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U58512; AAC53132.1; -; mRNA.
DR EMBL; AK050269; BAC34154.1; ALT_INIT; mRNA.
DR EMBL; AK085974; BAC39581.1; -; mRNA.
DR EMBL; BC057154; AAH57154.1; ALT_SEQ; mRNA.
DR CCDS; CCDS29053.2; -. [P70335-1]
DR PIR; S74244; S74244.
DR RefSeq; NP_033097.1; NM_009071.2. [P70335-1]
DR RefSeq; XP_006525788.1; XM_006525725.1. [P70335-2]
DR AlphaFoldDB; P70335; -.
DR SMR; P70335; -.
DR BioGRID; 202950; 44.
DR DIP; DIP-35521N; -.
DR IntAct; P70335; 29.
DR MINT; P70335; -.
DR STRING; 10090.ENSMUSP00000069549; -.
DR iPTMnet; P70335; -.
DR PhosphoSitePlus; P70335; -.
DR EPD; P70335; -.
DR jPOST; P70335; -.
DR MaxQB; P70335; -.
DR PaxDb; P70335; -.
DR PeptideAtlas; P70335; -.
DR PRIDE; P70335; -.
DR ProteomicsDB; 300565; -. [P70335-1]
DR ProteomicsDB; 300566; -. [P70335-2]
DR Antibodypedia; 1128; 703 antibodies from 46 providers.
DR DNASU; 19877; -.
DR Ensembl; ENSMUST00000067947; ENSMUSP00000069549; ENSMUSG00000024290. [P70335-1]
DR GeneID; 19877; -.
DR KEGG; mmu:19877; -.
DR UCSC; uc008eaq.1; mouse. [P70335-1]
DR CTD; 6093; -.
DR MGI; MGI:107927; Rock1.
DR VEuPathDB; HostDB:ENSMUSG00000024290; -.
DR eggNOG; KOG0612; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR HOGENOM; CLU_000288_140_0_1; -.
DR InParanoid; P70335; -.
DR OMA; XETLATQ; -.
DR PhylomeDB; P70335; -.
DR TreeFam; TF313551; -.
DR Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-MMU-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR Reactome; R-MMU-9013422; RHOBTB1 GTPase cycle.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR BioGRID-ORCS; 19877; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Rock1; mouse.
DR PRO; PR:P70335; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P70335; protein.
DR Bgee; ENSMUSG00000024290; Expressed in aorta tunica media and 254 other tissues.
DR ExpressionAtlas; P70335; baseline and differential.
DR Genevisible; P70335; MM.
DR GO; GO:0106003; C:amyloid-beta complex; ISO:MGI.
DR GO; GO:0032059; C:bleb; IEA:UniProtKB-SubCell.
DR GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:ARUK-UCL.
DR GO; GO:0005856; C:cytoskeleton; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0072518; F:Rho-dependent protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:BHF-UCL.
DR GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
DR GO; GO:0003383; P:apical constriction; IGI:MGI.
DR GO; GO:0032060; P:bleb assembly; IMP:MGI.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IMP:ARUK-UCL.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:MGI.
DR GO; GO:0048598; P:embryonic morphogenesis; IBA:GO_Central.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IGI:BHF-UCL.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:MGI.
DR GO; GO:0050900; P:leukocyte migration; ISO:MGI.
DR GO; GO:0050901; P:leukocyte tethering or rolling; ISO:MGI.
DR GO; GO:0022614; P:membrane to membrane docking; ISO:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; IBA:GO_Central.
DR GO; GO:0097049; P:motor neuron apoptotic process; IMP:MGI.
DR GO; GO:0061157; P:mRNA destabilization; IMP:ARUK-UCL.
DR GO; GO:0051451; P:myoblast migration; IMP:UniProtKB.
DR GO; GO:1902992; P:negative regulation of amyloid precursor protein catabolic process; ISO:MGI.
DR GO; GO:1902430; P:negative regulation of amyloid-beta formation; ISO:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:1903347; P:negative regulation of bicellular tight junction assembly; ISO:MGI.
DR GO; GO:2000672; P:negative regulation of motor neuron apoptotic process; IMP:MGI.
DR GO; GO:0035509; P:negative regulation of myosin-light-chain-phosphatase activity; ISO:MGI.
DR GO; GO:0042326; P:negative regulation of phosphorylation; IMP:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:MGI.
DR GO; GO:0140058; P:neuron projection arborization; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0090521; P:podocyte cell migration; IMP:UniProtKB.
DR GO; GO:1900223; P:positive regulation of amyloid-beta clearance; ISO:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:MGI.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:MGI.
DR GO; GO:1905205; P:positive regulation of connective tissue replacement; ISO:MGI.
DR GO; GO:0035306; P:positive regulation of dephosphorylation; ISO:MGI.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; ISO:MGI.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0032970; P:regulation of actin filament-based process; IGI:MGI.
DR GO; GO:0110061; P:regulation of angiotensin-activated signaling pathway; ISO:MGI.
DR GO; GO:1901888; P:regulation of cell junction assembly; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; ISO:MGI.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; ISO:MGI.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; ISO:MGI.
DR GO; GO:1990776; P:response to angiotensin; IGI:ARUK-UCL.
DR GO; GO:0071559; P:response to transforming growth factor beta; IGI:ARUK-UCL.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI.
DR CDD; cd00029; C1; 1.
DR CDD; cd11639; HR1_ROCK1; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR020684; ROCK1/ROCK2.
DR InterPro; IPR037310; ROCK1_HR1.
DR InterPro; IPR015008; ROCK_Rho-bd_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08912; Rho_Binding; 1.
DR PIRSF; PIRSF037568; Rho_kinase; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51860; REM_1; 1.
DR PROSITE; PS51859; RHO_BD; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Apoptosis; ATP-binding; Cell membrane;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW Kinase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13464"
FT CHAIN 2..1354
FT /note="Rho-associated protein kinase 1"
FT /id="PRO_0000086620"
FT DOMAIN 76..338
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 341..409
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 479..556
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 949..1015
FT /note="RhoBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01206"
FT DOMAIN 1118..1317
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 1228..1283
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 368..727
FT /note="Interaction with FHOD1"
FT /evidence="ECO:0000250"
FT REGION 707..946
FT /note="SHROOM3 binding"
FT /evidence="ECO:0000269|PubMed:22493320"
FT REGION 998..1010
FT /note="RHOA binding"
FT /evidence="ECO:0000250"
FT REGION 1115..1354
FT /note="Auto-inhibitory"
FT /evidence="ECO:0000250"
FT REGION 1333..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 422..692
FT /evidence="ECO:0000255"
FT COILED 1011..1102
FT /evidence="ECO:0000255"
FT ACT_SITE 198
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 82..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 1113..1114
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13464"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13464"
FT VAR_SEQ 425
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010448"
SQ 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
