Q13464 (ROCK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rho-associated protein kinase 1
EC=2.7.11.1

Alternative name(s):
Renal carcinoma antigen NY-REN-35
Rho-associated, coiled-coil-containing protein kinase 1
Rho-associated, coiled-coil-containing protein kinase I
Short name=ROCK-I
p160 ROCK-1
Short name=p160ROCK

Gene names

Name:

ROCK1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1354 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.1 Ref.6 Ref.8 Ref.9 Ref.10 Ref.11 Ref.16 Ref.17 Ref.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.29
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Activated by RHOA binding. Inhibited by Y-27632.
Subunit structure	Homodimer. Interacts with RHOB, RHOC, MYLC2B and PTEN 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. Ref.1 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.19 Ref.21 Ref.23 Ref.27 Ref.33
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton › centrosome › centriole By similarity. Golgi apparatus membrane; Peripheral membrane protein. Cell projection › bleb. Note: Associated with the mother centriole and an intercentriolar linker By similarity. A small proportion is associated with Golgi membranes. Ref.1 Ref.13 Ref.17
Tissue specificity	Detected in blood platelets. Ref.1
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.
Post-translational modification	Autophosphorylated on serine and threonine residues. Ref.1 Cleaved by caspase-3 during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. Contains 1 AGC-kinase C-terminal domain. Contains 1 PH domain. Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 protein kinase domain. Contains 1 REM (Hr1) repeat.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cell projection Cytoplasm Cytoskeleton Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil Zinc-finger
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Traceable author statement PubMed 8798490. Source: ProtInc actin cytoskeleton organization Traceable author statement Ref.8. Source: ProtInc apical constriction Inferred from electronic annotation. Source: Compara axon guidance Traceable author statement. Source: Reactome bleb assembly Inferred from electronic annotation. Source: Compara cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome leukocyte tethering or rolling Inferred from direct assay PubMed 12082081. Source: BHF-UCL membrane to membrane docking Inferred from direct assay PubMed 12082081. Source: BHF-UCL negative regulation of angiogenesis Inferred from mutant phenotype Ref.22. Source: UniProtKB negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara regulation of cell motility Traceable author statement Ref.14. Source: UniProtKB regulation of establishment of cell polarity Traceable author statement Ref.30. Source: UniProtKB regulation of focal adhesion assembly Traceable author statement Ref.14. Source: UniProtKB regulation of keratinocyte differentiation Inferred from mutant phenotype Ref.24. Source: UniProtKB regulation of stress fiber assembly Traceable author statement Ref.14. Source: UniProtKB smooth muscle contraction Traceable author statement Ref.14. Source: UniProtKB
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell bleb Inferred from electronic annotation. Source: UniProtKB-SubCell centriole Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipid binding Inferred from electronic annotation. Source: InterPro protein serine/threonine kinase activity Inferred from direct assay Ref.9Ref.10Ref.19Ref.17Ref.21. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.4

Chain

2 – 1354

1353

Rho-associated protein kinase 1

PRO_0000086619

Regions

Domain

76 – 338

263

Protein kinase

Domain

341 – 409

69

AGC-kinase C-terminal

Repeat

458 – 542

85

REM

Domain

1118 – 1317

200

PH

Nucleotide binding

82 – 90

9

ATP By similarity

Zinc finger

1228 – 1281

54

Phorbol-ester/DAG-type

Region

368 – 727

360

Interaction with FHOD1

Region

998 – 1010

13

RHOA binding

Region

1115 – 1354

240

Auto-inhibitory

Coiled coil

422 – 612

191

Potential

Coiled coil

1011 – 1102

92

Potential

Compositional bias

636 – 980

345

Glu-rich

Sites

Active site

198

1

Proton acceptor By similarity

Binding site

105

1

ATP By similarity

Site

1113 – 1114

2

Cleavage; by caspase-3

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.4

Modified residue

647

1

N6-acetyllysine Ref.26

Modified residue

1105

1

Phosphoserine Ref.18 Ref.25

Natural variations

Natural variant

108

1

S → N. Ref.34
Corresponds to variant rs55811609 [ dbSNP | Ensembl ].

VAR_041055

Natural variant

773

1

T → S. Ref.34
Corresponds to variant rs45562542 [ dbSNP | Ensembl ].

VAR_041056

Natural variant

1112

1

T → P. Ref.34
Corresponds to variant rs35881519 [ dbSNP | Ensembl ].

VAR_041057

Natural variant

1193

1

P → S in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.34

VAR_041058

Natural variant

1217

1

Q → E. Ref.34
Corresponds to variant rs2847092 [ dbSNP | Ensembl ].

VAR_041059

Natural variant

1262

1

R → Q. Ref.34
Corresponds to variant rs1045142 [ dbSNP | Ensembl ].

VAR_041060

Natural variant

1264

1

C → R. Ref.34
Corresponds to variant rs2663698 [ dbSNP | Ensembl ].

VAR_041061

Experimental info

Mutagenesis

1113

1

D → A: Abolishes cleavage by caspase-3. Ref.11

Sequence conflict

170

1

V → A in AAI13115. Ref.3

Sequence conflict

197

1

R → G in AAI13115. Ref.3

Sequence conflict

220

1

C → R in AAI13115. Ref.3

Sequence conflict

323 – 325

3

RLG → GTR in BAD92202. Ref.5

Sequence conflict

521

1

D → N in AAI13115. Ref.3

Sequence conflict

965

1

K → R in AAI13115. Ref.3

Sequence conflict

1354

1

S → R in ACA06069. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1354

Helix Strand Turn

Details...

Helix

9 – 19

11

Helix

27 – 41

15

Helix

44 – 47

4

Helix

50 – 69

20

Helix

73 – 75

3

Beta strand

76 – 84

9

Beta strand

86 – 95

10

Turn

96 – 98

3

Beta strand

101 – 108

8

Helix

109 – 114

6

Helix

121 – 130

10

Beta strand

139 – 144

6

Beta strand

146 – 153

8

Beta strand

157 – 160

4

Helix

161 – 167

7

Helix

172 – 191

20

Helix

201 – 203

3

Beta strand

204 – 206

3

Beta strand

212 – 214

3

Beta strand

227 – 230

4

Helix

238 – 240

3

Helix

243 – 247

5

Turn

248 – 252

5

Beta strand

254 – 256

3

Helix

258 – 273

16

Helix

283 – 291

9

Helix

293 – 296

4

Helix

307 – 316

10

Helix

320 – 322

3

Turn

324 – 327

4

Helix

329 – 333

5

Helix

336 – 338

3

Turn

345 – 347

3

Helix

348 – 350

3

Helix

365 – 367

3

Helix

392 – 394

3

Beta strand

399 – 402

4

Helix

544 – 691

148

Helix

947 – 982

36

Helix

984 – 1011

28

Sequences

	Sequence		Length	Mass (Da)
	Q13464 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 93078CBB009A6F27	FASTA	1,354	158,175
	10 20 30 40 50 60 MSTGDSFETR FEKMDNLLRD PKSEVNSDCL LDGLDALVYD LDFPALRKNK NIDNFLSRYK 70 80 90 100 110 120 DTINKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSTRK VYAMKLLSKF EMIKRSDSAF 130 140 150 160 170 180 FWEERDIMAF ANSPWVVQLF YAFQDDRYLY MVMEYMPGGD LVNLMSNYDV PEKWARFYTA 190 200 210 220 230 240 EVVLALDAIH SMGFIHRDVK PDNMLLDKSG HLKLADFGTC MKMNKEGMVR CDTAVGTPDY 250 260 270 280 290 300 ISPEVLKSQG GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNSLTFP 310 320 330 340 350 360 DDNDISKEAK NLICAFLTDR EVRLGRNGVE EIKRHLFFKN DQWAWETLRD TVAPVVPDLS 370 380 390 400 410 420 SDIDTSNFDD LEEDKGEEET FPIPKAFVGN QLPFVGFTYY SNRRYLSSAN PNDNRTSSNA 430 440 450 460 470 480 DKSLQESLQK TIYKLEEQLH NEMQLKDEME QKCRTSNIKL DKIMKELDEE GNQRRNLEST 490 500 510 520 530 540 VSQIEKEKML LQHRINEYQR KAEQENEKRR NVENEVSTLK DQLEDLKKVS QNSQLANEKL 550 560 570 580 590 600 SQLQKQLEEA NDLLRTESDT AVRLRKSHTE MSKSISQLES LNRELQERNR ILENSKSQTD 610 620 630 640 650 660 KDYYQLQAIL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLEKVEG ERKEAQDMLN 670 680 690 700 710 720 HSEKEKNNLE IDLNYKLKSL QQRLEQEVNE HKVTKARLTD KHQSIEEAKS VAMCEMEKKL 730 740 750 760 770 780 KEEREAREKA ENRVVQIEKQ CSMLDVDLKQ SQQKLEHLTG NKERMEDEVK NLTLQLEQES 790 800 810 820 830 840 NKRLLLQNEL KTQAFEADNL KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR 850 860 870 880 890 900 ELQDQLEAEQ YFSTLYKTQV KELKEEIEEK NRENLKKIQE LQNEKETLAT QLDLAETKAE 910 920 930 940 950 960 SEQLARGLLE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEEANSMLTK DIEILRRENE 970 980 990 1000 1010 1020 ELTEKMKKAE EEYKLEKEEE ISNLKAAFEK NINTERTLKT QAVNKLAEIM NRKDFKIDRK 1030 1040 1050 1060 1070 1080 KANTQDLRKK EKENRKLQLE LNQEREKFNQ MVVKHQKELN DMQAQLVEEC AHRNELQMQL 1090 1100 1110 1120 1130 1140 ASKESDIEQL RAKLLDLSDS TSVASFPSAD ETDGNLPESR IEGWLSVPNR GNIKRYGWKK 1150 1160 1170 1180 1190 1200 QYVVVSSKKI LFYNDEQDKE QSNPSMVLDI DKLFHVRPVT QGDVYRAETE EIPKIFQILY 1210 1220 1230 1240 1250 1260 ANEGECRKDV EMEPVQQAEK TNFQNHKGHE FIPTLYHFPA NCDACAKPLW HVFKPPPALE 1270 1280 1290 1300 1310 1320 CRRCHVKCHR DHLDKKEDLI CPCKVSYDVT SARDMLLLAC SQDEQKKWVT HLVKKIPKNP 1330 1340 1350 PSGFVRASPR TLSTRSTANQ SFRKVVKNTS GKTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase." Ishizaki T., Maekawa M., Fujisawa K., Okawa K., Iwamatsu A., Fujita A., Watanabe N., Saito Y., Kakizuka A., Morii N., Narumiya S. EMBO J. 15:1885-1893(1996) [PubMed] [Europe PMC] [Abstract] Cited for: 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, TISSUE SPECIFICITY. Tissue: Leukemia.
[2]	NHLBI resequencing and genotyping service (RS&G) Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	Bienvenut W.V., Ramsay A., Leung H.Y. Submitted (MAR-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13; 85-94; 327-334; 405-415 AND 546-563, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 323-1027. Tissue: Brain.
[6]	"Different molecular mechanisms for Rho family GTPase-dependent, Ca2+-independent contraction of smooth muscle." 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. J. Biol. Chem. 273:23433-23439(1998) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN SMOOTH MUSCLE CONTRACTION.
[7]	"Antigens recognized by autologous antibody in patients with renal-cell carcinoma." 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. Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[8]	"Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase." Maekawa M., Ishizaki T., Boku S., Watanabe N., Fujita A., Iwamatsu A., Obinata T., Ohashi K., Mizuno K., Narumiya S. Science 285:895-898(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH LIMK1 AND LIMK2, INHIBITION BY Y-27632.
[9]	"Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop." Ohashi K., Nagata K., Maekawa M., Ishizaki T., Narumiya S., Mizuno K. J. Biol. Chem. 275:3577-3582(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH LIMK1.
[10]	"Specific activation of LIM kinase 2 via phosphorylation of threonine 505 by ROCK, a Rho-dependent protein kinase." Sumi T., Matsumoto K., Nakamura T. J. Biol. Chem. 276:670-676(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH LIMK2.
[11]	"Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing." Sebbagh M., Renvoize C., Hamelin J., Riche N., Bertoglio J., Breard J. Nat. Cell Biol. 3:346-352(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE BY CASPASE-3, MUTAGENESIS OF ASP-1113, INTERACTION WITH PPP1R12A, FUNCTION.
[12]	"The GTP binding proteins Gem and Rad are negative regulators of the Rho-Rho kinase pathway." Ward Y., Yap S.-F., Ravichandran V., Matsumura F., Ito M., Spinelli B., Kelly K. J. Cell Biol. 157:291-302(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GEM.
[13]	"RhoE binds to ROCK I and inhibits downstream signaling." Riento K., Guasch R.M., Garg R., Jin B., Ridley A.J. Mol. Cell. Biol. 23:4219-4229(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RHOE AND PPP1R12A, SUBCELLULAR LOCATION.
[14]	"Rocks: multifunctional kinases in cell behaviour." Riento K., Ridley A.J. Nat. Rev. Mol. Cell Biol. 4:446-456(2003) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[15]	"Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis." Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I. EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TSG101.
[16]	"ROCK1 phosphorylates and activates zipper-interacting protein kinase." Hagerty L., Weitzel D.H., Chambers J., Fortner C.N., Brush M.H., Loiselle D., Hosoya H., Haystead T.A. J. Biol. Chem. 282:4884-4893(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DAPK3.
[17]	"The diaphanous-related formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing." 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. J. Biol. Chem. 283:27891-27903(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH FHOD1, SUBCELLULAR LOCATION.
[18]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1105, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation." Shao J., Welch W.J., Diprospero N.A., Diamond M.I. Mol. Cell. Biol. 28:5196-5208(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PFN1.
[20]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[21]	"Identification of ROCK1 as an upstream activator of the JIP-3 to JNK signaling axis in response to UVB damage." 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. Sci. Signal. 1:RA14-RA14(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH JIP3.
[22]	"Inhibition of Rho-dependent kinases ROCK I/II activates VEGF-driven retinal neovascularization and sprouting angiogenesis." Kroll J., Epting D., Kern K., Dietz C.T., Feng Y., Hammes H.P., Wieland T., Augustin H.G. Am. J. Physiol. 296:H893-H899(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[23]	"ROCK isoform regulation of myosin phosphatase and contractility in vascular smooth muscle cells." Wang Y., Zheng X.R., Riddick N., Bryden M., Baur W., Zhang X., Surks H.K. Circ. Res. 104:531-540(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PPP1R12A.
[24]	"Distinct roles for ROCK1 and ROCK2 in the regulation of keratinocyte differentiation." Lock F.E., Hotchin N.A. PLoS ONE 4:E8190-E8190(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[25]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1105, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-647, MASS SPECTROMETRY.
[27]	"Morgana/chp-1, a ROCK inhibitor involved in centrosome duplication and tumorigenesis." 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. Dev. Cell 18:486-495(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHORDC1.
[28]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]	"Caspase-activated ROCK-1 allows erythroblast terminal maturation independently of cytokine-induced Rho signaling." 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. Cell Death Differ. 18:678-689(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CLEAVAGE BY CASPASE-3.
[30]	"Rho-kinase/ROCK: A key regulator of the cytoskeleton and cell polarity." Amano M., Nakayama M., Kaibuchi K. Cytoskeleton 67:545-554(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[31]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]	"Structural insights into the interaction of ROCKI with the switch regions of RhoA." Dvorsky R., Blumenstein L., Vetter I.R., Ahmadian M.R. J. Biol. Chem. 279:7098-7104(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 947-1015 IN COMPLEX WITH RHOA.
[33]	"The structure of dimeric ROCK I reveals the mechanism for ligand selectivity." Jacobs M., Hayakawa K., Swenson L., Bellon S., Fleming M., Taslimi P., Doran J. J. Biol. Chem. 281:260-268(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 6-415, SUBUNIT.
[34]	"Patterns of somatic mutation in human cancer genomes." 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. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-108; SER-773; PRO-1112; SER-1193; GLU-1217; GLN-1262 AND ARG-1264.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U43195 mRNA. Translation: AAB02814.1.
EF445027 Genomic DNA. Translation: ACA06069.1.
BC113114 mRNA. Translation: AAI13115.1.
AB208965 mRNA. Translation: BAD92202.1.

IPI

IPI00022542.

PIR

S69211.

RefSeq

NP_005397.1. NM_005406.2.

UniGene

Hs.306307.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1S1C	X-ray	2.60	X/Y	946-1015	[»]
2ESM	X-ray	3.20	A/B	6-415	[»]
2ETK	X-ray	2.96	A/B	6-415	[»]
2ETR	X-ray	2.60	A/B	6-415	[»]
2V55	X-ray	3.70	A/C	1-406	[»]
3D9V	X-ray	3.30	A/B	6-415	[»]
3NCZ	X-ray	3.00	A/B/C/D	6-415	[»]
3NDM	X-ray	3.30	A/B/C/D	6-415	[»]
3O0Z	X-ray	2.33	A/B/C/D	535-700	[»]
3TV7	X-ray	2.75	A/B/C/D	6-415	[»]
3TWJ	X-ray	2.90	A/B/C/D	6-415	[»]
3V8S	X-ray	2.29	A/B/C/D	6-415	[»]

ProteinModelPortal

Q13464.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13464. 2 interactions.

MINT

MINT-1195170.

STRING

9606.ENSP00000382697.

PTM databases

PhosphoSite

Q13464.

Polymorphism databases

DMDM

47605999.

Proteomic databases

PaxDb

Q13464.

PRIDE

Q13464.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000399799; ENSP00000382697; ENSG00000067900.

GeneID

6093.

KEGG

hsa:6093.

UCSC

uc002kte.3. human.

Organism-specific databases

CTD

6093.

GeneCards

GC18M018529.

HGNC

HGNC:10251. ROCK1.

HPA

CAB004562.
HPA007567.
HPA045639.

MIM

601702. gene.

neXtProt

NX_Q13464.

PharmGKB

PA34623.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000017259.

HOVERGEN

HBG053111.

InParanoid

Q13464.

KO

K04514.

OMA

QIEKQCS.

OrthoDB

EOG4C2H8P.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.
epha_fwdpathway. EPHA forward signaling.
ephbfwdpathway. EPHB forward signaling.
avb3_integrin_pathway. Integrins in angiogenesis.
prlsignalingeventspathway. Signaling events mediated by PRL.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
txa2pathway. Thromboxane A2 receptor signaling.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_578. Apoptosis.

Gene expression databases

Bgee

Q13464.

CleanEx

HS_ROCK1.

Genevestigator

Q13464.

Family and domain databases

Gene3D

2.30.29.30. 2 hits.

InterPro

IPR000961. AGC-kinase_C.
IPR011072. HR1_rho-bd.
IPR011009. Kinase-like_dom.
IPR011993. PH_like_dom.
IPR017892. Pkinase_C.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR020684. Rho-assoc_coiled-coil_kin.
IPR015008. Rho-bd_dom.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

PANTHER

PTHR22988:SF3. PTHR22988:SF3. 1 hit.

Pfam

PF02185. HR1. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
PF08912. Rho_Binding. 1 hit.
[Graphical view]

PIRSF

PIRSF037568. Rho_kinase. 1 hit.

SMART

SM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS51285. AGC_KINASE_CTER. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS00479. ZF_DAG_PE_1. False negative.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q13464.

ChEMBL

CHEMBL3231.

EvolutionaryTrace

Q13464.

GenomeRNAi

6093.

NextBio

23695.

PMAP-CutDB

B0YJ91.

SOURCE

Search...

Entry information

Entry name

ROCK1_HUMAN

Accession

Primary (citable) accession number: Q13464
Secondary accession number(s): B0YJ91, Q2KHM4, Q59GZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.