Reviewed, UniProtKB/Swiss-Prot Q13464 (ROCK1_HUMAN)

Names and origin

Protein names

Recommended name:
    Rho-associated protein kinase 1
    EC=2.7.11.1
Alternative name(s):
    Rho-associated, coiled-coil-containing protein kinase 1
    p160 ROCK-1
      Short name=p160ROCK
    Renal carcinoma antigen NY-REN-35

Gene names

Name:

ROCK1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	Phosphorylates and activates DAPK3, which then regulates myosin light chain phosphatase through phosphorylation of MYPT1 thereby regulating the assembly of the actin cytoskeleton, cell migration, invasiveness of tumor cells, smooth muscle contraction and neurite outgrowth. Required for centromere positioning and centromere-dependent exit from mitosis. Necessary for apoptotic membrane blebbing. Ref.1 Ref.6 Ref.9 Ref.11 Ref.15
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Activated by RHOA binding.
Subunit structure	Binds RHOA (activated by GTP). Interacts with ADD1, GEM, RHOB, RHOC, MYLC2B and VIM By similarity. Binds RHOE, PPP1R12A, LIMK1 and LIMK2. Interacts with TSG101. Interacts with DAPK3. Ref.1 Ref.9 Ref.11 Ref.15 Ref.8 Ref.10 Ref.12 Ref.14
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton › centrosome › centriole By similarity. Golgi apparatus membrane; Peripheral membrane protein. Note: Associated with the mother centriole and an intercentriolar linker By similarity. A small proportion is associated with Golgi membranes. Ref.1 Ref.12
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. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.1 Ref.16 Ref.17 Ref.18 Ref.20 Cleaved by caspase-3 during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing.
Miscellaneous	Inhibited by Y-27632.
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	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
Gene Ontology (GO)
Biological process	Rho protein signal transduction Traceable author statement. Source: ProtInc actin cytoskeleton organization Ref.9 Traceable author statement. Source: ProtInc apoptosis Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis Inferred from electronic annotation. Source: InterPro leukocyte tethering or rolling Inferred from direct assay. Source: UniProtKB membrane to membrane docking Inferred from direct assay. Source: UniProtKB protein amino acid phosphorylation Ref.9 Traceable author statement. Source: ProtInc
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW centriole Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Ref.1 Inferred from Experiment. Source: Reactome extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction. Source: IntAct magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-876651,EBI-876651

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

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

455

1

Phosphothreonine Ref.17

Modified residue

456

1

Phosphoserine Ref.17

Modified residue

647

1

N6-acetyllysine Ref.21

Modified residue

1105

1

Phosphoserine Ref.18 Ref.20

Modified residue

1180

1

Phosphothreonine Ref.16

Natural variations

Natural variant

108

1

S → N: dbSNP rs55811609. Ref.23

VAR_041055

Natural variant

773

1

T → S: dbSNP rs45562542. Ref.23

VAR_041056

Natural variant

1112

1

T → P: dbSNP rs35881519. Ref.23

VAR_041057

Natural variant

1193

1

P → S in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.23

VAR_041058

Natural variant

1217

1

Q → E

VAR_041059

Natural variant

1262

1

R → Q

VAR_041060

Natural variant

1264

1

C → R

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

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1354

Helix Strand Turn

Details...

Helix

7 – 19

13

Helix

27 – 39

13

Helix

44 – 47

4

Helix

50 – 69

20

Helix

73 – 75

3

Beta strand

76 – 83

8

Beta strand

90 – 95

6

Turn

96 – 98

3

Beta strand

101 – 108

8

Helix

109 – 113

5

Helix

121 – 130

10

Beta strand

139 – 144

6

Beta strand

146 – 153

8

Helix

161 – 167

7

Helix

172 – 191

20

Turn

201 – 203

3

Beta strand

204 – 206

3

Beta strand

212 – 214

3

Turn

238 – 240

3

Helix

243 – 247

5

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

330 – 333

4

Helix

336 – 338

3

Helix

345 – 350

6

Helix

392 – 394

3

Beta strand

399 – 402

4

Helix

947 – 982

36

Helix

984 – 1011

28

Sequences

	Sequence		Length	Mass (Da)
	Q13464-1 [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: 8617235] [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: 15489334] [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: 9722579] [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: 10508479] [Abstract] Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN. Tissue: Renal cell carcinoma.
[8]	"Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo." Kawano Y., Fukata Y., Oshiro N., Amano M., Nakamura T., Ito M., Matsumura F., Inagaki M., Kaibuchi K. J. Cell Biol. 147:1023-1038(1999) [PubMed: 10579722] [Abstract] Cited for: INTERACTION WITH PPP1R12A.
[9]	"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: 10436159] [Abstract] Cited for: FUNCTION, INTERACTION WITH LIMK1 AND LIMK2, INHIBITION BY Y-27632.
[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: 11018042] [Abstract] Cited for: 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: 11283607] [Abstract] Cited for: CLEAVAGE BY CASP3, MUTAGENESIS OF ASP-1113, INTERACTION WITH PPP1R12A, FUNCTION.
[12]	"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: 12773565] [Abstract] Cited for: INTERACTION WITH RHOE AND PPP1R12A, SUBCELLULAR LOCATION.
[13]	"Rocks: multifunctional kinases in cell behaviour." Riento K., Ridley A.J. Nat. Rev. Mol. Cell Biol. 4:446-456(2003) [PubMed: 12778124] [Abstract] Cited for: REVIEW.
[14]	"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: 17853893] [Abstract] Cited for: INTERACTION WITH TSG101.
[15]	"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: 17158456] [Abstract] Cited for: FUNCTION, INTERACTION WITH DAPK3.
[16]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1180, MASS SPECTROMETRY.
[17]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455 AND SER-456, MASS SPECTROMETRY.
[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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1105, MASS SPECTROMETRY.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1105, MASS SPECTROMETRY. Tissue: T-cell.
[21]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-647, MASS SPECTROMETRY.
[22]	"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: 14660612] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 947-1015 IN COMPLEX WITH RHOA.
[23]	"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: 17344846] [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.

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	[»]

SMR

Q13464. Positions 1119-1204, 1205-1288.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13464. 2 interactions.

STRING

Q13464.

PTM databases

PhosphoSite

Q13464.

Proteomic databases

PRIDE

Q13464.

Genome annotation databases

Ensembl

ENST00000399799; ENSP00000382697; ENSG00000067900; Homo sapiens. [Genome view]

GeneID

6093.

KEGG

hsa:6093.

UCSC

uc002kte.1. human.

Organism-specific databases

CTD

6093.

GeneCards

GC18M016783.
GC18M016787.
GC18P000106.

H-InvDB

HIX0014355.
HIX0039887.

HGNC

HGNC:10251. ROCK1.

HPA

CAB004562.
HPA007567.

MIM

601702. gene.

PharmGKB

PA34623.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12593.

HOGENOM

HBG445047.

HOVERGEN

Q13464.

InParanoid

Q13464.

OMA

RTSSNVD.

OrthoDB

EOG9GQSQW.

PhylomeDB

Q13464.

Enzyme and pathway databases

BRENDA

2.7.11.1. 247.

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_14797. Signaling by GPCR.
REACT_18266. Axon guidance.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

Q13464.

Bgee

Q13464.

CleanEx

HS_ROCK1.

Genevestigator

Q13464.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR000861. HR1-like_rho-bd.
IPR011009. Kinase-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-like.
IPR015751. Rho-assoc_coiled-coil_kinase.
IPR015008. Rho_bd.
IPR017442. Se/Thr_prot_kinase-like_dom.
IPR008271. Ser/Thr_prot_kinase_AS.
IPR002290. Ser/Thr_prot_kinase_dom.
[Graphical view]

Gene3D

G3DSA:1.20.5.730. Rho_bd. 1 hit.

PANTHER

PTHR22988:SF3. Rho_kinase. 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]

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

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Other Resources

BindingDB

Q13464.

NextBio

23695.

SOURCE

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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:	January 19, 2010
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.