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Q13464 (ROCK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. 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. Interacts with ITGB1BP1 (via N-terminus and PTB domain) 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.34

Subcellular location

Cytoplasm. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole By similarity. Golgi apparatus membrane; Peripheral membrane protein. Cell projectionbleb. Cytoplasmcytoskeleton By similarity. Cell membrane By similarity. Cell projectionlamellipodium By similarity. Cell projectionruffle By similarity. Note: Associated with the mother centriole and an intercentriolar linker. 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 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 processApoptosis
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Golgi apparatus
Membrane
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Zinc-finger
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRho 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: Ensembl

axon guidance

Traceable author statement. Source: Reactome

bleb assembly

Inferred from electronic annotation. Source: Ensembl

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

myoblast migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of angiogenesis

Inferred from mutant phenotype Ref.22. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of focal adhesion assembly

Inferred from sequence or structural similarity. Source: UniProtKB

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 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_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

bleb

Inferred from electronic annotation. Source: UniProtKB-SubCell

centriole

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoskeleton

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine kinase activity

Inferred from direct assay Ref.9Ref.10Ref.19Ref.17Ref.21. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 13541353Rho-associated protein kinase 1
PRO_0000086619

Regions

Domain76 – 338263Protein kinase
Domain341 – 40969AGC-kinase C-terminal
Repeat458 – 54285REM
Domain1118 – 1317200PH
Nucleotide binding82 – 909ATP By similarity
Zinc finger1228 – 128154Phorbol-ester/DAG-type
Region368 – 727360Interaction with FHOD1
Region998 – 101013RHOA binding
Region1115 – 1354240Auto-inhibitory
Coiled coil422 – 612191 Potential
Coiled coil1011 – 110292 Potential
Compositional bias636 – 980345Glu-rich

Sites

Active site1981Proton acceptor By similarity
Binding site1051ATP By similarity
Site1113 – 11142Cleavage; by caspase-3

Amino acid modifications

Modified residue21N-acetylserine Ref.4 Ref.32
Modified residue6471N6-acetyllysine Ref.26
Modified residue11051Phosphoserine Ref.18 Ref.25

Natural variations

Natural variant1081S → N. Ref.35
Corresponds to variant rs55811609 [ dbSNP | Ensembl ].
VAR_041055
Natural variant7731T → S. Ref.35
Corresponds to variant rs45562542 [ dbSNP | Ensembl ].
VAR_041056
Natural variant11121T → P. Ref.35
Corresponds to variant rs35881519 [ dbSNP | Ensembl ].
VAR_041057
Natural variant11931P → S in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.35
VAR_041058
Natural variant12171Q → E. Ref.35
Corresponds to variant rs2847092 [ dbSNP | Ensembl ].
VAR_041059
Natural variant12621R → Q. Ref.35
Corresponds to variant rs1045142 [ dbSNP | Ensembl ].
VAR_041060
Natural variant12641C → R. Ref.35
Corresponds to variant rs2663698 [ dbSNP | Ensembl ].
VAR_041061

Experimental info

Mutagenesis11131D → A: Abolishes cleavage by caspase-3. Ref.11
Sequence conflict1701V → A in AAI13115. Ref.3
Sequence conflict1971R → G in AAI13115. Ref.3
Sequence conflict2201C → R in AAI13115. Ref.3
Sequence conflict323 – 3253RLG → GTR in BAD92202. Ref.5
Sequence conflict5211D → N in AAI13115. Ref.3
Sequence conflict9651K → R in AAI13115. Ref.3
Sequence conflict13541S → R in ACA06069. Ref.2

Secondary structure

.......................................................................... 1354
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q13464 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 93078CBB009A6F27

FASTA1,354158,175
        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 

« Hide

References

« Hide '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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[33]"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.
[34]"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.
[35]"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. expand/collapse author list , 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.
PIRS69211.
RefSeqNP_005397.1. NM_005406.2.
UniGeneHs.306307.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S1CX-ray2.60X/Y946-1015[»]
2ESMX-ray3.20A/B6-415[»]
2ETKX-ray2.96A/B6-415[»]
2ETRX-ray2.60A/B6-415[»]
2V55X-ray3.70A/C1-406[»]
3D9VX-ray3.30A/B6-415[»]
3NCZX-ray3.00A/B/C/D6-415[»]
3NDMX-ray3.30A/B/C/D6-415[»]
3O0ZX-ray2.33A/B/C/D535-700[»]
3TV7X-ray2.75A/B/C/D6-415[»]
3TWJX-ray2.90A/B/C/D6-415[»]
3V8SX-ray2.29A/B/C/D6-415[»]
ProteinModelPortalQ13464.
SMRQ13464. Positions 6-402, 535-693, 946-1014, 1119-1288.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112020. 23 interactions.
IntActQ13464. 10 interactions.
MINTMINT-1195170.
STRING9606.ENSP00000382697.

Chemistry

BindingDBQ13464.
ChEMBLCHEMBL3231.
GuidetoPHARMACOLOGY1503.

PTM databases

PhosphoSiteQ13464.

Polymorphism databases

DMDM47605999.

Proteomic databases

PaxDbQ13464.
PRIDEQ13464.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000399799; ENSP00000382697; ENSG00000067900.
GeneID6093.
KEGGhsa:6093.
UCSCuc002kte.3. human.

Organism-specific databases

CTD6093.
GeneCardsGC18M018529.
HGNCHGNC:10251. ROCK1.
HPACAB004562.
HPA007567.
HPA045639.
MIM601702. gene.
neXtProtNX_Q13464.
PharmGKBPA34623.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000017259.
HOVERGENHBG053111.
InParanoidQ13464.
KOK04514.
OMAQIEKQCS.
OrthoDBEOG7DZ8J4.
TreeFamTF313551.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_578. Apoptosis.
SignaLinkQ13464.

Gene expression databases

ArrayExpressQ13464.
BgeeQ13464.
CleanExHS_ROCK1.
GenevestigatorQ13464.

Family and domain databases

Gene3D2.30.29.30. 2 hits.
InterProIPR000961. 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_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]
PANTHERPTHR22988:SF3. PTHR22988:SF3. 1 hit.
PfamPF02185. HR1. 1 hit.
PF00169. PH. 1 hit.
PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
PF08912. Rho_Binding. 1 hit.
[Graphical view]
PIRSFPIRSF037568. Rho_kinase. 1 hit.
SMARTSM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13464.
GeneWikiROCK1.
GenomeRNAi6093.
NextBio23695.
PMAP-CutDBB0YJ91.
PROQ13464.
SOURCESearch...

Entry information

Entry nameROCK1_HUMAN
AccessionPrimary (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: March 19, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM