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Reviewed, UniProtKB/Swiss-Prot Q13464 (ROCK1_HUMAN)

Last modified January 19, 2010. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Complete 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

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. Cytoplasmcytoskeletoncentrosomecentriole 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 processApoptosis
   Cellular componentCytoplasm
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
Gene Ontology (GO)
   Biological processRho 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 componentGolgi 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 functionATP 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

itself1EBI-876651,EBI-876651

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
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
Modified residue4551Phosphothreonine Ref.17
Modified residue4561Phosphoserine Ref.17
Modified residue6471N6-acetyllysine Ref.21
Modified residue11051Phosphoserine Ref.18 Ref.20
Modified residue11801Phosphothreonine Ref.16

Natural variations

Natural variant1081S → N: dbSNP rs55811609. Ref.23
VAR_041055
Natural variant7731T → S: dbSNP rs45562542. Ref.23
VAR_041056
Natural variant11121T → P: dbSNP rs35881519. Ref.23
VAR_041057
Natural variant11931P → S in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.23
VAR_041058
Natural variant12171Q → E
VAR_041059
Natural variant12621R → Q
VAR_041060
Natural variant12641C → R
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
Q13464-1 [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: 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. 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: 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.
IPIIPI00022542.
PIRS69211.
RefSeqNP_005397.1.
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[»]
SMRQ13464. Positions 1119-1204, 1205-1288.
ModBaseSearch...

Protein-protein interaction databases

IntActQ13464. 2 interactions.
STRINGQ13464.

PTM databases

PhosphoSiteQ13464.

Proteomic databases

PRIDEQ13464.

Genome annotation databases

EnsemblENST00000399799; ENSP00000382697; ENSG00000067900; Homo sapiens. [Genome view]
GeneID6093.
KEGGhsa:6093.
UCSCuc002kte.1. human.

Organism-specific databases

CTD6093.
GeneCardsGC18M016783.
GC18M016787.
GC18P000106.
H-InvDBHIX0014355.
HIX0039887.
HGNCHGNC:10251. ROCK1.
HPACAB004562.
HPA007567.
MIM601702. gene.
PharmGKBPA34623.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12593.
HOGENOMHBG445047.
HOVERGENQ13464.
InParanoidQ13464.
OMARTSSNVD.
OrthoDBEOG9GQSQW.
PhylomeDBQ13464.

Enzyme and pathway databases

BRENDA2.7.11.1. 247.
Pathway_Interaction_DBamb2_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.
ReactomeREACT_14797. Signaling by GPCR.
REACT_18266. Axon guidance.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressQ13464.
BgeeQ13464.
CleanExHS_ROCK1.
GenevestigatorQ13464.

Family and domain databases

InterProIPR000961. 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]
Gene3DG3DSA:1.20.5.730. Rho_bd. 1 hit.
PANTHERPTHR22988:SF3. Rho_kinase. 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]
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.
PS00479. ZF_DAG_PE_1. False negative.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBQ13464.
NextBio23695.
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: January 19, 2010
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 18

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents