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Q13464

- ROCK1_HUMAN

UniProt

Q13464 - ROCK1_HUMAN

Protein

Rho-associated protein kinase 1

Gene

ROCK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    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.14 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activated by RHOA binding. Inhibited by Y-27632.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei105 – 1051ATPPROSITE-ProRule annotation
    Active sitei198 – 1981Proton acceptorPROSITE-ProRule annotation
    Sitei1113 – 11142Cleavage; by caspase-3

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi82 – 909ATPPROSITE-ProRule annotation
    Zinc fingeri1228 – 128154Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. protein kinase activity Source: ProtInc
    5. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: ProtInc
    2. apical constriction Source: Ensembl
    3. apoptotic process Source: Reactome
    4. axon guidance Source: Reactome
    5. bleb assembly Source: Ensembl
    6. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    7. leukocyte cell-cell adhesion Source: BHF-UCL
    8. leukocyte migration Source: BHF-UCL
    9. leukocyte tethering or rolling Source: BHF-UCL
    10. membrane to membrane docking Source: BHF-UCL
    11. myoblast migration Source: UniProtKB
    12. negative regulation of angiogenesis Source: UniProtKB
    13. negative regulation of neuron apoptotic process Source: Ensembl
    14. positive regulation of focal adhesion assembly Source: UniProtKB
    15. protein phosphorylation Source: ProtInc
    16. regulation of actin cytoskeleton organization Source: UniProtKB
    17. regulation of cell adhesion Source: UniProtKB
    18. regulation of cell motility Source: UniProtKB
    19. regulation of establishment of cell polarity Source: UniProtKB
    20. regulation of focal adhesion assembly Source: UniProtKB
    21. regulation of keratinocyte differentiation Source: UniProtKB
    22. regulation of stress fiber assembly Source: UniProtKB
    23. Rho protein signal transduction Source: ProtInc
    24. signal transduction Source: ProtInc
    25. smooth muscle contraction Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.
    SignaLinkiQ13464.

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:ROCK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:10251. ROCK1.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. bleb Source: UniProtKB-SubCell
    2. centriole Source: UniProtKB-SubCell
    3. cytoskeleton Source: UniProtKB
    4. cytosol Source: Reactome
    5. Golgi membrane Source: UniProtKB-SubCell
    6. lamellipodium Source: UniProtKB
    7. plasma membrane Source: UniProtKB
    8. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1113 – 11131D → A: Abolishes cleavage by caspase-3. 1 Publication

    Organism-specific databases

    PharmGKBiPA34623.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 13541353Rho-associated protein kinase 1PRO_0000086619Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei647 – 6471N6-acetyllysine1 Publication
    Modified residuei1105 – 11051Phosphoserine3 Publications

    Post-translational modificationi

    Autophosphorylated on serine and threonine residues.3 Publications
    Cleaved by caspase-3 during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing.

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ13464.
    PaxDbiQ13464.
    PRIDEiQ13464.

    PTM databases

    PhosphoSiteiQ13464.

    Miscellaneous databases

    PMAP-CutDBB0YJ91.

    Expressioni

    Tissue specificityi

    Detected in blood platelets.1 Publication

    Gene expression databases

    ArrayExpressiQ13464.
    BgeeiQ13464.
    CleanExiHS_ROCK1.
    GenevestigatoriQ13464.

    Organism-specific databases

    HPAiCAB004562.
    HPA007567.
    HPA045639.

    Interactioni

    Subunit structurei

    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.By similarity16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MYBPHQ132032EBI-876651,EBI-5655165
    RHOAP615864EBI-876651,EBI-446668
    TSG101Q998164EBI-876651,EBI-346882

    Protein-protein interaction databases

    BioGridi112020. 23 interactions.
    IntActiQ13464. 10 interactions.
    MINTiMINT-1195170.
    STRINGi9606.ENSP00000382697.

    Structurei

    Secondary structure

    1
    1354
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 1911
    Helixi27 – 4115
    Helixi44 – 474
    Helixi50 – 6920
    Helixi73 – 753
    Beta strandi76 – 849
    Beta strandi86 – 9510
    Turni96 – 983
    Beta strandi101 – 1088
    Helixi109 – 1146
    Helixi121 – 13010
    Beta strandi139 – 1446
    Beta strandi146 – 1538
    Beta strandi157 – 1604
    Helixi161 – 1677
    Helixi172 – 19120
    Helixi201 – 2033
    Beta strandi204 – 2063
    Beta strandi212 – 2143
    Beta strandi227 – 2304
    Helixi238 – 2403
    Helixi243 – 2475
    Turni248 – 2525
    Beta strandi254 – 2563
    Helixi258 – 27316
    Helixi283 – 2919
    Helixi293 – 2964
    Helixi307 – 31610
    Helixi320 – 3223
    Turni324 – 3274
    Helixi329 – 3335
    Helixi336 – 3383
    Turni345 – 3473
    Helixi348 – 3503
    Helixi365 – 3673
    Helixi392 – 3943
    Beta strandi399 – 4024
    Helixi544 – 691148
    Helixi840 – 90263
    Helixi947 – 98236
    Helixi984 – 101128

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1S1CX-ray2.60X/Y947-1015[»]
    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[»]
    4L2WX-ray2.49A/B/C/D834-914[»]
    ProteinModelPortaliQ13464.
    SMRiQ13464. Positions 6-402, 535-693, 946-1014, 1119-1288.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13464.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini76 – 338263Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini341 – 40969AGC-kinase C-terminalAdd
    BLAST
    Repeati458 – 54285REMAdd
    BLAST
    Domaini1118 – 1317200PHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni368 – 727360Interaction with FHOD1Add
    BLAST
    Regioni998 – 101013RHOA bindingAdd
    BLAST
    Regioni1115 – 1354240Auto-inhibitoryAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili422 – 612191Sequence AnalysisAdd
    BLAST
    Coiled coili1011 – 110292Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi636 – 980345Glu-richAdd
    BLAST

    Domaini

    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.

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 REM (Hr1) repeat.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1228 – 128154Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000017259.
    HOVERGENiHBG053111.
    InParanoidiQ13464.
    KOiK04514.
    OMAiQIEKQCS.
    OrthoDBiEOG7DZ8J4.
    PhylomeDBiQ13464.
    TreeFamiTF313551.

    Family and domain databases

    Gene3Di2.30.29.30. 2 hits.
    InterProiIPR000961. AGC-kinase_C.
    IPR011072. HR1_rho-bd.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR017892. Pkinase_C.
    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]
    PfamiPF02185. HR1. 1 hit.
    PF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    PF08912. Rho_Binding. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037568. Rho_kinase. 1 hit.
    SMARTiSM00109. C1. 1 hit.
    SM00233. PH. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. 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]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q13464-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTGDSFETR FEKMDNLLRD PKSEVNSDCL LDGLDALVYD LDFPALRKNK     50
    NIDNFLSRYK DTINKIRDLR MKAEDYEVVK VIGRGAFGEV QLVRHKSTRK 100
    VYAMKLLSKF EMIKRSDSAF FWEERDIMAF ANSPWVVQLF YAFQDDRYLY 150
    MVMEYMPGGD LVNLMSNYDV PEKWARFYTA EVVLALDAIH SMGFIHRDVK 200
    PDNMLLDKSG HLKLADFGTC MKMNKEGMVR CDTAVGTPDY ISPEVLKSQG 250
    GDGYYGRECD WWSVGVFLYE MLVGDTPFYA DSLVGTYSKI MNHKNSLTFP 300
    DDNDISKEAK NLICAFLTDR EVRLGRNGVE EIKRHLFFKN DQWAWETLRD 350
    TVAPVVPDLS SDIDTSNFDD LEEDKGEEET FPIPKAFVGN QLPFVGFTYY 400
    SNRRYLSSAN PNDNRTSSNA DKSLQESLQK TIYKLEEQLH NEMQLKDEME 450
    QKCRTSNIKL DKIMKELDEE GNQRRNLEST VSQIEKEKML LQHRINEYQR 500
    KAEQENEKRR NVENEVSTLK DQLEDLKKVS QNSQLANEKL SQLQKQLEEA 550
    NDLLRTESDT AVRLRKSHTE MSKSISQLES LNRELQERNR ILENSKSQTD 600
    KDYYQLQAIL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLEKVEG 650
    ERKEAQDMLN HSEKEKNNLE IDLNYKLKSL QQRLEQEVNE HKVTKARLTD 700
    KHQSIEEAKS VAMCEMEKKL KEEREAREKA ENRVVQIEKQ CSMLDVDLKQ 750
    SQQKLEHLTG NKERMEDEVK NLTLQLEQES NKRLLLQNEL KTQAFEADNL 800
    KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR ELQDQLEAEQ 850
    YFSTLYKTQV KELKEEIEEK NRENLKKIQE LQNEKETLAT QLDLAETKAE 900
    SEQLARGLLE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEEANSMLTK 950
    DIEILRRENE ELTEKMKKAE EEYKLEKEEE ISNLKAAFEK NINTERTLKT 1000
    QAVNKLAEIM NRKDFKIDRK KANTQDLRKK EKENRKLQLE LNQEREKFNQ 1050
    MVVKHQKELN DMQAQLVEEC AHRNELQMQL ASKESDIEQL RAKLLDLSDS 1100
    TSVASFPSAD ETDGNLPESR IEGWLSVPNR GNIKRYGWKK QYVVVSSKKI 1150
    LFYNDEQDKE QSNPSMVLDI DKLFHVRPVT QGDVYRAETE EIPKIFQILY 1200
    ANEGECRKDV EMEPVQQAEK TNFQNHKGHE FIPTLYHFPA NCDACAKPLW 1250
    HVFKPPPALE CRRCHVKCHR DHLDKKEDLI CPCKVSYDVT SARDMLLLAC 1300
    SQDEQKKWVT HLVKKIPKNP PSGFVRASPR TLSTRSTANQ SFRKVVKNTS 1350
    GKTS 1354
    Length:1,354
    Mass (Da):158,175
    Last modified:November 1, 1996 - v1
    Checksum:i93078CBB009A6F27
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti170 – 1701V → A in AAI13115. (PubMed:15489334)Curated
    Sequence conflicti197 – 1971R → G in AAI13115. (PubMed:15489334)Curated
    Sequence conflicti220 – 2201C → R in AAI13115. (PubMed:15489334)Curated
    Sequence conflicti323 – 3253RLG → GTR in BAD92202. 1 PublicationCurated
    Sequence conflicti521 – 5211D → N in AAI13115. (PubMed:15489334)Curated
    Sequence conflicti965 – 9651K → R in AAI13115. (PubMed:15489334)Curated
    Sequence conflicti1354 – 13541S → R in ACA06069. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti108 – 1081S → N.1 Publication
    Corresponds to variant rs55811609 [ dbSNP | Ensembl ].
    VAR_041055
    Natural varianti773 – 7731T → S.1 Publication
    Corresponds to variant rs45562542 [ dbSNP | Ensembl ].
    VAR_041056
    Natural varianti1112 – 11121T → P.1 Publication
    Corresponds to variant rs35881519 [ dbSNP | Ensembl ].
    VAR_041057
    Natural varianti1193 – 11931P → S in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
    VAR_041058
    Natural varianti1217 – 12171Q → E.1 Publication
    Corresponds to variant rs2847092 [ dbSNP | Ensembl ].
    VAR_041059
    Natural varianti1262 – 12621R → Q.1 Publication
    Corresponds to variant rs1045142 [ dbSNP | Ensembl ].
    VAR_041060
    Natural varianti1264 – 12641C → R.1 Publication
    Corresponds to variant rs2663698 [ dbSNP | Ensembl ].
    VAR_041061

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43195 mRNA. Translation: AAB02814.1.
    EF445027 Genomic DNA. Translation: ACA06069.1.
    BC113114 mRNA. Translation: AAI13115.1.
    AB208965 mRNA. Translation: BAD92202.1.
    CCDSiCCDS11870.2.
    PIRiS69211.
    RefSeqiNP_005397.1. NM_005406.2.
    UniGeneiHs.306307.

    Genome annotation databases

    EnsembliENST00000399799; ENSP00000382697; ENSG00000067900.
    GeneIDi6093.
    KEGGihsa:6093.
    UCSCiuc002kte.3. human.

    Polymorphism databases

    DMDMi47605999.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43195 mRNA. Translation: AAB02814.1 .
    EF445027 Genomic DNA. Translation: ACA06069.1 .
    BC113114 mRNA. Translation: AAI13115.1 .
    AB208965 mRNA. Translation: BAD92202.1 .
    CCDSi CCDS11870.2.
    PIRi S69211.
    RefSeqi NP_005397.1. NM_005406.2.
    UniGenei Hs.306307.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1S1C X-ray 2.60 X/Y 947-1015 [» ]
    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 [» ]
    4L2W X-ray 2.49 A/B/C/D 834-914 [» ]
    ProteinModelPortali Q13464.
    SMRi Q13464. Positions 6-402, 535-693, 946-1014, 1119-1288.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112020. 23 interactions.
    IntActi Q13464. 10 interactions.
    MINTi MINT-1195170.
    STRINGi 9606.ENSP00000382697.

    Chemistry

    BindingDBi Q13464.
    ChEMBLi CHEMBL3231.
    GuidetoPHARMACOLOGYi 1503.

    PTM databases

    PhosphoSitei Q13464.

    Polymorphism databases

    DMDMi 47605999.

    Proteomic databases

    MaxQBi Q13464.
    PaxDbi Q13464.
    PRIDEi Q13464.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000399799 ; ENSP00000382697 ; ENSG00000067900 .
    GeneIDi 6093.
    KEGGi hsa:6093.
    UCSCi uc002kte.3. human.

    Organism-specific databases

    CTDi 6093.
    GeneCardsi GC18M018529.
    HGNCi HGNC:10251. ROCK1.
    HPAi CAB004562.
    HPA007567.
    HPA045639.
    MIMi 601702. gene.
    neXtProti NX_Q13464.
    PharmGKBi PA34623.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000017259.
    HOVERGENi HBG053111.
    InParanoidi Q13464.
    KOi K04514.
    OMAi QIEKQCS.
    OrthoDBi EOG7DZ8J4.
    PhylomeDBi Q13464.
    TreeFami TF313551.

    Enzyme and pathway databases

    Reactomei REACT_107. Apoptotic cleavage of cellular proteins.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.
    SignaLinki Q13464.

    Miscellaneous databases

    EvolutionaryTracei Q13464.
    GeneWikii ROCK1.
    GenomeRNAii 6093.
    NextBioi 23695.
    PMAP-CutDB B0YJ91.
    PROi Q13464.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13464.
    Bgeei Q13464.
    CleanExi HS_ROCK1.
    Genevestigatori Q13464.

    Family and domain databases

    Gene3Di 2.30.29.30. 2 hits.
    InterProi IPR000961. AGC-kinase_C.
    IPR011072. HR1_rho-bd.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR017892. Pkinase_C.
    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 ]
    Pfami PF02185. HR1. 1 hit.
    PF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    PF08912. Rho_Binding. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037568. Rho_kinase. 1 hit.
    SMARTi SM00109. C1. 1 hit.
    SM00233. PH. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi 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.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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, IDENTIFICATION BY 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. 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. 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. 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. Cited for: INTERACTION WITH CHORDC1.
    28. 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. 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.
      , 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.

    Entry informationi

    Entry nameiROCK1_HUMAN
    AccessioniPrimary (citable) accession number: Q13464
    Secondary accession number(s): B0YJ91, Q2KHM4, Q59GZ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 153 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3