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P70335

- ROCK1_MOUSE

UniProt

P70335 - ROCK1_MOUSE

Protein

Rho-associated protein kinase 1

Gene

Rock1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      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. Required for centrosome positioning and centrosome-dependent exit from mitosis. Plays a role in terminal erythroid differentiation. Promotes keratinocyte terminal differentiation By similarity. 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. Involved in osteoblast compaction through the fibronectin fibrillogenesis cell-mediated matrix assembly process, essential for osteoblast mineralization. May regulate closure of the eyelids and ventral body wall by inducing the assembly of actomyosin bundles.By similarity5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    Activated by RHOA binding. Inhibited by Y-27632 By similarity.By similarity

    Sites

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi82 – 909ATPPROSITE-ProRule annotation
    Zinc fingeri1228 – 128356Phorbol-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 serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. actin cytoskeleton organization Source: MGI
    2. apical constriction Source: MGI
    3. apoptotic process Source: UniProtKB-KW
    4. bleb assembly Source: MGI
    5. leukocyte tethering or rolling Source: Ensembl
    6. membrane to membrane docking Source: Ensembl
    7. myoblast migration Source: UniProtKB
    8. negative regulation of angiogenesis Source: Ensembl
    9. negative regulation of neuron apoptotic process Source: MGI
    10. positive regulation of focal adhesion assembly Source: UniProtKB
    11. regulation of actin filament-based process Source: MGI
    12. regulation of keratinocyte differentiation Source: Ensembl
    13. Rho protein signal transduction Source: MGI

    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_204733. G alpha (12/13) signalling events.
    REACT_224460. Apoptotic cleavage of cellular proteins.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho-associated protein kinase 1 (EC:2.7.11.1)
    Alternative name(s):
    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:107927. Rock1.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriole 1 Publication. Golgi apparatus membrane By similarity; Peripheral membrane protein By similarity. Cell projectionbleb By similarity. Cytoplasmcytoskeleton 1 Publication. Cell membrane 1 Publication. Cell projectionlamellipodium 1 Publication. Cell projectionruffle 1 Publication
    Note: Associated with the mother centriole and an intercentriolar linker. A small proportion is associated with Golgi membranes By similarity. 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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Disruption phenotypei

    Mice exhibit both EOB (eyes open at birth) and omphalocele phenotypes as a result of disorganization of actomyosin cables in the eyelid epithelium and defective actin assembly in the umbilical ring.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 13541353Rho-associated protein kinase 1PRO_0000086620Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei1105 – 11051PhosphoserineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP70335.
    PaxDbiP70335.
    PRIDEiP70335.

    PTM databases

    PhosphoSiteiP70335.

    Expressioni

    Tissue specificityi

    Highly expressed in brain, heart, lung, liver, stomach, spleen, kidney, testis, muscle, embryo and placenta.1 Publication

    Gene expression databases

    BgeeiP70335.
    GenevestigatoriP70335.

    Interactioni

    Subunit structurei

    Homodimer By similarity. Interacts with RHOA (activated by GTP), RHOB, RHOC, GEM, MYLC2B, RHOE, PPP1R12A, LIMK1, LIMK2, TSG101, CHORDC1, DAPK3, PFN1 and JIP3 By similarity. Interacts with FHOD1 in a Src-dependent manner By similarity. Interacts with PTEN. Interacts with ITGB1BP1 (via N-terminus and PTB domain).By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Rnd3P615887EBI-989293,EBI-6930266

    Protein-protein interaction databases

    BioGridi202950. 5 interactions.
    IntActiP70335. 4 interactions.
    MINTiMINT-4132852.

    Structurei

    3D structure databases

    ProteinModelPortaliP70335.
    SMRiP70335. Positions 6-402, 542-693, 946-1014, 1119-1288.
    ModBaseiSearch...
    MobiDBiSearch...

    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 FHOD1By similarityAdd
    BLAST
    Regioni998 – 101013RHOA bindingBy similarityAdd
    BLAST
    Regioni1115 – 1354240Auto-inhibitoryBy similarityAdd
    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 – 128356Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117396.
    HOGENOMiHOG000017259.
    HOVERGENiHBG053111.
    InParanoidiP70335.
    KOiK04514.
    OMAiQIEKQCS.
    OrthoDBiEOG7DZ8J4.
    PhylomeDBiP70335.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P70335-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSTGDSFETR FEKIDNLLRD 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 LEEDKGDEET FPIPKAFVGN QLPFVGFTYY 400
    SNRRYLPSAN ASENRSSSNV DKSLQESLQK TIYKLEEQLH NEMQLKDEME 450
    QKCRTSNLKL DKIMKELDEE GNQRRNLESA VSQIEKEKML LQHRINEYQR 500
    KVEQENEKRR NIENEVSTLK DQLEDLRKAS QTSQLANEKL TQLQKQLEEA 550
    NDLLRTESDT AVRLRKSHTE MSKSISQLES LNRELQERNR ILENSKSQAD 600
    KDYYQLQAVL EAERRDRGHD SEMIGDLQAR ITSLQEEVKH LKHNLERVEG 650
    ERKEAQDMLN HSEKEKNNLE IDLNYKLKSI QQRLEQEVNE HKVTKARLTD 700
    KHQSIEEAKS VAMCEMEKKL KEEREAREKA ENRVVETEKQ CSMLDVDLKQ 750
    SQQKLEHLTE NKERMEDEVK NLALQLEQES NKRLLLQNEL KTQAFEADNL 800
    KGLEKQMKQE INTLLEAKRL LEFELAQLTK QYRGNEGQMR ELQDQLEAEQ 850
    YFSTLYKTQV KELKEEIEEK NRENLRKIQE LQSEKETLST QLDLAETKAE 900
    SEQLARGILE EQYFELTQES KKAASRNRQE ITDKDHTVSR LEETNSVLTK 950
    DIEMLRKENE ELNERMRTAE EEYKLKKEEE INNLKAAFEK NISTERTLKT 1000
    QAVNKLAEIM NRKDFKIDRK KANTQDLRKK EKENRKLQLE LNQEREKFNQ 1050
    MVVKHQKELN DMQAQLVEEC THRNELQMQL ASKESDIEQL RAKLLDLSDS 1100
    TSVASFPSAD ETDGNLPESR IEGWLSVPNR GNIKRYGWKK QYVVVSSKKI 1150
    LFYNDEQDKE QSSPSMVLDI DKLFHVRPVT QGDVYRAETE EIPKIFQILY 1200
    ANEGECRKDI EVEPVQQGEK TNFQNHKGHE FIPTLYHFPA NCEACAKPLW 1250
    HVFKPPPALE CRRCHVKCHR DHLDKKEDLI SPCKVSYDVT SARDMLLLAC 1300
    SQDEQKKWVT HLVKKIPKNP PSGFVRASPR TLSTRSTANQ SFRKVVKNTS 1350
    GKTS 1354
    Length:1,354
    Mass (Da):158,171
    Last modified:February 1, 1997 - v1
    Checksum:iA1CBD543B831CF96
    GO
    Isoform 2 (identifier: P70335-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         425-425: Missing.

    Note: May be due to a competing donor splice site. No experimental confirmation available.

    Show »
    Length:1,353
    Mass (Da):158,042
    Checksum:i209CACFD07E756CF
    GO

    Sequence cautioni

    The sequence AAH57154.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence BAC34154.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei425 – 4251Missing in isoform 2. 1 PublicationVSP_010448

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58512 mRNA. Translation: AAC53132.1.
    AK050269 mRNA. Translation: BAC34154.1. Different initiation.
    AK085974 mRNA. Translation: BAC39581.1.
    BC057154 mRNA. Translation: AAH57154.1. Sequence problems.
    CCDSiCCDS29053.2. [P70335-1]
    PIRiS74244.
    RefSeqiNP_033097.1. NM_009071.2. [P70335-1]
    XP_006525788.1. XM_006525725.1. [P70335-2]
    UniGeneiMm.6710.

    Genome annotation databases

    EnsembliENSMUST00000067947; ENSMUSP00000069549; ENSMUSG00000024290. [P70335-1]
    GeneIDi19877.
    KEGGimmu:19877.
    UCSCiuc008eaq.1. mouse. [P70335-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U58512 mRNA. Translation: AAC53132.1 .
    AK050269 mRNA. Translation: BAC34154.1 . Different initiation.
    AK085974 mRNA. Translation: BAC39581.1 .
    BC057154 mRNA. Translation: AAH57154.1 . Sequence problems.
    CCDSi CCDS29053.2. [P70335-1 ]
    PIRi S74244.
    RefSeqi NP_033097.1. NM_009071.2. [P70335-1 ]
    XP_006525788.1. XM_006525725.1. [P70335-2 ]
    UniGenei Mm.6710.

    3D structure databases

    ProteinModelPortali P70335.
    SMRi P70335. Positions 6-402, 542-693, 946-1014, 1119-1288.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202950. 5 interactions.
    IntActi P70335. 4 interactions.
    MINTi MINT-4132852.

    PTM databases

    PhosphoSitei P70335.

    Proteomic databases

    MaxQBi P70335.
    PaxDbi P70335.
    PRIDEi P70335.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000067947 ; ENSMUSP00000069549 ; ENSMUSG00000024290 . [P70335-1 ]
    GeneIDi 19877.
    KEGGi mmu:19877.
    UCSCi uc008eaq.1. mouse. [P70335-1 ]

    Organism-specific databases

    CTDi 6093.
    MGIi MGI:107927. Rock1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117396.
    HOGENOMi HOG000017259.
    HOVERGENi HBG053111.
    InParanoidi P70335.
    KOi K04514.
    OMAi QIEKQCS.
    OrthoDBi EOG7DZ8J4.
    PhylomeDBi P70335.
    TreeFami TF313551.

    Enzyme and pathway databases

    Reactomei REACT_204733. G alpha (12/13) signalling events.
    REACT_224460. Apoptotic cleavage of cellular proteins.

    Miscellaneous databases

    ChiTaRSi ROCK1. mouse.
    NextBioi 297366.
    PROi P70335.
    SOURCEi Search...

    Gene expression databases

    Bgeei P70335.
    Genevestigatori P70335.

    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. "ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice."
      Nakagawa O., Fujisawa K., Ishizaki T., Saito Y., Nakao K., Narumiya S.
      FEBS Lett. 392:189-193(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Embryo and Heart.
    2. "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] OF 1-506 (ISOFORM 2).
      Strain: FVB/N.
      Tissue: Mammary gland.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 472-1354.
      Strain: C57BL/6J.
      Tissue: Heart and Liver.
    4. "ROCK-I regulates closure of the eyelids and ventral body wall by inducing assembly of actomyosin bundles."
      Shimizu Y., Thumkeo D., Keel J., Ishizaki T., Oshima H., Oshima M., Noda Y., Matsumura F., Taketo M.M., Narumiya S.
      J. Cell Biol. 168:941-953(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    5. "Integrin cytoplasmic domain-associated protein-1 (ICAP-1) interacts with the ROCK-I kinase at the plasma membrane."
      Stroeken P.J., Alvarez B., Van Rheenen J., Wijnands Y.M., Geerts D., Jalink K., Roos E.
      J. Cell. Physiol. 208:620-628(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGB1BP1, SUBCELLULAR LOCATION.
    6. "Integrin Cytoplasmic domain-Associated Protein-1 (ICAP-1) promotes migration of myoblasts and affects focal adhesions."
      Alvarez B., Stroeken P.J., Edel M.J., Roos E.
      J. Cell. Physiol. 214:474-482(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGB1BP1.
    7. "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.
    8. "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.
    9. "ROCK1 functions as a suppressor of inflammatory cell migration by regulating PTEN phosphorylation and stability."
      Vemula S., Shi J., Hanneman P., Wei L., Kapur R.
      Blood 115:1785-1796(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PTEN.
    10. "Osteoblast mineralization requires beta1 integrin/ICAP-1-dependent fibronectin deposition."
      Brunner M., Millon-Fremillon A., Chevalier G., Nakchbandi I.A., Mosher D., Block M.R., Albiges-Rizo C., Bouvard D.
      J. Cell Biol. 194:307-322(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiROCK1_MOUSE
    AccessioniPrimary (citable) accession number: P70335
    Secondary accession number(s): Q8C3G4, Q8C7H0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: February 1, 1997
    Last modified: October 1, 2014
    This is version 146 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3