Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O75116

- ROCK2_HUMAN

UniProt

O75116 - ROCK2_HUMAN

Protein

Rho-associated protein kinase 2

Gene

ROCK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 4 (24 Nov 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca2+ sensitivity and vascular contractility by modulating the myosin light chain phosphorylation.8 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 sitei121 – 1211ATPPROSITE-ProRule annotation
    Active sitei214 – 2141Proton acceptorPROSITE-ProRule annotation
    Sitei1131 – 11322Cleavage; by granzyme B

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi98 – 1069ATPPROSITE-ProRule annotation
    Zinc fingeri1260 – 131556Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein serine/threonine kinase activity Source: UniProtKB
    6. structural molecule activity Source: ProtInc

    GO - Biological processi

    1. actin cytoskeleton organization Source: Ensembl
    2. axon guidance Source: Reactome
    3. centrosome duplication Source: UniProtKB
    4. cytokinesis Source: ProtInc
    5. extrinsic apoptotic signaling pathway via death domain receptors Source: Ensembl
    6. intracellular signal transduction Source: InterPro
    7. negative regulation of angiogenesis Source: UniProtKB
    8. neural tube closure Source: Ensembl
    9. positive regulation of centrosome duplication Source: Ensembl
    10. protein phosphorylation Source: UniProtKB
    11. regulation of actin cytoskeleton organization Source: UniProtKB
    12. regulation of cell adhesion Source: UniProtKB
    13. regulation of cell motility Source: UniProtKB
    14. regulation of circadian rhythm Source: UniProtKB
    15. regulation of establishment of cell polarity Source: UniProtKB
    16. regulation of focal adhesion assembly Source: UniProtKB
    17. regulation of keratinocyte differentiation Source: UniProtKB
    18. regulation of stress fiber assembly Source: UniProtKB
    19. rhythmic process Source: UniProtKB-KW
    20. smooth muscle contraction Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Biological rhythms

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_18407. G alpha (12/13) signalling events.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.
    SignaLinkiO75116.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rho-associated protein kinase 2 (EC:2.7.11.1)
    Alternative name(s):
    Rho kinase 2
    Rho-associated, coiled-coil-containing protein kinase 2
    Rho-associated, coiled-coil-containing protein kinase II
    Short name:
    ROCK-II
    p164 ROCK-2
    Gene namesi
    Name:ROCK2
    Synonyms:KIAA0619
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:10252. ROCK2.

    Subcellular locationi

    Cytoplasm. Cell membrane By similarity; Peripheral membrane protein By similarity. Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
    Note: Cytoplasmic, and associated with actin microfilaments and the plasma membrane.By similarity

    GO - Cellular componenti

    1. centrosome Source: UniProtKB
    2. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    3. cytosol Source: Reactome
    4. nucleus Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB-SubCell
    6. spindle pole centrosome Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1131 – 11311D → A: Abolishes cleavage by granzyme B. 1 Publication

    Organism-specific databases

    PharmGKBiPA34624.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13881388Rho-associated protein kinase 2PRO_0000086625Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei414 – 4141Phosphothreonine; by ROCK2By similarity
    Modified residuei722 – 7221Phosphotyrosine; by SRC2 Publications
    Modified residuei1137 – 11371Phosphoserine5 Publications

    Post-translational modificationi

    Phosphorylation at Tyr-722 reduces its binding to RHOA and is crucial for focal adhesion dynamics. Dephosphorylation by PTPN11 stimulates its RHOA binding activity.7 Publications
    Cleaved by granzyme B during apoptosis. This leads to constitutive activation of the kinase and membrane blebbing.

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75116.
    PaxDbiO75116.
    PRIDEiO75116.

    PTM databases

    PhosphoSiteiO75116.

    Expressioni

    Gene expression databases

    ArrayExpressiO75116.
    BgeeiO75116.
    CleanExiHS_ROCK2.
    GenevestigatoriO75116.

    Organism-specific databases

    HPAiCAB008666.
    HPA007459.
    HPA044109.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with IRS1, RHOB and RHOC By similarity. Interacts with RHOA (activated by GTP), PPP1R12A, CHORDC1, SORL1, EP300 and BRCA2. Interacts with NPM1 and this interaction enhances its activity. Interacts with RAF1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi114860. 15 interactions.
    IntActiO75116. 8 interactions.
    MINTiMINT-4299744.
    STRINGi9606.ENSP00000317985.

    Structurei

    Secondary structure

    1
    1388
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi29 – 357
    Helixi43 – 5715
    Helixi60 – 634
    Helixi66 – 8520
    Helixi89 – 913
    Beta strandi92 – 1009
    Beta strandi102 – 11110
    Turni112 – 1143
    Beta strandi117 – 1248
    Helixi125 – 1306
    Helixi138 – 1469
    Beta strandi155 – 1606
    Beta strandi162 – 1698
    Helixi177 – 1837
    Helixi188 – 20720
    Helixi217 – 2193
    Beta strandi220 – 2223
    Beta strandi228 – 2303
    Beta strandi241 – 2466
    Helixi254 – 2563
    Helixi259 – 2646
    Beta strandi270 – 2723
    Helixi274 – 28916
    Helixi299 – 3079
    Helixi309 – 3124
    Helixi323 – 33210
    Helixi336 – 3383
    Turni340 – 3434
    Helixi346 – 3494
    Helixi352 – 3543
    Turni361 – 3633
    Helixi364 – 3663
    Helixi408 – 4103

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4L6QX-ray2.79A/B19-417[»]
    ProteinModelPortaliO75116.
    SMRiO75116. Positions 27-417, 559-709, 979-1045, 1151-1351.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini92 – 354263Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini357 – 42569AGC-kinase C-terminalAdd
    BLAST
    Repeati475 – 55985REMAdd
    BLAST
    Domaini1150 – 1349200PHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni363 – 784422Interaction with PPP1R12AAdd
    BLAST
    Regioni373 – 42048Interaction with NPM1Add
    BLAST
    Regioni979 – 104769RHOA bindingBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili429 – 1024596Sequence AnalysisAdd
    BLAST
    Coiled coili1053 – 113179Sequence AnalysisAdd
    BLAST

    Domaini

    An interaction between Thr-414 and Asp-48 is essential for kinase activity and dimerization.By similarity

    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 fingeri1260 – 131556Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000017259.
    HOVERGENiHBG053111.
    KOiK17388.
    OMAiNQSIRRP.
    OrthoDBiEOG7DZ8J4.
    PhylomeDBiO75116.
    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.
    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.
    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.

    O75116-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRPPPTGKM PGAPETAPGD GAGASRQRKL EALIRDPRSP INVESLLDGL     50
    NSLVLDLDFP ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR 100
    GAFGEVQLVR HKASQKVYAM KLLSKFEMIK RSDSAFFWEE RDIMAFANSP 150
    WVVQLFYAFQ DDRYLYMVME YMPGGDLVNL MSNYDVPEKW AKFYTAEVVL 200
    ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD ETGMVHCDTA 250
    VGTPDYISPE VLKSQGGDGF YGRECDWWSV GVFLYEMLVG DTPFYADSLV 300
    GTYSKIMDHK NSLCFPEDAE ISKHAKNLIC AFLTDREVRL GRNGVEEIRQ 350
    HPFFKNDQWH WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP 400
    KAFVGNQLPF IGFTYYRENL LLSDSPSCRE TDSIQSRKNE ESQEIQKKLY 450
    TLEEHLSNEM QAKEELEQKC KSVNTRLEKT AKELEEEITL RKSVESALRQ 500
    LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL EDLKKRNQNS 550
    QISTEKVNQL QRQLDETNAL LRTESDTAAR LRKTQAESSK QIQQLESNNR 600
    DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRICG 650
    LEEDLKNGKI LLAKVELEKR QLQERFTDLE KEKSNMEIDM TYQLKVIQQS 700
    LEQEEAEHKA TKARLADKNK IYESIEEAKS EAMKEMEKKL LEERTLKQKV 750
    ENLLLEAEKR CSLLDCDLKQ SQQKINELLK QKDVLNEDVR NLTLKIEQET 800
    QKRCLTQNDL KMQTQQVNTL KMSEKQLKQE NNHLMEMKMN LEKQNAELRK 850
    ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEECEEK TKLGKELQQK 900
    KQELQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI 950
    KEMMARHKQE LTEKDATIAS LEETNRTLTS DVANLANEKE ELNNKLKDVQ 1000
    EQLSRLKDEE ISAAAIKAQF EKQLLTERTL KTQAVNKLAE IMNRKEPVKR 1050
    GNDTDVRRKE KENRKLHMEL KSEREKLTQQ MIKYQKELNE MQAQIAEESQ 1100
    IRIELQMTLD SKDSDIEQLR SQLQALHIGL DSSSIGSGPG DAEADDGFPE 1150
    SRLEGWLSLP VRNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL 1200
    DIDKLFHVRP VTQTDVYRAD AKEIPRIFQI LYANEGESKK EQEFPVEPVG 1250
    EKSNYICHKG HEFIPTLYHF PTNCEACMKP LWHMFKPPPA LECRRCHIKC 1300
    HKDHMDKKEE IIAPCKVYYD ISTAKNLLLL ANSTEEQQKW VSRLVKKIPK 1350
    KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR QLAPNKPS 1388
    Length:1,388
    Mass (Da):160,900
    Last modified:November 24, 2009 - v4
    Checksum:i876240F410C2487E
    GO

    Sequence cautioni

    The sequence BAA31594.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAX93049.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 831R → K in BAA75636. (PubMed:9933571)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti431 – 4311T → N.3 Publications
    Corresponds to variant rs2230774 [ dbSNP | Ensembl ].
    VAR_041062
    Natural varianti601 – 6011D → V.1 Publication
    Corresponds to variant rs35768389 [ dbSNP | Ensembl ].
    VAR_041063
    Natural varianti1083 – 10831K → M.
    Corresponds to variant rs34945852 [ dbSNP | Ensembl ].
    VAR_057110
    Natural varianti1194 – 11941S → P in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_041064

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87931 mRNA. Translation: BAA75636.1.
    AB014519 mRNA. Translation: BAA31594.2. Different initiation.
    AC018463 Genomic DNA. Translation: AAX93049.1. Sequence problems.
    AC099344 Genomic DNA. Translation: AAY14825.1.
    CCDSiCCDS42654.1.
    RefSeqiNP_004841.2. NM_004850.3.
    UniGeneiHs.681743.

    Genome annotation databases

    EnsembliENST00000315872; ENSP00000317985; ENSG00000134318.
    GeneIDi9475.
    KEGGihsa:9475.
    UCSCiuc002rbd.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D87931 mRNA. Translation: BAA75636.1 .
    AB014519 mRNA. Translation: BAA31594.2 . Different initiation.
    AC018463 Genomic DNA. Translation: AAX93049.1 . Sequence problems.
    AC099344 Genomic DNA. Translation: AAY14825.1 .
    CCDSi CCDS42654.1.
    RefSeqi NP_004841.2. NM_004850.3.
    UniGenei Hs.681743.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4L6Q X-ray 2.79 A/B 19-417 [» ]
    ProteinModelPortali O75116.
    SMRi O75116. Positions 27-417, 559-709, 979-1045, 1151-1351.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114860. 15 interactions.
    IntActi O75116. 8 interactions.
    MINTi MINT-4299744.
    STRINGi 9606.ENSP00000317985.

    Chemistry

    ChEMBLi CHEMBL2111459.
    GuidetoPHARMACOLOGYi 1504.

    PTM databases

    PhosphoSitei O75116.

    Proteomic databases

    MaxQBi O75116.
    PaxDbi O75116.
    PRIDEi O75116.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315872 ; ENSP00000317985 ; ENSG00000134318 .
    GeneIDi 9475.
    KEGGi hsa:9475.
    UCSCi uc002rbd.1. human.

    Organism-specific databases

    CTDi 9475.
    GeneCardsi GC02M011272.
    H-InvDB HIX0001828.
    HGNCi HGNC:10252. ROCK2.
    HPAi CAB008666.
    HPA007459.
    HPA044109.
    MIMi 604002. gene.
    neXtProti NX_O75116.
    PharmGKBi PA34624.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000017259.
    HOVERGENi HBG053111.
    KOi K17388.
    OMAi NQSIRRP.
    OrthoDBi EOG7DZ8J4.
    PhylomeDBi O75116.
    TreeFami TF313551.

    Enzyme and pathway databases

    Reactomei REACT_18407. G alpha (12/13) signalling events.
    REACT_19277. Sema4D induced cell migration and growth-cone collapse.
    SignaLinki O75116.

    Miscellaneous databases

    GenomeRNAii 9475.
    NextBioi 35508.
    PROi O75116.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75116.
    Bgeei O75116.
    CleanExi HS_ROCK2.
    Genevestigatori O75116.

    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.
    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.
    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. "Localization of the gene coding for ROCK II/Rho kinase on human chromosome 2p24."
      Takahashi N., Tuiki H., Saya H., Kaibuchi K.
      Genomics 55:235-237(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ASN-431.
      Tissue: Brain.
    2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-431.
      Tissue: Brain.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PPP1R12A.
    5. "Direct cleavage of ROCK II by granzyme B induces target cell membrane blebbing in a caspase-independent manner."
      Sebbagh M., Hamelin J., Bertoglio J., Solary E., Breard J.
      J. Exp. Med. 201:465-471(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE BY GRANZYME B, MUTAGENESIS OF ASP-1131, FUNCTION.
    6. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EP300.
    7. "Interaction between ROCK II and nucleophosmin/B23 in the regulation of centrosome duplication."
      Ma Z., Kanai M., Kawamura K., Kaibuchi K., Ye K., Fukasawa K.
      Mol. Cell. Biol. 26:9016-9034(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NPM1.
    8. "Regulation of RhoA-dependent ROCKII activation by Shp2."
      Lee H.H., Chang Z.F.
      J. Cell Biol. 181:999-1012(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-722, DEPHOSPHORYLATION.
    9. "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-1137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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.
    12. "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.
    13. "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-1137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. Cited for: INTERACTION WITH CHORDC1.
    15. "Src-dependent phosphorylation of ROCK participates in regulation of focal adhesion dynamics."
      Lee H.H., Tien S.C., Jou T.S., Chang Y.C., Jhong J.G., Chang Z.F.
      J. Cell Sci. 123:3368-3377(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-722.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "BRCA2 and nucleophosmin coregulate centrosome amplification and form a complex with the Rho effector kinase ROCK2."
      Wang H.F., Takenaka K., Nakanishi A., Miki Y.
      Cancer Res. 71:68-77(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BRCA2.
    19. "Rho kinase II phosphorylation of the lipoprotein receptor LR11/SORLA alters amyloid-beta production."
      Herskowitz J.H., Seyfried N.T., Gearing M., Kahn R.A., Peng J., Levey A.I., Lah J.J.
      J. Biol. Chem. 286:6117-6127(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SORL1.
    20. "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.
    21. "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.
    22. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASN-431; VAL-601 AND PRO-1194.

    Entry informationi

    Entry nameiROCK2_HUMAN
    AccessioniPrimary (citable) accession number: O75116
    Secondary accession number(s): Q53QZ0, Q53SJ7, Q9UQN5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 149 of the entry and version 4 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, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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