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Index > Protein center > Cdc42bpb(Gene name) > Rat
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  • Cdc42bpb (Gene name),
  • Serine/threonine-protein kinase MRCK beta (Protein name ),  MRCKB_RAT from NCBI database.
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  • General Annotation
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  • Gene name:
    Cdc42bpb;
    Protein name:
    Serine/threonine-protein kinase MRCK beta;
    Alternative:
    DMPK-like beta;CDC42-binding protein kinase beta;Myotonic dystrophy kinase-related CDC42-binding kinase beta(MRCK beta;Myotonic dystrophy protein kinase-like beta);
    Organism:
    Rat (Rattus norvegicus). 
    General Annotation
    Sub Unit:
    Homodimer and homotetramer via the coiled coil regions. Interacts tightly with GTP-bound but not GDP-bound CDC42 (By similarity). Interacts with TJP1; this interaction requires the presence of catalytically active CDC42.
    Function:
    Serine/threonine-protein kinase that plays a role in the regulation of cytoskeleton reorganization, cell migration, wound healing and invasion. Acts as a downstream effector of CDC42. Contributes to the actomyosin contractility required for cell invasion, through the regulation of MYPT1 and thus MLC2 phosphorylation.
    Subcellular Location:
    Cytoplasm Cell membrane Peripheral membrane protein Cytoplasmic side Cell junction Displays a dispersed punctate distribution and concentrates along the cell periphery, especially at the leading edge and cell-cell junction. This concentration is PH-domain dependent (By similarity). Detected at the leading edge of migrating and wounded cells; this localization requires the presence of catalytically active CDC42.
    Protein Attributes:
    Sequence length:
    1713
    Sequence:
    50:
    MSAKVRLKKL | EQLLLDGPWR | NESSLSVETL | LDVLVCLYTE | CSHSALRRDK | 
    100:
    YVAEFLEWAK | PFTQLVKDMQ | LHREDFEIIK | VIGRGAFGEV | AVVKMKNTER | 
    150:
    IYAMKILNKW | EMLKRAETAC | FREERDVLVN | GDCQWITALH | YAFQDENYLY | 
    200:
    LVMDYYVGGD | LLTLLSKFED | KLPEDMARFY | IGEMVLAIDS | IHQLHYVHRD | 
    250:
    IKPDNVLLDV | NGHIRLADFG | SCLKMNDDGT | VQSSVAVGTP | DYISPEILQA | 
    300:
    MEDGMGKYGP | ECDWWSLGVC | MYEMLYGETP | FYAESLVETY | GKIMNHEERF | 
    350:
    QFPSHVTDVS | EEAKDLIQRL | ICSRERRLGQ | NGIEDFKKHA | FFEGLNWENI | 
    400:
    RNLEAPYIPD | VSSPSDTSNF | DVDDDVLRNI | EILPPGSHTG | FSGLHLPFIG | 
    450:
    FTFTTESCFS | DRGSLKSMIQ | SNTLTKDEDV | QRDLENSLQI | EAYERRIRRL | 
    500:
    EQEKLELSRK | LQESTQTVQS | LHGSTRALGN | SNRDKEIKRL | NEELERMKSK | 
    550:
    MADSNRLERQ | LEDTVTLRQE | HEDSTQRLKG | LEKQYRLARQ | EKEELHKQLV | 
    600:
    EASERLKSQT | KELKDAHQQR | KRALQEFSEL | NERMAELRSQ | KQKVSRQLRD | 
    650:
    KEEEMEVAMQ | KIDSMRQDIR | KSEKSRKELE | ARLEDAVAEA | SKERKLREHS | 
    700:
    ESFSKQMERE | LETLKVKQGG | RGPGATLEHQ | QEISKIRSEL | EKKVLFYEEE | 
    750:
    LVRREASHVL | EVKNVKKEVH | ESESHQLALQ | KEVLMLKDKL | EKSKRERHSE | 
    800:
    MEEAIGAMKD | KYERERAMLF | DENKKLTAEN | EKLCSFVDKL | TAQNRQLEDE | 
    850:
    LQDLASKKES | VAHWEAQIAE | IIQWVSDEKD | ARGYLQALAS | KMTEELETLR | 
    900:
    SSSLGSRTLD | PLWKVRRSQK | LDMSARLELQ | SALEAEIRAK | QLVHEELRKV | 
    950:
    KDTSLAFESK | LKESEAKNRE | LLEEMQSLKK | RMEEKFRADT | GLKLPDFQDP | 
    1000:
    IFEYFNTAPL | AHDLTFRTSS | ASDQETQASK | LDLSPSVSVA | TSTEQQEDAA | 
    1050:
    RSQQRPSTVP | LPNTQALAMA | GPKPKAHQFS | IKSFPSPTQC | SHCTSLMVGL | 
    1100:
    IRQGYACEVC | AFSCHVSCKD | SAPQVCPIPP | EQSKRPLGVD | VQRGIGTAYK | 
    1150:
    GYVKVPKPTG | VKKGWQRAYA | VVCDCKLFLY | DLPEGKSTQP | GVIASQVLDL | 
    1200:
    RDDEFAVSSV | LASDVIHATR | RDIPCIFRVT | ASLLGSPSKT | SSLLILTENE | 
    1250:
    NEKRKWVGIL | EGLQAILHKN | RLRSQVVHVA | QEAYDSSLPL | IKTVLAAAIV | 
    1300:
    DGDRIAVGLE | EGLYVIELTR | DVIVRAADCK | KVYQIELAPK | EKLILLLCGR | 
    1350:
    NHHVHLYPWT | SFDGAEASNF | DIKLPETKGC | QLIATGTLRK | SSSTCLFVAV | 
    1400:
    KRLVLCYEIQ | RTKPFHRKFN | EIVAPGHVQW | MAMFKDRLCV | GYPSGFSLLS | 
    1450:
    IQGDGQPLDL | VNPADPSLAF | LSQQSFDALC | AVELKSEEYL | LCFSHMGLYV | 
    1500:
    DPQGRRSRTQ | ELMWPAAPVA | CSCSSSHVTV | YSEYGVDVFD | VRTMEWVQTI | 
    1550:
    GLRRIRPLNS | DGSLNLLGCE | PPRLIYFKNK | FSGTVLNVPD | TSDNSKKQML | 
    1600:
    RTRSKRRFVF | KVPEEERLQQ | RREMLRDPEL | RSKMISNPTN | FNHVAHMGPG | 
    1650:
    DGMQVLMDLP | LSAAPTAQEE | KQGPAPTGLP | RQLPSRNKPY | VSWPSSGGSE | 
    1700:
    PGVPVPLRSM | SDPDQDFDKE | PDSDSTKHST | PSNSSNPSGP | PSPNSPHRSQ | 
    1713:
    LPLEGLDQPA | CDA
    3D Structure:
    N/A
    Predicted Eptitope:
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    EIAab Sequence  Vaild Sequence:
    Please Sign in.
    Related Databases
    UniGene:
    SMR:
    String:
    Pfam:
    Uniprot:
     
    FOR
    ELISA Kit for Rat Serine/threonine-protein kinase MRCK beta
    ELISA Kit for Rat Serine/threonine-protein kinase MRCK beta
    ELISA Kit for Rat Serine/threonine-protein kinase MRCK beta
    CLIA Kit for Rat Serine/threonine-protein kinase MRCK beta
    CLIA Kit for Rat Serine/threonine-protein kinase MRCK beta
    CLIA Kit for Rat Serine/threonine-protein kinase MRCK beta
    Polyclonal Antibody for Rat Serine/threonine-protein kinase MRCK beta
    Polyclonal Antibody for Rat Serine/threonine-protein kinase MRCK beta
    Polyclonal Antibody for Rat Serine/threonine-protein kinase MRCK beta
    Monoclonal Antibody for Rat Serine/threonine-protein kinase MRCK beta
    Monoclonal Antibody for Rat Serine/threonine-protein kinase MRCK beta
    Monoclonal Antibody for Rat Serine/threonine-protein kinase MRCK beta
    Protein for Rat Serine/threonine-protein kinase MRCK beta
    Protein for Rat Serine/threonine-protein kinase MRCK beta
    Protein for Rat Serine/threonine-protein kinase MRCK beta

    R&D Technical Data
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    Precision
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    Recovery
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    Linearity
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    References
    1. 1.
      "Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization."
      Leung T. , Chen X.-Q. , Tan I. , Manser E. , Lim L.
      Mol. Cell. Biol.18:130-140(1998) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];TISSUE SPECIFICITY
      tissue: Brain.
    2. 2.
      Huang C.Q. , Wu S.L. , Cheng Z.
      Submitted (2003-04) to the EMBL/GenBank/DDBJ databases
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA]
    3. 3.
      "A tripartite complex containing MRCK modulates lamellar actomyosin retrograde flow."
      Tan I. , Yong J. , Dong J.M. , Lim L. , Leung T.
      Cell135:123-136(2008) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;INTERACTION WITH LURAP1 AND MYO18A
    4. 4.
      "Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge controls cell migration."
      Huo L. , Wen W. , Wang R. , Kam C. , Xia J. , Feng W. , Zhang M.
      EMBO J.30:665-678(2011) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;INTERACTION WITH TJP1;MUTAGENESIS OF PHE-952; TYR-954; LEU-964 AND PHE-966;SUBCELLULAR LOCATION
    5. 5.
      "Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase."
      Tan I. , Lai J. , Yong J. , Li S.F. , Leung T.
      FEBS Lett.585:1260-1268(2011) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION IN PHOSPHORYLATION OF PPP1R12A AND MYL9/MLC2;ENZYME REGULATION
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