Sequence of MRCKB_RAT
EC Number:2.7.11.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
ATP + a [protein]-(L-serine/L-threonine) = ADP + a [protein]-(L-serine/L-threonine) phosphate
Other sequences found for EC No. 2.7.11.1
General information:
Sequence
0 MSAKVRLKKL EQLLLDGPWR NESSLSVETL LDVLVCLYTE CSHSALRRDK YVAEFLEWAK
60 PFTQLVKDMQ LHREDFEIIK VIGRGAFGEV AVVKMKNTER IYAMKILNKW EMLKRAETAC
120 FREERDVLVN GDCQWITALH YAFQDENYLY LVMDYYVGGD LLTLLSKFED KLPEDMARFY
180 IGEMVLAIDS IHQLHYVHRD IKPDNVLLDV NGHIRLADFG SCLKMNDDGT VQSSVAVGTP
240 DYISPEILQA MEDGMGKYGP ECDWWSLGVC MYEMLYGETP FYAESLVETY GKIMNHEERF
300 QFPSHVTDVS EEAKDLIQRL ICSRERRLGQ NGIEDFKKHA FFEGLNWENI RNLEAPYIPD
360 VSSPSDTSNF DVDDDVLRNI EILPPGSHTG FSGLHLPFIG FTFTTESCFS DRGSLKSMIQ
420 SNTLTKDEDV QRDLENSLQI EAYERRIRRL EQEKLELSRK LQESTQTVQS LHGSTRALGN
480 SNRDKEIKRL NEELERMKSK MADSNRLERQ LEDTVTLRQE HEDSTQRLKG LEKQYRLARQ
540 EKEELHKQLV EASERLKSQT KELKDAHQQR KRALQEFSEL NERMAELRSQ KQKVSRQLRD
600 KEEEMEVAMQ KIDSMRQDIR KSEKSRKELE ARLEDAVAEA SKERKLREHS ESFSKQMERE
660 LETLKVKQGG RGPGATLEHQ QEISKIRSEL EKKVLFYEEE LVRREASHVL EVKNVKKEVH
720 ESESHQLALQ KEVLMLKDKL EKSKRERHSE MEEAIGAMKD KYERERAMLF DENKKLTAEN
780 EKLCSFVDKL TAQNRQLEDE LQDLASKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS
840 KMTEELETLR SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVHEELRKV
900 KDTSLAFESK LKESEAKNRE LLEEMQSLKK RMEEKFRADT GLKLPDFQDP IFEYFNTAPL
960 AHDLTFRTSS ASDQETQASK LDLSPSVSVA TSTEQQEDAA RSQQRPSTVP LPNTQALAMA
1020 GPKPKAHQFS IKSFPSPTQC SHCTSLMVGL IRQGYACEVC AFSCHVSCKD SAPQVCPIPP
1080 EQSKRPLGVD VQRGIGTAYK GYVKVPKPTG VKKGWQRAYA VVCDCKLFLY DLPEGKSTQP
1140 GVIASQVLDL RDDEFAVSSV LASDVIHATR RDIPCIFRVT ASLLGSPSKT SSLLILTENE
1200 NEKRKWVGIL EGLQAILHKN RLRSQVVHVA QEAYDSSLPL IKTVLAAAIV DGDRIAVGLE
1260 EGLYVIELTR DVIVRAADCK KVYQIELAPK EKLILLLCGR NHHVHLYPWT SFDGAEASNF
1320 DIKLPETKGC QLIATGTLRK SSSTCLFVAV KRLVLCYEIQ RTKPFHRKFN EIVAPGHVQW
1380 MAMFKDRLCV GYPSGFSLLS IQGDGQPLDL VNPADPSLAF LSQQSFDALC AVELKSEEYL
1440 LCFSHMGLYV DPQGRRSRTQ ELMWPAAPVA CSCSSSHVTV YSEYGVDVFD VRTMEWVQTI
1500 GLRRIRPLNS DGSLNLLGCE PPRLIYFKNK FSGTVLNVPD TSDNSKKQML RTRSKRRFVF
1560 KVPEEERLQQ RREMLRDPEL RSKMISNPTN FNHVAHMGPG DGMQVLMDLP LSAAPTAQEE
1620 KQGPAPTGLP RQLPSRNKPY VSWPSSGGSE PGVPVPLRSM SDPDQDFDKE PDSDSTKHST
1680 PSNSSNPSGP PSPNSPHRSQ LPLEGLDQPA CDA
Download this sequence
Download all sequences for 2.7.11.1
Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
61015
Leung T.,Chen X.-Q.,Tan I.,Manser E.,Lim L.
Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization.
Mol. Cell. Biol.
18
130-140
1998
61017
Tan I.,Yong J.,Dong J.M.,Lim L.,Leung T.
A tripartite complex containing MRCK modulates lamellar actomyosin retrograde flow.
Cell
135
123-136
2008
61018
Huo L.,Wen W.,Wang R.,Kam C.,Xia J.,Feng W.,Zhang M.
Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge controls cell migration.
EMBO J.
30
665-678
2011
61019
Tan I.,Lai J.,Yong J.,Li S.F.,Leung T.
Chelerythrine perturbs lamellar actomyosin filaments by selective inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase.
FEBS Lett.
585
1260-1268
2011
61020
Lundby A.,Secher A.,Lage K.,Nordsborg N.B.,Dmytriyev A.,Lundby C.,Olsen J.V.
Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.
Nat. Commun.
3
876-876
2012
61021
Lee I.C.,Leung T.,Tan I.
Adaptor protein LRAP25 mediates myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) regulation of LIMK1 protein in lamellipodial F-actin dynamics.
J. Biol. Chem.
289
26989-27003
2014