Sequence of MRCKA_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 MSGEVRLRQL EQFILDGPAQ TNGQCFSVET LLDILICLYD ECNNSPLRRE KNILEYLEWA
60 KPFTSKVKQM RLHREDFEIL KVIGRGAFGE VAVVKLKNAD KVFAMKILNK WEMLKRAETA
120 CFREERDVLV NGDSKWITTL HYAFQDDNNL YLVMDYYVGG DLLTLLSKFE DRLPEEMARF
180 YLAEMVIAID SVHQLHYVHR DIKPDNILMD MNGHIRLADF GSCLKLMEDG TVQSSVAVGT
240 PDYISPEILQ AMEDGKGRYG PECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKER
300 FQFPTQVTDV SENAKDLIRR LICSREHRLG QNGIEDFKKH PFFSGIDWDN IRNCEAPYIP
360 EVSSPTDTSN FDVDDDCLKN SETMPPPTHT AFSGHHLPFV GFTYTSSCVL SDRSCLRVTA
420 GPTSLDLDVN VQRTLDNNLA TEAYERRIKR LEQEKLELTR KLQESTQTVQ ALQYSTVDGP
480 LTASKDLEIK SLKEEIEKLR KQVAEVNHLE QQLEEANSVR RELDDAFRQI KAFEKQIKTL
540 QQEREELNKE LVQASERLKN QSKELKDAHC QRKLAMQEFM EINERLTELH TQKQKLARHV
600 RDKEEEVDLV MQKAESLRQE LRRAERAKKE LEVHTEALIA EASKDRKLRE QSRHYSKQLE
660 NELEGLKQKQ ISYSPGICSI EHQQEITKLK TDLEKKSIFY EEEISKREGI HASEIKNLKK
720 ELHDSEGQQL ALNKEIMVLK DKLEKTRRES QSEREEFENE FKQQYEREKV LLTEENKKLT
780 SELDKLTSLY ESLSLRNQHL EEEVKDLADK KESVAHWEAQ ITEIIQWVSD EKDARGYLQA
840 LASKMTEELE ALRNSSLGTR ATDMPWKMRR FAKLDMSARL ELQSALDAEI RAKQAIQEEL
900 NKVKASNIIT ECKLKDSEKK NLELLSEIEQ LIKDTEELRS EKGVEHRDSQ HSFLAFLNTP
960 TDALDQFERS PSCTPAGKGR RIADSAPLPV HTPTLRKKGC PASAGFPPKR KTHQFFVKSF
1020 TAPTKCHQCT SLMVGLIRQG CSCEVCGFSC HITCVNKAPT TCPVPPEQTK GPLGIDPQKG
1080 VGTAYEGHVR IPKPAGVKKG WQRALAVVCD FKLFLYDIAE GKASQPSSVI SQVIDMRDEE
1140 FSVSSVLASD VIHASRKDIP CIFRVTASQL SAPSDKCSIL MLADSETERS KWVGVLSELH
1200 KVLKKNKFRD RSVYVPKEAY DSTLPLIKTT QAAAIIDHER VALGNEEGLF VVHVTKDEII
1260 RVGDNKKIHQ IELIPSDQLV AVISGRNRHV RLFPMSALDG RETDFYKLAE TKGCQTIAAG
1320 KVRHGALSCL CVAMKRQVLC YELFQSKTRH RKFKEIQVPC NVQWMAIFSE HLCVGFQSGF
1380 LRYPLNGEGS PCNMLHSNDH TLAFITHQPM DAICAVEISN KEYLLCFSSI GIYTDCQGRR
1440 SRQQELMWPA NPSSCCYNAP YLSIYSENAV DIFDVNSMEW IQTLPLKKVR PLNTEGSLNL
1500 LGLETIRLIY FKNKMAEGDE LVVPETSDNS RKQMVRNINN KRRYSFRVPE EERMQQRREM
1560 LRDPEMRNKL ISNPTNFNHI AHMGPGDGIQ ILKDLPMNPR PQESRTVFSG SVSIPSITKS
1620 RPEPGRSMSA SSGLSARSSA QNGSALKREF SGGSYNTKRQ PMPSPSEGSL SSGGVDQGSD
1680 APVRDYDGED SDSPRHSTAS NSSNLSSPPS PVSPRKTKSL SLESTDRGSW DP
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
60974
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
60975
Tan I.,Seow K.T.,Lim L.,Leung T.
Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase alpha.
Mol. Cell. Biol.
21
2767-2778
2001
60976
Tan I.,Cheong A.,Lim L.,Leung T.
Genomic organization of human myotonic dystrophy kinase-related Cdc42-binding kinase alpha reveals multiple alternative splicing and functional diversity.
Gene
304
107-115
2003
60977
Hoffert J.D.,Pisitkun T.,Wang G.,Shen R.-F.,Knepper M.A.
Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites.
Proc. Natl. Acad. Sci. U.S.A.
103
7159-7164
2006
60978
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
60979
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
60980
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
60981
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
