Sequence of KPCB_RAT
EC Number:2.7.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
Other sequences found for EC No. 2.7.1
EC Number:2.7.1.107
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate
Other sequences found for EC No. 2.7.1.107
EC Number:2.7.11.13
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. 2.7.11.13
General information:
Sequence
0 MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC SHCTDFIWGF
60 GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS KHKFKIHTYS SPTFCDHCGS
120 LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL CGTDHTERRG RIYIQAHIDR EVLIVVVRDA
180 KNLVPMDPNG LSDPYVKLKL IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL
240 SVEIWDWDLT SRNDFMGSLS FGISELQKAG VDGWFKLLSQ EEGEYFNVPV PPEGSEGNEE
300 LRQKFERAKI GQGTKAPEEK TANTISKFDN NGNRDRMKLT DFNFLMVLGK GSFGKVMLSE
360 RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP PFLTQLHSCF QTMDRLYFVM
420 EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI
480 KIADFGMCKE NIWDGVTTKT FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP
540 FEGEDEDELF QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF
600 RYIDWEKLER KEIQPPYKPK ARDKRDTSNF DKEFTRQPVE LTPTDKLFIM NLDQNEFAGF
660 SYTNPEFVIN V
Download this sequence
in fasta formatDownload all sequences for 2.7.11.13
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
180712
Knopf J.L.,Lee M.-H.,Sultzman L.A.,Kriz R.W.,Loomis C.R.,Hewick R.M.,Bell R.M.
Cloning and expression of multiple protein kinase C cDNAs.
Cell
46
491-502
1986
180713
Ono Y.,Kurokawa T.,Fujii T.,Kawahara K.,Igarashi K.,Kikkawa U.,Ogita K.,Nishizuka Y.
Two types of complementary DNAs of rat brain protein kinase C. Heterogeneity determined by alternative splicing.
FEBS Lett.
206
347-352
1986
180714
Housey G.M.,Johnson M.D.,Hsiao W.L.W.,O'Brian C.A.,Murphy J.P.,Kirschmeier P.,Weinstein I.B.
Overproduction of protein kinase C causes disordered growth control in rat fibroblasts.
Cell
52
343-354
1988
180715
Ono Y.,Kurokawa T.,Kawahara K.,Nishimura O.,Marumoto R.,Igarashi K.,Sugino Y.,Kikkawa U.,Ogita K.,Nishizuka Y.
Cloning of rat brain protein kinase C complementary DNA.
FEBS Lett.
203
111-115
1986
180716
Housey G.M.,O'Brian C.A.,Johnson M.D.,Kirschmeier P.,Weinstein I.B.
Isolation of cDNA clones encoding protein kinase C: evidence for a protein kinase C-related gene family.
Proc. Natl. Acad. Sci. U.S.A.
84
1065-1069
1987
180717
Keranen L.M.,Dutil E.M.,Newton A.C.
Protein kinase C is regulated in vivo by three functionally distinct phosphorylations.
Curr. Biol.
5
1394-1403
1995
180718
Zhang J.,Wang L.,Petrin J.,Bishop W.R.,Bond R.W.
Characterization of site-specific mutants altered at protein kinase C beta 1 isozyme autophosphorylation sites.
Proc. Natl. Acad. Sci. U.S.A.
90
6130-6134
1993
180719
Zhang J.,Wang L.,Schwartz J.,Bond R.W.,Bishop W.R.
Phosphorylation of Thr642 is an early event in the processing of newly synthesized protein kinase C beta 1 and is essential for its activation.
J. Biol. Chem.
269
19578-19584
1994
180720
Orr J.W.,Newton A.C.
Requirement for negative charge on 'activation loop' of protein kinase C.
J. Biol. Chem.
269
27715-27718
1994
180721
Formisano P.,Oriente F.,Fiory F.,Caruso M.,Miele C.,Maitan M.A.,Andreozzi F.,Vigliotta G.,Condorelli G.,Beguinot F.
Insulin-activated protein kinase Cbeta bypasses Ras and stimulates mitogen-activated protein kinase activity and cell proliferation in muscle cells.
Mol. Cell. Biol.
20
6323-6333
2000
180722
Kaneto H.,Suzuma K.,Sharma A.,Bonner-Weir S.,King G.L.,Weir G.C.
Involvement of protein kinase C beta 2 in c-myc induction by high glucose in pancreatic beta-cells.
J. Biol. Chem.
277
3680-3685
2002
180723
Yamasaki T.,Takahashi A.,Pan J.,Yamaguchi N.,Yokoyama K.K.
Phosphorylation of activation transcription factor-2 at serine 121 by protein kinase c controls c-Jun-mediated activation of transcription.
J. Biol. Chem.
284
8567-8581
2009
180724
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
180725
Sutton R.B.,Sprang S.R.
Structure of the protein kinase Cbeta phospholipid-binding C2 domain complexed with Ca2+.
Structure
6
1395-1405
1998
180726
Leonard T.A.,Rozycki B.,Saidi L.F.,Hummer G.,Hurley J.H.
Crystal structure and allosteric activation of protein kinase C betaII.
Cell
144
55-66
2011
