Sequence of MK03_RAT
EC Number:2.7.11.24
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. 2.7.11.24
General information:
Sequence
0 MAAAAAAPGG GGGEPRGTAG VVPVVPGEVE VVKGQPFDVG PRYTQLQYIG EGAYGMVSSA
60 YDHVRKTRVA IKKISPFEHQ TYCQRTLREI QILLRFRHEN VIGIRDILRA PTLEAMRDVY
120 IVQDLMETDL YKLLKSQQLS NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLINTTCD
180 LKICDFGLAR IADPEHDHTG FLTEYVATRW YRAPEIMLNS KGYTKSIDIW SVGCILAEML
240 SNRPIFPGKH YLDQLNHILG ILGSPSQEDL NCIINMKARN YLQSLPSKTK VAWAKLFPKS
300 DSKALDLLDR MLTFNPNKRI TVEEALAHPY LEQYYDPTDE PVAEEPFTFD MELDDLPKER
360 LKELIFQETA RFQPGAPEAP
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1214109
Marquardt B.,Stabel S.
Sequence of a rat cDNA encoding the ERK1-MAP kinase.
Gene
120
297-299
1992
1214113
Boulton T.G.,Yancopoulos G.D.,Gregory J.S.,Slaughter C.,Moomaw C.,Hsu J.,Cobb M.H.
An insulin-stimulated protein kinase similar to yeast kinases involved in cell cycle control.
Science
249
64-67
1990
1214114
de Miguel C.,Kligman D.,Patel J.,Detera-Wadleigh S.D.
Molecular analysis of microtubule-associated protein-2 kinase cDNA from mouse and rat brain.
DNA Cell Biol.
10
505-514
1991
1214115
Boulton T.G.,Gregory J.S.,Cobb M.H.
Purification and properties of extracellular signal-regulated kinase 1, an insulin-stimulated microtubule-associated protein 2 kinase.
Biochemistry
30
278-286
1991
1214116
Yung Y.,Yao Z.,Hanoch T.,Seger R.
ERK1b, a 46-kDa ERK isoform that is differentially regulated by MEK.
J. Biol. Chem.
275
15799-15808
2000
1214117
Yin G.,Zheng Q.,Yan C.,Berk B.C.
GIT1 is a scaffold for ERK1/2 activation in focal adhesions.
J. Biol. Chem.
280
27705-27712
2005
1214119
Seger R.,Ahn N.G.,Boulton T.G.,Yancopoulos G.D.,Panayotatos N.,Radziejewska E.,Ericsson L.,Bratlien R.L.,Cobb M.H.,Krebs E.G.
Microtubule-associated protein 2 kinases, ERK1 and ERK2, undergo autophosphorylation on both tyrosine and threonine residues: implications for their mechanism of activation.
Proc. Natl. Acad. Sci. U.S.A.
88
6142-6146
1991
1214120
Lin T.-A.,Kong X.,Haystead T.A.J.,Pause A.,Belsham G.J.,Sonenberg N.,Lawrence J.C. Jr.
PHAS-I as a link between mitogen-activated protein kinase and translation initiation.
Science
266
653-656
1994
1214121
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
1214122
Willard F.S.,Willard M.D.,Kimple A.J.,Soundararajan M.,Oestreich E.A.,Li X.,Sowa N.A.,Kimple R.J.,Doyle D.A.,Der C.J.,Zylka M.J.,Snider W.D.,Siderovski D.P.
Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras effector.
PLoS ONE
4
0-0
2009
1214123
Yoon S.,Seger R.
The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions.
Growth Factors
24
21-44
2006
1214124
Yao Z.,Seger R.
The ERK signaling cascade--views from different subcellular compartments.
BioFactors
35
407-416
2009
1214125
Wortzel I.,Seger R.
The ERK cascade: distinct functions within various subcellular organelles.
Genes Cancer
2
195-209
2011
1214126
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
1214127
Ogata T.,Naito D.,Nakanishi N.,Hayashi Y.K.,Taniguchi T.,Miyagawa K.,Hamaoka T.,Maruyama N.,Matoba S.,Ikeda K.,Yamada H.,Oh H.,Ueyama T.
MURC/Cavin-4 facilitates recruitment of ERK to caveolae and concentric cardiac hypertrophy induced by alpha1-adrenergic receptors.
Proc. Natl. Acad. Sci. U.S.A.
111
3811-3816
2014
