Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.12 Dual-specificity kinases (those acting on Ser/Thr and Tyr residues)
ID:2.7.12.2
Description:Mitogen-activated protein kinase kinase.
Alternative Name: MKK.
MEK.
MAPKK.
MAP2K.
MAP kinase kinase.
Prosite: PDOC00100;
PDB:
PDBScop
Cath: 1.10.150.50; 1.10.287.4220; 1.10.510.10; 3.30.200.20; 2.30.30.40; 3.10.20.90;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.12.2
BRENDA Enzyme Link: BRENDA 2.7.12.2
KEGG Enzyme Link: KEGG2.7.12.2
BioCyc Enzyme Link: BioCyc 2.7.12.2
ExPASy Enzyme Link: ExPASy2.7.12.2
EC2PDB Enzyme Link: EC2PDB 2.7.12.2
ExplorEnz Enzyme Link: ExplorEnz 2.7.12.2
PRIAM enzyme-specific profiles Link: PRIAM 2.7.12.2
IntEnz Enzyme Link: IntEnz 2.7.12.2
MEDLINE Enzyme Link: MEDLINE 2.7.12.2
MSA:

2.7.12.2;

Phylogenetic Tree:

2.7.12.2;

Uniprot:
M-CSA:
RHEA:46608 ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily.Jones PF, Jakubowicz T, Pitossi FJ, Maurer F, Hemmings BA1991 May 151851997
Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families.Coffer PJ, Woodgett JR1991 Oct 151718748

RHEA:17989 ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily.Jones PF, Jakubowicz T, Pitossi FJ, Maurer F, Hemmings BA1991 May 151851997
Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families.Coffer PJ, Woodgett JR1991 Oct 151718748

RHEA:10596 ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Molecular characterization of ALK, a receptor tyrosine kinase expressed specifically in the nervous system.Iwahara T, Fujimoto J, Wen D, Cupples R, Bucay N, Arakawa T, Mori S, Ratzkin B, Yamamoto T1997 Jan 309053841
Cloning and biochemical characterization of a plant protein kinase that phosphorylates serine, threonine, and tyrosine.Ali N, Halfter U, Chua NH1994 Dec 167527390
Src protein-tyrosine kinase structure and regulation.Roskoski R Jr2004 Nov 2615504335
dDYRK2: a novel dual-specificity tyrosine-phosphorylation-regulated kinase in Drosophila.Lochhead PA, Sibbet G, Kinstrie R, Cleghon T, Rylatt M, Morrison DK, Cleghon V2003 Sep 112786602
Identification and characterization of DAlk: a novel Drosophila melanogaster RTK which drives ERK activation in vivo.Lorén CE, Scully A, Grabbe C, Edeen PT, Thomas J, McKeown M, Hunter T, Palmer RH2001 Jun11442633
Biochemical characterization and localization of the dual specificity kinase CLK1.Menegay HJ, Myers MP, Moeslein FM, Landreth GE2000 Sep10954422