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MetaCyc Reaction: 2.7.11.1/2.7.11.12/2.7.11.13/2.7.11.17/2.7.11.21/2.7.11.22

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 2.7.11.1 , 2.7.11.12 , 2.7.11.13 , 2.7.11.17 , 2.7.11.21 , 2.7.11.22

Enzymes and Genes:

Escherichia coli K-12 substr. MG1655 : protein kinase Inferred from experiment : yeaG
serine/threonine protein kinase Inferred from experiment : rdoA
Homo sapiens : MAP kinase-activated protein kinase 2 Inferred from experiment : MAPKAPK2

Supersedes EC numbers: 2.7.1.123, 2.7.1.120, 2.7.1.37

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name for 2.7.11.1: non-specific serine/threonine protein kinase

Enzyme Commission Synonyms for 2.7.11.1: A-kinase, AP50 kinase, ATP-protein transphosphorylase, calcium-dependent protein kinase C, calcium/phospholipid-dependent protein kinase, cAMP-dependent protein kinase, cAMP-dependent protein kinase A, casein kinase, casein kinase (phosphorylating), casein kinase 2, casein kinase I, casein kinase II, cGMP-dependent protein kinase, CK-2, CKI, CKII, cyclic AMP-dependent protein kinase, cyclic AMP-dependent protein kinase A, cyclic monophosphate-dependent protein kinase, cyclic nucleotide-dependent protein kinase, cyclin-dependent kinase, cytidine 3',5'-cyclic monophosphate-responsive protein kinase, dsk1, glycogen synthase a kinase, glycogen synthase kinase, HIPK2, Hpr kinase, hydroxyalkyl-protein kinase, M phase-specific cdc2 kinase, mitogen-activated S6 kinase, p82 kinase, phosphorylase b kinase kinase, PKA, protein glutamyl kinase, protein kinase (phosphorylating), protein kinase A, protein kinase CK2, protein kinase p58, protein phosphokinase, protein serine kinase, protein serine-threonine kinase, protein-aspartyl kinase, protein-cysteine kinase, protein-serine kinase, Prp4 protein kinase, Raf kinase, Raf-1, ribosomal protein S6 kinase II, ribosomal S6 protein kinase, serine kinase, serine protein kinase, serine-specific protein kinase, serine(threonine) protein kinase, serine/threonine protein kinase, STK32, T-antigen kinase, threonine-specific protein kinase, twitchin kinase, type-2 casein kinase, βIIPKC, ε PKC, Wee 1-like kinase, Wee-kinase, WEE1Hu

Enzyme Commission Primary Name for 2.7.11.12: cGMP-dependent protein kinase

Enzyme Commission Synonyms for 2.7.11.12: 3':5'-cyclic GMP-dependent protein kinase, cGMP-dependent protein kinase Iβ, guanosine 3':5'-cyclic monophosphate-dependent protein kinase, PKG, PKG 1α, PKG 1β, PKG II, STK23

Enzyme Commission Primary Name for 2.7.11.13: protein kinase C

Enzyme Commission Synonyms for 2.7.11.13: calcium-dependent protein kinase C, calcium-independent protein kinase C, calcium/phospholipid dependent protein kinase, cPKCα, cPKCβ, cPKCγ, nPKCδ, nPKCε, nPKC, PKC, PKCα, PKCβ, PKCγ, PKCδ, PKCε, PKCζ, Pkc1p, protein kinase Cε, STK24

Enzyme Commission Primary Name for 2.7.11.17: Ca2+/calmodulin-dependent protein kinase

Enzyme Commission Synonyms for 2.7.11.17: ATP:caldesmon O-phosphotransferase, caldesmon kinase, caldesmon kinase (phosphorylating), Ca2+/calmodulin-dependent microtubule-associated protein 2 kinase, Ca2+/calmodulin-dependent protein kinase 1, Ca2+/calmodulin-dependent protein kinase II, Ca2+/calmodulin-dependent protein kinase IV, Ca2+/calmodulin-dependent protein kinase kinase, Ca2+/calmodulin-dependent protein kinase kinase β, calmodulin-dependent kinase II, CaM kinase, CaM kinase II, CAM PKII, CaM-regulated serine/threonine kinase, CaMKI, CaMKII, CaMKIV, CaMKKα, CaMKKβ, microtubule-associated protein 2 kinase, STK20

Enzyme Commission Primary Name for 2.7.11.21: polo kinase

Enzyme Commission Synonyms for 2.7.11.21: Cdc5, Cdc5p, Plk, PLK, Plk1, Plo1, POLO kinase, polo serine-threonine kinase, polo-like kinase, polo-like kinase 1, serine/threonine-specific Drosophila kinase polo, STK21

Enzyme Commission Primary Name for 2.7.11.22: cyclin-dependent kinase

Enzyme Commission Synonyms for 2.7.11.22: Bur1, Bur1 Cdk, Cak1, Cak1p, cdc2, cdc2 kinase, Cdc28p, CDK, cdk-activating kinase, Cdk-activating protein kinase, cdk1, cdk2, Cdk2, cdk3, cdk4, cdk5, cdk6, cdk7, cdk8, cdk9, cyclin A-activated cdc2, cyclin A-activated cdk2, cyclin D-cdk6 kinase, cyclin D-dependent kinase, cyclin E kinase, cyclin-A associated kinase, cyclin-dependent kinase 6, cyclin-dependent kinase-2, cyclin-dependent kinase-4, cyclin-dependent protein kinase activating kinase, cyk, D-type cyclin kinase, nclk, neuronal cdc2-like kinase, PCTAIRE-1, STK25

Taxonomic Range: Fungi , Viridiplantae , Metazoa

Standard Gibbs Free Energy (ΔrG in kcal/mol): -4.544739 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary for 2.7.11.1:
This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. Formerly EC 2.7.1.37.

Enzyme Commission Summary for 2.7.11.12:
cGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyzes the phosphorylation by ATP to specific serine or threonine residues in protein substrates. The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase.

Enzyme Commission Summary for 2.7.11.13:
A family of serine- and threonine-specific protein kinases that depend on lipids for activity. They can be activated by calcium but have a requirement for the second messenger diacylglycerol. Members of this group of enzymes phosphorylate a wide variety of protein targets and are known to be involved in diverse cell signaling pathways. Members of the protein kinase C family also serve as major receptors for phorbol esters, a class of tumor promoters.

Enzyme Commission Summary for 2.7.11.17:
The calcium/calmodulin-dependent protein kinase is a multifunctional serine/threonine kinase with numerous roles in mammalian physiology. A wide range of proteins can act as acceptors, including vimentin, synapsin, glycogen synthase, myosin light-chains and the microtubule associated tau protein. Not identical with EC 2.7.11.18, myosin-light-chain kinase, or EC 2.7.11.26, tau-protein kinase.

Enzyme Commission Summary for 2.7.11.21:
The enzyme associates with the spindle pole during mitosis and is thought to play an important role in the dynamic function of the mitotic spindle during chromosome segregation. The human form of the enzyme, Plk1, does not phosphorylate histone H1, enolase and phosvitin but it can phosphorylate myelin basic protein and microtubule-associated protein MAP-2, although to a lesser extent than casein.

Enzyme Commission Summary for 2.7.11.22:
Activation of cyclin-dependent kinases requires association of the enzyme with a regulatory subunit referred to as a cyclin. It is the sequential activation and inactivation of cyclin-dependent kinases, through the periodic synthesis and destruction of cyclins, that provides the primary means of cell-cycle regulation.

Citations: [Wang01b, Gross97, Takeuchi93, Langan69, Jergil70, Baggio70, Damuni88, Zhao97, RichieJannetta03, Murthy04, Gill76, Brooks98, Lendenfeld98, Valledor00, Parekh00, Jaken90, Gomes00, Iwasa86, Rieker87, Ohmstede89, Matsushita98, Anderson98, Schulman85, Baudier87, Adlersberg87, Mal02, Ngai84, Ikebe90, Mulvihill02, Golsteyn95, Llamazares91, Ohkura03, Pan93, Johnson99, Yee96a]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:2.7.11.1 , BRENDA:EC:2.7.11.12 , BRENDA:EC:2.7.11.13 , BRENDA:EC:2.7.11.17 , BRENDA:EC:2.7.11.21 , BRENDA:EC:2.7.11.22 , ENZYME:EC:2.7.11.1 , ENZYME:EC:2.7.11.12 , ENZYME:EC:2.7.11.13 , ENZYME:EC:2.7.11.17 , ENZYME:EC:2.7.11.21 , ENZYME:EC:2.7.11.22 , IUBMB-ExplorEnz:EC:2.7.11.1 , IUBMB-ExplorEnz:EC:2.7.11.12 , IUBMB-ExplorEnz:EC:2.7.11.13 , IUBMB-ExplorEnz:EC:2.7.11.17 , IUBMB-ExplorEnz:EC:2.7.11.21 , IUBMB-ExplorEnz:EC:2.7.11.22 , UniProt:RELATED-TO:O08815 , UniProt:RELATED-TO:O09433 , UniProt:RELATED-TO:O09434 , UniProt:RELATED-TO:O10416 , UniProt:RELATED-TO:O22411 , UniProt:RELATED-TO:O22412 , UniProt:RELATED-TO:O39305 , UniProt:RELATED-TO:O49120 , UniProt:RELATED-TO:O54874 , UniProt:RELATED-TO:P00513 , UniProt:RELATED-TO:P00514 , UniProt:RELATED-TO:P00515 , UniProt:RELATED-TO:P00516 , UniProt:RELATED-TO:P00517 , UniProt:RELATED-TO:P00531 , UniProt:RELATED-TO:P00532 , UniProt:RELATED-TO:P00536 , UniProt:RELATED-TO:P00537 , UniProt:RELATED-TO:P00538 , UniProt:RELATED-TO:P00539 , UniProt:RELATED-TO:P00540 , UniProt:RELATED-TO:P00546 , UniProt:RELATED-TO:P04049 , UniProt:RELATED-TO:P04413 , UniProt:RELATED-TO:P04551 , UniProt:RELATED-TO:P05131 , UniProt:RELATED-TO:P05132 , UniProt:RELATED-TO:P05207 , UniProt:RELATED-TO:P05383 , UniProt:RELATED-TO:P05986 , UniProt:RELATED-TO:P05987 , UniProt:RELATED-TO:P06244 , UniProt:RELATED-TO:P06245 , UniProt:RELATED-TO:P06493 , UniProt:RELATED-TO:P06803 , UniProt:RELATED-TO:P07278 , UniProt:RELATED-TO:P07331 , UniProt:RELATED-TO:P07802 , UniProt:RELATED-TO:P08018 , UniProt:RELATED-TO:P09251 , UniProt:RELATED-TO:P09456 , UniProt:RELATED-TO:P10421 , UniProt:RELATED-TO:P10533 , UniProt:RELATED-TO:P10644 , UniProt:RELATED-TO:P10650 , UniProt:RELATED-TO:P10741 , UniProt:RELATED-TO:P11309 , UniProt:RELATED-TO:P11440 , UniProt:RELATED-TO:P11802 , UniProt:RELATED-TO:P12367 , UniProt:RELATED-TO:P12368 , UniProt:RELATED-TO:P12369 , UniProt:RELATED-TO:P12370 , UniProt:RELATED-TO:P12849 , UniProt:RELATED-TO:P12965 , UniProt:RELATED-TO:P13287 , UniProt:RELATED-TO:P13861 , UniProt:RELATED-TO:P13863 , UniProt:RELATED-TO:P14619 , UniProt:RELATED-TO:P16892 , UniProt:RELATED-TO:P16905 , UniProt:RELATED-TO:P16913 , UniProt:RELATED-TO:P17612 , UniProt:RELATED-TO:P17613 , UniProt:RELATED-TO:P18265 , UniProt:RELATED-TO:P18431 , UniProt:RELATED-TO:P19026 , UniProt:RELATED-TO:P20505 , UniProt:RELATED-TO:P21136 , UniProt:RELATED-TO:P21137 , UniProt:RELATED-TO:P21901 , UniProt:RELATED-TO:P22612 , UniProt:RELATED-TO:P22694 , UniProt:RELATED-TO:P23298 , UniProt:RELATED-TO:P23437 , UniProt:RELATED-TO:P24033 , UniProt:RELATED-TO:P24100 , UniProt:RELATED-TO:P24256 , UniProt:RELATED-TO:P24923 , UniProt:RELATED-TO:P24941 , UniProt:RELATED-TO:P25321 , UniProt:RELATED-TO:P25859 , UniProt:RELATED-TO:P26794 , UniProt:RELATED-TO:P27361 , UniProt:RELATED-TO:P27704 , UniProt:RELATED-TO:P27791 , UniProt:RELATED-TO:P27966 , UniProt:RELATED-TO:P28482 , UniProt:RELATED-TO:P28926 , UniProt:RELATED-TO:P29618 , UniProt:RELATED-TO:P29619 , UniProt:RELATED-TO:P29620 , UniProt:RELATED-TO:P30285 , UniProt:RELATED-TO:P30625 , UniProt:RELATED-TO:P31319 , UniProt:RELATED-TO:P31320 , UniProt:RELATED-TO:P31322 , UniProt:RELATED-TO:P31323 , UniProt:RELATED-TO:P31324 , UniProt:RELATED-TO:P31749 , UniProt:RELATED-TO:P31750 , UniProt:RELATED-TO:P31751 , UniProt:RELATED-TO:P32023 , UniProt:RELATED-TO:P32516 , UniProt:RELATED-TO:P32593 , UniProt:RELATED-TO:P33800 , UniProt:RELATED-TO:P34099 , UniProt:RELATED-TO:P34100 , UniProt:RELATED-TO:P34112 , UniProt:RELATED-TO:P34117 , UniProt:RELATED-TO:P34556 , UniProt:RELATED-TO:P35426 , UniProt:RELATED-TO:P35567 , UniProt:RELATED-TO:P36507 , UniProt:RELATED-TO:P36887 , UniProt:RELATED-TO:P36897 , UniProt:RELATED-TO:P38937 , UniProt:RELATED-TO:P38973 , UniProt:RELATED-TO:P39134 , UniProt:RELATED-TO:P39951 , UniProt:RELATED-TO:P40376 , UniProt:RELATED-TO:P41720 , UniProt:RELATED-TO:P43063 , UniProt:RELATED-TO:P43450 , UniProt:RELATED-TO:P47196 , UniProt:RELATED-TO:P47197 , UniProt:RELATED-TO:P48609 , UniProt:RELATED-TO:P49615 , UniProt:RELATED-TO:P49673 , UniProt:RELATED-TO:P50530 , UniProt:RELATED-TO:P50750 , UniProt:RELATED-TO:P51136 ... [75 more not displayed]


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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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