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MKNK2

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From Wikipedia, the free encyclopedia

Protein-coding gene in the species Homo sapiens

MKNK2

Available structures

PDB

Ortholog search:PDBe RCSB

List of PDB id codes
2AC3,2AC5

Identifiers

Aliases

MKNK2, GPRK7, MNK2, MAP kinase interacting serine/threonine kinase 2, MAPK interacting serine/threonine kinase 2

External IDs

OMIM:605069;MGI:894279;HomoloGene:49674;GeneCards:MKNK2;OMA:MKNK2 - orthologs

Gene location (Human)

Chr.	Chromosome 19 (human)^[1]

Band	19p13.3	Start	2,037,465bp^[1]
Band	19p13.3	End	2,051,244bp^[1]

Gene location (Mouse)

Chr.	Chromosome 10 (mouse)^[2]

Band	10\|10 C1	Start	80,501,161bp^[2]
Band	10\|10 C1	End	80,513,946bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

superior surface of tongue

parotid gland

body of tongue

mucosa of pharynx

amniotic fluid

gastrocnemius muscle

buccal mucosa cell

skin of thigh

tibialis anterior muscle

Skeletal muscle tissue of rectus abdominis

Top expressed in

subcutaneous adipose tissue

brown adipose tissue

temporal muscle

ankle

digastric muscle

white adipose tissue

tunica adventitia of aorta

intercostal muscle

sternocleidomastoid muscle

triceps brachii muscle

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	transferase activity nucleotide binding protein kinase activity calcium-dependent protein serine/threonine kinase activity metal ion binding calmodulin binding kinase activity protein serine/threonine kinase activity protein binding calmodulin-dependent protein kinase activity ATP binding
Cellular component	cytoplasm PML body nuclear body nucleus nucleoplasm
Biological process	intracellular signal transduction phosphorylation protein phosphorylation cell surface receptor signaling pathway cellular response to arsenic-containing substance peptidyl-serine phosphorylation extrinsic apoptotic signaling pathway in absence of ligand protein autophosphorylation regulation of translation apoptotic process hemopoiesis
Sources:Amigo /QuickGO

Orthologs

Species

Human

Mouse

Entrez


2872


17347

Ensembl


ENSG00000099875


ENSMUSG00000020190

UniProt


Q9HBH9


Q8CDB0

RefSeq (mRNA)


NM_199054 NM_017572


NM_021462

RefSeq (protein)


NP_060042 NP_951009


NP_067437

Location (UCSC)

Chr 19: 2.04 – 2.05 Mb

Chr 10: 80.5 – 80.51 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

MAP kinase-interacting serine/threonine-protein kinase 2 is anenzyme that in humans is encoded by theMKNK2gene.^[5]^[6]

Interactions

[edit]

MNK2 has been shown tointeract withMAPK1^[7]^[8] andEukaryotic translation initiation factor 4 gamma.^[7]

MNK2 has been identified as a therapeutic target fordiabetes. Specifically, blocking MNK2 interaction with eIF4G has been shown to boost protein synthesis and promotebeta cell regeneration.^[9]

References

[edit]

^^a ^b ^cGRCh38: Ensembl release 89: ENSG00000099875 –Ensembl, May 2017
^^a ^b ^cGRCm38: Ensembl release 89: ENSMUSG00000020190 –Ensembl, May 2017
^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
^Slentz-Kesler K, Moore JT, Lombard M, Zhang J, Hollingsworth R, Weiner MP (October 2000). "Identification of the human Mnk2 gene (MKNK2) through protein interaction with estrogen receptor beta".Genomics.69 (1):63–71.doi:10.1006/geno.2000.6299.PMID 11013076.
^"Entrez Gene: MKNK2 MAP kinase interacting serine/threonine kinase 2".
^^a ^bScheper GC, Parra JL, Wilson M, Van Kollenburg B, Vertegaal AC, Han ZG, Proud CG (August 2003)."The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization".Molecular and Cellular Biology.23 (16):5692–5705.doi:10.1128/MCB.23.16.5692-5705.2003.PMC 166352.PMID 12897141.
^Waskiewicz AJ, Flynn A, Proud CG, Cooper JA (April 1997)."Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2".The EMBO Journal.16 (8):1909–1920.doi:10.1093/emboj/16.8.1909.PMC 1169794.PMID 9155017.
^Karampelias C, Watt K, Mattsson CL, Ruiz ÁF, Rezanejad H, Mi J, et al. (September 2022)."MNK2 deficiency potentiates β-cell regeneration via translational regulation".Nature Chemical Biology.18 (9):942–953.doi:10.1038/s41589-022-01047-x.PMC 7613404.PMID 35697798.

Haribabu B, Snyderman R (October 1993)."Identification of additional members of human G-protein-coupled receptor kinase multigene family".Proceedings of the National Academy of Sciences of the United States of America.90 (20):9398–9402.Bibcode:1993PNAS...90.9398H.doi:10.1073/pnas.90.20.9398.PMC 47575.PMID 8415712.
Bonaldo MF, Lennon G, Soares MB (September 1996)."Normalization and subtraction: two approaches to facilitate gene discovery".Genome Research.6 (9):791–806.doi:10.1101/gr.6.9.791.PMID 8889548.
Waskiewicz AJ, Flynn A, Proud CG, Cooper JA (April 1997)."Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2".The EMBO Journal.16 (8):1909–1920.doi:10.1093/emboj/16.8.1909.PMC 1169794.PMID 9155017.
Scheper GC, Morrice NA, Kleijn M, Proud CG (February 2001)."The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells".Molecular and Cellular Biology.21 (3):743–754.doi:10.1128/MCB.21.3.743-754.2001.PMC 86666.PMID 11154262.
Knauf U, Tschopp C, Gram H (August 2001)."Negative regulation of protein translation by mitogen-activated protein kinase-interacting kinases 1 and 2".Molecular and Cellular Biology.21 (16):5500–5511.doi:10.1128/MCB.21.16.5500-5511.2001.PMC 87272.PMID 11463832.
Scheper GC, Parra JL, Wilson M, Van Kollenburg B, Vertegaal AC, Han ZG, Proud CG (August 2003)."The N and C termini of the splice variants of the human mitogen-activated protein kinase-interacting kinase Mnk2 determine activity and localization".Molecular and Cellular Biology.23 (16):5692–5705.doi:10.1128/MCB.23.16.5692-5705.2003.PMC 166352.PMID 12897141.
Yoshizuka N, Yoshizuka-Chadani Y, Krishnan V, Zeichner SL (September 2005)."Human immunodeficiency virus type 1 Vpr-dependent cell cycle arrest through a mitogen-activated protein kinase signal transduction pathway".Journal of Virology.79 (17):11366–11381.doi:10.1128/JVI.79.17.11366-11381.2005.PMC 1193619.PMID 16103188.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network".Nature.437 (7062):1173–1178.Bibcode:2005Natur.437.1173R.doi:10.1038/nature04209.PMID 16189514.S2CID 4427026.
Jauch R, Jäkel S, Netter C, Schreiter K, Aicher B, Jäckle H, Wahl MC (October 2005). "Crystal structures of the Mnk2 kinase domain reveal an inhibitory conformation and a zinc binding site".Structure.13 (10):1559–1568.doi:10.1016/j.str.2005.07.013.hdl:11858/00-001M-0000-0010-9408-D.PMID 16216586.
Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, et al. (January 2006)."Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes".Genome Research.16 (1):55–65.doi:10.1101/gr.4039406.PMC 1356129.PMID 16344560.
Wang P, Wang X, Wang F, Cai T, Luo Y (June 2006). "Interaction between Mnk2 and CBC(VHL) ubiquitin ligase E3 complex".Science in China Series C: Life Sciences.49 (3):265–273.doi:10.1007/s11427-006-0265-5.PMID 16856496.S2CID 23339861.

v t e PDB gallery
2ac3: Structure of human Mnk2 Kinase Domain 2ac5: Structure of human Mnk2 Kinase Domain mutant D228G 2hw7: Crystal Structure of Mnk2-D228G in complex with Staurosporine

Kinases:Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated mTOR EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1
Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3 PDK4
Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3
3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB
(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G
(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4
Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase Aurora C kinase
Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10
Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-
IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP
cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY
cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1
Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3
Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase
Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2
G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6
Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK1A CAMK1B CAMK1D CAMK1G CAMK2 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1
Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4
Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2
Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19
Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4
Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1
(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1
Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14
MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14
Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3
(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-
Tropomyosin kinase (EC 2.7.11.28)	-
Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-
Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1Oxidoreductases (list) EC2Transferases (list) EC3Hydrolases (list) EC4Lyases (list) EC5Isomerases (list) EC6Ligases (list) EC7Translocases (list)

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