Gene Information
Gene Symbol
Entrez Gene ID
Gene Name
MAPK interacting serine/threonine kinase 2
Chromosomal Location
This gene encodes a member of the calcium/calmodulin-dependent protein kinases (CAMK) Ser/Thr protein kinase family, which belongs to the protein kinase superfamily. This protein contains conserved DLG (asp-leu-gly) and ENIL (glu-asn-ile-leu) motifs, and an N-terminal polybasic region which binds importin A and the translation factor scaffold protein eukaryotic initiation factor 4G (eIF4G). This protein is one of the downstream kinases activated by mitogen-activated protein (MAP) kinases. It phosphorylates the eukaryotic initiation factor 4E (eIF4E), thus playing important roles in the initiation of mRNA translation, oncogenic transformation and malignant cell proliferation. In addition to eIF4E, this protein also interacts with von Hippel-Lindau tumor suppressor (VHL), ring-box 1 (Rbx1) and Cullin2 (Cul2), which are all components of the CBC(VHL) ubiquitin ligase E3 complex. Multiple alternatively spliced transcript variants have been found, but the full-length nature and biological activity of only two variants are determined. These two variants encode distinct isoforms which differ in activity and regulation, and in subcellular localization. [provided by RefSeq, Aug 2011]
RefSeq DNA
RefSeq mRNA

Gene Ontology (GO)

GO ID Ontology Function Evidence Reference
GO:0006468 Biological process Protein phosphorylation IDA 11463832
GO:0007166 Biological process Cell surface receptor signaling pathway TAS 8415712
GO:0018105 Biological process Peptidyl-serine phosphorylation IBA 21873635
GO:0030097 Biological process Hemopoiesis IDA 21149447
GO:0035556 Biological process Intracellular signal transduction IBA 21873635
Protein Information
Protein Name
MAP kinase-interacting serine/threonine-protein kinase 2, G protein-coupled receptor kinase 7, MAP kinase interacting serine/threonine kinase 2, MAP kinase signal-integrating kinase 2, MAPK signal-integrating kinase 2
Serine/threonine-protein kinase that phosphorylates SFPQ/PSF, HNRNPA1 and EIF4E. May play a role in the response to environmental stress and cytokines. Appears to regulate translation by phosphorylating EIF4E, thus increasing the affinity of this protein for the 7-methylguanosine-containing mRNA cap. Required for mediating PP2A-inhibition-induced EIF4E phosphorylation. Triggers EIF4E shuttling from cytoplasm to nucleus. Isoform 1 displays a high basal kinase activity, but isoform 2 exhibits a very low kinase activity. Acts as a mediator of the suppressive effects of IFNgamma on hematopoiesis. Negative regulator for signals that control generation of arsenic trioxide As(2)O(3)-dependent apoptosis and anti-leukemic responses. Involved in anti-apoptotic signaling in response to serum withdrawal.
Refseq Proteins
Pfam Accession Pfam ID
PF00069 Pkinase

MAPK signaling pathway
HIF-1 signaling pathway
Insulin signaling pathway


ENSP00000263681 Q15054 Q15054
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Associated Diseases

Disease groupDisease NameReferences
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
Cleft upper lip
Endocrine System Diseases

Natalizumab-Related Progressive Multifocal Leukoencephalopathy in Multiple Sclerosis: Findings from an Italian Independent Registry.

Prosperini Luca, de Rossi Nicola, Scarpazza Cristina, Moiola Lucia, Cosottini Mirco, Gerevini Simonetta, Capra Ruggero
Dept. of Neurology and Psychiatry, Sapienza University, Viale Dell'Universita, Rome, Italy.| Multiple Sclerosis Centre, Spedali Civili di Brescia, Via Ciotti, Montichiari, Brescia, Italy.| Multiple Sclerosis Centre, Spedali Civili di Brescia, Via Ciotti, Montichiari, Brescia, Italy.| Dept. of Neurology, San Raffaele Scientific Institute, Via Olgettina, Milan, Italy.| Dept. of Translational Research and New Surgical and Medical Technologies, University of Pisa, Via Paradisa, Pisa, Italy.| Dept. of Neuroradiology, San Raffaele Scientific Institute, Vita-Salute San Raffaele University, Via Olgettina, Milan, Italy.| Multiple Sclerosis Centre, Spedali Civili di Brescia, Via Ciotti, Montichiari, Brescia, Italy.
PLoS One. 2016 Dec 20;11(12):e0168376. doi: 10.1371/journal.pone.0168376.

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