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MAP kinase-interacting serine/threonine-protein kinase 2 (EC 2.7.11.1) (MAP kinase signal-integrating kinase 2) (MAPK signal-integrating kinase 2) (Mnk2)

 MKNK2_HUMAN             Reviewed;         465 AA.
Q9HBH9; Q6GPI3; Q9HBH8; Q9UHR0; Q9Y2N6;
30-APR-2003, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 3.
25-OCT-2017, entry version 167.
RecName: Full=MAP kinase-interacting serine/threonine-protein kinase 2;
EC=2.7.11.1;
AltName: Full=MAP kinase signal-integrating kinase 2;
Short=MAPK signal-integrating kinase 2;
Short=Mnk2;
Name=MKNK2; Synonyms=GPRK7, MNK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:AAG26336.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), TISSUE
SPECIFICITY, AND INTERACTION WITH ESR2.
TISSUE=Fetal brain;
PubMed=11013076; DOI=10.1006/geno.2000.6299;
Slentz-Kesler K., Moore J.T., Lombard M., Zhang J., Hollingsworth R.,
Weiner M.P.;
"Identification of the human Mnk2 gene (MKNK2) through protein
interaction with estrogen receptor beta.";
Genomics 69:63-71(2000).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Adrenal gland;
Li Y., Shi J., Huang C., Ren S., Fu S., Zhou J., Yu Y., Xu S.,
Wang Y., Fu G., Chen Z., Han Z.;
"A novel gene expressed in human adrenal gland.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION AS EIF4E KINASE, ENZYME REGULATION, ALTERNATIVE SPLICING,
PHOSPHORYLATION BY MAPK1/ERK2; MAPK11 AND MAPK14, AND INTERACTION WITH
EIF4G PROTEINS.
PubMed=11154262; DOI=10.1128/MCB.21.3.743-754.2001;
Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.;
"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.";
Mol. Cell. Biol. 21:743-754(2001).
[6] {ECO:0000305}
FUNCTION, PHOSPHORYLATION AT THR-244; THR-249 AND THR-379, AND
MUTAGENESIS OF THR-244; THR-249 AND THR-379.
TISSUE=Leukocyte;
PubMed=11463832; DOI=10.1128/MCB.21.16.5500-5511.2001;
Knauf U., Tschopp C., Gram H.;
"Negative regulation of protein translation by mitogen-activated
protein kinase-interacting kinases 1 and 2.";
Mol. Cell. Biol. 21:5500-5511(2001).
[7]
FUNCTION AS EIF4E KINASE, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION,
PHOSPHORYLATION, AND INTERACTION WITH EIF4E; EIF4G1 AND EIF4G2.
PubMed=12897141; DOI=10.1128/MCB.23.16.5692-5705.2003;
Scheper G.C., Parra J.L., Wilson M., Van Kollenburg B.,
Vertegaal A.C.O., Han Z.-G., Proud C.G.;
"The N and C termini of the splice variants of the human mitogen-
activated protein kinase-interacting kinase Mnk2 determine activity
and localization.";
Mol. Cell. Biol. 23:5692-5705(2003).
[8]
FUNCTION AS HNRNPA1 KINASE, AND ENZYME REGULATION.
PubMed=16111636; DOI=10.1016/j.immuni.2005.06.009;
Buxade M., Parra J.L., Rousseau S., Shpiro N., Marquez R., Morrice N.,
Bain J., Espel E., Proud C.G.;
"The Mnks are novel components in the control of TNF alpha
biosynthesis and phosphorylate and regulate hnRNP A1.";
Immunity 23:177-189(2005).
[9]
FUNCTION AS SFPQ/PSF KINASE.
PubMed=17965020; DOI=10.1074/jbc.M705286200;
Buxade M., Morrice N., Krebs D.L., Proud C.G.;
"The PSF.p54nrb complex is a novel Mnk substrate that binds the mRNA
for tumor necrosis factor alpha.";
J. Biol. Chem. 283:57-65(2008).
[10]
FUNCTION IN ARSENIC TRIOXIDE SIGNALING, AND PHOSPHORYLATION IN
RESPONSE TO ARSENIC TRIOXIDE.
PubMed=18299328; DOI=10.1074/jbc.M708816200;
Dolniak B., Katsoulidis E., Carayol N., Altman J.K., Redig A.J.,
Tallman M.S., Ueda T., Watanabe-Fukunaga R., Fukunaga R.,
Platanias L.C.;
"Regulation of arsenic trioxide-induced cellular responses by Mnk1 and
Mnk2.";
J. Biol. Chem. 283:12034-12042(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
ENZYME REGULATION.
PubMed=20722422; DOI=10.1021/jm1005513;
Oyarzabal J., Zarich N., Albarran M.I., Palacios I.,
Urbano-Cuadrado M., Mateos G., Reymundo I., Rabal O., Salgado A.,
Corrionero A., Fominaya J., Pastor J., Bischoff J.R.;
"Discovery of mitogen-activated protein kinase-interacting kinase 1
inhibitors by a comprehensive fragment-oriented virtual screening
approach.";
J. Med. Chem. 53:6618-6628(2010).
[15]
FUNCTION AS EIF4E KINASE, AND INTERACTION WITH EIF4G1.
PubMed=20823271; DOI=10.1128/MCB.00448-10;
Shveygert M., Kaiser C., Bradrick S.S., Gromeier M.;
"Regulation of eukaryotic initiation factor 4E (eIF4E) phosphorylation
by mitogen-activated protein kinase occurs through modulation of Mnk1-
eIF4G interaction.";
Mol. Cell. Biol. 30:5160-5167(2010).
[16]
ENZYME REGULATION.
PubMed=20664001; DOI=10.1124/mol.110.064642;
Altman J.K., Glaser H., Sassano A., Joshi S., Ueda T.,
Watanabe-Fukunaga R., Fukunaga R., Tallman M.S., Platanias L.C.;
"Negative regulatory effects of Mnk kinases in the generation of
chemotherapy-induced antileukemic responses.";
Mol. Pharmacol. 78:778-784(2010).
[17]
FUNCTION IN EIF4E PHOSPHORYLATION REGULATION, DEPHOSPHORYLATION BY
PP2A, AND ENZYME REGULATION.
PubMed=20927323; DOI=10.1593/neo.10704;
Li Y., Yue P., Deng X., Ueda T., Fukunaga R., Khuri F.R., Sun S.-Y.;
"Protein phosphatase 2A negatively regulates eukaryotic initiation
factor 4E phosphorylation and eIF4F assembly through direct
dephosphorylation of Mnk and eIF4E.";
Neoplasia 12:848-855(2010).
[18]
FUNCTION IN IFNGAMMA SIGNALING.
PubMed=21149447; DOI=10.1074/jbc.M110.197921;
Joshi S., Sharma B., Kaur S., Majchrzak B., Ueda T., Fukunaga R.,
Verma A.K., Fish E.N., Platanias L.C.;
"Essential role for Mnk kinases in type II interferon (IFNgamma)
signaling and its suppressive effects on normal hematopoiesis.";
J. Biol. Chem. 286:6017-6026(2011).
[19]
REVIEW.
PubMed=18508592; DOI=10.2741/3086;
Buxade M., Parra-Palau J.L., Proud C.G.;
"The Mnks: MAP kinase-interacting kinases (MAP kinase signal-
integrating kinases).";
Front. Biosci. 13:5359-5373(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 72-385 IN COMPLEX WITH ZINC,
AND SUBUNIT.
PubMed=16216586; DOI=10.1016/j.str.2005.07.013;
Jauch R., Jaekel S., Netter C., Schreiter K., Aicher B., Jaeckle H.,
Wahl M.C.;
"Crystal structures of the Mnk2 kinase domain reveal an inhibitory
conformation and a zinc binding site.";
Structure 13:1559-1568(2005).
[22]
X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 72-385 IN COMPLEX WITH ZINC
AND STAUROSPORINE, ENZYME REGULATION, AND MUTAGENESIS OF ASP-228.
PubMed=16917500; DOI=10.1038/sj.emboj.7601285;
Jauch R., Cho M.-K., Jaekel S., Netter C., Schreiter K., Aicher B.,
Zweckstetter M., Jaeckle H., Wahl M.C.;
"Mitogen-activated protein kinases interacting kinases are
autoinhibited by a reprogrammed activation segment.";
EMBO J. 25:4020-4032(2006).
[23]
VARIANT [LARGE SCALE ANALYSIS] ASN-73.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: 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. {ECO:0000269|PubMed:11154262,
ECO:0000269|PubMed:11463832, ECO:0000269|PubMed:12897141,
ECO:0000269|PubMed:16111636, ECO:0000269|PubMed:17965020,
ECO:0000269|PubMed:18299328, ECO:0000269|PubMed:20823271,
ECO:0000269|PubMed:20927323, ECO:0000269|PubMed:21149447}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:11463832}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:11463832};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 1 zinc ion per subunit.;
-!- ENZYME REGULATION: Inhibited by CGP57380 and staurosporine.
Activated by phosphorylation in a negative-feedback regulatory
manner in response to chemotherapy (e.g. cytarabine) and thus
impairs the generation of antileukemic responses.
{ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:16111636,
ECO:0000269|PubMed:16917500, ECO:0000269|PubMed:20664001,
ECO:0000269|PubMed:20722422, ECO:0000269|PubMed:20927323}.
-!- SUBUNIT: Monomer. Interacts with the C-terminal regions of EIF4G1
and EIF4G2; this interaction is promoted when MAPK pathways are
repressed but repressed upon ERK proteins activation. Also binds
to dephosphorylated MAPK3/ERK1 and MAPK1/ERK2. Isoform 1
interaction with phosphorylated MAPK3/ERK1 and MAPK1/ERK2 protects
it from dephosphorylation and inactivation. Isoform 2 interacts
with ESR2 and EIF4E in the nucleus. {ECO:0000269|PubMed:11013076,
ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:12897141,
ECO:0000269|PubMed:16216586, ECO:0000269|PubMed:16917500,
ECO:0000269|PubMed:20823271}.
-!- INTERACTION:
Q16539:MAPK14; NbExp=3; IntAct=EBI-2864341, EBI-73946;
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus, PML body.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1 {ECO:0000269|PubMed:11013076}; Synonyms=2a
{ECO:0000303|PubMed:11013076};
IsoId=Q9HBH9-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:11013076}; Synonyms=2b
{ECO:0000303|PubMed:11013076};
IsoId=Q9HBH9-2; Sequence=VSP_007353, VSP_007354;
Name=3 {ECO:0000303|PubMed:11013076};
IsoId=Q9HBH9-3; Sequence=Not described;
Name=4 {ECO:0000303|PubMed:11013076};
IsoId=Q9HBH9-4; Sequence=Not described;
Name=5 {ECO:0000303|PubMed:11013076};
IsoId=Q9HBH9-5; Sequence=Not described;
-!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues
examined. Isoform 2 is expressed at higher levels in the ovary
than is isoform 1. {ECO:0000269|PubMed:11013076}.
-!- PTM: Dual phosphorylation of Thr-244 and Thr-249 activates the
kinase. Phosphorylation of Thr-379 activates the kinase.
Phosphorylated upon arsenic trioxide As(2)O(3) treatment.
Phosphorylated by MAPK1/ERK2, MAPK11 and MAPK14. Dephosphorylated
by PP2A. {ECO:0000269|PubMed:11154262,
ECO:0000269|PubMed:11463832, ECO:0000269|PubMed:12897141,
ECO:0000269|PubMed:18299328}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. {ECO:0000305}.
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EMBL; AF237775; AAG26336.1; -; mRNA.
EMBL; AF237776; AAG26337.1; -; mRNA.
EMBL; AF125532; AAF17226.1; -; mRNA.
EMBL; BC073140; AAH73140.1; -; mRNA.
CCDS; CCDS12079.1; -. [Q9HBH9-2]
CCDS; CCDS12080.1; -. [Q9HBH9-1]
RefSeq; NP_060042.2; NM_017572.3. [Q9HBH9-2]
RefSeq; NP_951009.1; NM_199054.2. [Q9HBH9-1]
UniGene; Hs.515032; -.
PDB; 2AC3; X-ray; 2.10 A; A=72-385.
PDB; 2AC5; X-ray; 3.20 A; A=72-385.
PDB; 2HW7; X-ray; 2.71 A; A=72-385.
PDBsum; 2AC3; -.
PDBsum; 2AC5; -.
PDBsum; 2HW7; -.
ProteinModelPortal; Q9HBH9; -.
SMR; Q9HBH9; -.
BioGrid; 109130; 38.
IntAct; Q9HBH9; 34.
STRING; 9606.ENSP00000250896; -.
BindingDB; Q9HBH9; -.
ChEMBL; CHEMBL4204; -.
GuidetoPHARMACOLOGY; 2105; -.
iPTMnet; Q9HBH9; -.
PhosphoSitePlus; Q9HBH9; -.
BioMuta; MKNK2; -.
DMDM; 90102033; -.
EPD; Q9HBH9; -.
PaxDb; Q9HBH9; -.
PeptideAtlas; Q9HBH9; -.
PRIDE; Q9HBH9; -.
DNASU; 2872; -.
Ensembl; ENST00000250896; ENSP00000250896; ENSG00000099875. [Q9HBH9-1]
Ensembl; ENST00000309340; ENSP00000309485; ENSG00000099875. [Q9HBH9-2]
Ensembl; ENST00000591601; ENSP00000467811; ENSG00000099875. [Q9HBH9-1]
GeneID; 2872; -.
KEGG; hsa:2872; -.
UCSC; uc002lus.3; human. [Q9HBH9-1]
CTD; 2872; -.
DisGeNET; 2872; -.
EuPathDB; HostDB:ENSG00000099875.14; -.
GeneCards; MKNK2; -.
HGNC; HGNC:7111; MKNK2.
HPA; CAB037253; -.
HPA; HPA021875; -.
HPA; HPA053989; -.
MIM; 605069; gene.
neXtProt; NX_Q9HBH9; -.
OpenTargets; ENSG00000099875; -.
PharmGKB; PA30830; -.
eggNOG; KOG0607; Eukaryota.
eggNOG; ENOG410XQA9; LUCA.
GeneTree; ENSGT00900000140876; -.
HOVERGEN; HBG106949; -.
InParanoid; Q9HBH9; -.
KO; K04372; -.
OMA; EAIAMNR; -.
OrthoDB; EOG091G0G1X; -.
PhylomeDB; Q9HBH9; -.
SignaLink; Q9HBH9; -.
SIGNOR; Q9HBH9; -.
ChiTaRS; MKNK2; human.
EvolutionaryTrace; Q9HBH9; -.
GeneWiki; MKNK2; -.
GenomeRNAi; 2872; -.
PRO; PR:Q9HBH9; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000099875; -.
CleanEx; HS_MKNK2; -.
ExpressionAtlas; Q9HBH9; baseline and differential.
Genevisible; Q9HBH9; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0071243; P:cellular response to arsenic-containing substance; IDA:UniProtKB.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0030097; P:hemopoiesis; IDA:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; ATP-binding;
Complete proteome; Cytoplasm; Kinase; Magnesium; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase;
Translation regulation; Zinc.
CHAIN 1 465 MAP kinase-interacting serine/threonine-
protein kinase 2.
/FTId=PRO_0000086336.
DOMAIN 84 388 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 90 98 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 160 162 Staurosporine binding.
MOTIF 60 66 Nuclear localization signal.
MOTIF 444 448 MAP kinase binding. {ECO:0000250}.
ACT_SITE 205 205 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
METAL 299 299 Zinc. {ECO:0000269|PubMed:16216586,
ECO:0000269|PubMed:16917500}.
METAL 311 311 Zinc. {ECO:0000269|PubMed:16216586,
ECO:0000269|PubMed:16917500}.
METAL 314 314 Zinc. {ECO:0000269|PubMed:16216586,
ECO:0000269|PubMed:16917500}.
BINDING 113 113 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 209 209 Staurosporine.
{ECO:0000269|PubMed:16917500}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CDB0}.
MOD_RES 244 244 Phosphothreonine.
{ECO:0000269|PubMed:11463832}.
MOD_RES 249 249 Phosphothreonine.
{ECO:0000269|PubMed:11463832}.
MOD_RES 379 379 Phosphothreonine.
{ECO:0000269|PubMed:11463832}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CDB0}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000250|UniProtKB:Q8CDB0}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 386 414 NSCAKDLTSFAAEAIAMNRQLAQHDEDLA -> WDSHFLLP
PHPCRIHVRPGGLVRTVTVNE (in isoform 2).
{ECO:0000303|PubMed:11013076,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_007353.
VAR_SEQ 415 465 Missing (in isoform 2).
{ECO:0000303|PubMed:11013076,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_007354.
VARIANT 10 10 Q -> K (in dbSNP:rs3746101).
/FTId=VAR_051648.
VARIANT 73 73 D -> N (in dbSNP:rs56158214).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040805.
VARIANT 428 428 R -> Q (in dbSNP:rs34475638).
/FTId=VAR_051649.
MUTAGEN 228 228 D->G: Reduced phosphorylation.
{ECO:0000269|PubMed:16917500}.
MUTAGEN 244 244 T->A: Loss of kinase activity; when
associated with T-249.
{ECO:0000269|PubMed:11463832}.
MUTAGEN 249 249 T->A: Loss of kinase activity; when
associated with T-244.
{ECO:0000269|PubMed:11463832}.
MUTAGEN 379 379 T->D: Constitutively active.
{ECO:0000269|PubMed:11463832}.
CONFLICT 261 261 V -> L (in Ref. 2; AAF17226).
{ECO:0000305}.
STRAND 74 76 {ECO:0000244|PDB:2AC5}.
TURN 79 81 {ECO:0000244|PDB:2AC3}.
STRAND 83 85 {ECO:0000244|PDB:2HW7}.
STRAND 94 102 {ECO:0000244|PDB:2AC3}.
STRAND 104 106 {ECO:0000244|PDB:2AC3}.
STRAND 109 116 {ECO:0000244|PDB:2AC3}.
HELIX 123 135 {ECO:0000244|PDB:2AC3}.
STRAND 145 151 {ECO:0000244|PDB:2AC3}.
STRAND 154 160 {ECO:0000244|PDB:2AC3}.
HELIX 167 174 {ECO:0000244|PDB:2AC3}.
HELIX 179 198 {ECO:0000244|PDB:2AC3}.
HELIX 208 210 {ECO:0000244|PDB:2AC3}.
STRAND 211 214 {ECO:0000244|PDB:2AC3}.
STRAND 216 219 {ECO:0000244|PDB:2AC3}.
STRAND 221 224 {ECO:0000244|PDB:2AC3}.
HELIX 254 256 {ECO:0000244|PDB:2AC3}.
HELIX 259 264 {ECO:0000244|PDB:2AC3}.
HELIX 267 272 {ECO:0000244|PDB:2AC3}.
HELIX 273 275 {ECO:0000244|PDB:2AC3}.
HELIX 276 290 {ECO:0000244|PDB:2AC3}.
HELIX 312 324 {ECO:0000244|PDB:2AC3}.
HELIX 331 334 {ECO:0000244|PDB:2AC3}.
HELIX 339 348 {ECO:0000244|PDB:2AC3}.
TURN 353 355 {ECO:0000244|PDB:2AC3}.
HELIX 359 364 {ECO:0000244|PDB:2AC3}.
TURN 366 368 {ECO:0000244|PDB:2HW7}.
SEQUENCE 465 AA; 51875 MW; D6D4BE6C541012B1 CRC64;
MVQKKPAELQ GFHRSFKGQN PFELAFSLDQ PDHGDSDFGL QCSARPDMPA SQPIDIPDAK
KRGKKKKRGR ATDSFSGRFE DVYQLQEDVL GEGAHARVQT CINLITSQEY AVKIIEKQPG
HIRSRVFREV EMLYQCQGHR NVLELIEFFE EEDRFYLVFE KMRGGSILSH IHKRRHFNEL
EASVVVQDVA SALDFLHNKG IAHRDLKPEN ILCEHPNQVS PVKICDFDLG SGIKLNGDCS
PISTPELLTP CGSAEYMAPE VVEAFSEEAS IYDKRCDLWS LGVILYILLS GYPPFVGRCG
SDCGWDRGEA CPACQNMLFE SIQEGKYEFP DKDWAHISCA AKDLISKLLV RDAKQRLSAA
QVLQHPWVQG CAPENTLPTP MVLQRNSCAK DLTSFAAEAI AMNRQLAQHD EDLAEEEAAG
QGQPVLVRAT SRCLQLSPPS QSKLAQRRQR ASLSSAPVVL VGDHA


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