ID   MKNK2_XENLA             Reviewed;         467 AA.
AC   Q6P431;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=MAP kinase-interacting serine/threonine-protein kinase 2;
DE            EC=2.7.11.1;
DE   AltName: Full=MAP kinase signal-integrating kinase 2;
DE            Short=MAPK signal-integrating kinase 2;
DE            Short=Mnk2;
GN   Name=mknk2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Liver;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in the response to environmental stress and
CC       cytokines. Appears to regulate translation by phosphorylating EIF4E,
CC       thus increasing the affinity of this protein for the 7-methylguanosine-
CC       containing mRNA cap (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC063717; AAH63717.1; -; mRNA.
DR   EMBL; BC077783; AAH77783.1; -; mRNA.
DR   RefSeq; NP_001083700.1; NM_001090231.1.
DR   AlphaFoldDB; Q6P431; -.
DR   SMR; Q6P431; -.
DR   DNASU; 399068; -.
DR   GeneID; 399068; -.
DR   KEGG; xla:399068; -.
DR   CTD; 399068; -.
DR   Xenbase; XB-GENE-866072; mknk2.L.
DR   OMA; PANILCE; -.
DR   OrthoDB; 608695at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 399068; Expressed in spleen and 19 other tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Translation regulation; Zinc.
FT   CHAIN           1..467
FT                   /note="MAP kinase-interacting serine/threonine-protein
FT                   kinase 2"
FT                   /id="PRO_0000226966"
FT   DOMAIN          83..367
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          432..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        204
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         89..97
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         298
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         310
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   467 AA;  52671 MW;  ECD94A40C293246C CRC64;
     MVQKKTTEMK GFHRSFKGQN PFDAAYEMEA RNMESVFNFD CPSRPDVPSS APIDIPDAKK
     RTKKKKRCRA TDSFTGRFDD MYQLQQEILG EGAYAKVQSC INLITNKEYA VKIIEKRPGH
     SRSRVFREVE MLYQCQGHSN VLELIEFFEE EDKFYLVFEK MCGGSILNHI HRRRHFNERE
     ASFVVRDIAE ALNYLHNKGI AHRDLKPENI LCESPHQVSP VKICDFDLGS GIKLNSDCSP
     ISTPELLTPC GSAEYMAPEV VEAFNEEASI YDKRCDLWSL GVILYIMLSG YPPFVGHCGS
     DCGWDRGEAC PACQNMLFVS IQEGKYEFPE KDWAHISYGA KDLISKLLLR DAKKRLSAAQ
     VLQHPWVQGN APYNTLPTPI ILQRNSSAKD LTSFAAEAIA MNRQLMEREE EEEGTENSSL
     CPFVVKATSC SMQLSPPSES KLAKRRQQGS KGGISPPSLA PLLIVSD