MKNK2_XENTR
ID MKNK2_XENTR Reviewed; 466 AA.
AC Q66I46;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2004) 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}.
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DR EMBL; BC081543; AAH81543.1; -; mRNA.
DR RefSeq; NP_001072772.1; NM_001079304.1.
DR AlphaFoldDB; Q66I46; -.
DR SMR; Q66I46; -.
DR STRING; 8364.ENSXETP00000035495; -.
DR PaxDb; Q66I46; -.
DR DNASU; 780232; -.
DR Ensembl; ENSXETT00000084757; ENSXETP00000065265; ENSXETG00000013667.
DR GeneID; 780232; -.
DR KEGG; xtr:780232; -.
DR CTD; 2872; -.
DR Xenbase; XB-GENE-491527; mknk2.
DR eggNOG; KOG0607; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q66I46; -.
DR OrthoDB; 608695at2759; -.
DR PhylomeDB; Q66I46; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000013667; Expressed in skeletal muscle tissue and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009931; F:calcium-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IBA:GO_Central.
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:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
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..466
FT /note="MAP kinase-interacting serine/threonine-protein
FT kinase 2"
FT /id="PRO_0000226967"
FT DOMAIN 83..367
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 430..466
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 466 AA; 52313 MW; 6E73EEED34AB04B8 CRC64;
MVQKKTTEMK GFHRSFKGQN PFDAAYEMES RNMASVFNFD CPSRPDVPSS APIDIPDAKK
RTKKKKRCRA TDSFTGRFED 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 KDWAHISSGA KDLISKLLLR DAKKRLSAAQ
VLQHPWVQGN APDNTLPTPI ILQRNSSAKD LTSFAAEAIA MNRQLMEREE EEEGTESSSS
CPIVVKATSC SMQLSPPSES KLAKRRHGSK GGISPPSLAP LLIVSD
