MKNK1_BOVIN
ID MKNK1_BOVIN Reviewed; 420 AA.
AC Q58D94; Q2T9R8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=MAP kinase-interacting serine/threonine-protein kinase 1;
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q9BUB5};
DE AltName: Full=MAP kinase signal-integrating kinase 1;
DE Short=MAPK signal-integrating kinase 1;
DE Short=Mnk1;
GN Name=MKNK1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) 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 Evidence={ECO:0000250|UniProtKB:Q9BUB5};
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; Evidence={ECO:0000250|UniProtKB:Q9BUB5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9BUB5};
CC -!- ACTIVITY REGULATION: Phosphorylated and activated by the p38 kinases
CC and kinases in the Erk pathway. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the C-terminal regions of EIF4G1 and EIF4G2.
CC Also binds to dephosphorylated ERK1 and ERK2, and to the p38 kinases
CC (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q58D94-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q58D94-2; Sequence=VSP_017513, VSP_017514;
CC -!- PTM: Dual phosphorylation of Thr-197 and Thr-202 activates the kinase.
CC Phosphorylation of Thr-332 activates the kinase. MAPK3/ERK1 is one of
CC the kinases which activate MKNK1/MNK1. Phosphorylation by PAK2 leads to
CC a reduced phosphorylation of EIF4G1 (By similarity). {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; BT021703; AAX46550.1; -; mRNA.
DR EMBL; BC111299; AAI11300.1; -; mRNA.
DR RefSeq; NP_001030435.1; NM_001035358.1.
DR AlphaFoldDB; Q58D94; -.
DR SMR; Q58D94; -.
DR STRING; 9913.ENSBTAP00000026556; -.
DR PaxDb; Q58D94; -.
DR PRIDE; Q58D94; -.
DR GeneID; 525647; -.
DR KEGG; bta:525647; -.
DR CTD; 8569; -.
DR eggNOG; KOG0607; Eukaryota.
DR InParanoid; Q58D94; -.
DR OrthoDB; 608695at2759; -.
DR Proteomes; UP000009136; Unplaced.
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 Alternative splicing; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Translation regulation.
FT CHAIN 1..420
FT /note="MAP kinase-interacting serine/threonine-protein
FT kinase 1"
FT /id="PRO_0000226968"
FT DOMAIN 37..321
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 158
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 43..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 66
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 27
FT /note="Phosphoserine; by PAK2"
FT /evidence="ECO:0000250|UniProtKB:O08605"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUB5"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUB5"
FT MOD_RES 197
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUB5"
FT MOD_RES 202
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUB5"
FT MOD_RES 332
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BUB5"
FT VAR_SEQ 324
FT /note="Q -> E (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_017513"
FT VAR_SEQ 325..420
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_017514"
FT CONFLICT 149
FT /note="R -> L (in Ref. 1; AAX46550)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="E -> D (in Ref. 1; AAX46550)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 46700 MW; AD00EE4C0879D0ED CRC64;
MGSSEPIPIA ESDKRKKKKR KARATDSLPG KFEDVYKLTS ELLGEGANAK VQVAVSLQNG
NEYAVKIIEK HAGHSRSRVF REVETLYQCQ GNKHILELIE FFEDDTRFYL VFEKLQGGSI
LAHIQKQKHF NEREASRVVR DVAAALDFRH TKGIAHRDLK PENILCESPE KVSPVKICDF
DLGSGVKLNN SCTPITTPEL TTPCGSAEYM APEVVEVFTD EATFYDKRCD LWSLGVVLYI
MLSGYPPFVG HCGADCGWDR GEVCTVCQNK LFESIQKGKY EFPDKDWAHI SNEAKDLISK
LLVRDAKQRL SAAQVLQHPW VQGQAPERGL PTPQVLQRNS STMDLTLFAA EAIALNRQLS
QHEENEQNKL AEESEVLAEG LCSVKLSPPS KSRLARRRAL AQAGRSGDAP PSPTPTTPAP
