MKNK1_RAT
ID MKNK1_RAT Reviewed; 413 AA.
AC Q4G050;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
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; Synonyms=Mnk1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- 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; BC098754; AAH98754.1; -; mRNA.
DR RefSeq; NP_001037732.1; NM_001044267.1.
DR RefSeq; XP_006238760.1; XM_006238698.3.
DR RefSeq; XP_006238761.1; XM_006238699.3.
DR AlphaFoldDB; Q4G050; -.
DR SMR; Q4G050; -.
DR STRING; 10116.ENSRNOP00000061535; -.
DR PhosphoSitePlus; Q4G050; -.
DR PaxDb; Q4G050; -.
DR GeneID; 500526; -.
DR KEGG; rno:500526; -.
DR UCSC; RGD:1559603; rat.
DR CTD; 8569; -.
DR RGD; 1559603; Mknk1.
DR VEuPathDB; HostDB:ENSRNOG00000010381; -.
DR eggNOG; KOG0607; Eukaryota.
DR HOGENOM; CLU_000288_63_0_1; -.
DR InParanoid; Q4G050; -.
DR OrthoDB; 608695at2759; -.
DR PhylomeDB; Q4G050; -.
DR Reactome; R-RNO-1295596; Spry regulation of FGF signaling.
DR PRO; PR:Q4G050; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000010381; Expressed in pancreas and 20 other tissues.
DR ExpressionAtlas; Q4G050; baseline and differential.
DR Genevisible; Q4G050; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IC:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
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:0004674; F:protein serine/threonine kinase activity; IMP:RGD.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0006446; P:regulation of translational initiation; IMP:RGD.
DR GO; GO:0009651; P:response to salt stress; ISO:RGD.
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 Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase; Translation regulation.
FT CHAIN 1..413
FT /note="MAP kinase-interacting serine/threonine-protein
FT kinase 1"
FT /id="PRO_0000226969"
FT DOMAIN 37..321
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..26
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 22
FT /note="Phosphothreonine; by PAK2"
FT /evidence="ECO:0000250|UniProtKB:O08605"
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"
SQ SEQUENCE 413 AA; 46214 MW; DE0DA795C64D0161 CRC64;
MGSSEPLPIV DSDKRRKKKR KTRATDSLPG KFEDVYQLTS ELLGEGAYAK VQGAVSLQSG
KEYAVKIIEK QAGHSRSRVF REVETLYQCQ GNRNILELIE FFEDDTRFYL VFEKLQGGSI
LAHIQKRKHF NELEASRVVR DVATALDFLH TKGIAHRDLK PENILCESPE KVSPVKICDF
DLGSGVKLNN SCTPITTPEL TTPCGSAEYM APEVVEVFRD EATFYDKRCD LWSLGVVLYI
MLSGYPPFVG HCGADCGWDR GEVCRMCQNK LFESIQEGKY EFPDKDWAHI STEAKDLISK
LLVRDAKQRL SAAQVLQHPW VQGQAPERGL PTPQVLQRNS STMDLTLFAA EAIALNRQLS
QHEENELAEE HEALAEGLCS MKLSPPSKSR LARRRALAHA GREANSCSTP AGL
