ID MP2K1_XENLA Reviewed; 395 AA.
AC Q05116; Q5D0B8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 27-MAR-2024, entry version 137.
DE RecName: Full=Dual specificity mitogen-activated protein kinase kinase 1;
DE Short=MAP kinase kinase 1;
DE Short=MAPKK 1;
DE EC=2.7.12.2;
DE AltName: Full=ERK activator kinase 1;
DE AltName: Full=MAPK/ERK kinase 1;
DE Short=MEK1;
GN Name=map2k1;
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 [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8440264; DOI=10.1002/j.1460-2075.1993.tb05713.x;
RA Kosako H., Nishida E., Gotoh Y.;
RT "cDNA cloning of MAP kinase kinase reveals kinase cascade pathways in
RT yeasts to vertebrates.";
RL EMBO J. 12:787-794(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Dual specificity protein kinase which acts as an essential
CC component of the MAP kinase signal transduction pathway. Binding of
CC extracellular ligands such as growth factors, cytokines and hormones to
CC their cell-surface receptors activates the MAPK/ERK cascade, ultimately
CC leading to phosphorylation of a threonine and a tyrosine residue in a
CC Thr-Glu-Tyr sequence located in MAP kinases. Depending on the cellular
CC context, this pathway mediates diverse biological functions such as
CC cell growth, adhesion, survival and differentiation predominantly
CC through the regulation of transcription, metabolism and cytoskeletal
CC rearrangements (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=2.7.12.2;
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=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, spindle pole body {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the central nervous system, kidney,
CC liver, intestine and the hematopoietic system.
CC -!- PTM: Activated by phosphorylation on Ser/Thr catalyzed by MAP kinase
CC kinase kinases (RAF or MOS).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR EMBL; D13700; BAA02860.1; -; mRNA.
DR EMBL; BC043913; AAH43913.1; -; mRNA.
DR PIR; S36186; S36186.
DR RefSeq; NP_001080299.1; NM_001086830.1.
DR AlphaFoldDB; Q05116; -.
DR SMR; Q05116; -.
DR BioGRID; 98233; 7.
DR ELM; Q05116; -.
DR MINT; Q05116; -.
DR DNASU; 379991; -.
DR GeneID; 379991; -.
DR KEGG; xla:379991; -.
DR AGR; Xenbase:XB-GENE-865216; -.
DR CTD; 379991; -.
DR Xenbase; XB-GENE-865216; map2k1.L.
DR OMA; LTPYDWH; -.
DR OrthoDB; 2900742at2759; -.
DR BRENDA; 2.7.12.2; 6725.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 379991; Expressed in brain and 19 other cell types or tissues.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IEA:UniProt.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProt.
DR GO; GO:0005770; C:late endosome; IEA:UniProt.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004708; F:MAP kinase kinase activity; IEA:UniProtKB-EC.
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:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:2000641; P:regulation of early endosome to late endosome transport; IEA:UniProt.
DR GO; GO:0090170; P:regulation of Golgi inheritance; IEA:UniProt.
DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; IEA:UniProt.
DR CDD; cd06650; PKc_MEK1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR47448; DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE DSOR1-LIKE PROTEIN; 1.
DR PANTHER; PTHR47448:SF2; MITOGEN-ACTIVATED PROTEIN KINASE KINASE 1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..395
FT /note="Dual specificity mitogen-activated protein kinase
FT kinase 1"
FT /id="PRO_0000086371"
FT DOMAIN 68..363
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 74..82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 218
FT /note="Phosphoserine; by RAF"
FT /evidence="ECO:0000250"
FT MOD_RES 222
FT /note="Phosphoserine; by RAF"
FT /evidence="ECO:0000250"
SQ SEQUENCE 395 AA; 43742 MW; F09607CCD1C206BE CRC64;
MPKKKPTPIQ LNPNPEGTAV NGTPTAETNL EALQKKLEEL ELDEQQRKRL EAFLTQKQKV
GELKDDDFEK VSELGAGNGG VVFKVSHKPT SLIMARKLIH LEIKPAIRNQ IIRELQVLHE
CNSPYIVGFY GAFYSDGEIS ICMEHMDGGS LDQVLKKAGK IPEKILGKVS IAVIKGLTYL
REKHKIMHRD VKPSNILVNS RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY
SVQSDIWSMG LSLVEMAIGR YPIPPPDAKE LELIFGCSVE RDPASSELAP RPRPPGRPIS
SYGPDSRPPM AIFELLDYIV NEPPPKLPSG VFGAEFQDFV NKCLVKNPAE RADLKQLMVH
SFIKQSELEE VDFAGWLCST MGLKQPSTPT HAAGV
//
