ID A0A7L4APQ2_9CHAR Unreviewed; 395 AA. AC A0A7L4APQ2; DT 07-APR-2021, integrated into UniProtKB/TrEMBL. DT 07-APR-2021, sequence version 1. DT 02-OCT-2024, entry version 14. DE RecName: Full=Dual specificity mitogen-activated protein kinase kinase 1 {ECO:0000256|ARBA:ARBA00040618}; DE EC=2.7.12.2 {ECO:0000256|ARBA:ARBA00038999}; DE AltName: Full=ERK activator kinase 1 {ECO:0000256|ARBA:ARBA00042350}; DE AltName: Full=MAPK/ERK kinase 1 {ECO:0000256|ARBA:ARBA00042276}; DE Flags: Fragment; GN Name=Map2k1 {ECO:0000313|EMBL:NXW27536.1}; GN ORFNames=PHASIM_R03001 {ECO:0000313|EMBL:NXW27536.1}; OS Phaetusa simplex (large-billed tern). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Charadriiformes; Laridae; Phaetusa. OX NCBI_TaxID=297813 {ECO:0000313|EMBL:NXW27536.1, ECO:0000313|Proteomes:UP000556165}; RN [1] {ECO:0000313|EMBL:NXW27536.1, ECO:0000313|Proteomes:UP000556165} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B10K-DU-009-16 {ECO:0000313|EMBL:NXW27536.1}; RC TISSUE=Muscle {ECO:0000313|EMBL:NXW27536.1}; RA Zhang G.; RT "Bird 10,000 Genomes (B10K) Project - Family phase."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. 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 Evidence={ECO:0000256|ARBA:ARBA00036883}; 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; Evidence={ECO:0000256|ARBA:ARBA00036524}; 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 Evidence={ECO:0000256|ARBA:ARBA00035978}; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, CC cytoskeleton, microtubule organizing center, spindle pole body CC {ECO:0000256|ARBA:ARBA00004317}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr CC protein kinase family. MAP kinase kinase subfamily. CC {ECO:0000256|ARBA:ARBA00038035}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NXW27536.1}. 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; VZZW01000058; NXW27536.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7L4APQ2; -. DR Proteomes; UP000556165; Unassembled WGS sequence. 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:0005816; C:spindle pole body; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004708; F:MAP kinase kinase activity; IEA:UniProt. DR GO; GO:0004674; F:protein serine/threonine kinase activity; 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; IPR050915; MAP_kinase_kinase. 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 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:NXW27536.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000556165}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000313|EMBL:NXW27536.1}. FT DOMAIN 68..363 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 282..306 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 97 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:NXW27536.1" FT NON_TER 395 FT /evidence="ECO:0000313|EMBL:NXW27536.1" SQ SEQUENCE 395 AA; 43622 MW; ECA7F75B7B193A29 CRC64; MPKKKPGPIQ LNPAPDGSAV NGTSSAETNL EALQKKLEEL ELDEQQRKRL EAFLTQKQKV GELKDDDFEK ISELGAGNGG VVFKVSHKPS GLIMARKLIH LEIKPAIRNQ IIRELQVLHE CNSPYIVGFY GAFYSDGEIS ICMEHMDGGS LDQVLKKAGR IPEQILGKVS IAVIKGLTYL REKHKIMHRD VKPSNILVNS RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY SVQSDIWSMG LSLVEMAIGR YPIPPPDSKE LELMFGCPVE GDSPVTETSP RQRTPGRPVS SYGPDSRPPM AIFELLDYIV NEPPPKLPNG VFGSEFQDFV NKCLIKNPAE RADLKQLMIH AFIKRSEAEE VDFAGWLCST IGLNQPSTPT HAAGV //