ID Q6FI23_HUMAN Unreviewed; 347 AA. AC Q6FI23; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 24-JAN-2024, entry version 148. DE RecName: Full=mitogen-activated protein kinase kinase {ECO:0000256|ARBA:ARBA00038999}; DE EC=2.7.12.2 {ECO:0000256|ARBA:ARBA00038999}; GN Name=MAP2K3 {ECO:0000313|EMBL:CAG38752.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:CAG38752.1}; RN [1] {ECO:0000313|EMBL:CAG38752.1} RP NUCLEOTIDE SEQUENCE. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAG37889.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Tongue {ECO:0000313|EMBL:BAG37889.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y., RA Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R., RA Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N., RA Isogai T.; RT "NEDO functional analysis of protein and research application project."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:BAG70040.1} RP NUCLEOTIDE SEQUENCE. RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J.-I., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K.-I., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., RA Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., RA Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., RA Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., RA Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., RA Imai J.-I., Watanabe S., Nomura N.; RT "Human Protein Factory: an infrastructure to convert the human RT transcriptome into the in vitro-expressed human proteome of versatile RT utility."; RL Submitted (JUL-2008) 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr CC protein kinase family. MAP kinase kinase subfamily. CC {ECO:0000256|ARBA:ARBA00038035}. 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; AK315505; BAG37889.1; -; mRNA. DR EMBL; AB451226; BAG70040.1; -; mRNA. DR EMBL; AB451349; BAG70163.1; -; mRNA. DR EMBL; CR536514; CAG38752.1; -; mRNA. DR RefSeq; NP_659731.1; NM_145109.2. DR AlphaFoldDB; Q6FI23; -. DR SMR; Q6FI23; -. DR MaxQB; Q6FI23; -. DR Antibodypedia; 4342; 1676 antibodies from 43 providers. DR DNASU; 5606; -. DR GeneID; 5606; -. DR KEGG; hsa:5606; -. DR UCSC; uc002gys.4; human. DR CTD; 5606; -. DR PharmGKB; PA30588; -. DR VEuPathDB; HostDB:ENSG00000034152; -. DR OMA; LRISCVY; -. DR OrthoDB; 2900742at2759; -. DR BioGRID-ORCS; 5606; 65 hits in 1214 CRISPR screens. DR ChiTaRS; MAP2K3; human. DR GenomeRNAi; 5606; -. DR ExpressionAtlas; Q6FI23; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004708; F:MAP kinase kinase activity; IEA:Ensembl. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0072709; P:cellular response to sorbitol; IEA:Ensembl. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl. DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IEA:Ensembl. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl. DR GO; GO:0001817; P:regulation of cytokine production; IEA:Ensembl. DR GO; GO:0002931; P:response to ischemia; IEA:Ensembl. DR CDD; cd06617; PKc_MKK3_6; 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; PTHR48013:SF21; DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 3; 1. DR PANTHER; PTHR48013; DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 5-RELATED; 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 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:BAG37889.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|ARBA:ARBA00023137}; KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}. FT DOMAIN 64..325 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT REGION 1..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..15 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 93 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" SQ SEQUENCE 347 AA; 39318 MW; A80BA4FDFF8F75A2 CRC64; MESPASSQPA SMPQSKGKSK RKKDLRISCM SKPPAPNPTP PRNLDSRTFI TIGDRNFEVE ADDLVTISEL GRGAYGVVEK VRHAQSGTIM AVKRIRATVN SQEQKRLLMD LDINMRTVDC FYTVTFYGAL FREGDVWICM ELMDTSLDKF YRKVLDKNMT IPEDILGEIA VSIVRALEHL HSKLSVIHRD VKPSNVLINK EGHVKMCDFG ISGYLVDSVA KTMDAGCKPY MAPERINPEL NQKGYNVKSD VWSLGITMIE MAILRFPYES WGTPFQQLKQ VVEEPSPQLP ADRFSPEFVD FTAQCLRKNP AERMSYLELM EHPFFTLHKT KKTDIAAFVK EILGEDS //