M3K15_MOUSE
ID M3K15_MOUSE Reviewed; 1331 AA.
AC A2AQW0;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 15;
DE EC=2.7.11.25;
DE AltName: Full=MAPK/ERK kinase kinase 15;
DE Short=MEK kinase 15;
DE Short=MEKK 15;
GN Name=Map3k15 {ECO:0000312|EMBL:CAM22391.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May function in a signal transduction pathway that is
CC activated by various cell stresses and leads to apoptosis.
CC {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=2.7.11.25;
CC Evidence={ECO:0000250|UniProtKB:Q99683};
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=2.7.11.25; Evidence={ECO:0000250|UniProtKB:Q99683};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q99683};
CC -!- ACTIVITY REGULATION: Contains an N-terminal autoinhibitory domain.
CC Activated by phosphorylation at Thr-816, inhibited by phosphorylation
CC at Ser-928 (By similarity). {ECO:0000250|UniProtKB:Q99683}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000250|UniProtKB:Q99683}.
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DR EMBL; AL845167; CAM22391.1; -; Genomic_DNA.
DR EMBL; AL929452; CAM22391.1; JOINED; Genomic_DNA.
DR EMBL; AL929452; CAM21674.1; -; Genomic_DNA.
DR EMBL; AL845167; CAM21674.1; JOINED; Genomic_DNA.
DR CCDS; CCDS53236.1; -.
DR RefSeq; NP_001156557.2; NM_001163085.2.
DR AlphaFoldDB; A2AQW0; -.
DR SMR; A2AQW0; -.
DR BioGRID; 234812; 3.
DR STRING; 10090.ENSMUSP00000033665; -.
DR iPTMnet; A2AQW0; -.
DR PhosphoSitePlus; A2AQW0; -.
DR MaxQB; A2AQW0; -.
DR PaxDb; A2AQW0; -.
DR PRIDE; A2AQW0; -.
DR ProteomicsDB; 295748; -.
DR Antibodypedia; 571; 150 antibodies from 27 providers.
DR Ensembl; ENSMUST00000033665; ENSMUSP00000033665; ENSMUSG00000031303.
DR GeneID; 270672; -.
DR KEGG; mmu:270672; -.
DR UCSC; uc009utb.2; mouse.
DR CTD; 389840; -.
DR MGI; MGI:2448588; Map3k15.
DR VEuPathDB; HostDB:ENSMUSG00000031303; -.
DR eggNOG; KOG4279; Eukaryota.
DR GeneTree; ENSGT00940000159562; -.
DR HOGENOM; CLU_003687_1_0_1; -.
DR InParanoid; A2AQW0; -.
DR OMA; KFVESRH; -.
DR OrthoDB; 226722at2759; -.
DR PhylomeDB; A2AQW0; -.
DR TreeFam; TF105115; -.
DR BioGRID-ORCS; 270672; 3 hits in 78 CRISPR screens.
DR ChiTaRS; Map3k15; mouse.
DR PRO; PR:A2AQW0; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; A2AQW0; protein.
DR Bgee; ENSMUSG00000031303; Expressed in granulocyte and 54 other tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR043969; MAP3K_PH.
DR InterPro; IPR025136; MAP3K_TRAF-bd.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF19039; ASK_PH; 1.
DR Pfam; PF13281; MAP3K_TRAF_bd; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF47769; SSF47769; 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 1: Evidence at protein level;
KW ATP-binding; Coiled coil; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1331
FT /note="Mitogen-activated protein kinase kinase kinase 15"
FT /id="PRO_0000307633"
FT DOMAIN 656..912
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1216..1236
FT /evidence="ECO:0000255"
FT COMPBIAS 935..959
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 777
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 662..670
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P28523,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 685
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q99683,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 1331 AA; 149327 MW; 6BB38F2B8A59B942 CRC64;
MEGGGGSGGG GGPVPAEAPE EAGEPPQGRL PPGPEGAAGL AEPESTGDAA GGEAEGGRGP
RRALRAVYVR SESSQGAAAG GGPEAGALKC LLRACEAEGA HLTSVPFGEL DFGETAVLDA
FYDADVAIVD MSDISRQPSL FYHLGVRESF DMANNVILYY DTDADTALSL KDMVTQKNTA
SSGNYYFIPY TVTPCADYFC CESDAQRRAS EYMQPNWDTI LGPLCMPLVD RFTSLLKDIR
VTSCAYYKET LLNDIRKARE KYQGDELAKE LTRIKFRMDN IEVLTSDIII NLLLSYRDIQ
DYDAMVKLVE TLKMLPTCDL ADQHNIKFHY AFALNRRNST GDREKALQVM LQVLQSCDHP
APDMFCLCGR IYKDIFLDSG CEEDASRDSA IEWYRKGFEL QSSLYSGINL AVLLIVSGQQ
FETSMELRKI GVRLNSLLGR KGSLEKMNNY WDVGQFFTVS MLASDIGKAV QAAERLFKLK
PPVWYLRSLV QNLLLIQRFK KPITEHSPRQ ERLNFWLDII FEATNEVTNG LRFPVLVIEP
TKVYQPSYVS INNEAEERTV SLWHVSPTEM KQIHEWNFTA SSIKGISLSK FDERCCFLYV
HDNSDDFQIY FSTEDQCNRF CSLVKEMLNN GVGSTVELEG EADGDTLEYE YDHDANGERV
VLGKGSYGIV YAGRDLSNQV RIAIKEIPER DIRYSQPLHE EIALHKYLKH RNIVQYLGSV
SENGYIKIFM EQVPGGSLSA LLRSKWGPMK EPTIKFYTKQ ILEGLKYLHE NQIVHRDIKG
DNVLVNTYSG VVKISDFGTS KRLAGINPCT ETFTGTLQYM APEIIDQGPR GYGAPADIWS
LGCTIIEMAT SRPPFHELGE PQAAMFKVGM FKIHPEIPEA LSAEARAFIL SCFEPDPQKR
VTAADLLQEG FLRQVNKGKK NRIAFKPSEG VRSGTGTLAL PSSGELVGSS SSEHGSISPD
SDAQPDAFFE KVQVPKHQLS HLLSVPDESP ALDDRSTALP PEERDPGLFL LRKDSERRAI
LYRILWEEQN QVASNLQECV VQSSEELLLS VSHIKQIIGI LRDFIRSPEH RVMAATISKL
KVDLDFDSSS INQIHLILFG FQDAVNRILR NHLIRPHWMF AMDNIIRRAV QAAVTILIPE
LQAHFEPASE TEGVDKDTEV EGDYPLVDLL SQEVHVTPRG TRPGSVAIQE GQPHQQDPSL
QLSKLRQETN RLWEHLVQKE REYQNLLRLI LDQKTQELYH LQLQYKSNGG TENPPPPDGL
GTDRELIDWL QLQGVDANTI EKIVEEDYTL SDILNDITKE DLRCLRLRGG VLCRLWHAVS
QHRRQMQESS Q
