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Database: UniProt
Entry: H3DGB6_TETNG
LinkDB: H3DGB6_TETNG
Original site: H3DGB6_TETNG 
ID   H3DGB6_TETNG            Unreviewed;       891 AA.
AC   H3DGB6;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406, ECO:0000256|PIRNR:PIRNR038165};
DE            EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406, ECO:0000256|PIRNR:PIRNR038165};
GN   Name=MAP3K13 {ECO:0000313|Ensembl:ENSTNIP00000019560.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000019560.1, ECO:0000313|Proteomes:UP000007303};
RN   [1] {ECO:0000313|Proteomes:UP000007303}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|Ensembl:ENSTNIP00000019560.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000478};
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:0000256|ARBA:ARBA00000106};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00006529, ECO:0000256|PIRNR:PIRNR038165}.
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DR   AlphaFoldDB; H3DGB6; -.
DR   STRING; 99883.ENSTNIP00000019560; -.
DR   Ensembl; ENSTNIT00000019790.1; ENSTNIP00000019560.1; ENSTNIG00000016461.1.
DR   GeneTree; ENSGT00940000158216; -.
DR   HOGENOM; CLU_009311_2_1_1; -.
DR   InParanoid; H3DGB6; -.
DR   OMA; CAEDRGY; -.
DR   TreeFam; TF105119; -.
DR   Proteomes; UP000007303; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14059; STKc_MAP3K12_13; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017419; MAP3K12_MAP3K13.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR44329:SF14; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 13; 1.
DR   PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PIRSF; PIRSF038165; MAPKKK12_MAPKKK13; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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|PIRNR:PIRNR038165, ECO:0000256|PIRSR:PIRSR038165-
KW   51}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|PIRNR:PIRNR038165};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR038165,
KW   ECO:0000256|PIRSR:PIRSR038165-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007303};
KW   Serine/threonine-protein kinase {ECO:0000256|PIRNR:PIRNR038165};
KW   Transferase {ECO:0000256|PIRNR:PIRNR038165}.
FT   DOMAIN          107..348
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          28..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..809
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          401..435
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        701..716
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        764..787
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        218
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038165-50"
FT   BINDING         113..121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038165-51"
FT   BINDING         134
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038165-51"
SQ   SEQUENCE   891 AA;  98789 MW;  E89E3F02168AD62B CRC64;
     SPLNTALSVD STRSEGQHFE NSVLQLQDQD QDEAGSPASC EHGGCGSHHH QPEDIKLHFH
     RAGPGSGGFL EGLFGCLRPV LNIIGKTYST EYKLQQQDMW EVPFEEISEL QWLGSGAQGA
     VFLGKFRSEE VAIKKVREQK ETEIKHLRKL KHPNIISFKA VCTQAPCYCI IMEYCAQGQL
     YEVLRAGRKV TPRMLVDWAS GIASGMNYLH LHKIIHRDLK SPNVLVTHND TVKISDFGTS
     KELSDKSTKM SFAGTVAWMA PEVIRNEPVS EKVDIWSFGV VLWELLTGEI PYKDVDSSAI
     IWGVGSNSLH LPVPSTCPDG FKILMKQTWQ AKPRNRPSFR QILLHLDIAS ADVLGAPQET
     YFKCQSEWRE EVKKHFEKIK SEGTCIHRLD EELIRRRRDE LRHALDIREH YERKLERANN
     LYMELSAIML QLEVREKELM KREQAVEKKY PGTYKRHLVR PIVRSNAVEK LIKKKGSLSH
     KPGMPSAKRP DLLRSDGIGS DPLPSPSPLS ASPKVSTPPG KARYRSKPRH RRANSKGSHS
     EFAGVLKPVS GPPEGPQAPK EQQLLHHHPH PPTPGPFLPL KGREEAVVNC ANNLRYFGPA
     AALRSPQTDH LQGRVSSSGP DLICTAVDAD TRQRTSSTGA GSDPAPGCGS LCPCSQAHPF
     PGCLKCQETS PAFEDAAPPY CSQLQTEDRA LPPGSPHSHP ASEREAAERR GGEEEGARPQ
     TQPLPTPTPR TLRALRKGGD ESSEEEEGEV DSEVEFPRRQ RPHRCMSSFQ SCSTFSSENL
     SVSDGEEGNT SDHSHSGPLE RLSASQEEHL DELLSHTPDI PIDISTQSDG LSDKECAVRR
     VKTQISLGKL CSDEHSYENP LQFGDSDCDS SEAECSDATI RNNKVGAPSS W
//
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