GenomeNet

Database: UniProt
Entry: G3PKL0_GASAC
LinkDB: G3PKL0_GASAC
Original site: G3PKL0_GASAC 
ID   G3PKL0_GASAC            Unreviewed;      1263 AA.
AC   G3PKL0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=mitogen-activated protein kinase kinase kinase {ECO:0000256|ARBA:ARBA00012406};
DE            EC=2.7.11.25 {ECO:0000256|ARBA:ARBA00012406};
GN   Name=MAP3K6 {ECO:0000313|Ensembl:ENSGACP00000018140.1};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000018140.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000018140.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000018140.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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}.
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   AlphaFoldDB; G3PKL0; -.
DR   Ensembl; ENSGACT00000018175.1; ENSGACP00000018140.1; ENSGACG00000013722.1.
DR   GeneTree; ENSGT00940000159398; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000013722; Expressed in mesonephros and 5 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd06624; STKc_ASK; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR046872; DRHyd-ASK.
DR   InterPro; IPR046873; HisK-N-like.
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   PANTHER; PTHR11584:SF391; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 6; 1.
DR   PANTHER; PTHR11584; SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF19039; ASK_PH; 1.
DR   Pfam; PF20309; DRHyd-ASK; 1.
DR   Pfam; PF20302; HisK-N-like; 1.
DR   Pfam; PF13281; MAP3K_TRAF_bd; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 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};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT   DOMAIN          631..889
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          883..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1104..1132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1134..1168
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        888..903
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1115..1130
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         660
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1263 AA;  141097 MW;  D0B3CC68D784F7EB CRC64;
     LHDQRRKDPV RVSAGSLWQD ASAVDPSGAG KPLTSPRSRT RAVSVAYIVN EDASEPRGEE
     NLTVDCLKEA CADAHALFKT ISFERISLGA TDILDSFYNA DVAVVEMSDS LCQPSLYYHL
     GVRESFSMTN NIILYCYKQD SDVQALKRDD GAVRGSREQC GTYTFIPYVV SPQGKAFACD
     ATIMMSGIKD LMQPSFQLEP LLTPLVERMV HLLNNVQVQS SEYFQESIRH EIRTARERFS
     GRALSEELSR IQKRLDSVEL LTPDIVMNLL LSYRDIQDYD AIIKLVETLN DLPTCLVAKH
     QNIKFTYIFA LNRRNKSGDR AKALEVILPI VESGVNVVSD IYCLCGRIYK DMFMSSGFTD
     QGSRDQACYW YGKAFETEPT LHSGINNVVL LMVAGHEFDT SIELRKTGVT LSTLLGRKGS
     LEKMKNYWDV GFYLGANILV NEHRKVTAAS EKLYRLQAPV WYVASIMETY ILYRQFAKLP
     EVKSAKQDTM DFWMELLLQA CKPTDSTGRC PVLILEPSKV LQPAIVCVSE EDQSRTVQLE
     HVTPLEKGLH QWTFPASAIR GVSASKIDER SCFLYVHFNS DDFQLCFPSE LHCKGFCELV
     NSLLQLAQQP DRDQDPVAEG IPEYIYETND NGDKVVLGKG TYGVVYAGRD QSNHVRIAIK
     EIPERDRTYS QPLHEEIALH KRLKHRNIVQ YLGSVSQNGF IKIFMEEVPG GSLSSLLRSK
     WGPLKDNEAT ITFYTKQILD GLKYLHDNQI VHRDIKGDNV LINTYSGVLK ISDFGTSKRL
     AGINPCTETF AGTLQYMAPE IIDQGPRGYG KPADIWSLGC TIIEMATGKP PFHELGSPQA
     AMFKVGMFKI HPKVPECMSD EAKAFIMKCF VPEPDDRASS AELLSDPYLR PSHRKRAKAP
     QESEPVDHVS AGGTSPSAGR MTTPGAPPAP AACCRESGCC PTGDQDLLVI PEDPSDMSSP
     ASADENMGLF MLRKNSERRA TLHRVLTDYI SLVVSNILEH DRGTALTADN ITELISCLRD
     NIHTPDRKQL SGRLQALRAA MRSAAVSPSS LQAVLFSFQD AVKKVLRQEQ VKPHWMFALD
     NLLRQAVQDA ITVLLPGAAS SCPLKDDAEQ TASTCDVERP DSPADSSSSL SEKLRELRLE
     TGRLLSQLNE KEREYQQLLR NSVQRKQEQI DALRCAPATE NSSEPEAKAL VDWLNSLPVD
     QNTINKLLAH DFTLDCLLYV ASREDLMYCG IRCGMLCRIW AAISARRKTP LRTHNEDSED
     TLL
//
DBGET integrated database retrieval system