ID G3QZ40_GORGO Unreviewed; 1313 AA.
AC G3QZ40;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 73.
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=MAP3K15 {ECO:0000313|Ensembl:ENSGGOP00000008139.3};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000008139.3, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000008139.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000008139.3, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000008139.3}
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}.
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DR EMBL; CABD030123061; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030123062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030123063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030123064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030123065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030123066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030123067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030123068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030123069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030123070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_018874938.1; XM_019019393.1.
DR STRING; 9593.ENSGGOP00000008139; -.
DR Ensembl; ENSGGOT00000008365.3; ENSGGOP00000008139.3; ENSGGOG00000008317.3.
DR eggNOG; KOG4279; Eukaryota.
DR GeneTree; ENSGT00940000159562; -.
DR HOGENOM; CLU_003687_1_0_1; -.
DR InParanoid; G3QZ40; -.
DR OMA; MQPNWDS; -.
DR TreeFam; TF105115; -.
DR Proteomes; UP000001519; Chromosome X.
DR Bgee; ENSGGOG00000008317; Expressed in testis and 1 other cell type or tissue.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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: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:SF363; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 15; 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:UP000001519};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022527}.
FT DOMAIN 652..908
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 939..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1180..1214
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 681
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1313 AA; 147495 MW; 10FCB31BBB108195 CRC64;
MESGGGNTSA GALGAASESP QCPPPPGVEG AAGPAEPDGA AEGAAGGSGE GESGGGPRRA
LRAVYVRSES SQGGAAGGPE AGARQCLLRA CEAEGAHLTS VPFGELDFGE TAVLDAFYDA
DVAVVDMSDV SRQPSLFYHL GVRESFDMAN NVILYHDTDA DTALSLKDMV IQKNTASSGN
YYFIPYIVTP CADYFCCESD AQRRASEYMQ PNWDNILGPL CMPLVDRFIS LLKDIHVTSC
VYYKETLLND IRKAREKYQG EELAKELARI KLRMDNTEVL TSDIIINLLL SYRDIQDYDA
MVKLVETLEM LPTCDLADQH NIKFHYAFAL NRRNSTGDRE KALQIMLQVL QSCDHPGPDM
FCLCGRIYKD IFLDSDCKDD TSRDSAIEWY RKGFELQSSL YSGINLAVLL IVAGQQFETS
LELRKIGVRL NSLLGRKGSL EKMNNYWDVG QFFIVSMLAN DVGKAVQAAE RLFKLKPPVW
YLRSLVQNLL LIRRFKKPII EHSPRQERLN FWLDIIFEAT NEVTNGLRFP VLVIEPTKVY
QPSYVSINNE AEERTVSLWH VSPTEMKQMH EWNFTASSIK GISLSKFDER CCFLYVHDNS
DDFQIYFSTE EQCSRFFSLV KEMITNTAGS TVELEGETDG DTLEYEYDHD ANGERVVLGK
GTYGIVYAGR DLSNQVRIAI KEIPERDSRY SQPLHEEIAL HKYLKHRNIV QYLGSVSENG
YIKIFMEQVP GGSLSALLRS KWGPMKEPTI KFYTKQILEG LKYLHENQIV HRDIKGDNVL
VNTYSGVVKI SDFGTSKRLA GVNPCTETFT GTLQYMAPEI IDQGPRGYGA PADIWSLGCT
IIEMATSKPP FHELGEPQAA MFKVGMFKIH PEIPEALSAE ARAFILSCFE PDPHKRATTA
ELLREGFLRQ VNKGKKNRIA FKPSEGPRGV VLALPTQGEP MATSSSEHGS VSPDSDAQPD
ALFERTRAPR HHLGHLLSVP DESSALEDRG LASSPEDRDQ GLFLLRKDSE RRAILYKILW
EEQNQVASNL QECVAQSSEE LHLSVGHIKQ IIGILRDFIR SPEHRVMATT ISKLKVDLDF
DSSSISQIHL VLFGFQDAVN KILRNHLIRP HWMFAMDNII RRAVQAAVTI LIPELRAHFE
PTCETEGVDK DMDEAEEGYP PATGPGQEAQ PHQQHLSLQL GELRQETNRL LEHLVEKERE
YQNLLRQTLE QKTQELYHLQ LKLKSNCITE NPAGPYGQRT DKELIDWLRL QGADAKTIEK
IVEEGYTLSD ILNEITKEDL RYLRLRGGLL CRLWNAVSQY RRAQEASETK DKA
//
