M313B_XENLA
ID M313B_XENLA Reviewed; 961 AA.
AC A7J1T0;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 13-B;
DE EC=2.7.11.25;
GN Name=map3k13-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=xLZK-B_20703;
RA Itoh A., Ryan K., Itoh T.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May have a role in the JNK signaling pathway. {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 -!- 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;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; DQ862004; ABK15542.1; -; mRNA.
DR RefSeq; NP_001165659.1; NM_001172188.1.
DR AlphaFoldDB; A7J1T0; -.
DR SMR; A7J1T0; -.
DR GeneID; 100337577; -.
DR KEGG; xla:100337577; -.
DR CTD; 100337577; -.
DR Xenbase; XB-GENE-6464340; map3k13.S.
DR OMA; EYEYCEQ; -.
DR OrthoDB; 938929at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 100337577; Expressed in liver and 9 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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:0046777; P:protein autophosphorylation; IEA:InterPro.
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 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; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Coiled coil; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..961
FT /note="Mitogen-activated protein kinase kinase kinase 13-B"
FT /id="PRO_0000366130"
FT DOMAIN 171..412
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 89..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..457
FT /note="Leucine-zipper 1"
FT REGION 489..510
FT /note="Leucine-zipper 2"
FT REGION 507..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..827
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT REGION 933..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 460..497
FT /evidence="ECO:0000255"
FT COMPBIAS 90..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 282
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 177..185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 961 AA; 107570 MW; CD82B672163A4AB5 CRC64;
MHLNDIMASP HEPLNWSSSP NLIVDTIQED KDYRVDYGDC TTIGHHEIKE TPDKCDFLDN
TNSPVNATVL NSISEDSRDQ FENSVLQLRD QDEPENTAPQ GSSHSGDGGN NSANEDIRIH
FSRSRSGSGN GGFLEGLFGC LRPVWNIIGK AYSTDYKLQQ QDTWEVPFEE ISELQWLGSG
AQGAVFLGKF RGEEVAIKKV REQKETDIKH LRKLKHPNII AFKGVCTQAP CYCILMEYCA
QGQLYEVLRA GRKVTPKLLV EWSTGIASGM NYLHLHKIIH RDLKSPNVLV THADTVKISD
FGTSKELSDK STKMSFAGTV AWMAPEVIRN EPVSEKVDIW SFGVLLWELL TGEIPYKDVD
SSAIIWGVGS NSLHLPVPST CPDGFKILMK QTWQSKPRNR PSFRQILMHL DIAAADVLGT
PQETYFKSQA EWREEVKKHF EKIKSEGTCI HRLDEELIRR RREELRHALD IREHYERKLE
RANNLYMELS SIMLQLEVRE KELTRREQTV EKKYPGTYKR HPVRPIVHPN SFEKLIKKKG
PPSRVPSQSK RPDLLKSDGI VNAEGSAASA SPISGSPKTS SGGGKGRYRS KPRHRRGNSK
GSHADFVGVL KYQESPAPSQ QSSQHQTPAS PPVTPCSPYH ETSQVMPTRH QTLNVHGQNI
ANCANNLRYF GPAAALRSPL SSHAHRRMSG FSPDLLSSTL EADSRIQPER EYEYCEQHPY
NPSQGCTETS VQHDIDTENL NNTNVVTAEY RTSDGDLPDS PRHNLVQEDY EKLETGGEQF
SSLKAAVGVS ALTVPTPPAL PRRIHTLRKN GDDSSEGEEG EVDSEVEFPR RHRPPRGMST
CQSYSTFSSE NFSVSDGEEG NTSDHSNSPD DVACGNKVWQ VDKLDDLLSQ TPEIPIEISM
QSDGLSDKEC AVRRVKTQMS LGKLCPEEHN YENAESDCDS SEGECSDATV RTNNPVNSST
W
