M3K13_PONAB
ID M3K13_PONAB Reviewed; 966 AA.
AC Q5R8X7;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 13;
DE EC=2.7.11.25;
GN Name=MAP3K13 {ECO:0000250|UniProtKB:O43283};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH91783.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex {ECO:0000312|EMBL:CAH91783.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Activates the JUN N-terminal pathway through activation of
CC the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3 to
CC regulate the activation of NF-kappa-B in the cytosol. This activation
CC is kinase-dependent and involves activating the IKK complex, the IKBKB-
CC containing complex that phosphorylates inhibitors of NF-kappa-B (By
CC similarity). {ECO:0000250|UniProtKB:O43283}.
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:0000305};
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:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q60700};
CC -!- ACTIVITY REGULATION: Activated by autophosphorylation and
CC homodimerization. {ECO:0000250|UniProtKB:O43283}.
CC -!- SUBUNIT: Homodimer; forms dimers through the leucine-zipper motif.
CC Interacts with the C-terminus of MAPK8IP1 through the kinase catalytic
CC domain. Binds PRDX3. Associates with the IKK complex through the kinase
CC domain (By similarity). {ECO:0000250|UniProtKB:O43283}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- PTM: Autophosphorylated on serine and threonine residues.
CC {ECO:0000250|UniProtKB:O43283}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
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DR EMBL; CR859621; CAH91783.1; -; mRNA.
DR RefSeq; NP_001126034.1; NM_001132562.1.
DR AlphaFoldDB; Q5R8X7; -.
DR SMR; Q5R8X7; -.
DR STRING; 9601.ENSPPYP00000016066; -.
DR GeneID; 100172983; -.
DR KEGG; pon:100172983; -.
DR CTD; 9175; -.
DR eggNOG; KOG4721; Eukaryota.
DR InParanoid; Q5R8X7; -.
DR OrthoDB; 938929at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106137; F:IkappaB kinase complex binding; ISS:UniProtKB.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0007254; P:JNK cascade; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051403; P:stress-activated MAPK cascade; ISS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017419; MAP3K12_MAP3K13.
DR InterPro; IPR027258; MAPKKK13.
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 PIRSF; PIRSF500742; 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; Cytoplasm; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..966
FT /note="Mitogen-activated protein kinase kinase kinase 13"
FT /id="PRO_0000086265"
FT DOMAIN 168..409
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..454
FT /note="Leucine-zipper 1"
FT REGION 486..507
FT /note="Leucine-zipper 2"
FT REGION 534..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..828
FT /note="Acidic"
FT /evidence="ECO:0000305"
FT REGION 846..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 846..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 279
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q12852,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 174..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q12852,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 195
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q60700,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 966 AA; 108442 MW; 275CEC4BE01D6A02 CRC64;
MANFQEHLSC SSSPHLPFSE SKTFNGLQDE LTAMGNHPSP KLLEDQQEKG MVRAELIESV
HSPVTTTVLT SVSEDSRDQF ENSVLQLREH DESEMAVSQG NSNTVDAEST SGTEDIKIQF
SRSGSGSGGF LEGLFGCLRP VWNIIGKAYA TDYKLQQQDT WEVPFEEISE LQWLGSGAQG
AVFLGKFRAE EVAIKKVREQ NETDIKHLRK LKHPNIIAFK GVCTQAPCYC IIMEYCAHGQ
LYEVLRAGRK ITPRLLVDWS TGIASGMNYL HLHKIIHRDL KSPNVLVTHT DAVKISDFGT
SKELSDKSTK MSFAGTVAWL APEVIRNEPV SEKVDIWSFG VVLWELLTGE IPYKDVDSSA
IIWGVGSNSL HLPVPSTCPD GFKILMKQTW QSKPRNRPSF RQTLMHLDIA SADVLATPQE
TYFKSQAEWR EEVKKHFEKI KSEGTCIHRL DEELIRRRRE ELRHALDIRE HYERKLERAN
NLYMELSAIM LQLEMREKEL VKREQAVEKK YPGTYKRHPV RPIIHPNAME KLMKRKGVPH
KSGMQTKRPD LLRSEGIPTT EVAPTASPLS GSPKMSTSSS KSRYRSKPRH RRGNSRGSHS
DFVAILKNQP AQENSPNPTY LHQAQSQYPS LHHRNSLQQQ YQQPPPAMSQ SHHPRLNMHG
QDIATCANNL RYFGPAAALR SPLSNHAQRQ LPGSSPDLIS TAMAADCWRG SEPDKDQAGP
WGCCQADPYD PCLQCRPEQY GSLDIPSAEP VGRSPDLSKS PAHNPLLENA QSSEKMEENE
FSSCRSESSL GTSHLVTPPA LPRKTRPLQK SGDDSSEEEE GEVDSEVEFP RRQRPHRCIS
SCQSYSTFSS ENFSVSDGEE GNTSDHSNSP DELADKLEDR LAEKLDDLLS QTPEIPIDIS
SHSDGLSDKE CAVRRVKTQM SLGKLCVEER GYENPMQFEE SDCDSSDGEC SDATVRTNKH
YSSATW
