M3K1_MOUSE
ID M3K1_MOUSE Reviewed; 1493 AA.
AC P53349; Q60831; Q9R0U3; Q9R256;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Mitogen-activated protein kinase kinase kinase 1;
DE EC=2.7.11.25;
DE AltName: Full=MAPK/ERK kinase kinase 1;
DE Short=MEK kinase 1;
DE Short=MEKK 1;
GN Name=Map3k1; Synonyms=Mekk, Mekk1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lange C.A., Blumer K.J., Sather S.L., Johnson G.L.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-659.
RC TISSUE=Spleen;
RX PubMed=10523642; DOI=10.1128/mcb.19.11.7539;
RA Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N., Sugiyama K.,
RA Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.;
RT "JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that
RT functions as a scaffold factor in the JNK signaling pathway.";
RL Mol. Cell. Biol. 19:7539-7548(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 660-1493.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8385802; DOI=10.1126/science.8385802;
RA Lange-Carter C.A., Pleiman C.M., Gardner A.M., Blumer K.J., Johnson G.L.;
RT "A divergence in the MAP kinase regulatory network defined by MEK kinase
RT and Raf.";
RL Science 260:315-319(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 796-1493.
RC STRAIN=BALB/cJ; TISSUE=Heart;
RA Whitmarsh A.J., Shore P., Sharrocks A.D., Davis R.J.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP ACTIVITY REGULATION, MUTAGENESIS OF THR-1381 AND THR-1393, AND
RP PHOSPHORYLATION AT THR-1381 AND THR-1393.
RX PubMed=9078260; DOI=10.1042/bj3220185;
RA Deak J.C., Templeton D.J.;
RT "Regulation of the activity of MEK kinase 1 (MEKK1) by autophosphorylation
RT within the kinase activation domain.";
RL Biochem. J. 322:185-192(1997).
RN [6]
RP FUNCTION, INTERACTION WITH IKBKB AND MAP2K4, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF THR-1381; THR-1393; ILE-1394; PHE-1396; MET-1397; VAL-1401;
RP LEU-1402; ARG-1403 AND GLY-1404.
RX PubMed=14500727; DOI=10.1074/jbc.m304234200;
RA Tu Z., Lee F.S.;
RT "Subdomain VIII is a specificity-determining region in MEKK1.";
RL J. Biol. Chem. 278:48498-48505(2003).
RN [7]
RP INTERACTION WITH AXIN1.
RX PubMed=15262978; DOI=10.1074/jbc.m404598200;
RA Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.;
RT "The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal kinase
RT activation by Axin and dishevelled through distinct mechanisms.";
RL J. Biol. Chem. 279:39366-39373(2004).
RN [8]
RP FUNCTION.
RX PubMed=17761173; DOI=10.1016/j.febslet.2007.08.008;
RA Ye B., Yu W.P., Thomas G.M., Huganir R.L.;
RT "GRASP-1 is a neuronal scaffold protein for the JNK signaling pathway.";
RL FEBS Lett. 581:4403-4410(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND SER-287, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Component of a protein kinase signal transduction cascade
CC (PubMed:14500727). Activates the ERK and JNK kinase pathways by
CC phosphorylation of MAP2K1 and MAP2K4 (PubMed:14500727). May
CC phosphorylate the MAPK8/JNK1 kinase (PubMed:17761173). Activates CHUK
CC and IKBKB, the central protein kinases of the NF-kappa-B pathway
CC (PubMed:14500727). {ECO:0000269|PubMed:14500727,
CC ECO:0000269|PubMed:17761173}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Activated by autophosphorylation on Thr-1381 and
CC Thr-1393 following oligomerization. {ECO:0000269|PubMed:14500727,
CC ECO:0000269|PubMed:9078260}.
CC -!- SUBUNIT: Binds both upstream activators and downstream substrates in
CC multimolecular complexes through its N-terminus. Oligomerizes after
CC binding MAP4K2 or TRAF2. Interacts with AXIN1. Interacts (via the
CC kinase catalytic domain) with STK38 (By similarity). Interacts with
CC GRIPAP1 (By similarity). {ECO:0000250|UniProtKB:Q13233,
CC ECO:0000250|UniProtKB:Q62925}.
CC -!- INTERACTION:
CC P53349; P47809: Map2k4; NbExp=2; IntAct=EBI-447913, EBI-447934;
CC P53349; Q9ESN9-2: Mapk8ip3; NbExp=3; IntAct=EBI-447913, EBI-9549291;
CC P53349; Q8CF89: Tab1; NbExp=4; IntAct=EBI-447913, EBI-1778503;
CC P53349; P62991: Ubc; NbExp=2; IntAct=EBI-447913, EBI-413074;
CC -!- TISSUE SPECIFICITY: Highly expressed in the heart and spleen while a
CC lower level expression is seen in the liver.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:9078260}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. MAP kinase kinase kinase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97500.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF117340; AAD25049.1; -; mRNA.
DR EMBL; AB014614; BAA85878.1; -; mRNA.
DR EMBL; L13103; AAA97500.1; ALT_INIT; mRNA.
DR EMBL; U23470; AAA85038.1; -; mRNA.
DR CCDS; CCDS26771.1; -.
DR PIR; A46212; A46212.
DR AlphaFoldDB; P53349; -.
DR SMR; P53349; -.
DR CORUM; P53349; -.
DR DIP; DIP-32487N; -.
DR IntAct; P53349; 7.
DR MINT; P53349; -.
DR STRING; 10090.ENSMUSP00000104890; -.
DR iPTMnet; P53349; -.
DR PhosphoSitePlus; P53349; -.
DR EPD; P53349; -.
DR jPOST; P53349; -.
DR MaxQB; P53349; -.
DR PaxDb; P53349; -.
DR PeptideAtlas; P53349; -.
DR PRIDE; P53349; -.
DR ProteomicsDB; 292161; -.
DR MGI; MGI:1346872; Map3k1.
DR eggNOG; KOG0198; Eukaryota.
DR InParanoid; P53349; -.
DR PhylomeDB; P53349; -.
DR BRENDA; 2.7.11.25; 3474.
DR Reactome; R-MMU-166058; MyD88:MAL(TIRAP) cascade initiated on plasma membrane.
DR Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
DR Reactome; R-MMU-975138; TRAF6 mediated induction of NFkB and MAP kinases upon TLR7/8 or 9 activation.
DR Reactome; R-MMU-975871; MyD88 cascade initiated on plasma membrane.
DR ChiTaRS; Map3k1; mouse.
DR PRO; PR:P53349; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P53349; protein.
DR GO; GO:0030054; C:cell junction; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031941; C:filamentous actin; IDA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:MGI.
DR GO; GO:0008432; F:JUN kinase binding; ISO:MGI.
DR GO; GO:0004706; F:JUN kinase kinase kinase activity; IDA:MGI.
DR GO; GO:0004708; F:MAP kinase kinase activity; EXP:Reactome.
DR GO; GO:0004709; F:MAP kinase kinase kinase activity; ISO:MGI.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:MGI.
DR GO; GO:0031434; F:mitogen-activated protein kinase kinase binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0046625; F:sphingolipid binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IMP:MGI.
DR GO; GO:0007254; P:JNK cascade; IDA:MGI.
DR GO; GO:0000165; P:MAPK cascade; ISO:MGI.
DR GO; GO:0002011; P:morphogenesis of an epithelial sheet; IMP:MGI.
DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0046330; P:positive regulation of JNK cascade; ISO:MGI.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:BHF-UCL.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0050434; P:positive regulation of viral transcription; ISO:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR GO; GO:0006970; P:response to osmotic stress; ISO:MGI.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0042060; P:wound healing; IMP:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR007527; Znf_SWIM.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF04434; SWIM; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50966; ZF_SWIM; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13233"
FT CHAIN 2..1493
FT /note="Mitogen-activated protein kinase kinase kinase 1"
FT /id="PRO_0000086241"
FT DOMAIN 1224..1489
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ZN_FING 333..361
FT /note="SWIM-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00325"
FT ZN_FING 438..487
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 895..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1066
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1066
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1350
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 1230..1238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 1253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q13233"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13233"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13233"
FT MOD_RES 280
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13233"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13233"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13233"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13233"
FT MOD_RES 526
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13233"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13233"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13233"
FT MOD_RES 1024
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13233"
FT MOD_RES 1381
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:9078260"
FT MOD_RES 1393
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:9078260"
FT MUTAGEN 1381
FT /note="T->A: Fails to activate MAP2K1, MAP2K4, MAP2K7, CHUK
FT and IKBKB."
FT /evidence="ECO:0000269|PubMed:14500727,
FT ECO:0000269|PubMed:9078260"
FT MUTAGEN 1381
FT /note="T->E: Loss of kinase activity and
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:14500727,
FT ECO:0000269|PubMed:9078260"
FT MUTAGEN 1381
FT /note="T->S: Reduced kinase activity and
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:14500727,
FT ECO:0000269|PubMed:9078260"
FT MUTAGEN 1393
FT /note="T->A: Loss of kinase activity and
FT autophosphorylation. Fails to activate MAP2K1, MAP2K4,
FT MAP2K7, CHUK and IKBKB."
FT /evidence="ECO:0000269|PubMed:14500727,
FT ECO:0000269|PubMed:9078260"
FT MUTAGEN 1393
FT /note="T->E: Loss of kinase activity and
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:14500727,
FT ECO:0000269|PubMed:9078260"
FT MUTAGEN 1393
FT /note="T->S: Reduced kinase activity and
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:14500727,
FT ECO:0000269|PubMed:9078260"
FT MUTAGEN 1394
FT /note="I->A: Loss of NF-kappa-B transcription factor
FT activity and reduced ability to activate MAP2K1, MAP2K4,
FT MAP2K7. No effect on AP-1 activity or activation of CHUK
FT and IKBKB. Loss of binding to IKBKB."
FT /evidence="ECO:0000269|PubMed:14500727"
FT MUTAGEN 1396
FT /note="F->A: Loss of AP-1 and NF-kappa-B transcription
FT factor activity. Reduced ability to activate MAP2K1,
FT MAP2K4, MAP2K7, CHUK and IKBKB."
FT /evidence="ECO:0000269|PubMed:14500727"
FT MUTAGEN 1397
FT /note="M->A: Loss of AP-1 and NF-kappa-B transcription
FT factor activity. Reduced ability to activate MAP2K1,
FT MAP2K4, MAP2K7, CHUK and IKBKB."
FT /evidence="ECO:0000269|PubMed:14500727"
FT MUTAGEN 1401
FT /note="V->A: Loss of AP-1 and NF-kappa-B transcription
FT factor activity. Reduced ability to activate MAP2K1,
FT MAP2K4, MAP2K7, CHUK and IKBKB."
FT /evidence="ECO:0000269|PubMed:14500727"
FT MUTAGEN 1402
FT /note="L->A: Loss of AP-1 transcription factor activity and
FT reduced ability to activate CHUK and IKBKB. No effect on
FT NF-kappa-B activity or activation of MAP2K1, MAP2K4,
FT MAP2K7. Loss of binding to MAP2K4."
FT /evidence="ECO:0000269|PubMed:14500727"
FT MUTAGEN 1403
FT /note="R->A: Loss of AP-1 transcription factor activity, no
FT effect on NF-kappa-B activity."
FT /evidence="ECO:0000269|PubMed:14500727"
FT MUTAGEN 1404
FT /note="G->A: Loss of AP-1 and NF-kappa-B transcription
FT factor activity."
FT /evidence="ECO:0000269|PubMed:14500727"
FT CONFLICT 30..39
FT /note="GGGALQGSGA -> ALQGSG (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 103
FT /note="Missing (in Ref. 2; BAA85878)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="V -> E (in Ref. 2; BAA85878)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="M -> V (in Ref. 2; BAA85878)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="S -> C (in Ref. 2; BAA85878)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="V -> A (in Ref. 2; BAA85878)"
FT /evidence="ECO:0000305"
FT CONFLICT 883
FT /note="V -> L (in Ref. 3; AAA85038)"
FT /evidence="ECO:0000305"
FT CONFLICT 1467
FT /note="V -> L (in Ref. 3; AAA85038)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1493 AA; 161289 MW; CA65C9B7703C6BF9 CRC64;
MAAAAGDRAS SSGFPGAAAA SPEAGGGGGG GGALQGSGAP AAGAAGLLRE PGSAGRERAD
WRRRQLRKVR SVELDQLPEQ PLFLAAASPP CPSTSPSPEP ADAAAGASRF QPAAGPPPPG
AASRCGSHSA ELAAARDSGA RSPAGAEPPS AAAPSGREME NKETLKGLHK MEDRPEERMI
REKLKATCMP AWKHEWLERR NRRGPVVVKP IPIKGDGSEV NNLAAEPQGE GQAGSAAPAP
KGRRSPSPGS SPSGRSVKPE SPGVRRKRVS PVPFQSGRIT PPRRAPSPDG FSPYSPEETS
RRVNKVMRAR LYLLQQIGPN SFLIGGDSPD NKYRVFIGPQ NCSCGRGAFC IHLLFVMLRV
FQLEPSDPML WRKTLKNFEV ESLFQKYHSR RSSRIKAPSR NTIQKFVSRM SNSHTLSSSS
TSTSSSENSI KDEEEQMCPI CLLGMLDEES LTVCEDGCRN KLHHHCMSIW AEECRRNREP
LICPLCRSKW RSHDFYSHEL SSPVESPASL RAVQQPSSPQ QPVAGSQRRN QESSFNLTHF
GTQQIPSAYK DLAEPWIQVF GMELVGCLFS RNWNVREMAL RRLSHDVSGA LLLANGESTG
NSGGGSGGSL SAGAASGSSQ PSISGDVVEA CCSVLSIVCA DPVYKVYVAA LKTLRAMLVY
TPCHSLAERI KLQRLLRPVV DTILVKCADA NSRTSQLSIS TVLELCKGQA GELAVGREIL
KAGSIGVGGV DYVLSCILGN QAESNNWQEL LGRLCLIDRL LLEFPAEFYP HIVSTDVSQA
EPVEIRYKKL LSLLTFALQS IDNSHSMVGK LSRRIYLSSA RMVTAVPAVF SKLVTMLNAS
GSTHFTRMRR RLMAIADEVE IAEVIQLGVE DTVDGHQDSL QAVAPTSCLE NSSLEHTVHR
EKTGKGLSAT RLSASSEDIS DRLAGVSVGL PSSTTTEQPK PAVQTKGRPH SQCLNSSPLS
HAQLMFPAPS APCSSAPSVP DISKHRPQAF VPCKIPSASP QTQRKFSLQF QRNCSEHRDS
DQLSPVFTQS RPPPSSNIHR PKPSRPVPGS TSKLGDATKS SMTLDLGSAS RCDDSFGGGG
NSGNAVIPSD ETVFTPVEDK CRLDVNTELN SSIEDLLEAS MPSSDTTVTF KSEVAVLSPE
KAENDDTYKD DVNHNQKCKE KMEAEEEEAL AIAMAMSASQ DALPIVPQLQ VENGEDIIII
QQDTPETLPG HTKAKQPYRE DAEWLKGQQI GLGAFSSCYQ AQDVGTGTLM AVKQVTYVRN
TSSEQEEVVE ALREEIRMMG HLNHPNIIRM LGATCEKSNY NLFIEWMAGG SVAHLLSKYG
AFKESVVINY TEQLLRGLSY LHENQIIHRD VKGANLLIDS TGQRLRIADF GAAARLASKG
TGAGEFQGQL LGTIAFMAPE VLRGQQYGRS CDVWSVGCAI IEMACAKPPW NAEKHSNHLA
LIFKIASATT APSIPSHLSP GLRDVAVRCL ELQPQDRPPS RELLKHPVFR TTW
