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Mitogen-activated protein kinase kinase kinase 4 (EC 2.7.11.25) (MAPK/ERK kinase kinase 4) (MEK kinase 4) (MEKK 4)

 M3K4_MOUSE              Reviewed;        1597 AA.
O08648; O08649; O70124; Q6PDG6;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
27-SEP-2017, entry version 152.
RecName: Full=Mitogen-activated protein kinase kinase kinase 4;
EC=2.7.11.25;
AltName: Full=MAPK/ERK kinase kinase 4;
Short=MEK kinase 4;
Short=MEKK 4;
Name=Map3k4; Synonyms=Mekk4;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, INTERACTION
WITH CDC42, AND MUTAGENESIS OF LYS-1361.
TISSUE=Brain;
PubMed=9079650; DOI=10.1074/jbc.272.13.8288;
Gerwins P., Blank J.L., Johnson G.L.;
"Cloning of a novel mitogen-activated protein kinase kinase kinase,
MEKK4, that selectively regulates the c-Jun amino terminal kinase
pathway.";
J. Biol. Chem. 272:8288-8295(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 363-1049.
STRAIN=C57BL/6J; TISSUE=Ectoplacental cone;
PubMed=9268631; DOI=10.1006/geno.1997.4816;
Schweifer N., Valk P.J., Delwel R., Cox R., Francis F.,
Meier-Ewert S., Lehrach H., Barlow D.P.;
"Characterization of the C3 YAC contig from proximal mouse chromosome
17 and analysis of allelic expression of genes flanking the imprinted
Igf2r gene.";
Genomics 43:285-297(1997).
[4]
INTERACTION WITH AXIN1 AND DIXDC1.
PubMed=15262978; DOI=10.1074/jbc.M404598200;
Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.;
"The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal
kinase activation by Axin and dishevelled through distinct
mechanisms.";
J. Biol. Chem. 279:39366-39373(2004).
[5]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-1361, AND
INTERACTION WITH TRAF4.
PubMed=16157600; DOI=10.1074/jbc.C500260200;
Abell A.N., Johnson G.L.;
"MEKK4 is an effector of the embryonic TRAF4 for JNK activation.";
J. Biol. Chem. 280:35793-35796(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-449; THR-451;
SER-454 AND SER-492, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Component of a protein kinase signal transduction
cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not
the ERK pathway. Specifically phosphorylates and activates MAP2K4
and MAP2K6. {ECO:0000269|PubMed:16157600,
ECO:0000269|PubMed:9079650}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: N-terminal autoinhibitory domain interacts with
the C-terminal kinase domain, inhibiting kinase activity, and
preventing interaction with its substrate, MAP2K6. The GADD45
proteins activate the kinase by binding to the N-terminal domain.
Activated by phosphorylation on Thr-1494 (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Monomer and homodimer. Homodimerization enhances kinase
activity. Interacts with CDC42 (PubMed:9079650). Interacts with
TRAF4; this promotes homodimerization (PubMed:16157600). Binds
both upstream activators and downstream substrates in
multimolecular complexes. Interacts with AXIN1 and DIXDC1;
interaction with DIXDC1 prevents interaction with AXIN1
(PubMed:15262978). Interacts with GADD45 and MAP2K6 (By
similarity). Interacts with ZFP36; this interaction enhances the
association with SH3KBP1/CIN85. Interacts with SH3KBP1; this
interaction enhances the association with ZFP36 (By similarity).
{ECO:0000250|UniProtKB:Q9Y6R4, ECO:0000269|PubMed:15262978,
ECO:0000269|PubMed:16157600, ECO:0000269|PubMed:9079650}.
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000269|PubMed:16157600}. Note=Localized in perinuclear
vesicular-like structures, probably Golgi-associated vesicles.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=O08648-1; Sequence=Displayed;
Name=B;
IsoId=O08648-2; Sequence=VSP_004885;
-!- TISSUE SPECIFICITY: Widely expressed. High expression was found in
skeletal muscle, kidney, testis followed by heart brain and lung.
Low expression was found in spleen.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase kinase subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U85607; AAC53126.1; -; mRNA.
EMBL; U85608; AAC53127.1; -; mRNA.
EMBL; BC058719; AAH58719.1; -; mRNA.
EMBL; U66240; AAC08286.1; -; mRNA.
CCDS; CCDS37435.1; -. [O08648-1]
RefSeq; NP_036078.2; NM_011948.2. [O08648-1]
RefSeq; XP_006523392.1; XM_006523329.3. [O08648-2]
UniGene; Mm.28587; -.
ProteinModelPortal; O08648; -.
SMR; O08648; -.
BioGrid; 204960; 4.
CORUM; O08648; -.
STRING; 10090.ENSMUSP00000086459; -.
iPTMnet; O08648; -.
PhosphoSitePlus; O08648; -.
MaxQB; O08648; -.
PaxDb; O08648; -.
PeptideAtlas; O08648; -.
PRIDE; O08648; -.
Ensembl; ENSMUST00000089058; ENSMUSP00000086459; ENSMUSG00000014426. [O08648-1]
GeneID; 26407; -.
KEGG; mmu:26407; -.
UCSC; uc008akn.1; mouse. [O08648-1]
UCSC; uc008ako.1; mouse. [O08648-2]
CTD; 4216; -.
MGI; MGI:1346875; Map3k4.
eggNOG; KOG4645; Eukaryota.
eggNOG; ENOG410XQZE; LUCA.
GeneTree; ENSGT00880000138034; -.
HOGENOM; HOG000139909; -.
HOVERGEN; HBG006304; -.
InParanoid; O08648; -.
KO; K04428; -.
OMA; HYIRGGE; -.
OrthoDB; EOG091G00SM; -.
TreeFam; TF105114; -.
BRENDA; 2.7.11.25; 3474.
ChiTaRS; Map3k4; mouse.
PRO; PR:O08648; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000014426; -.
CleanEx; MM_MAP3K4; -.
Genevisible; O08648; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004709; F:MAP kinase kinase kinase activity; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0000186; P:activation of MAPKK activity; ISO:MGI.
GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
GO; GO:0060718; P:chorionic trophoblast cell differentiation; IMP:MGI.
GO; GO:0048263; P:determination of dorsal identity; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0019100; P:male germ-line sex determination; IMP:MGI.
GO; GO:0001890; P:placenta development; IMP:MGI.
GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:UniProtKB.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:MGI.
GO; GO:0051973; P:positive regulation of telomerase activity; ISO:MGI.
GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0010225; P:response to UV-C; ISO:MGI.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 1597 Mitogen-activated protein kinase kinase
kinase 4.
/FTId=PRO_0000086248.
DOMAIN 1332 1590 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 1338 1346 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 1178 1182 Poly-Ala.
ACT_SITE 1452 1452 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 1361 1361 ATP.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6R4}.
MOD_RES 440 440 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Y6R4}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 451 451 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 492 492 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 1241 1241 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6R4}.
MOD_RES 1263 1263 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y6R4}.
VAR_SEQ 1162 1213 Missing (in isoform B).
{ECO:0000303|PubMed:9079650}.
/FTId=VSP_004885.
MUTAGEN 1361 1361 K->A,R: Loss of kinase activity.
{ECO:0000269|PubMed:16157600,
ECO:0000269|PubMed:9079650}.
CONFLICT 363 364 SL -> NS (in Ref. 3; AAC08286).
{ECO:0000305}.
CONFLICT 473 473 A -> T (in Ref. 1; AAC53126/AAC53127).
{ECO:0000305}.
CONFLICT 1184 1184 A -> R (in Ref. 1; AAC53126).
{ECO:0000305}.
SEQUENCE 1597 AA; 179834 MW; E9C43EB9A4F056BC CRC64;
MRDAIAEPVP PPALADTPAA AMEELRPAPP PQPEPDPECC PAARQECMLG ESARKSMESD
PEDFSDETNT ETLYGTSPPS TPRQMKRLSA KHQRNSAGRP ASRSNLKEKM NTPSQSPHKD
LGKGVETVEE YSYKQEKKIR ATLRTTERDH KKNAQCSFML DSVAGSLPKK SIPDVDLNKP
YLSLGCSNAK LPVSMPMPIA RTARQTSRTD CPADRLKFFE TLRLLLKLTS VSKKKDREQR
GQENTAAFWF NRSNELIWLE LQAWHAGRTI NDQDLFLYTA RQAIPDIINE ILTFKVNYGS
IAFSSNGAGF NGPLVEGQCR TPQETNRVGC SSYHEHLQRQ RVSFEQVKRI MELLEYMEAL
YPSLQALQKD YERYAAKDFE DRVQALCLWL NITKDLNQKL RIMGTVLGIK NLSDIGWPVF
EIPSPRPSKG YEPEDEVEDT EVELRELESG TEESDEEPTP SPRVPELRLS TDAILDSRSQ
GCVSRKLERL ESEEDSIGWG TADCGPEASR HCLTSIYRPF VDKALKQMGL RKLILRLHKL
MNGSLQRARV ALVKDDRPVE FSDFPGPMWG SDYVQLSGTP PSSEQKCSAV SWEELRAMDL
PSFEPAFLVL CRVLLNVIHE CLKLRLEQRP AGEPSLLSIK QLVRECKEVL KGGLLMKQYY
QFMLQEVLGG LEKTDCNMDA FEEDLQKMLM VYFDYMRSWI QMLQQLPQAS HSLKNLLEEE
WNFTKEITHY IRGGEAQAGK LFCDIAGMLL KSTGSFLESG LQESCAELWT SADDNGAADE
LRRSVIEISR ALKELFHEAR ERASKALGFA KMLRKDLEIA AEFVLSASAR ELLDALKAKQ
YVKVQIPGLE NLHVFVPDSL AEEKKIILQL LNAATGKDCS KDPDDVFMDA FLLLTKHGDR
ARDSEDGWGT WEARAVKIVP QVETVDTLRS MQVDNLLLVV MESAHLVLQR KAFQQSIEGL
MTVRHEQTSS QPIIAKGLQQ LKNDALELCN RISDAIDRVD HMFTLEFDAE VEESESATLQ
QYYREAMIQG YNFGFEYHKE VVRLMSGEFR QKIGDKYISF AQKWMNYVLT KCESGRGTRP
RWATQGFDFL QAIEPAFISA LPEDDFLSLQ ALMNECIGHV IGKPHSPVTA IHRNSPRPVK
VPRCHSDPPN PHLIIPTPEG FSTRSVPSDA RTHGNSVAAA AAVAAAATTA AGRPGPGGGD
SVPAKPVNTA PDTRGSSVPE NDRLASIAAE LQFRSLSRHS SPTEERDEPA YPRSDSSGST
RRSWELRTLI SQTKDSASKQ GPIEAIQKSV RLFEERRYRE MRRKNIIGQV CDTPKSYDNV
MHVGLRKVTF KWQRGNKIGE GQYGKVYTCI SVDTGELMAM KEIRFQPNDH KTIKETADEL
KIFEGIKHPN LVRYFGVELH REEMYIFMEY CDEGTLEEVS RLGLQEHVIR LYTKQITVAI
NVLHEHGIVH RDIKGANIFL TSSGLIKLGD FGCSVKLKNN AQTMPGEVNS TLGTAAYMAP
EVITRAKGEG HGRAADIWSL GCVVIEMVTG KRPWHEYEHN FQIMYKVGMG HKPPIPERLS
PEGKAFLSHC LESDPKIRWT ASQLLDHAFV KVCTDEE


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