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Dual specificity mitogen-activated protein kinase kinase 1 (MAP kinase kinase 1) (MAPKK 1) (EC 2.7.12.2) (ERK activator kinase 1) (MAPK/ERK kinase 1) (MEK 1)

 MP2K1_MOUSE             Reviewed;         393 AA.
P31938;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
27-SEP-2017, entry version 180.
RecName: Full=Dual specificity mitogen-activated protein kinase kinase 1;
Short=MAP kinase kinase 1;
Short=MAPKK 1;
EC=2.7.12.2;
AltName: Full=ERK activator kinase 1;
AltName: Full=MAPK/ERK kinase 1;
Short=MEK 1;
Name=Map2k1; Synonyms=Mek1, Prkmk1;
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], AND PARTIAL PROTEIN SEQUENCE.
PubMed=1411546; DOI=10.1126/science.1411546;
Crews C.M., Alessandrini A., Erikson R.L.;
"The primary structure of MEK, a protein kinase that phosphorylates
the ERK gene product.";
Science 258:478-480(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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]
PROTEIN SEQUENCE OF 4-20; 71-84; 114-136; 206-234 AND 363-384.
TISSUE=T-cell;
PubMed=1381507; DOI=10.1073/pnas.89.17.8205;
Crews C.M., Erikson R.L.;
"Purification of a murine protein-tyrosine/threonine kinase that
phosphorylates and activates the Erk-1 gene product: relationship to
the fission yeast byr1 gene product.";
Proc. Natl. Acad. Sci. U.S.A. 89:8205-8209(1992).
[4]
PROTEIN SEQUENCE OF 206-227; 270-291 AND 325-340, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[5]
PHOSPHORYLATION AND ENZYME REGULATION.
PubMed=8385802; DOI=10.1126/science.8385802;
Lange-Carter C.A., Pleiman C.M., Gardner A.M., Blumer K.J.,
Johnson G.L.;
"A divergence in the MAP kinase regulatory network defined by MEK
kinase and Raf.";
Science 260:315-319(1993).
[6]
CLEAVAGE BY ANTHRAX LETHAL FACTOR.
PubMed=9563949; DOI=10.1126/science.280.5364.734;
Duesbery N.S., Webb C.P., Leppla S.H., Gordon V.M., Klimpel K.R.,
Copeland T.D., Ahn N.G., Oskarsson M.K., Fukasawa K., Paull K.D.,
Vande Woude G.F.;
"Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal
factor.";
Science 280:734-737(1998).
[7]
INTERACTION WITH KSR1, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT
SER-218.
PubMed=10409742; DOI=10.1128/MCB.19.8.5523;
Stewart S., Sundaram M., Zhang Y., Lee J., Han M., Guan K.L.;
"Kinase suppressor of Ras forms a multiprotein signaling complex and
modulates MEK localization.";
Mol. Cell. Biol. 19:5523-5534(1999).
[8]
INTERACTION WITH MORG1.
PubMed=15118098; DOI=10.1073/pnas.0305894101;
Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E.,
Bissonette E.A., Weber M.J.;
"Modular construction of a signaling scaffold: MORG1 interacts with
components of the ERK cascade and links ERK signaling to specific
agonists.";
Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004).
[9]
DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH MAP2K2/MEK2,
PHOSPHORYLATION AT THR-292, AND MUTAGENESIS OF ASN-78 AND THR-292.
PubMed=19219045; DOI=10.1038/nsmb.1564;
Catalanotti F., Reyes G., Jesenberger V., Galabova-Kovacs G.,
de Matos Simoes R., Carugo O., Baccarini M.;
"A Mek1-Mek2 heterodimer determines the strength and duration of the
Erk signal.";
Nat. Struct. Mol. Biol. 16:294-303(2009).
[10]
REVIEW ON FUNCTION.
PubMed=9779990; DOI=10.1038/sj.onc.1202251;
Dhanasekaran N., Premkumar Reddy E.;
"Signaling by dual specificity kinases.";
Oncogene 17:1447-1455(1998).
[11]
REVIEW ON ENZYME REGULATION.
PubMed=15520807; DOI=10.1038/nrm1498;
Wellbrock C., Karasarides M., Marais R.;
"The RAF proteins take centre stage.";
Nat. Rev. Mol. Cell Biol. 5:875-885(2004).
[12]
REVIEW ON FUNCTION.
PubMed=19565474; DOI=10.1002/biof.52;
Yao Z., Seger R.;
"The ERK signaling cascade--views from different subcellular
compartments.";
BioFactors 35:407-416(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, and Spleen;
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).
[14]
REVIEW ON FUNCTION.
PubMed=21779493; DOI=10.1177/1947601911407328;
Wortzel I., Seger R.;
"The ERK cascade: distinct functions within various subcellular
organelles.";
Genes Cancer 2:195-209(2011).
-!- FUNCTION: Dual specificity protein kinase which acts as an
essential component of the MAP kinase signal transduction pathway.
Binding of extracellular ligands such as growth factors, cytokines
and hormones to their cell-surface receptors activates RAS and
this initiates RAF1 activation. RAF1 then further activates the
dual-specificity protein kinases MAP2K1/MEK1 and MAP2K2/MEK2. Both
MAP2K1/MEK1 and MAP2K2/MEK2 function specifically in the MAPK/ERK
cascade, and catalyze the concomitant phosphorylation of a
threonine and a tyrosine residue in a Thr-Glu-Tyr sequence located
in the extracellular signal-regulated kinases MAPK3/ERK1 and
MAPK1/ERK2, leading to their activation and further transduction
of the signal within the MAPK/ERK cascade. Depending on the
cellular context, this pathway mediates diverse biological
functions such as cell growth, adhesion, survival and
differentiation, predominantly through the regulation of
transcription, metabolism and cytoskeletal rearrangements. One
target of the MAPK/ERK cascade is peroxisome proliferator-
activated receptor gamma (PPARG), a nuclear receptor that promotes
differentiation and apoptosis. MAP2K1/MEK1 has been shown to
export PPARG from the nucleus. The MAPK/ERK cascade is also
involved in the regulation of endosomal dynamics, including
lysosome processing and endosome cycling through the perinuclear
recycling compartment (PNRC), as well as in the fragmentation of
the Golgi apparatus during mitosis. {ECO:0000269|PubMed:19219045}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Ras proteins such as HRAS mediate the
activation of RAF proteins such as RAF1 or BRAF which in turn
activate extracellular signal-regulated kinases (ERK) through MAPK
(mitogen-activated protein kinases) and ERK kinases MAP2K1/MEK1
and MAP2K2/MEK2. Activation occurs through phosphorylation of Ser-
218 and Ser-222. MAP2K1/MEK1 is also the target of negative feed-
back regulation by its substrate kinases, such as MAPK1/ERK2.
These phosphorylate MAP2K1/MEK1 on Thr-292, thereby facilitating
dephosphorylation of the activating residues Ser-218 and Ser-222.
Inhibited by serine/threonine phosphatase 2A.
-!- SUBUNIT: Found in a complex with at least BRAF, HRAS, MAP2K1,
MAPK3/ERK1 and RGS14. Forms heterodimers with KSR2 which further
dimerize to form tetramers. Interacts with ARRB2, LAMTOR3,
MAPK1/ERK2, RAF1, PPARG AND VRK2. Interacts with SGK1, BIRC6/bruce
(By similarity). Interacts with KSR-1 (PubMed:10409742). Interacts
with MORG1 (PubMed:15118098). Forms a heterodimer with MAP2K2/MEK2
(PubMed:19219045). {ECO:0000250|UniProtKB:P29678,
ECO:0000250|UniProtKB:Q01986, ECO:0000250|UniProtKB:Q02750,
ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:15118098,
ECO:0000269|PubMed:19219045}.
-!- INTERACTION:
Q8CFP6:Dnajc27; NbExp=3; IntAct=EBI-298860, EBI-9548773;
Q9ESN9-2:Mapk8ip3; NbExp=3; IntAct=EBI-298860, EBI-9549291;
Q13526:PIN1 (xeno); NbExp=4; IntAct=EBI-298860, EBI-714158;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome {ECO:0000250|UniProtKB:Q02750}.
Cytoplasm, cytoskeleton, microtubule organizing center, spindle
pole body {ECO:0000250|UniProtKB:Q02750}. Cytoplasm
{ECO:0000269|PubMed:10409742}. Nucleus
{ECO:0000250|UniProtKB:Q02750}. Membrane
{ECO:0000269|PubMed:10409742}; Peripheral membrane protein
{ECO:0000269|PubMed:10409742}. Note=Localizes at centrosomes
during prometaphase, midzone during anaphase and midbody during
telophase/cytokinesis (By similarity). Membrane localization is
probably regulated by its interaction with KSR1 (PubMed:10409742).
{ECO:0000250|UniProtKB:Q02750, ECO:0000269|PubMed:10409742}.
-!- DOMAIN: The proline-rich region localized between residues 270 and
307 is important for binding to RAF1 and activation of
MAP2K1/MEK1. {ECO:0000250}.
-!- PTM: Phosphorylation at Ser-218 and Ser-222 by MAP kinase kinase
kinases (RAF or MEKK1) positively regulates kinase activity. Also
phosphorylated at Thr-292 by MAPK1/ERK2 and at Ser-298 by PAK.
MAPK1/ERK2 phosphorylation of Thr-292 occurs in response to
cellular adhesion and leads to inhibition of Ser-298
phosphorylation by PAK. {ECO:0000269|PubMed:19219045,
ECO:0000269|PubMed:8385802}.
-!- DISRUPTION PHENOTYPE: Affects fibroblast shape and impairs
haptotaxis and adhesion-dependent ERK-signaling.
{ECO:0000269|PubMed:19219045}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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EMBL; L02526; AAA39523.1; -; mRNA.
EMBL; BC054754; AAH54754.1; -; mRNA.
CCDS; CCDS23277.1; -.
PIR; I59571; I59571.
RefSeq; NP_032953.1; NM_008927.3.
UniGene; Mm.248907; -.
ProteinModelPortal; P31938; -.
SMR; P31938; -.
BioGrid; 204949; 17.
CORUM; P31938; -.
DIP; DIP-467N; -.
IntAct; P31938; 7.
MINT; MINT-1518233; -.
STRING; 10090.ENSMUSP00000005066; -.
BindingDB; P31938; -.
ChEMBL; CHEMBL5860; -.
iPTMnet; P31938; -.
PhosphoSitePlus; P31938; -.
UCD-2DPAGE; P31938; -.
EPD; P31938; -.
PaxDb; P31938; -.
PeptideAtlas; P31938; -.
PRIDE; P31938; -.
Ensembl; ENSMUST00000005066; ENSMUSP00000005066; ENSMUSG00000004936.
GeneID; 26395; -.
KEGG; mmu:26395; -.
UCSC; uc009qbp.1; mouse.
CTD; 5604; -.
MGI; MGI:1346866; Map2k1.
eggNOG; KOG0581; Eukaryota.
eggNOG; ENOG410XQ5A; LUCA.
GeneTree; ENSGT00760000119199; -.
HOGENOM; HOG000234206; -.
HOVERGEN; HBG108518; -.
InParanoid; P31938; -.
KO; K04368; -.
OMA; ELMFGCP; -.
OrthoDB; EOG091G0DEC; -.
PhylomeDB; P31938; -.
TreeFam; TF105137; -.
BRENDA; 2.7.12.2; 3474.
Reactome; R-MMU-110056; MAPK3 (ERK1) activation.
Reactome; R-MMU-445144; Signal transduction by L1.
Reactome; R-MMU-5673000; RAF activation.
Reactome; R-MMU-5674135; MAP2K and MAPK activation.
Reactome; R-MMU-5674499; Negative feedback regulation of MAPK pathway.
ChiTaRS; Map2k1; mouse.
PRO; PR:P31938; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000004936; -.
CleanEx; MM_MAP2K1; -.
ExpressionAtlas; P31938; baseline and differential.
Genevisible; P31938; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005769; C:early endosome; TAS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005925; C:focal adhesion; TAS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; TAS:UniProtKB.
GO; GO:0005770; C:late endosome; TAS:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; TAS:UniProtKB.
GO; GO:0005634; C:nucleus; TAS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004708; F:MAP kinase kinase activity; IMP:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; TAS:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
GO; GO:0004728; F:signal transducer, downstream of receptor, with protein tyrosine phosphatase activity; IMP:MGI.
GO; GO:0000187; P:activation of MAPK activity; IMP:MGI.
GO; GO:0060020; P:Bergmann glial cell differentiation; IGI:MGI.
GO; GO:0007050; P:cell cycle arrest; ISO:MGI.
GO; GO:0048870; P:cell motility; IMP:MGI.
GO; GO:0090398; P:cellular senescence; ISO:MGI.
GO; GO:0021697; P:cerebellar cortex formation; IGI:MGI.
GO; GO:0060502; P:epithelial cell proliferation involved in lung morphogenesis; IGI:MGI.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IGI:MGI.
GO; GO:0060324; P:face development; IGI:MGI.
GO; GO:0007507; P:heart development; IGI:MGI.
GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
GO; GO:0060711; P:labyrinthine layer development; IMP:MGI.
GO; GO:0060425; P:lung morphogenesis; IGI:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0030182; P:neuron differentiation; IMP:MGI.
GO; GO:0060674; P:placenta blood vessel development; IMP:MGI.
GO; GO:0050772; P:positive regulation of axonogenesis; IGI:MGI.
GO; GO:0045597; P:positive regulation of cell differentiation; IDA:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0048679; P:regulation of axon regeneration; IGI:MGI.
GO; GO:2000641; P:regulation of early endosome to late endosome transport; TAS:UniProtKB.
GO; GO:0090170; P:regulation of Golgi inheritance; TAS:UniProtKB.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0001932; P:regulation of protein phosphorylation; IGI:MGI.
GO; GO:0032872; P:regulation of stress-activated MAPK cascade; TAS:UniProtKB.
GO; GO:0048538; P:thymus development; IGI:MGI.
GO; GO:0030878; P:thyroid gland development; IGI:MGI.
GO; GO:0060440; P:trachea formation; IGI: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;
ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
Direct protein sequencing; Kinase; Membrane; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
CHAIN 1 393 Dual specificity mitogen-activated
protein kinase kinase 1.
/FTId=PRO_0000086366.
DOMAIN 68 361 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 74 82 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 270 307 RAF1-binding. {ECO:0000250}.
COMPBIAS 262 307 Pro-rich.
ACT_SITE 190 190 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 97 97 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
SITE 8 9 Cleavage; by anthrax lethal factor.
{ECO:0000250}.
MOD_RES 218 218 Phosphoserine; by RAF.
{ECO:0000269|PubMed:10409742}.
MOD_RES 222 222 Phosphoserine; by RAF.
{ECO:0000250|UniProtKB:Q02750}.
MOD_RES 286 286 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 292 292 Phosphothreonine; by MAPK1.
{ECO:0000250|UniProtKB:Q01986}.
MOD_RES 298 298 Phosphoserine; by PAK.
{ECO:0000250|UniProtKB:Q02750}.
MUTAGEN 78 78 N->G: Impairs interaction with
MAP2K2/MEK2.
{ECO:0000269|PubMed:19219045}.
MUTAGEN 292 292 T->A: Results in hyperphosphorylation of
the RAF-dependent sites and prolonged ERK
phosphorylation.
{ECO:0000269|PubMed:19219045}.
MUTAGEN 292 292 T->D: Results in hypophosphorylation of
the RAF-dependent sites and faster ERK
inactivation.
{ECO:0000269|PubMed:19219045}.
CONFLICT 374 374 W -> Q (in Ref. 3; AA sequence).
{ECO:0000305}.
SEQUENCE 393 AA; 43474 MW; 01D1D18572AE40E7 CRC64;
MPKKKPTPIQ LNPAPDGSAV NGTSSAETNL EALQKKLEEL ELDEQQRKRL EAFLTQKQKV
GELKDDDFEK ISELGAGNGG VVFKVSHKPS GLVMARKLIH LEIKPAIRNQ IIRELQVLHE
CNSPYIVGFY GAFYSDGEIS ICMEHMDGGS LDQVLKKAGR IPEQILGKVS IAVIKGLTYL
REKHKIMHRD VKPSNILVNS RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY
SVQSDIWSMG LSLVEMAVGR YPIPPPDAKE LELLFGCHVE GDAAETPPRP RTPGRPLSSY
GMDSRPPMAI FELLDYIVNE PPPKLPSGVF SLEFQDFVNK CLIKNPAERA DLKQLMVHAF
IKRSDAEEVD FAGWLCSTIG LNQPSTPTHA ASI


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EIAAB25233 Canis familiaris,Canis lupus familiaris,Dog,Dual specificity mitogen-activated protein kinase kinase 2,ERK activator kinase 2,MAP kinase kinase 2,MAP2K2,MAPK_ERK kinase 2,MAPKK 2,MEK 2,MEK2
E1721b ELISA kit Bos taurus,Bovine,Dual specificity mitogen-activated protein kinase kinase 6,MAP kinase kinase 6,MAP2K6,MAPK_ERK kinase 6,MAPKK 6,MEK 6 96T
E1721b ELISA Bos taurus,Bovine,Dual specificity mitogen-activated protein kinase kinase 6,MAP kinase kinase 6,MAP2K6,MAPK_ERK kinase 6,MAPKK 6,MEK 6 96T
U1721b CLIA Bos taurus,Bovine,Dual specificity mitogen-activated protein kinase kinase 6,MAP kinase kinase 6,MAP2K6,MAPK_ERK kinase 6,MAPKK 6,MEK 6 96T


 

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