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Dual specificity mitogen-activated protein kinase kinase mek-2 (MAP kinase kinase mek-2) (EC 2.7.12.2)

 MEK2_CAEEL              Reviewed;         387 AA.
Q10664;
20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-FEB-2018, entry version 147.
RecName: Full=Dual specificity mitogen-activated protein kinase kinase mek-2;
Short=MAP kinase kinase mek-2;
EC=2.7.12.2;
Name=mek-2; ORFNames=Y54E10BL.6;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF PRO-237 AND GLU-238.
PubMed=7729690; DOI=10.1101/gad.9.6.742;
Wu Y., Han M., Guan K.-L.;
"MEK-2, a Caenorhabditis elegans MAP kinase kinase, functions in Ras-
mediated vulval induction and other developmental events.";
Genes Dev. 9:742-755(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[3]
INTERACTION WITH KSR-1.
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).
[4]
FUNCTION, AND MUTAGENESIS OF ASP-213.
STRAIN=Bristol N2;
PubMed=11689700; DOI=10.1128/MCB.21.23.8104-8116.2001;
Schutzman J.L., Borland C.Z., Newman J.C., Robinson M.K., Kokel M.,
Stern M.J.;
"The Caenorhabditis elegans EGL-15 signaling pathway implicates a DOS-
like multisubstrate adaptor protein in fibroblast growth factor signal
transduction.";
Mol. Cell. Biol. 21:8104-8116(2001).
[5]
FUNCTION, AND MUTAGENESIS OF SER-217; SER-223 AND SER-227.
PubMed=15268855; DOI=10.1016/j.cub.2004.07.022;
Nicholas H.R., Hodgkin J.;
"The ERK MAP kinase cascade mediates tail swelling and a protective
response to rectal infection in C. elegans.";
Curr. Biol. 14:1256-1261(2004).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19826475; DOI=10.1371/journal.pone.0007450;
Schouest K.R., Kurasawa Y., Furuta T., Hisamoto N., Matsumoto K.,
Schumacher J.M.;
"The germinal center kinase GCK-1 is a negative regulator of MAP
kinase activation and apoptosis in the C. elegans germline.";
PLoS ONE 4:E7450-E7450(2009).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20624915; DOI=10.1074/jbc.M110.146274;
Okuyama T., Inoue H., Ookuma S., Satoh T., Kano K., Honjoh S.,
Hisamoto N., Matsumoto K., Nishida E.;
"The ERK-MAPK pathway regulates longevity through SKN-1 and insulin-
like signaling in Caenorhabditis elegans.";
J. Biol. Chem. 285:30274-30281(2010).
-!- FUNCTION: Functions in the let-60 Ras signaling pathway; acts
downstream of lin-45 raf kinase, but before the sur-1/mpk-1 gene
product in controlling vulval cell differentiation
(PubMed:7729690). Required for progression of developing oocytes
through the pachytene stage (PubMed:19826475). Plays a role in
responses to M.nematophilum-mediated bacterial infection by
promoting tail swelling and preventing constipation
(PubMed:15268855). Involved in fluid homeostasis
(PubMed:11689700). Positively regulates lifespan upstream of mpk-1
(PubMed:20624915). {ECO:0000269|PubMed:11689700,
ECO:0000269|PubMed:15268855, ECO:0000269|PubMed:19826475,
ECO:0000269|PubMed:20624915, ECO:0000269|PubMed:7729690}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Activated by tyrosine and threonine
phosphorylation catalyzed by MAP kinase kinase kinases.
-!- SUBUNIT: Interacts with ksr-1. {ECO:0000269|PubMed:10409742}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes a defect in
pachytene progression resulting in a proximal gonad devoid of
nuclei. The phenotype is more severe in gck-1 km15 mutant
background (PubMed:19826475). RNAi-mediated knockdown in adults
decreases lifespan (PubMed:20624915).
{ECO:0000269|PubMed:19826475, ECO:0000269|PubMed:20624915}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U21107; AAA85118.1; -; mRNA.
EMBL; FO081804; CCD73487.1; -; Genomic_DNA.
PIR; A56466; A56466.
RefSeq; NP_491087.1; NM_058686.4.
UniGene; Cel.19739; -.
ProteinModelPortal; Q10664; -.
SMR; Q10664; -.
BioGrid; 37349; 5.
IntAct; Q10664; 3.
MINT; Q10664; -.
STRING; 6239.Y54E10BL.6; -.
iPTMnet; Q10664; -.
EPD; Q10664; -.
PaxDb; Q10664; -.
PeptideAtlas; Q10664; -.
PRIDE; Q10664; -.
EnsemblMetazoa; Y54E10BL.6; Y54E10BL.6; WBGene00003186.
GeneID; 171872; -.
KEGG; cel:CELE_Y54E10BL.6; -.
UCSC; Y54E10BL.6; c. elegans.
CTD; 171872; -.
WormBase; Y54E10BL.6; CE25437; WBGene00003186; mek-2.
eggNOG; KOG0581; Eukaryota.
eggNOG; ENOG410XQ5A; LUCA.
GeneTree; ENSGT00760000119199; -.
HOGENOM; HOG000234206; -.
InParanoid; Q10664; -.
KO; K04368; -.
OMA; IAGWVCK; -.
OrthoDB; EOG091G0DEC; -.
PhylomeDB; Q10664; -.
BRENDA; 2.7.12.2; 1045.
Reactome; R-CEL-110056; MAPK3 (ERK1) activation.
Reactome; R-CEL-112411; MAPK1 (ERK2) activation.
Reactome; R-CEL-445144; Signal transduction by L1.
Reactome; R-CEL-5673000; RAF activation.
Reactome; R-CEL-5674135; MAP2K and MAPK activation.
Reactome; R-CEL-5674499; Negative feedback regulation of MAPK pathway.
SignaLink; Q10664; -.
PRO; PR:Q10664; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00003186; -.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004708; F:MAP kinase kinase activity; IDA:WormBase.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
GO; GO:0006468; P:protein phosphorylation; IDA:WormBase.
GO; GO:0007265; P:Ras protein signal transduction; IGI:WormBase.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
GO; GO:0031098; P:stress-activated protein kinase signaling cascade; IBA:GO_Central.
GO; GO:0040025; P:vulval development; IGI:WormBase.
InterPro; IPR011009; Kinase-like_dom_sf.
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; Developmental protein;
Differentiation; Kinase; Meiosis; Nucleotide-binding; Oogenesis;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Transferase; Tyrosine-protein kinase.
CHAIN 1 387 Dual specificity mitogen-activated
protein kinase kinase mek-2.
/FTId=PRO_0000086322.
DOMAIN 73 360 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 79 87 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 195 195 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 102 102 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 223 223 Phosphoserine. {ECO:0000250}.
MOD_RES 227 227 Phosphoserine. {ECO:0000250}.
MUTAGEN 213 213 D->N: In n2678; rescues fluid
accumulation in crl-1 e1745ts mutant.
{ECO:0000269|PubMed:11689700}.
MUTAGEN 217 217 S->F: In n1989; severe constipation
following M.nematophilium infection.
{ECO:0000269|PubMed:15268855}.
MUTAGEN 223 223 S->E: Phosphomimetic mutant which, in a
wild type background, induces tail
swelling; in association with D-227.
MUTAGEN 227 227 S->D: Phosphomimetic mutant which, in a
wild type background, induces tail
swelling; in association with E-223.
{ECO:0000269|PubMed:15268855}.
MUTAGEN 237 237 P->S: In KU114; 8% larval lethality.
{ECO:0000269|PubMed:7729690}.
MUTAGEN 238 238 E->K: In H294; 100% larval lethality.
{ECO:0000269|PubMed:7729690}.
SEQUENCE 387 AA; 42794 MW; 8FD8556236B6624B CRC64;
MSSGKRRNPL GLSLPPTVNE QSESGEATAE EATATVPLEE QLKKLGLTEP QTQRLSEFLQ
VKEGIKELSE DMLQTEGELG HGNGGVVNKC VHRKTGVIMA RKLVHLEIKP SVRQQIVKEL
AVLHKCNSPF IVGFYGAFVD NNDISICMEY MDGLSLDIVL KKVGRLPEKF VGRISVAVVR
GLTYLKDEIK ILHRDVKPSN MLVNSNGEIK LCDFGVSGML IDSMANSFVG TRSYMAPERL
TGSHYTISSD IWSFGLSLVE LLIGRYPVPA PSQAEYATMF NVAENEIELA DSLEEPNYHP
PSNPASMAIF EMLDYIVNGP PPTLPKRFFT DEVIGFVSKC LRKLPSERAT LKSLTADVFF
TQYADHDDQG EFAVFVKGTI NLPKLNP


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