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Histone-lysine N-methyltransferase mes-2 (EC 2.1.1.43) (E(z) homolog) (Maternal-effect sterile protein 2)

 MES2_CAEEL              Reviewed;         773 AA.
O17514; O62335;
28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
28-MAR-2003, sequence version 2.
22-NOV-2017, entry version 130.
RecName: Full=Histone-lysine N-methyltransferase mes-2;
EC=2.1.1.43;
AltName: Full=E(z) homolog;
AltName: Full=Maternal-effect sterile protein 2;
Name=mes-2; ORFNames=R06A4.7;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 628-SER-LYS-629 AND TYR-674.
STRAIN=Bristol N2;
PubMed=9609829;
Holdeman R., Nehrt S., Strome S.;
"MES-2, a maternal protein essential for viability of the germline in
Caenorhabditis elegans, is homologous to a Drosophila Polycomb group
protein.";
Development 125:2457-2467(1998).
[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]
IDENTIFICATION IN A COMPLEX WITH MES-3 AND MES-6.
PubMed=11320248; DOI=10.1073/pnas.081016198;
Xu L., Fong Y., Strome S.;
"The Caenorhabditis elegans maternal-effect sterile proteins, MES-2,
MES-3, and MES-6, are associated in a complex in embryos.";
Proc. Natl. Acad. Sci. U.S.A. 98:5061-5066(2001).
[4]
FUNCTION.
PubMed=12077420; DOI=10.1126/science.1070790;
Fong Y., Bender L., Wang W., Strome S.;
"Regulation of the different chromatin states of autosomes and X
chromosomes in the germ line of C. elegans.";
Science 296:2235-2238(2002).
[5]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH MES-3 AND MES-6, AND
MUTAGENESIS OF 628-SER-LYS-629 AND TYR-674.
PubMed=15380065; DOI=10.1016/j.cub.2004.08.062;
Bender L.B., Cao R., Zhang Y., Strome S.;
"The MES-2/MES-3/MES-6 complex and regulation of histone H3
methylation in C. elegans.";
Curr. Biol. 14:1639-1643(2004).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=22212395; DOI=10.1111/j.1474-9726.2011.00785.x;
Ni Z., Ebata A., Alipanahiramandi E., Lee S.S.;
"Two SET domain containing genes link epigenetic changes and aging in
Caenorhabditis elegans.";
Aging Cell 11:315-325(2012).
[7]
FUNCTION.
PubMed=26365259; DOI=10.1016/j.cub.2015.07.051;
Mao H., Zhu C., Zong D., Weng C., Yang X., Huang H., Liu D., Feng X.,
Guang S.;
"The Nrde pathway mediates small-RNA-directed histone H3 lysine 27
trimethylation in Caenorhabditis elegans.";
Curr. Biol. 25:2398-2403(2015).
[8]
DISRUPTION PHENOTYPE.
PubMed=26904949; DOI=10.1016/j.celrep.2016.01.065;
Lee B.C., Lin Z., Yuen K.W.;
"RbAp46/48(LIN-53) is required for holocentromere assembly in
Caenorhabditis elegans.";
Cell Rep. 14:1819-1828(2016).
-!- FUNCTION: Polycomb group (PcG) protein. Catalytic subunit of a the
mes-2/mes-3/mes-6 complex, which methylates 'Lys-27' of histone
H3, leading to transcriptional repression of the affected target
genes. PcG proteins act by forming multiprotein complexes, which
are required to maintain the transcriptionally repressive state of
homeotic genes throughout development. PcG proteins are not
required to initiate repression, but to maintain it during later
stages of development. The mes-2/mes-3/mes-6 complex may
participate in the global inactivation of the X chromosomes in
germline cells. This complex is required to exclude mes-4 from the
inactivated X-chromosomes in germline cells (PubMed:12077420,
PubMed:15380065). Required for small-RNA-induced H3K27
trimethylation (PubMed:26365259). Involved in the negative
regulation of lifespan in a germline-independent fashion
(PubMed:22212395). {ECO:0000269|PubMed:12077420,
ECO:0000269|PubMed:15380065, ECO:0000269|PubMed:22212395,
ECO:0000269|PubMed:26365259}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
-!- SUBUNIT: Interacts directly with mes-6 via its N-terminal domain
(PubMed:11320248). Forms a heterotrimeric complex with mes-3 and
mes-6 (PubMed:11320248, PubMed:15380065). Does not interact with
mes-4 (PubMed:11320248). {ECO:0000269|PubMed:11320248,
ECO:0000269|PubMed:15380065}.
-!- INTERACTION:
Q9GYS1:mes-6; NbExp=5; IntAct=EBI-11615731, EBI-314965;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9609829}.
-!- TISSUE SPECIFICITY: In adults, it is predominantly expressed in
the germline, and weakly expressed in intestinal cells.
{ECO:0000269|PubMed:9609829}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Expressed in all cells of early embryos. In late embryos and L1
larva, it is weakly expressed, while it is expressed at
intermediate levels in the germline of L4 larvae.
{ECO:0000269|PubMed:9609829}.
-!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in extended
lifespan in wild type worms and in a glp-1(e2141) mutant
background which lacks a germline (PubMed:22212395). Also leads to
reduced H3K27me3 levels on metaphase chromosomes
(PubMed:26904949). {ECO:0000269|PubMed:22212395,
ECO:0000269|PubMed:26904949}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. EZ subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
-----------------------------------------------------------------------
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EMBL; AF011893; AAC27124.1; -; mRNA.
EMBL; Z83120; CAB05589.2; -; Genomic_DNA.
EMBL; Z81515; CAB05589.2; JOINED; Genomic_DNA.
PIR; T21436; T21436.
RefSeq; NP_496992.3; NM_064591.5.
UniGene; Cel.19654; -.
ProteinModelPortal; O17514; -.
BioGrid; 40377; 2.
IntAct; O17514; 2.
MINT; MINT-197410; -.
STRING; 6239.R06A4.7; -.
EPD; O17514; -.
PaxDb; O17514; -.
PeptideAtlas; O17514; -.
PRIDE; O17514; -.
EnsemblMetazoa; R06A4.7; R06A4.7; WBGene00003220.
GeneID; 175096; -.
KEGG; cel:CELE_R06A4.7; -.
UCSC; R06A4.7; c. elegans.
CTD; 175096; -.
WormBase; R06A4.7; CE28067; WBGene00003220; mes-2.
eggNOG; KOG1079; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00760000119228; -.
InParanoid; O17514; -.
KO; K11430; -.
OMA; VHWIPIE; -.
OrthoDB; EOG091G09L0; -.
PhylomeDB; O17514; -.
Reactome; R-CEL-212300; PRC2 methylates histones and DNA.
Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
Reactome; R-CEL-8953750; Transcriptional Regulation by E2F6.
PRO; PR:O17514; -.
Proteomes; UP000001940; Chromosome II.
Bgee; WBGene00003220; -.
GO; GO:0000786; C:nucleosome; IDA:WormBase.
GO; GO:0031519; C:PcG protein complex; IPI:WormBase.
GO; GO:0042054; F:histone methyltransferase activity; IDA:WormBase.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-EC.
GO; GO:0007276; P:gamete generation; IMP:WormBase.
GO; GO:0007281; P:germ cell development; IMP:WormBase.
GO; GO:0042078; P:germ-line stem cell division; IMP:WormBase.
GO; GO:0070734; P:histone H3-K27 methylation; IMP:WormBase.
GO; GO:0098532; P:histone H3-K27 trimethylation; IMP:WormBase.
GO; GO:0016571; P:histone methylation; IDA:WormBase.
GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:WormBase.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:WormBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR026489; CXC_dom.
InterPro; IPR001214; SET_dom.
Pfam; PF00856; SET; 1.
SMART; SM00317; SET; 1.
PROSITE; PS51633; CXC; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
Complete proteome; Developmental protein; Methyltransferase; Nucleus;
Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
Transcription regulation; Transferase.
CHAIN 1 773 Histone-lysine N-methyltransferase mes-2.
/FTId=PRO_0000213994.
DOMAIN 505 614 CXC. {ECO:0000255|PROSITE-
ProRule:PRU00970}.
DOMAIN 616 737 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
REGION 1 194 Interaction with mes-6.
COMPBIAS 531 600 Cys-rich.
MUTAGEN 628 629 SK->PE: In bn48; maternal-effect
mutation. Progeny defects in gonad
proliferation. Germ cell degeneration.
Reduced levels of 'H3-K27Me2' and 'H3-
K27Me3'. {ECO:0000269|PubMed:15380065,
ECO:0000269|PubMed:9609829}.
MUTAGEN 674 674 Y->H: In bn72; maternal-effect mutation.
Progeny defects in gonad proliferation.
Germ cell degeneration. Reduced levels of
'H3-K27Me2' and 'H3-K27Me3'.
{ECO:0000269|PubMed:15380065,
ECO:0000269|PubMed:9609829}.
CONFLICT 483 484 RK -> VQ (in Ref. 1; AAC27124).
{ECO:0000305}.
SEQUENCE 773 AA; 88821 MW; 91ABEBAD94A1D51E CRC64;
MSNSEPSTST PSGKTKKRGK KCETSMGKSK KSKNLPRFVK IQPIFSSEKI KETVCEQGIE
ECKRMLKGHF NAIKDDYDIR VKDELDTDIK DWLKDASSSV NEYRRRLQEN LGEGRTIAKF
SFKNCEKYEE NDYKVSDSTV TWIKPDRTEE GDLMKKFRAP CSRIEVGDIS PPMIYWVPIE
QSVATPDQLR LTHMPYFGDG IDDGNIYEHL IDMFPDGIHG FSDNWSYVND WILYKLCRAA
LKDYQGSPDV FYYTLYRLWP NKSSQREFSS AFPVLCENFA EKGFDPSSLE PWKKTKIAEG
AQNLRNPTCY ACLAYTCAIH GFKAEIPIEF PNGEFYNAML PLPNNPENDG KMCSGNCWKS
VTMKEVSEVL VPDSEEILQK EVKIYFMKSR IAKMPIEDGA LIVNIYVFNT YIPFCEFVKK
YVDEDDEESK IRSCRDAYHL MMSMAENVSA RRLKMGQPSN RLSIKDRVNN FRRNQLSQEK
AKRKLRHDSL RIQALRDGLD AEKLIREDDM RDSQRNSEKV RMTAVTPITA CRHAGPCNAT
AENCACRENG VCSYMCKCDI NCSQRFPGCN CAAGQCYTKA CQCYRANWEC NPMTCNMCKC
DAIDSNIIKC RNFGMTRMIQ KRTYCGPSKI AGNGLFLLEP AEKDEFITEY TGERISDDEA
ERRGAIYDRY QCSYIFNIET GGAIDSYKIG NLARFANHDS KNPTCYARTM VVAGEHRIGF
YAKRRLEISE ELTFDYSYSG EHQIAFRMVQ TKERSEKPSR PKSQKLSKPM TSE


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