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Histone-lysine N-methyltransferase mes-4 (EC 2.1.1.43) (Maternal-effect sterile protein 4)

 MES4_CAEEL              Reviewed;         898 AA.
Q9NH52; Q9XXS4;
28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
27-SEP-2017, entry version 132.
RecName: Full=Histone-lysine N-methyltransferase mes-4;
EC=2.1.1.43;
AltName: Full=Maternal-effect sterile protein 4;
Name=mes-4; ORFNames=Y2H9A.1;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, DEVELOPMENTAL STAGE,
FUNCTION, MUTAGENESIS OF 877-VAL--ILE-898, AND DISRUPTION PHENOTYPE.
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).
[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]
FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF
877-VAL--ILE-898, AND DISRUPTION PHENOTYPE.
PubMed=16968818; DOI=10.1242/dev.02584;
Bender L.B., Suh J., Carroll C.R., Fong Y., Fingerman I.M.,
Briggs S.D., Cao R., Zhang Y., Reinke V., Strome S.;
"MES-4: an autosome-associated histone methyltransferase that
participates in silencing the X chromosomes in the C. elegans germ
line.";
Development 133:3907-3917(2006).
[4]
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).
-!- FUNCTION: Histone methyltransferase. Dimethylates 'Lys-36' of
histone H3, a specific tag for epigenetic transcriptional
activation. Plays a central role in early development and is
responsible for all H3 'Lys-36' dimethylation until about the 40-
cell stage. Indirectly involved in the global inactivation of the
X chromosomes in germline cells, possibly by excluding the mes-2-
mes-3-mes-6 repressive Polycomb complex from the autosomes
(PubMed:12077420, PubMed:16968818). Not related to transcription
elongation (PubMed:12077420, PubMed:16968818). Required for small-
RNA-induced H3K27 trimethylation (PubMed:26365259).
{ECO:0000269|PubMed:12077420, ECO:0000269|PubMed:16968818,
ECO:0000269|PubMed:26365259}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:16968818}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16968818}.
Chromosome {ECO:0000269|PubMed:16968818}. Note=Specifically
associated with the autosomes and with the distal tip of
chromosome X. Colocalizes with methylated 'Lys-4' of histone H3.
-!- TISSUE SPECIFICITY: In adults, it is predominantly expressed in
the germline, and weakly expressed in intestinal cells.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Expressed in all cells of early embryos. In late embryos and L1
larva, it is weakly expressed in somatic cells, while it is
expressed at intermediate levels in the primordial germ cells Z2
and Z3. {ECO:0000269|PubMed:12077420}.
-!- DISRUPTION PHENOTYPE: Derepression of X-linked genes in the
germline. {ECO:0000269|PubMed:12077420,
ECO:0000269|PubMed:16968818}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. Histone-lysine methyltransferase
family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF233290; AAF62516.1; -; mRNA.
EMBL; AL021448; CAA16276.2; -; Genomic_DNA.
PIR; T26577; T26577.
RefSeq; NP_506333.1; NM_073932.4.
UniGene; Cel.6195; -.
ProteinModelPortal; Q9NH52; -.
BioGrid; 44841; 16.
IntAct; Q9NH52; 11.
MINT; MINT-1040434; -.
STRING; 6239.Y2H9A.1.2; -.
EPD; Q9NH52; -.
PaxDb; Q9NH52; -.
PeptideAtlas; Q9NH52; -.
EnsemblMetazoa; Y2H9A.1; Y2H9A.1; WBGene00003222.
GeneID; 179824; -.
KEGG; cel:CELE_Y2H9A.1; -.
UCSC; Y2H9A.1; c. elegans.
CTD; 179824; -.
WormBase; Y2H9A.1; CE27781; WBGene00003222; mes-4.
eggNOG; KOG1081; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00780000121845; -.
InParanoid; Q9NH52; -.
KO; K07117; -.
OMA; CYPAGAR; -.
OrthoDB; EOG091G02U7; -.
PhylomeDB; Q9NH52; -.
PRO; PR:Q9NH52; -.
Proteomes; UP000001940; Chromosome V.
Bgee; WBGene00003222; -.
GO; GO:0030849; C:autosome; IDA:WormBase.
GO; GO:0005694; C:chromosome; IDA:WormBase.
GO; GO:0000228; C:nuclear chromosome; IDA:UniProtKB.
GO; GO:0000805; C:X chromosome; IDA:WormBase.
GO; GO:0042054; F:histone methyltransferase activity; IDA:WormBase.
GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IMP:WormBase.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016458; P:gene silencing; IMP:UniProtKB.
GO; GO:0018992; P:germ-line sex determination; IMP:UniProtKB.
GO; GO:0010452; P:histone H3-K36 methylation; IMP:WormBase.
GO; GO:0016571; P:histone methylation; IDA:WormBase.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:WormBase.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR001214; SET_dom.
Pfam; PF00856; SET; 1.
SMART; SM00508; PostSET; 1.
SMART; SM00317; SET; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
Chromatin regulator; Chromosome; Complete proteome;
Developmental protein; Metal-binding; Methyltransferase; Nucleus;
Reference proteome; Repeat; S-adenosyl-L-methionine; Transferase;
Zinc; Zinc-finger.
CHAIN 1 898 Histone-lysine N-methyltransferase mes-4.
/FTId=PRO_0000186083.
DOMAIN 537 665 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 671 687 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
ZN_FING 126 214 PHD-type 1.
ZN_FING 303 355 PHD-type 2.
MUTAGEN 877 898 Missing: In BN87; maternal-effect
mutation. Progeny defects in gonad
proliferation. Germ cell degeneration.
Abolishes histone methyltransferase
activity. {ECO:0000269|PubMed:12077420,
ECO:0000269|PubMed:16968818}.
SEQUENCE 898 AA; 100065 MW; 0FA6BC754FC9E295 CRC64;
MLPSSGDSSK ENCAPQDGIV EKEGPNKPFK KKNVKQRNAT PQGAGSETSS NAEDKQEEAP
ILTNAPKDII SMQIQETKAF LSEYEEFVDT DYPKTTFTHV PRKFLSVSPF TPIEADAEGE
FLPDADSKCV ICHEEKDKTG KSDLITCHGY INGEMDDGKR LLGNIPMFPC RSKFHASCMI
NYNSGGFHFQ YAARLECQAR LLCPLHCCNS CNLDHHKQSA YVGDIAECAL CLRAFHLTSC
YPSGGRDLNV SITIGGKVEK FEMIICPAHY LPGADVQFYN KHKKRKNAVT VVPKADVTMK
SHIKACCVIG CEKSSNSKTI MCKTCCRSFH SGCREVETLN GKPIPDDQCE SCVCGDPIPQ
NTLILAKWTD NSFWLALTLD WYKYPTGNRG NINFERLGYT VVQWLIPQEN DKEKQPLMSI
VPVSDIARLT KNYFSLAKNS TLRNLWEEKY EEQADTALKR CPYVCKTVFG RLRTSVYYKC
EPKLEEYHNN EVCNCEGADR CTKLSCQYLA DDYECPPSCS KKGVCHNRQV SMGIVSEKIK
LAATLCKGYG VFAKGQIEKD EYICEYVGEI IDKAEKKRRL DSVSISRDFQ ANHYMMELHK
GLTVDAARYG NISRYINHSC DPNAASFVTK VFVKKTKEGS LYDTRSYIRA IRTIDDGDEI
TFSYNMNNEE NLPDCECGAE NCMGTMGKAK REKPEVADSS EKAAKKNKSS KKKSVKNQNR
KSQEAGKNGT ASKKSEISPS KPSTSSASST SFVQQASWPI SQNKKNLKKN SNQPVADTGS
TLSTSTELNF HEKPQELLSP VSSRSRAASS STPRAQKSKS RRDDVESEAP PVKRATPSLQ
TIQETGKAIE FPATKSAITK ARALSTQSVP SPHTVEVKVR AISTRGRVQK ETKRFEPI


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