MES4_DROME
ID MES4_DROME Reviewed; 1427 AA.
AC Q8MT36; Q1LZ05; Q9VAY5;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Probable histone-lysine N-methyltransferase Mes-4;
DE EC=2.1.1.357;
DE AltName: Full=Maternal-effect sterile 4 homolog;
GN Name=Mes-4; ORFNames=CG4976;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-158; SER-169;
RP SER-433; SER-579; SER-581; SER-588; SER-604; THR-607; SER-721; THR-723 AND
RP SER-834, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Probable histone methyltransferase. Histone methylation gives
CC specific tags for epigenetic transcriptional activation or repression
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-methionine = 2 H(+)
CC + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60308, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61976; EC=2.1.1.357;
CC -!- INTERACTION:
CC Q8MT36; Q7JN06: BEAF-32; NbExp=3; IntAct=EBI-148375, EBI-134484;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM48433.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF56762.2; -; Genomic_DNA.
DR EMBL; AY118404; AAM48433.1; ALT_FRAME; mRNA.
DR EMBL; BT025221; ABF17912.1; -; mRNA.
DR RefSeq; NP_733239.1; NM_170360.2.
DR AlphaFoldDB; Q8MT36; -.
DR SMR; Q8MT36; -.
DR BioGRID; 68232; 3.
DR DIP; DIP-23366N; -.
DR IntAct; Q8MT36; 4.
DR MINT; Q8MT36; -.
DR STRING; 7227.FBpp0084636; -.
DR iPTMnet; Q8MT36; -.
DR PaxDb; Q8MT36; -.
DR PRIDE; Q8MT36; -.
DR EnsemblMetazoa; FBtr0085267; FBpp0084636; FBgn0039559.
DR GeneID; 43351; -.
DR KEGG; dme:Dmel_CG4976; -.
DR UCSC; CG4976-RA; d. melanogaster.
DR CTD; 43351; -.
DR FlyBase; FBgn0039559; Mes-4.
DR VEuPathDB; VectorBase:FBgn0039559; -.
DR eggNOG; KOG1081; Eukaryota.
DR InParanoid; Q8MT36; -.
DR OMA; MHADCLE; -.
DR OrthoDB; 507784at2759; -.
DR PhylomeDB; Q8MT36; -.
DR SignaLink; Q8MT36; -.
DR BioGRID-ORCS; 43351; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43351; -.
DR PRO; PR:Q8MT36; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0039559; Expressed in ovary and 30 other tissues.
DR ExpressionAtlas; Q8MT36; baseline and differential.
DR Genevisible; Q8MT36; DM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000228; C:nuclear chromosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:FlyBase.
DR GO; GO:0042054; F:histone methyltransferase activity; ISS:FlyBase.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0018992; P:germ-line sex determination; ISS:UniProtKB.
DR GO; GO:0010452; P:histone H3-K36 methylation; ISS:FlyBase.
DR GO; GO:0060820; P:inactivation of X chromosome by heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF00855; PWWP; 2.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00249; PHD; 3.
DR SMART; SM00293; PWWP; 2.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50812; PWWP; 2.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Chromosome; Metal-binding; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; S-adenosyl-L-methionine;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1427
FT /note="Probable histone-lysine N-methyltransferase Mes-4"
FT /id="PRO_0000186084"
FT DOMAIN 395..468
FT /note="PWWP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT DOMAIN 1049..1111
FT /note="PWWP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT DOMAIN 1182..1232
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 1234..1351
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1359..1375
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT ZN_FING 777..862
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 864..932
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 999..1044
FT /note="PHD-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 581
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 607
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 723
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 1427 AA; 159028 MW; FB6EFD62E814BEF3 CRC64;
MKLSTDAHSE IEGDAAHGNV LCNSASDSLT ATDEVAAGND ESVATEGDDV EIPRDTNNST
PVRLLDKPGQ NPVQNGAQPA AEESELESQR QTPVQKQQQQ RVSMVNRKRD LINLQSALSP
KYIGYANANS PTPLSDSDDT IRTTRRRVNQ AAALNNSSAG ETLAHDNASP RTPGGGGGGG
GDDSANQLLS KTYMSPIEKL LIKNGASSPN STGFEAGSED LGIRPIVRKH VKRKMKRVPK
AKVTLELDEK NQQEVDEKSV KTEPIDEEVD RTDEAPTQEA QTTAISIKSE TEAEHKAAVD
VHIKQEDTIR LDIVNNPVES TSIVITEEPK DLEKSTEELA FALPLASSTE VDLKSPPDLS
STALATSIKS PSSVSIDSAK GLSIVTDPGW PTYQVGDLFW GKVFSYCFWP CMVCPDPLGQ
IVGNMPSHPQ RSSLDNANVP IQVHVRFFAD NGRRNWIKPE NLLTFAGLKA FDDMREELRI
KHGPKSAKYR QMVPKRTKVV IWRQAIEEAQ AMTQIPYSDR LEKFYQTYEN VVTLNRQKRK
RTKYMMQDTS DVGSSLYDST DNLHNKQGTQ LLAVKRERSE SPFSPAFSPV KSKNEKRAKR
RKLSNGTEAD TGSNSMAVTP SQTETTVDSS AYENPEFRQL LSAVMEYVMM NRSDEKVEKV
LLSVVSNIWS LKQIQLRELE RDLASGEIEE PLGSSVVGRG SGVGTIKRLS NRLMTMMVRR
SMTPVVTPST TPAPSEPDRR LSEPPKTKKP VNRPIEEVIE DILQLDSKYL FRGLSREPIC
KYCYQAGSDL VRCSRTCSSW LHADCLERKV TGAPMPKIGS RKALVIPPTS KSPSPDEDHV
TADAKEVVAV GTSLVCHECN VGEPEGCVIC HQVESPAVPS TPRKEDSSSH TPIEDKLLTC
SQPMCGKRFH TSCCKYWPQA SSSKHSARCP RHVCHTCVSD DPSGKFQQLG SSKLAKCVRC
PATYHQLSKC IPAGTQMLNT TNIICPRHNI AKADAHVNVL WCYICVKGGE LVCCETCPIA
VHAHCRNIPI KTNESYICEE CESGRLPLYG EIVWAKFNNF RWWPAIILPP TEVPSNILKK
AHGENDFVVR FFGTHDHGWI SRRRVYLYIE GDTGDGHKTK SQLFRNYTTG VEEASRFLPI
IKARRQEQDM ERQSGNKLHP PPYVKIKTNK AVPPLRFSQN LEDLSTCNCL PVDEHPCGPE
AGCLNRMLFN ECNPEYCKAG SLCENRMFEQ RKSPRLEVVY MNERGFGLVN REPIAVGDFV
IEYVGEVINH AEFQRRMEQK QRDRDENYYF LGVEKDFIID AGPKGNLARF MNHSCEPNCE
TQKWTVNCIH RVGIFAIKDI PVNSELTFNY LWDDLMNNSK KACFCGAKRC SGEIGGKLKD
DAVKAHAKLK QMRRAKASAV RIHVKPKKTP KVKHISADDE PMDAKDE
