Reviewed, UniProtKB/Swiss-Prot Q8MT36 (MES4_DROME)

Names and origin

Protein names

Recommended name:
    Probable histone-lysine N-methyltransferase Mes-4
    EC=2.1.1.43
Alternative name(s):
    Maternal-effect sterile 4 homolog

Gene names

Name:	Mes-4
ORF Names:	CG4976

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	1427 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Probable histone methyltransferase. Histone methylation gives specific tags for epigenetic transcriptional activation or repression By similarity.
Catalytic activity	S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine.
Subcellular location	Nucleus By similarity.
Sequence similarities	Belongs to the histone-lysine methyltransferase family. SET2 subfamily. Contains 1 AWS domain. Contains 3 PHD-type zinc fingers. Contains 1 post-SET domain. Contains 2 PWWP domains. Contains 1 SET domain.
Sequence caution	The sequence AAM48433.1 differs from that shown. Reason: Frameshift at position 348.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW gene silencing Inferred from sequence or structural similarity. Source: UniProtKB germ-line sex determination Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	nuclear chromosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	histone-lysine N-methyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1427	1427	Probable histone-lysine N-methyltransferase Mes-4		PRO_0000186084
Regions
	Domain	395 – 468	74	PWWP 1
	Domain	1049 – 1111	63	PWWP 2
	Domain	1182 – 1232	51	AWS
	Domain	1233 – 1355	123	SET
	Domain	1359 – 1375	17	Post-SET
	Zinc finger	777 – 862	86	PHD-type 1
	Zinc finger	864 – 932	69	PHD-type 2
	Zinc finger	999 – 1044	46	PHD-type 3
	Compositional bias	95 – 100	6	Poly-Gln
	Compositional bias	174 – 181	8	Poly-Gly
Amino acid modifications
	Modified residue	157	1	Phosphoserine Ref.5
	Modified residue	158	1	Phosphoserine Ref.5
	Modified residue	169	1	Phosphoserine Ref.5
	Modified residue	433	1	Phosphoserine Ref.5
	Modified residue	579	1	Phosphoserine Ref.5
	Modified residue	581	1	Phosphoserine Ref.5
	Modified residue	588	1	Phosphoserine Ref.5
	Modified residue	604	1	Phosphoserine Ref.5
	Modified residue	607	1	Phosphothreonine Ref.5
	Modified residue	721	1	Phosphoserine Ref.5
	Modified residue	723	1	Phosphothreonine Ref.5
	Modified residue	834	1	Phosphoserine Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q8MT36-1 [UniParc]. Last modified March 28, 2003. Version 2. Checksum: FB6EFD62E814BEF3	FASTA	1,427	159,028
	10 20 30 40 50 60 MKLSTDAHSE IEGDAAHGNV LCNSASDSLT ATDEVAAGND ESVATEGDDV EIPRDTNNST 70 80 90 100 110 120 PVRLLDKPGQ NPVQNGAQPA AEESELESQR QTPVQKQQQQ RVSMVNRKRD LINLQSALSP 130 140 150 160 170 180 KYIGYANANS PTPLSDSDDT IRTTRRRVNQ AAALNNSSAG ETLAHDNASP RTPGGGGGGG 190 200 210 220 230 240 GDDSANQLLS KTYMSPIEKL LIKNGASSPN STGFEAGSED LGIRPIVRKH VKRKMKRVPK 250 260 270 280 290 300 AKVTLELDEK NQQEVDEKSV KTEPIDEEVD RTDEAPTQEA QTTAISIKSE TEAEHKAAVD 310 320 330 340 350 360 VHIKQEDTIR LDIVNNPVES TSIVITEEPK DLEKSTEELA FALPLASSTE VDLKSPPDLS 370 380 390 400 410 420 STALATSIKS PSSVSIDSAK GLSIVTDPGW PTYQVGDLFW GKVFSYCFWP CMVCPDPLGQ 430 440 450 460 470 480 IVGNMPSHPQ RSSLDNANVP IQVHVRFFAD NGRRNWIKPE NLLTFAGLKA FDDMREELRI 490 500 510 520 530 540 KHGPKSAKYR QMVPKRTKVV IWRQAIEEAQ AMTQIPYSDR LEKFYQTYEN VVTLNRQKRK 550 560 570 580 590 600 RTKYMMQDTS DVGSSLYDST DNLHNKQGTQ LLAVKRERSE SPFSPAFSPV KSKNEKRAKR 610 620 630 640 650 660 RKLSNGTEAD TGSNSMAVTP SQTETTVDSS AYENPEFRQL LSAVMEYVMM NRSDEKVEKV 670 680 690 700 710 720 LLSVVSNIWS LKQIQLRELE RDLASGEIEE PLGSSVVGRG SGVGTIKRLS NRLMTMMVRR 730 740 750 760 770 780 SMTPVVTPST TPAPSEPDRR LSEPPKTKKP VNRPIEEVIE DILQLDSKYL FRGLSREPIC 790 800 810 820 830 840 KYCYQAGSDL VRCSRTCSSW LHADCLERKV TGAPMPKIGS RKALVIPPTS KSPSPDEDHV 850 860 870 880 890 900 TADAKEVVAV GTSLVCHECN VGEPEGCVIC HQVESPAVPS TPRKEDSSSH TPIEDKLLTC 910 920 930 940 950 960 SQPMCGKRFH TSCCKYWPQA SSSKHSARCP RHVCHTCVSD DPSGKFQQLG SSKLAKCVRC 970 980 990 1000 1010 1020 PATYHQLSKC IPAGTQMLNT TNIICPRHNI AKADAHVNVL WCYICVKGGE LVCCETCPIA 1030 1040 1050 1060 1070 1080 VHAHCRNIPI KTNESYICEE CESGRLPLYG EIVWAKFNNF RWWPAIILPP TEVPSNILKK 1090 1100 1110 1120 1130 1140 AHGENDFVVR FFGTHDHGWI SRRRVYLYIE GDTGDGHKTK SQLFRNYTTG VEEASRFLPI 1150 1160 1170 1180 1190 1200 IKARRQEQDM ERQSGNKLHP PPYVKIKTNK AVPPLRFSQN LEDLSTCNCL PVDEHPCGPE 1210 1220 1230 1240 1250 1260 AGCLNRMLFN ECNPEYCKAG SLCENRMFEQ RKSPRLEVVY MNERGFGLVN REPIAVGDFV 1270 1280 1290 1300 1310 1320 IEYVGEVINH AEFQRRMEQK QRDRDENYYF LGVEKDFIID AGPKGNLARF MNHSCEPNCE 1330 1340 1350 1360 1370 1380 TQKWTVNCIH RVGIFAIKDI PVNSELTFNY LWDDLMNNSK KACFCGAKRC SGEIGGKLKD 1390 1400 1410 1420 DAVKAHAKLK QMRRAKASAV RIHVKPKKTP KVKHISADDE PMDAKDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-158; SER-169; SER-433; SER-579; SER-581; SER-588; SER-604; THR-607; SER-721; THR-723 AND SER-834, MASS SPECTROMETRY. Tissue: Embryo.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014297 Genomic DNA. Translation: AAF56762.2. AY118404 mRNA. Translation: AAM48433.1. Frameshift. BT025221 mRNA. Translation: ABF17912.1.
RefSeq	NP_733239.1.
UniGene	Dm.23351
3D structure databases
HSSP	HSSP built from PDB template 1MM2 based on UniProtKB Q14839.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:23366N.
IntAct	Q8MT36. 1 interaction.
Genome annotation databases
Ensembl	FBgn0039559. Drosophila melanogaster. [Contig view]
GeneID	43351.
KEGG	dme:Dmel_CG4976.
NMPDR	fig|7227.3.peg.15057.
Organism-specific databases
FlyBase	FBgn0039559. Mes-4.
Phylogenomic databases
HOGENOM	Q8MT36.
OMA	Q8MT36. ICEECES.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-013791-MON.
BRENDA	2.1.1.43. 48.
Gene expression databases
ArrayExpress	Q8MT36.
GermOnline	CG4976. Drosophila melanogaster.
Family and domain databases
InterPro	IPR006560. AWS. IPR003616. Post-SET_Zn_bd. IPR000313. PWWP. IPR001214. SET. IPR019786. Zinc_finger_PHD-type_CS. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR001841. Znf_RING. [Graphical view]
Pfam	PF00628. PHD. 2 hits. PF00855. PWWP. 2 hits. PF00856. SET. 1 hit. [Graphical view]
SMART	SM00570. AWS. 1 hit. SM00249. PHD. 3 hits. SM00508. PostSET. 1 hit. SM00293. PWWP. 2 hits. SM00184. RING. 2 hits. SM00317. SET. 1 hit. [Graphical view]
PROSITE	PS51215. AWS. 1 hit. PS50868. POST_SET. 1 hit. PS50812. PWWP. 2 hits. PS50280. SET. 1 hit. PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	833495.

Entry information

Entry name

MES4_DROME

Accession

Primary (citable) accession number: Q8MT36
Secondary accession number(s): Q1LZ05, Q9VAY5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	March 28, 2003
Last modified:	June 16, 2009
This is version 60 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project