Q32KD2 (SETB1_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone-lysine N-methyltransferase eggless
EC=2.1.1.43

Alternative name(s):
SETDB1 homolog

Gene names

Name:	egg
ORF Names:	CG12196

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	1262 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 in ovary. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting Su(var)205/HP1 to methylated histones. Plays a central role during oogenesis. Ref.5
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
Subcellular location	Nucleus. Chromosome Probable Ref.5.
Tissue specificity	Expressed in ovary (at protein level). Ref.5
Developmental stage	Present most strongly at early stages of oogenesis, in germ cells in the germarium. Present in germ stem cells and dividing germline cyst cells. Weakly or not expressed in somatic cells at the tip of the germarium, including the terminal filament, inner sheath cells, or cap cells, but it is present at low levels in somatic cells in regions 2 and 3 of the germarium, including the prefollicular cells and the follicle cells of stage 1 egg chambers. Soon after egg chambers budd off the germarium, levels increase in the follicle cells. By mid-oogenesis it decreases in the nurse cells, while levels continued to increase in the follicle cells (at protein level). Ref.5
Disruption phenotype	Oogenesis arrests at early stages. This arrest is accompanied by reduced proliferation of somatic cells required for egg chamber formation, and by apoptosis in both germ and somatic cell populations. Ref.5
Sequence similarities	Belongs to the histone-lysine methyltransferase family. Suvar3-9 subfamily. Contains 1 MBD (methyl-CpG-binding) domain. Contains 1 post-SET domain. Contains 1 pre-SET domain. Contains 1 SET domain. Contains 2 Tudor domains.
Sequence caution	The sequence AAK93223.1 differs from that shown. Reason: Erroneous initiation. The sequence AAN71064.2 differs from that shown. Reason: Erroneous initiation. The sequence ABC86335.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Differentiation Oogenesis Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Domain	Coiled coil Repeat
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Developmental protein Methyltransferase Repressor Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA hypermethylation Inferred from mutant phenotype PubMed 20498723. Source: FlyBase female germ-line stem cell division Inferred from direct assay PubMed 18493619. Source: FlyBase instar larval or pupal development Inferred from mutant phenotype PubMed 17362353. Source: FlyBase negative regulation of gene expression, epigenetic Inferred from direct assay PubMed 20498723. Source: FlyBase negative regulation of transcription during meiosis Inferred from mutant phenotype Ref.5. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW wing disc development Inferred from mutant phenotype PubMed 17362353. Source: FlyBase
Cellular_component	cytoplasm Inferred from direct assay Ref.5. Source: FlyBase nucleus Inferred from direct assay Ref.5. Source: UniProtKB polytene chromosome Inferred from direct assay PubMed 17362353PubMed 17500594. Source: FlyBase
Molecular_function	double-stranded methylated DNA binding Inferred from direct assay PubMed 20498723. Source: FlyBase histone methyltransferase activity (H3-K9 specific) Inferred from direct assay PubMed 17652514PubMed 20498723. Source: FlyBase zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1262	1262	Histone-lysine N-methyltransferase eggless		PRO_0000281822
Regions
	Domain	529 – 602	74	Tudor 1
	Domain	629 – 686	58	Tudor 2
	Domain	818 – 884	67	MBD
	Domain	946 – 1018	73	Pre-SET
	Domain	1020 – 1241	222	SET
	Domain	1246 – 1262	17	Post-SET
	Coiled coil	353 – 420	68	Potential
Amino acid modifications
	Modified residue	215	1	Phosphoserine Ref.6
	Modified residue	217	1	Phosphothreonine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q32KD2 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: A89DFF1CC6FCED1C	FASTA	1,262	141,946
	10 20 30 40 50 60 MSGQPTAVDC LESSGSTVED VQETPASREK SYGLPVRKGE NSLESPAEQA AKDVEIEELT 70 80 90 100 110 120 HSEAIAATGS TRKQCPYGGK APDEPGKLAD ESEDRKGENT KAIASSPVLV AVDSDSSVEL 130 140 150 160 170 180 IESPVKFSSA NESEKDPPKP DAVNEAAAKE AEEMTDSSIS SPTSESFPEK DEKTNKENEQ 190 200 210 220 230 240 EPPGMEVDQD VEESISRPAE EYKIENTLKG HKRISLTEIE EHKIVDKKDD VLEVELEKGT 250 260 270 280 290 300 APKAAEDEKL NALLSDGDVF YDKECVNCNC TKLHKQYVLA NMATLNFYQV LRKSSKQQFL 310 320 330 340 350 360 CMGCHDTAMD LYEEYAGQLM AKQPLLLKDF HQDHADFVAL DSSDEEEEEK QPEKSDFSKN 370 380 390 400 410 420 KLQLIEDELD DAIKNVLNKV DFTAQLSWSK TILQAKADHL ERQFALADVE LEKVQTTADK 430 440 450 460 470 480 MHCALYNSCP VAHKHLPTLD IEPSDYVHEV PPPGEIVRPP IQLGETYYAV KNKAIASWVS 490 500 510 520 530 540 IKVIEFTEST AINGNTMKSY KIRYLNTPYQ MIKTVTAKHI AYFEPPPVRL TIGTRVIAYF 550 560 570 580 590 600 DGTTLSRGKD KGVVQSAFYP GIIAEPLKQA NRYRYLIFYD DGYTQYVPHR DVRLVCQASE 610 620 630 640 650 660 KVWEDVHAAS RDFIQKYVEK YSVDRPMVQC TRGQSMTTES NGTWLYARVI DIDCSLVLMQ 670 680 690 700 710 720 FEGDKNHTEW IYRGSLRLGP VFRETQNNMN SSSAQQLRVP RRTEPFIRYT KEMESSSKVN 730 740 750 760 770 780 QQMRAFARKS SASAQNNALA AASSAATPAG GRTNAGGVST SNSASAVRHL NNSTIYVDDE 790 800 810 820 830 840 NRPKGHVVYF TAKRNLPPKM YKCHECSPNC LFKIVHRLDS YSPLAKPLLS GWERLVMRQK 850 860 870 880 890 900 TKKSVVYKGP CGKSLRSLAE VHRYLRATEN VLNVDNFDFT PDLKCLAEYS IDPSIVKDTD 910 920 930 940 950 960 ISKGQEKMAI PLVNYYDNTL PPPCTYAKQR IPTEGVHLNL DEEFLLCCDC EDDCSDKSKC 970 980 990 1000 1010 1020 ACWQLTVAGV RYCNPKKPIE EIGYQYKRLH EHVPTGIYEC NSRCKCKKNC LNRVVQFSLE 1030 1040 1050 1060 1070 1080 MKLQVFKTSN RGWGLRCVND IPKGAFICIY AGHLLTETMA NEGGQDAGDE YFADLDYIEV 1090 1100 1110 1120 1130 1140 AEQLKEGYES EVDHSDPDAE EDNGGPDAED DDDFRPNYHY QRKIKRSSRS GSTQNSSTQS 1150 1160 1170 1180 1190 1200 SELDSQERAV INFNPNADLD ETVRENSVRR LFGKDEAPYI MDAKTTGNLG RYFNHSCSPN 1210 1220 1230 1240 1250 1260 LFVQNVFVDT HDLRFPWVAF FSAAHIRSGT ELTWNYNYEV GVVPGKVLYC QCGAPNCRLR LL

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	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 (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 378-1262. Strain: Berkeley. Tissue: Embryo and Testis.
[5]	"Histone methylation is required for oogenesis in Drosophila." Clough E., Moon W., Wang S., Smith K., Hazelrigg T. Development 134:157-165(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND THR-217, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013599 Genomic DNA. Translation: AAF47268.3. BT023947 mRNA. Translation: ABB36451.1. BT024273 mRNA. Translation: ABC86335.1. Different initiation. AY051799 mRNA. Translation: AAK93223.1. Different initiation. BT001309 mRNA. Translation: AAN71064.2. Different initiation.
RefSeq	NP_611966.3. NM_138122.5.
UniGene	Dm.14397.
3D structure databases
ProteinModelPortal	Q32KD2.
SMR	Q32KD2. Positions 498-680, 900-1080, 1150-1257.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-46503N.
IntAct	Q32KD2. 2 interactions.
MINT	MINT-749161.
Proteomic databases
PaxDb	Q32KD2.
PRIDE	Q32KD2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0112777; FBpp0111689; FBgn0086908.
GeneID	37962.
KEGG	dme:Dmel_CG12196.
Organism-specific databases
CTD	37962.
FlyBase	FBgn0086908. egg.
Phylogenomic databases
eggNOG	COG2940.
GeneTree	ENSGT00690000101898.
KO	K11421.
OMA	CKCKKNC.
OrthoDB	EOG4THT82.
PhylomeDB	Q32KD2.
Gene expression databases
Bgee	Q32KD2.
Family and domain databases
Gene3D	3.30.890.10. 1 hit.
InterPro	IPR016177. DNA-bd_integrase-typ. IPR001739. Methyl_CpG_DNA-bd. IPR003616. Post-SET_dom. IPR007728. Pre-SET_dom. IPR001214. SET_dom. [Graphical view]
Pfam	PF01429. MBD. 1 hit. PF05033. Pre-SET. 1 hit. PF00856. SET. 1 hit. [Graphical view]
SMART	SM00317. SET. 1 hit. [Graphical view]
SUPFAM	SSF54171. DNA-binding_integrase-type. 1 hit.
PROSITE	PS50982. MBD. 1 hit. PS50868. POST_SET. 1 hit. PS50867. PRE_SET. 1 hit. PS50280. SET. 1 hit. PS50304. TUDOR. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	37962.
NextBio	806265.

Entry information

Entry name

SETB1_DROME

Accession

Primary (citable) accession number: Q32KD2
Secondary accession number(s): Q29QW7 , Q8IHC9, Q8MMD1, Q960X1, Q9W110

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	December 6, 2005
Last modified:	May 29, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project