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Q32KD2 (SETB1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase eggless

EC=2.1.1.43
Alternative name(s):
SETDB1 homolog
Gene names
Name:egg
ORF Names:CG12196
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1262 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Domain

In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster By similarity.

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 class V-like SAM-binding methyltransferase superfamily. 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 processDifferentiation
Oogenesis
Transcription
Transcription regulation
   Cellular componentChromosome
Nucleus
   DomainCoiled coil
Repeat
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Developmental protein
Methyltransferase
Repressor
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA hypermethylation

Inferred from mutant phenotype PubMed 20498723. Source: FlyBase

female germ-line stem cell division

Inferred from direct assay PubMed 18493619. Source: FlyBase

histone H3-K9 methylation

Inferred from direct assay PubMed 17652514. 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

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 20498723. Source: FlyBase

oogenesis

Inferred from mutant phenotype Ref.5. Source: UniProtKB

regulation of gene expression, epigenetic

Inferred from mutant phenotype PubMed 17652514. Source: FlyBase

regulation of gene silencing

Inferred from mutant phenotype PubMed 19487560. Source: FlyBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

wing disc development

Inferred from mutant phenotype PubMed 17362353. Source: FlyBase

   Cellular_componentcytoplasm

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 17500594PubMed 19487560. Source: FlyBase

   Molecular_functiondouble-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

histone-lysine N-methyltransferase activity

Inferred from mutant phenotype Ref.5. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17362353PubMed 17652514. Source: FlyBase

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12621262Histone-lysine N-methyltransferase eggless
PRO_0000281822

Regions

Domain529 – 60274Tudor 1
Domain629 – 68658Tudor 2
Domain818 – 88467MBD
Domain946 – 101873Pre-SET
Domain1021 – 1237217SET
Domain1246 – 126217Post-SET
Region1031 – 10333S-adenosyl-L-methionine binding By similarity
Region1194 – 11952S-adenosyl-L-methionine binding By similarity
Coiled coil353 – 42068 Potential

Sites

Metal binding9481Zinc 1 By similarity
Metal binding9481Zinc 2 By similarity
Metal binding9501Zinc 1 By similarity
Metal binding9541Zinc 1 By similarity
Metal binding9541Zinc 3 By similarity
Metal binding9601Zinc 1 By similarity
Metal binding9621Zinc 2 By similarity
Metal binding10001Zinc 2 By similarity
Metal binding10001Zinc 3 By similarity
Metal binding10041Zinc 2 By similarity
Metal binding10061Zinc 3 By similarity
Metal binding10101Zinc 3 By similarity
Metal binding11971Zinc 4 By similarity
Metal binding12501Zinc 4 By similarity
Metal binding12521Zinc 4 By similarity
Metal binding12571Zinc 4 By similarity
Binding site10691S-adenosyl-L-methionine By similarity
Binding site10711S-adenosyl-L-methionine By similarity
Binding site11911S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue2151Phosphoserine Ref.6
Modified residue2171Phosphothreonine Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q32KD2 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: A89DFF1CC6FCED1C

FASTA1,262141,946
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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.
RefSeqNP_611966.3. NM_138122.5.
UniGeneDm.14397.

3D structure databases

ProteinModelPortalQ32KD2.
SMRQ32KD2. Positions 498-680, 828-881, 896-1257.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid63532. 12 interactions.
DIPDIP-46503N.
IntActQ32KD2. 2 interactions.
MINTMINT-749161.

Proteomic databases

PaxDbQ32KD2.
PRIDEQ32KD2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0112777; FBpp0111689; FBgn0086908.
GeneID37962.
KEGGdme:Dmel_CG12196.

Organism-specific databases

CTD37962.
FlyBaseFBgn0086908. egg.

Phylogenomic databases

eggNOGCOG2940.
GeneTreeENSGT00750000117355.
KOK11421.
OMACKCKKNC.
OrthoDBEOG7ZD1TG.
PhylomeDBQ32KD2.

Gene expression databases

BgeeQ32KD2.

Family and domain databases

Gene3D3.30.890.10. 1 hit.
InterProIPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamPF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTSM00317. SET. 1 hit.
[Graphical view]
SUPFAMSSF54171. SSF54171. 1 hit.
PROSITEPS50982. MBD. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi37962.
NextBio806265.

Entry information

Entry nameSETB1_DROME
AccessionPrimary (citable) accession number: Q32KD2
Secondary accession number(s): Q29QW7 expand/collapse secondary AC list , Q8IHC9, Q8MMD1, Q960X1, Q9W110
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase