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Q32KD2

- SETB1_DROME

UniProt

Q32KD2 - SETB1_DROME

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Protein

Histone-lysine N-methyltransferase eggless

Gene

egg

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi948 – 9481Zinc 1By similarity
Metal bindingi948 – 9481Zinc 2By similarity
Metal bindingi950 – 9501Zinc 1By similarity
Metal bindingi954 – 9541Zinc 1By similarity
Metal bindingi954 – 9541Zinc 3By similarity
Metal bindingi960 – 9601Zinc 1By similarity
Metal bindingi962 – 9621Zinc 2By similarity
Metal bindingi1000 – 10001Zinc 2By similarity
Metal bindingi1000 – 10001Zinc 3By similarity
Metal bindingi1004 – 10041Zinc 2By similarity
Metal bindingi1006 – 10061Zinc 3By similarity
Metal bindingi1010 – 10101Zinc 3By similarity
Binding sitei1069 – 10691S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei1071 – 10711S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei1191 – 11911S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi1197 – 11971Zinc 4By similarity
Metal bindingi1250 – 12501Zinc 4By similarity
Metal bindingi1252 – 12521Zinc 4By similarity
Metal bindingi1257 – 12571Zinc 4By similarity

GO - Molecular functioni

  1. double-stranded methylated DNA binding Source: FlyBase
  2. histone-lysine N-methyltransferase activity Source: UniProtKB
  3. histone methyltransferase activity (H3-K9 specific) Source: FlyBase
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA hypermethylation Source: FlyBase
  2. female germ-line stem cell asymmetric division Source: FlyBase
  3. histone H3-K9 methylation Source: FlyBase
  4. instar larval or pupal development Source: FlyBase
  5. negative regulation of gene expression, epigenetic Source: FlyBase
  6. negative regulation of transcription, DNA-templated Source: FlyBase
  7. negative regulation of transcription during meiosis Source: UniProtKB
  8. oogenesis Source: UniProtKB
  9. regulation of gene expression, epigenetic Source: FlyBase
  10. regulation of gene silencing Source: FlyBase
  11. transcription, DNA-templated Source: UniProtKB-KW
  12. wing disc development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Differentiation, Oogenesis, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase eggless (EC:2.1.1.43)
Alternative name(s):
SETDB1 homolog
Gene namesi
Name:egg
ORF Names:CG12196
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0086908. egg.

Subcellular locationi

Nucleus 1 Publication. Chromosome 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. nucleus Source: UniProtKB
  3. polytene chromosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12621262Histone-lysine N-methyltransferase egglessPRO_0000281822Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei215 – 2151Phosphoserine1 Publication
Modified residuei217 – 2171Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ32KD2.
PRIDEiQ32KD2.

Expressioni

Tissue specificityi

Expressed in ovary (at protein level).1 Publication

Developmental stagei

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).1 Publication

Gene expression databases

BgeeiQ32KD2.

Interactioni

Protein-protein interaction databases

BioGridi63532. 12 interactions.
DIPiDIP-46503N.
IntActiQ32KD2. 2 interactions.
MINTiMINT-749161.

Structurei

3D structure databases

ProteinModelPortaliQ32KD2.
SMRiQ32KD2. Positions 498-680, 900-1080, 1150-1257.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini529 – 60274Tudor 1Add
BLAST
Domaini629 – 68658Tudor 2Add
BLAST
Domaini818 – 88467MBDPROSITE-ProRule annotationAdd
BLAST
Domaini946 – 101873Pre-SETPROSITE-ProRule annotationAdd
BLAST
Domaini1021 – 1237217SETPROSITE-ProRule annotationAdd
BLAST
Domaini1246 – 126217Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1031 – 10333S-adenosyl-L-methionine bindingBy similarity
Regioni1194 – 11952S-adenosyl-L-methionine bindingBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili353 – 42068Sequence AnalysisAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
Contains 1 MBD (methyl-CpG-binding) domain.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 pre-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation
Contains 2 Tudor domains.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000119330.
InParanoidiQ32KD2.
KOiK11421.
OMAiCKCKKNC.
OrthoDBiEOG7ZD1TG.
PhylomeDBiQ32KD2.

Family and domain databases

Gene3Di3.30.890.10. 1 hit.
InterProiIPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamiPF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF54171. SSF54171. 1 hit.
PROSITEiPS50982. MBD. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q32KD2 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGQPTAVDC LESSGSTVED VQETPASREK SYGLPVRKGE NSLESPAEQA
60 70 80 90 100
AKDVEIEELT HSEAIAATGS TRKQCPYGGK APDEPGKLAD ESEDRKGENT
110 120 130 140 150
KAIASSPVLV AVDSDSSVEL IESPVKFSSA NESEKDPPKP DAVNEAAAKE
160 170 180 190 200
AEEMTDSSIS SPTSESFPEK DEKTNKENEQ EPPGMEVDQD VEESISRPAE
210 220 230 240 250
EYKIENTLKG HKRISLTEIE EHKIVDKKDD VLEVELEKGT APKAAEDEKL
260 270 280 290 300
NALLSDGDVF YDKECVNCNC TKLHKQYVLA NMATLNFYQV LRKSSKQQFL
310 320 330 340 350
CMGCHDTAMD LYEEYAGQLM AKQPLLLKDF HQDHADFVAL DSSDEEEEEK
360 370 380 390 400
QPEKSDFSKN KLQLIEDELD DAIKNVLNKV DFTAQLSWSK TILQAKADHL
410 420 430 440 450
ERQFALADVE LEKVQTTADK MHCALYNSCP VAHKHLPTLD IEPSDYVHEV
460 470 480 490 500
PPPGEIVRPP IQLGETYYAV KNKAIASWVS IKVIEFTEST AINGNTMKSY
510 520 530 540 550
KIRYLNTPYQ MIKTVTAKHI AYFEPPPVRL TIGTRVIAYF DGTTLSRGKD
560 570 580 590 600
KGVVQSAFYP GIIAEPLKQA NRYRYLIFYD DGYTQYVPHR DVRLVCQASE
610 620 630 640 650
KVWEDVHAAS RDFIQKYVEK YSVDRPMVQC TRGQSMTTES NGTWLYARVI
660 670 680 690 700
DIDCSLVLMQ FEGDKNHTEW IYRGSLRLGP VFRETQNNMN SSSAQQLRVP
710 720 730 740 750
RRTEPFIRYT KEMESSSKVN QQMRAFARKS SASAQNNALA AASSAATPAG
760 770 780 790 800
GRTNAGGVST SNSASAVRHL NNSTIYVDDE NRPKGHVVYF TAKRNLPPKM
810 820 830 840 850
YKCHECSPNC LFKIVHRLDS YSPLAKPLLS GWERLVMRQK TKKSVVYKGP
860 870 880 890 900
CGKSLRSLAE VHRYLRATEN VLNVDNFDFT PDLKCLAEYS IDPSIVKDTD
910 920 930 940 950
ISKGQEKMAI PLVNYYDNTL PPPCTYAKQR IPTEGVHLNL DEEFLLCCDC
960 970 980 990 1000
EDDCSDKSKC ACWQLTVAGV RYCNPKKPIE EIGYQYKRLH EHVPTGIYEC
1010 1020 1030 1040 1050
NSRCKCKKNC LNRVVQFSLE MKLQVFKTSN RGWGLRCVND IPKGAFICIY
1060 1070 1080 1090 1100
AGHLLTETMA NEGGQDAGDE YFADLDYIEV AEQLKEGYES EVDHSDPDAE
1110 1120 1130 1140 1150
EDNGGPDAED DDDFRPNYHY QRKIKRSSRS GSTQNSSTQS SELDSQERAV
1160 1170 1180 1190 1200
INFNPNADLD ETVRENSVRR LFGKDEAPYI MDAKTTGNLG RYFNHSCSPN
1210 1220 1230 1240 1250
LFVQNVFVDT HDLRFPWVAF FSAAHIRSGT ELTWNYNYEV GVVPGKVLYC
1260
QCGAPNCRLR LL
Length:1,262
Mass (Da):141,946
Last modified:December 6, 2005 - v1
Checksum:iA89DFF1CC6FCED1C
GO

Sequence cautioni

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.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqiNP_611966.3. NM_138122.5.
UniGeneiDm.14397.

Genome annotation databases

EnsemblMetazoaiFBtr0112777; FBpp0111689; FBgn0086908.
GeneIDi37962.
KEGGidme:Dmel_CG12196.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
RefSeqi NP_611966.3. NM_138122.5.
UniGenei Dm.14397.

3D structure databases

ProteinModelPortali Q32KD2.
SMRi Q32KD2. Positions 498-680, 900-1080, 1150-1257.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 63532. 12 interactions.
DIPi DIP-46503N.
IntActi Q32KD2. 2 interactions.
MINTi MINT-749161.

Proteomic databases

PaxDbi Q32KD2.
PRIDEi Q32KD2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0112777 ; FBpp0111689 ; FBgn0086908 .
GeneIDi 37962.
KEGGi dme:Dmel_CG12196.

Organism-specific databases

CTDi 37962.
FlyBasei FBgn0086908. egg.

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00760000119330.
InParanoidi Q32KD2.
KOi K11421.
OMAi CKCKKNC.
OrthoDBi EOG7ZD1TG.
PhylomeDBi Q32KD2.

Miscellaneous databases

GenomeRNAii 37962.
NextBioi 806265.

Gene expression databases

Bgeei Q32KD2.

Family and domain databases

Gene3Di 3.30.890.10. 1 hit.
InterProi IPR016177. DNA-bd_dom.
IPR001739. Methyl_CpG_DNA-bd.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00317. SET. 1 hit.
[Graphical view ]
SUPFAMi SSF54171. SSF54171. 1 hit.
PROSITEi PS50982. MBD. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiSETB1_DROME
AccessioniPrimary (citable) accession number: Q32KD2
Secondary accession number(s): Q29QW7
, Q8IHC9, Q8MMD1, Q960X1, Q9W110
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: December 6, 2005
Last modified: October 29, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3