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Q32KD2

- SETB1_DROME

UniProt

Q32KD2 - SETB1_DROME

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Protein
Histone-lysine N-methyltransferase eggless
Gene
egg, CG12196
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 1 By similarity
Metal bindingi948 – 9481Zinc 2 By similarity
Metal bindingi950 – 9501Zinc 1 By similarity
Metal bindingi954 – 9541Zinc 1 By similarity
Metal bindingi954 – 9541Zinc 3 By similarity
Metal bindingi960 – 9601Zinc 1 By similarity
Metal bindingi962 – 9621Zinc 2 By similarity
Metal bindingi1000 – 10001Zinc 2 By similarity
Metal bindingi1000 – 10001Zinc 3 By similarity
Metal bindingi1004 – 10041Zinc 2 By similarity
Metal bindingi1006 – 10061Zinc 3 By similarity
Metal bindingi1010 – 10101Zinc 3 By similarity
Binding sitei1069 – 10691S-adenosyl-L-methionine By similarity
Binding sitei1071 – 10711S-adenosyl-L-methionine By similarity
Binding sitei1191 – 11911S-adenosyl-L-methionine By similarity
Metal bindingi1197 – 11971Zinc 4 By similarity
Metal bindingi1250 – 12501Zinc 4 By similarity
Metal bindingi1252 – 12521Zinc 4 By similarity
Metal bindingi1257 – 12571Zinc 4 By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. DNA hypermethylation Source: FlyBase
  2. female germ-line stem cell 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 during meiosis Source: UniProtKB
  7. negative regulation of transcription, DNA-templated Source: FlyBase
  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. Chromosome Inferred 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 eggless
PRO_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, 828-881, 896-1257.

Family & Domainsi

Domains and Repeats

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

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili353 – 42068 Reviewed prediction
Add
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

Contains 1 post-SET domain.
Contains 1 pre-SET domain.
Contains 1 SET domain.
Contains 2 Tudor domains.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00750000117355.
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.

Q32KD2-1 [UniParc]FASTAAdd to Basket

« Hide

MSGQPTAVDC LESSGSTVED VQETPASREK SYGLPVRKGE NSLESPAEQA     50
AKDVEIEELT HSEAIAATGS TRKQCPYGGK APDEPGKLAD ESEDRKGENT 100
KAIASSPVLV AVDSDSSVEL IESPVKFSSA NESEKDPPKP DAVNEAAAKE 150
AEEMTDSSIS SPTSESFPEK DEKTNKENEQ EPPGMEVDQD VEESISRPAE 200
EYKIENTLKG HKRISLTEIE EHKIVDKKDD VLEVELEKGT APKAAEDEKL 250
NALLSDGDVF YDKECVNCNC TKLHKQYVLA NMATLNFYQV LRKSSKQQFL 300
CMGCHDTAMD LYEEYAGQLM AKQPLLLKDF HQDHADFVAL DSSDEEEEEK 350
QPEKSDFSKN KLQLIEDELD DAIKNVLNKV DFTAQLSWSK TILQAKADHL 400
ERQFALADVE LEKVQTTADK MHCALYNSCP VAHKHLPTLD IEPSDYVHEV 450
PPPGEIVRPP IQLGETYYAV KNKAIASWVS IKVIEFTEST AINGNTMKSY 500
KIRYLNTPYQ MIKTVTAKHI AYFEPPPVRL TIGTRVIAYF DGTTLSRGKD 550
KGVVQSAFYP GIIAEPLKQA NRYRYLIFYD DGYTQYVPHR DVRLVCQASE 600
KVWEDVHAAS RDFIQKYVEK YSVDRPMVQC TRGQSMTTES NGTWLYARVI 650
DIDCSLVLMQ FEGDKNHTEW IYRGSLRLGP VFRETQNNMN SSSAQQLRVP 700
RRTEPFIRYT KEMESSSKVN QQMRAFARKS SASAQNNALA AASSAATPAG 750
GRTNAGGVST SNSASAVRHL NNSTIYVDDE NRPKGHVVYF TAKRNLPPKM 800
YKCHECSPNC LFKIVHRLDS YSPLAKPLLS GWERLVMRQK TKKSVVYKGP 850
CGKSLRSLAE VHRYLRATEN VLNVDNFDFT PDLKCLAEYS IDPSIVKDTD 900
ISKGQEKMAI PLVNYYDNTL PPPCTYAKQR IPTEGVHLNL DEEFLLCCDC 950
EDDCSDKSKC ACWQLTVAGV RYCNPKKPIE EIGYQYKRLH EHVPTGIYEC 1000
NSRCKCKKNC LNRVVQFSLE MKLQVFKTSN RGWGLRCVND IPKGAFICIY 1050
AGHLLTETMA NEGGQDAGDE YFADLDYIEV AEQLKEGYES EVDHSDPDAE 1100
EDNGGPDAED DDDFRPNYHY QRKIKRSSRS GSTQNSSTQS SELDSQERAV 1150
INFNPNADLD ETVRENSVRR LFGKDEAPYI MDAKTTGNLG RYFNHSCSPN 1200
LFVQNVFVDT HDLRFPWVAF FSAAHIRSGT ELTWNYNYEV GVVPGKVLYC 1250
QCGAPNCRLR LL 1262
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, 828-881, 896-1257.
ModBasei 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 ENSGT00750000117355.
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: July 9, 2014
This is version 81 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

Similar proteinsi