Q32KD2 · SETB1_DROME
- ProteinHistone-lysine N-methyltransferase eggless
- Geneegg
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1262 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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.
Catalytic activity
- L-lysyl9-[histone H3] + 3 S-adenosyl-L-methionine = 3 H+ + N6,N6,N6-trimethyl-L-lysyl9-[histone H3] + 3 S-adenosyl-L-homocysteine
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 948 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 948 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 950 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 954 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 954 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 960 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 962 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1000 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1000 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1004 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1006 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1010 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1031-1033 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: RGW | ||||||
Binding site | 1069 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1071 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 1191 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 1194-1195 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: NH | ||||||
Binding site | 1197 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1250 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1252 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1257 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | polytene chromosome | |
Molecular Function | DNA binding | |
Molecular Function | histone H3K9 methyltransferase activity | |
Molecular Function | histone H3K9 trimethyltransferase activity | |
Molecular Function | histone H3K9me2 methyltransferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | epigenetic regulation of gene expression | |
Biological Process | female germ-line stem cell asymmetric division | |
Biological Process | heterochromatin formation | |
Biological Process | heterochromatin organization | |
Biological Process | methylation | |
Biological Process | negative regulation of gene expression | |
Biological Process | oogenesis | |
Biological Process | piRNA-mediated retrotransposon silencing by heterochromatin formation | |
Biological Process | positive regulation of DNA methylation-dependent heterochromatin formation | |
Biological Process | retrotransposon silencing by heterochromatin formation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone-lysine N-methyltransferase eggless
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ32KD2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
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.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000281822 | 1-1262 | Histone-lysine N-methyltransferase eggless | |||
Sequence: MSGQPTAVDCLESSGSTVEDVQETPASREKSYGLPVRKGENSLESPAEQAAKDVEIEELTHSEAIAATGSTRKQCPYGGKAPDEPGKLADESEDRKGENTKAIASSPVLVAVDSDSSVELIESPVKFSSANESEKDPPKPDAVNEAAAKEAEEMTDSSISSPTSESFPEKDEKTNKENEQEPPGMEVDQDVEESISRPAEEYKIENTLKGHKRISLTEIEEHKIVDKKDDVLEVELEKGTAPKAAEDEKLNALLSDGDVFYDKECVNCNCTKLHKQYVLANMATLNFYQVLRKSSKQQFLCMGCHDTAMDLYEEYAGQLMAKQPLLLKDFHQDHADFVALDSSDEEEEEKQPEKSDFSKNKLQLIEDELDDAIKNVLNKVDFTAQLSWSKTILQAKADHLERQFALADVELEKVQTTADKMHCALYNSCPVAHKHLPTLDIEPSDYVHEVPPPGEIVRPPIQLGETYYAVKNKAIASWVSIKVIEFTESTAINGNTMKSYKIRYLNTPYQMIKTVTAKHIAYFEPPPVRLTIGTRVIAYFDGTTLSRGKDKGVVQSAFYPGIIAEPLKQANRYRYLIFYDDGYTQYVPHRDVRLVCQASEKVWEDVHAASRDFIQKYVEKYSVDRPMVQCTRGQSMTTESNGTWLYARVIDIDCSLVLMQFEGDKNHTEWIYRGSLRLGPVFRETQNNMNSSSAQQLRVPRRTEPFIRYTKEMESSSKVNQQMRAFARKSSASAQNNALAAASSAATPAGGRTNAGGVSTSNSASAVRHLNNSTIYVDDENRPKGHVVYFTAKRNLPPKMYKCHECSPNCLFKIVHRLDSYSPLAKPLLSGWERLVMRQKTKKSVVYKGPCGKSLRSLAEVHRYLRATENVLNVDNFDFTPDLKCLAEYSIDPSIVKDTDISKGQEKMAIPLVNYYDNTLPPPCTYAKQRIPTEGVHLNLDEEFLLCCDCEDDCSDKSKCACWQLTVAGVRYCNPKKPIEEIGYQYKRLHEHVPTGIYECNSRCKCKKNCLNRVVQFSLEMKLQVFKTSNRGWGLRCVNDIPKGAFICIYAGHLLTETMANEGGQDAGDEYFADLDYIEVAEQLKEGYESEVDHSDPDAEEDNGGPDAEDDDDFRPNYHYQRKIKRSSRSGSTQNSSTQSSELDSQERAVINFNPNADLDETVRENSVRRLFGKDEAPYIMDAKTTGNLGRYFNHSCSPNLFVQNVFVDTHDLRFPWVAFFSAAHIRSGTELTWNYNYEVGVVPGKVLYCQCGAPNCRLRLL | ||||||
Modified residue | 215 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 217 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in ovary (at protein level).
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).
Gene expression databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q32KD2 | Pof Q9W123 | 2 | EBI-140830, EBI-155974 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MSGQPTAVDCLESSGSTVEDVQ | ||||||
Region | 1-194 | Disordered | ||||
Sequence: MSGQPTAVDCLESSGSTVEDVQETPASREKSYGLPVRKGENSLESPAEQAAKDVEIEELTHSEAIAATGSTRKQCPYGGKAPDEPGKLADESEDRKGENTKAIASSPVLVAVDSDSSVELIESPVKFSSANESEKDPPKPDAVNEAAAKEAEEMTDSSISSPTSESFPEKDEKTNKENEQEPPGMEVDQDVEES | ||||||
Compositional bias | 84-100 | Basic and acidic residues | ||||
Sequence: EPGKLADESEDRKGENT | ||||||
Compositional bias | 132-152 | Basic and acidic residues | ||||
Sequence: ESEKDPPKPDAVNEAAAKEAE | ||||||
Compositional bias | 166-183 | Basic and acidic residues | ||||
Sequence: SFPEKDEKTNKENEQEPP | ||||||
Coiled coil | 353-420 | |||||
Sequence: EKSDFSKNKLQLIEDELDDAIKNVLNKVDFTAQLSWSKTILQAKADHLERQFALADVELEKVQTTADK | ||||||
Domain | 529-602 | Tudor 1 | ||||
Sequence: RLTIGTRVIAYFDGTTLSRGKDKGVVQSAFYPGIIAEPLKQANRYRYLIFYDDGYTQYVPHRDVRLVCQASEKV | ||||||
Domain | 629-686 | Tudor 2 | ||||
Sequence: QCTRGQSMTTESNGTWLYARVIDIDCSLVLMQFEGDKNHTEWIYRGSLRLGPVFRETQ | ||||||
Region | 743-764 | Disordered | ||||
Sequence: SSAATPAGGRTNAGGVSTSNSA | ||||||
Domain | 818-884 | MBD | ||||
Sequence: LDSYSPLAKPLLSGWERLVMRQKTKKSVVYKGPCGKSLRSLAEVHRYLRATENVLNVDNFDFTPDLK | ||||||
Domain | 946-1018 | Pre-SET | ||||
Sequence: LCCDCEDDCSDKSKCACWQLTVAGVRYCNPKKPIEEIGYQYKRLHEHVPTGIYECNSRCKCKKNCLNRVVQFS | ||||||
Domain | 1021-1237 | SET | ||||
Sequence: MKLQVFKTSNRGWGLRCVNDIPKGAFICIYAGHLLTETMANEGGQDAGDEYFADLDYIEVAEQLKEGYESEVDHSDPDAEEDNGGPDAEDDDDFRPNYHYQRKIKRSSRSGSTQNSSTQSSELDSQERAVINFNPNADLDETVRENSVRRLFGKDEAPYIMDAKTTGNLGRYFNHSCSPNLFVQNVFVDTHDLRFPWVAFFSAAHIRSGTELTWNYN | ||||||
Region | 1086-1148 | Disordered | ||||
Sequence: EGYESEVDHSDPDAEEDNGGPDAEDDDDFRPNYHYQRKIKRSSRSGSTQNSSTQSSELDSQER | ||||||
Compositional bias | 1093-1109 | Acidic residues | ||||
Sequence: DHSDPDAEEDNGGPDAE | ||||||
Compositional bias | 1127-1148 | Polar residues | ||||
Sequence: SSRSGSTQNSSTQSSELDSQER | ||||||
Domain | 1246-1262 | Post-SET | ||||
Sequence: KVLYCQCGAPNCRLRLL |
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.
Sequence similarities
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,262
- Mass (Da)141,946
- Last updated2005-12-06 v1
- ChecksumA89DFF1CC6FCED1C
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-22 | Polar residues | ||||
Sequence: MSGQPTAVDCLESSGSTVEDVQ | ||||||
Compositional bias | 84-100 | Basic and acidic residues | ||||
Sequence: EPGKLADESEDRKGENT | ||||||
Compositional bias | 132-152 | Basic and acidic residues | ||||
Sequence: ESEKDPPKPDAVNEAAAKEAE | ||||||
Compositional bias | 166-183 | Basic and acidic residues | ||||
Sequence: SFPEKDEKTNKENEQEPP | ||||||
Compositional bias | 1093-1109 | Acidic residues | ||||
Sequence: DHSDPDAEEDNGGPDAE | ||||||
Compositional bias | 1127-1148 | Polar residues | ||||
Sequence: SSRSGSTQNSSTQSSELDSQER |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE013599 EMBL· GenBank· DDBJ | AAF47268.3 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT023947 EMBL· GenBank· DDBJ | ABB36451.1 EMBL· GenBank· DDBJ | mRNA | ||
BT024273 EMBL· GenBank· DDBJ | ABC86335.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY051799 EMBL· GenBank· DDBJ | AAK93223.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BT001309 EMBL· GenBank· DDBJ | AAN71064.2 EMBL· GenBank· DDBJ | mRNA | Different initiation |