SETB1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SETB1_DROME
• UniProt AC: Q32KD2
• Protein Name: Histone-lysine N-methyltransferase eggless
• Gene Name: egg
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1262
• Subcellular Localization: Nucleus . Chromosome .
• Protein Description: 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..
• Protein Sequence: MSGQPTAVDCLESSGSTVEDVQETPASREKSYGLPVRKGENSLESPAEQAAKDVEIEELTHSEAIAATGSTRKQCPYGGKAPDEPGKLADESEDRKGENTKAIASSPVLVAVDSDSSVELIESPVKFSSANESEKDPPKPDAVNEAAAKEAEEMTDSSISSPTSESFPEKDEKTNKENEQEPPGMEVDQDVEESISRPAEEYKIENTLKGHKRISLTEIEEHKIVDKKDDVLEVELEKGTAPKAAEDEKLNALLSDGDVFYDKECVNCNCTKLHKQYVLANMATLNFYQVLRKSSKQQFLCMGCHDTAMDLYEEYAGQLMAKQPLLLKDFHQDHADFVALDSSDEEEEEKQPEKSDFSKNKLQLIEDELDDAIKNVLNKVDFTAQLSWSKTILQAKADHLERQFALADVELEKVQTTADKMHCALYNSCPVAHKHLPTLDIEPSDYVHEVPPPGEIVRPPIQLGETYYAVKNKAIASWVSIKVIEFTESTAINGNTMKSYKIRYLNTPYQMIKTVTAKHIAYFEPPPVRLTIGTRVIAYFDGTTLSRGKDKGVVQSAFYPGIIAEPLKQANRYRYLIFYDDGYTQYVPHRDVRLVCQASEKVWEDVHAASRDFIQKYVEKYSVDRPMVQCTRGQSMTTESNGTWLYARVIDIDCSLVLMQFEGDKNHTEWIYRGSLRLGPVFRETQNNMNSSSAQQLRVPRRTEPFIRYTKEMESSSKVNQQMRAFARKSSASAQNNALAAASSAATPAGGRTNAGGVSTSNSASAVRHLNNSTIYVDDENRPKGHVVYFTAKRNLPPKMYKCHECSPNCLFKIVHRLDSYSPLAKPLLSGWERLVMRQKTKKSVVYKGPCGKSLRSLAEVHRYLRATENVLNVDNFDFTPDLKCLAEYSIDPSIVKDTDISKGQEKMAIPLVNYYDNTLPPPCTYAKQRIPTEGVHLNLDEEFLLCCDCEDDCSDKSKCACWQLTVAGVRYCNPKKPIEEIGYQYKRLHEHVPTGIYECNSRCKCKKNCLNRVVQFSLEMKLQVFKTSNRGWGLRCVNDIPKGAFICIYAGHLLTETMANEGGQDAGDEYFADLDYIEVAEQLKEGYESEVDHSDPDAEEDNGGPDAEDDDDFRPNYHYQRKIKRSSRSGSTQNSSTQSSELDSQERAVINFNPNADLDETVRENSVRRLFGKDEAPYIMDAKTTGNLGRYFNHSCSPNLFVQNVFVDTHDLRFPWVAFFSAAHIRSGTELTWNYNYEVGVVPGKVLYCQCGAPNCRLRLL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
80	Acetylation	KQCPYGGKAPDEPGK CCCCCCCCCCCCCCC	53.00	21791702
105	Phosphorylation	ENTKAIASSPVLVAV CCCHHHHCCCEEEEE	29.12	19429919
106	Phosphorylation	NTKAIASSPVLVAVD CCHHHHCCCEEEEEC	15.25	19429919
114	Phosphorylation	PVLVAVDSDSSVELI CEEEEECCCCCEEEE	32.56	19429919
116	Phosphorylation	LVAVDSDSSVELIES EEEECCCCCEEEEEC	39.99	19429919
117	Phosphorylation	VAVDSDSSVELIESP EEECCCCCEEEEECC	25.30	19429919
123	Phosphorylation	SSVELIESPVKFSSA CCEEEEECCCCCCCC	28.18	19429919
215	Phosphorylation	LKGHKRISLTEIEEH CCCCCCCCCEEEEEC	33.02	19429919
217	Phosphorylation	GHKRISLTEIEEHKI CCCCCCCEEEEECCC	28.29	19429919
342	Phosphorylation	ADFVALDSSDEEEEE CCEEEECCCCHHHHH	40.31	19429919
343	Phosphorylation	DFVALDSSDEEEEEK CEEEECCCCHHHHHH	49.02	19429919
773	Phosphorylation	AVRHLNNSTIYVDDE HHHHCCCCEEEECCC	18.33	21082442
774	Phosphorylation	VRHLNNSTIYVDDEN HHHCCCCEEEECCCC	20.60	21082442

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SETB1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SETB1_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SETB1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HP1_DROME	Su(var)205	physical	20498723
WDS_DROME	wds	physical	22048023
SUV39_DROME	Su(var)3-9	genetic	19189944
USP_DROME	usp	physical	17362353
DYL1_DROME	ctp	physical	17362353
ZASP_DROME	Zasp52	physical	17362353
SPIR_DROME	spir	physical	17362353
ATC1_DROME	Ca-P60A	physical	17362353

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND THR-217, ANDMASS SPECTROMETRY.
PubMed: 18327897