TRR_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRR_DROME
• UniProt AC: Q8IRW8
• Protein Name: Histone-lysine N-methyltransferase trr
• Gene Name: trr
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 2431
• Subcellular Localization: Nucleus . Chromosome .
• Protein Description: Histone methyltransferase that acts as a coactivator for the ecdysone receptor during development. Specifically trimethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation. Recruited by EcR in an ecdysone-dependent manner causing H3 'Lys-4' trimethylation at ecdysone-inducible promoters, leading to activate expression. Plays a central role in the developing compound eye, during the progression of the morphogenetic furrow and in post-furrow differentiation of the retinal epithelium, notably by activating expression of hh. Also required for wing and abdominal development..
• Protein Sequence: MNIPKVTTSLGAAEKAKPERVASVAAAAFNAVSLQKRSGDDTATPAEDPTRKKAKTELLLGTGTAAPSLPAKASSTAPQQLLYQRSGQQAKAQVKAASEPQDVETADGVWDARDQQIIVCNFGSGTEMGAIKAEDADKQSEYRISTPRNSQSNPLLHRNTAFTSFTKKEGASSSASSSSSTASVISIEPSGSGQDHAENSGKSEDLDYVLMPASGADSSTSVGNSTGTGTPAGTPIGATTSTIILNANNGTAGVSGAGTTTILTQKSGHTNYNIFNTTATGSQTPTTTLLNRVNLHPKMKTQLMVNAKKLSEVTQTTAKVSIGNKTISVPLLKPLMSASGAATAGGATIVESKQLLQPGGQVTTVMSAAQQSGGQQVHPHVHSHAHHNFTKLIKRGPKNSGTIVSFSGLQIKPANTKIVATKVVSKKMLQLQQHQQQIQQQQQLQQLQVTSGGGLAPPTGSIVTITTTNPSQTYAMVQDSATVGPAAHSEDDAPAPRKITAYSENLQKILNKSKSQESTGGPEEFTNINSVVIKPLDKNTLNCPPSFNIFKQQQHSQAAQSQSISAVGSGAGTPVTFTMASGNASDLATTSTVSVSAGTICINSPMMGTRPIISIQNKNISLVLSKTTMAQQKPKMITTTTLSSQAALQMHHALIQDSSADKAGSSANSGSATSGASMQLKLTTANTPTKLSVSLAPDVVKLEEVGSESKAKLLVKQEAVVKDSTGTPTSEERAEEIGTPEKRLNANATMTAINQVQNQSANQIQMATSTSTASNPSTPNPTVNATPMNNQRSAAEDNALLKQLLQNNSSSHSLNQISITSAHVGSASASAPLSARKVINVRAPSMGKVRSLEDQLARPVIPPVPTATQAAGSSSSSGSVATSTTTTTVASGGSSQQVATASATALPVSAVAITTPGVGGEAKLEQKSDQPAAIMQNQSQNQAPPPPPPPQQQQQQQLHQPQQLQPSPHQVKQTVQIVSKETSFISGPVAAKTLVTEATSKPAELLPPPPYEMATAPISNVTISISTKQAAPKELQMKPKAVAMSLPMEQGDESLPEQAEPPLHSEQGATAAGVAPHSGGPLVSAQWTNNHLEGGVATTKIPFKPGEPQKRKLPMHPQLDEKQIQQQAEIPISTSLPTTPTGQGTPDKVQLISAIATYVKKSGVPNEAQPIQNQSQGQVQMQAQMQATMQGHLSGQMSGQISGHAAGQIPAQMHLQVQHQLHMAVHPQQQQQQLHQNQPQNATIPLPVTGQGAVPIPVPTMESKAGDQRKRRKREVQKPRRTNLNAGQAGGALKDLTGPLPAGAMVQLAGMPPGTQYIQGAASGTGHVITSTGQGVTLGGVGASTGASSSPMLKKRVRKFSKVEEDHDAFTEKLLTHIRQMQPLQVLEPHLNRNFHFLIGSNETSGGGSPASMSSAASAGSSSAGGGKLKGGSRGWPLSRHLEGLEDCDGTVLGRYGRVNLPGIPSLYDSERFGGSRGLVGGSARTRSPSPAESPGAEKMLPMSSIQNDFYDQEFSTHMERNPRERLVRHIGAVKDCNLETVDLVESEGVAAWATLPRLTRYPGLILLNGNSRCHGRMSPVALPEDPLTMRFPVSPLLRSCGEELRKTQQMELGMGPLGNNNNNNYQQKNQNVILALPASASENIAGVLRDLANLLHLAPALTCKIIEDKIGNKLEDQFMNQDDEKHVDFKRPLSQVSHGHLRKILNGRRKLCRSCGNVVHATGLRVPRHSVPALEEQLPRLAQLMDMLPRKSVPPPFVYFCDRACFARFKWNGKDGQAEAASLLLQPAGGSAVKSSNGDSPGSFCASSTAPAEMVVKQEPEDEDEKTPSVPGNPTNIPAQRKCIVKCFSADCFTTDSAPSGLELDGTAGAGTGAGPVNNTVWETETSGLQLEDTRQCVFCNQRGDGQADGPSRLLNFDVDKWVHLNCALWSNGVYETVSGALMNFQTALQAGLSQACSACHQPGATIKCFKSRCNSLYHLPCAIREECVFYKNKSVHCSVHGHAHAGITMGAGAGATTGAGLGGSVADNELSSLVVHRRVFVDRDENRQVATVMHYSELSNLLRVGNMTFLNVGQLLPHQLEAFHTPHYIYPIGYKVSRYYWCVRRPNRRCRYICSIAEAGCKPEFRIQVQDAGDKEPEREFRGSSPSAVWQQILQPITRLRKVHKWLQLFPQHISGEDLFGLTEPAIVRILESLPGIETLTDYRFKYGRNPLLEFPLAINPSGAARTEPKQRQLLVWRKPHTQRTAGSCSTQRMANSAAIAGEVACPYSKQFVHSKSSQYKKMKQEWRNNVYLARSKIQGLGLYAARDIEKHTMIIEYIGEVIRTEVSEIREKQYESKNRGIYMFRLDEDRVVDATLSGGLARYINHSCNPNCVTEIVEVDRDVRIIIFAKRKIYRGEELSYDYKFDIEDESHKIPCACGAPNCRKWMN

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
15	Acetylation	TSLGAAEKAKPERVA CCCCHHHHCCHHHHH	57.91	21791702
145	Phosphorylation	KQSEYRISTPRNSQS CCCCCCCCCCCCCCC	24.30	18511481
150	Phosphorylation	RISTPRNSQSNPLLH CCCCCCCCCCCCCCC	35.94	18511481
284	Phosphorylation	TTATGSQTPTTTLLN CCCCCCCCCCCCCHH	25.05	21082442
308	Acetylation	TQLMVNAKKLSEVTQ HHHEECHHHHHHHCE	49.39	21791702
422	Acetylation	NTKIVATKVVSKKML CCEEEEEHHHCHHHH	30.79	21791702
426	Acetylation	VATKVVSKKMLQLQQ EEEHHHCHHHHHHHH	30.50	21791702
513	Phosphorylation	LQKILNKSKSQESTG HHHHHHHCCCCCCCC	36.14	21082442
633	Acetylation	KTTMAQQKPKMITTT CCCCCCCCCCEEEEC	34.23	21791702
690	Acetylation	TTANTPTKLSVSLAP EECCCCCEEEEEECC	39.71	21791702
739	Phosphorylation	ERAEEIGTPEKRLNA HHHHHHCCHHHHHCC	33.66	19429919
742	Acetylation	EEIGTPEKRLNANAT HHHCCHHHHHCCHHH	64.49	21791702
848	Acetylation	VRAPSMGKVRSLEDQ EECCCCCCCCCHHHH	26.32	21791702
1104	Acetylation	ATTKIPFKPGEPQKR EEEECCCCCCCCCCC	46.92	21791702
1361	Phosphorylation	KKRVRKFSKVEEDHD HHHHHHHCCCCCCCH	38.54	22817900
1414	Phosphorylation	GGSPASMSSAASAGS CCCCCCHHCHHHCCC	17.84	22817900
1415	Phosphorylation	GSPASMSSAASAGSS CCCCCHHCHHHCCCC	21.15	22817900
1486	Phosphorylation	LVGGSARTRSPSPAE CCCCCCCCCCCCCCC	34.90	25749252
1488	Phosphorylation	GGSARTRSPSPAESP CCCCCCCCCCCCCCC	29.17	25749252
1490	Phosphorylation	SARTRSPSPAESPGA CCCCCCCCCCCCCCH	37.68	25749252
1579	Phosphorylation	SRCHGRMSPVALPED CCCCCCCCCCCCCCC	18.18	19429919
1595	Phosphorylation	LTMRFPVSPLLRSCG CCCCCCCHHHHHHCH	15.29	22817900

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRR_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 TRR_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ECR_DROME	EcR	physical	14603321
USP_DROME	usp	physical	14603321
ECR_DROME	EcR	genetic	14603321

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 THR-1486; SER-1488 ANDSER-1490, AND MASS SPECTROMETRY.
PubMed: 18327897