AP3D_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AP3D_DROME
• UniProt AC: P54362
• Protein Name: AP-3 complex subunit delta
• Gene Name: g
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1034
• Subcellular Localization: Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus. Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex..
• Protein Description: Part of the AP-3 complex, an adapter-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes (By similarity).; May be a coat protein involved in the formation of specialized structures like pigment granules..
• Protein Sequence: MALKKVKGNFFERMFDKNLTDLVRGIRNNKDNEAKYISTCIEEIKQELRQDNISVKCNAVAKLTYIQMLGYDISWAGFNIIEVMSSSRFTCKRIGYLAASQCFHPDSELLMLTTNMIRKDLNSQNQYDAGVALSGLSCFISPDLSRDLANDIMTLMSSTKPYLRMKAVLMMYKVFLRYPEALRPAFPKLKEKLEDPDPGVQSAAVNVICELARKNPKNYLPLAPIFFKLMTTSTNNWMLIKIIKLFGALTPLEPRLGKKLIEPLTNLIHSTSAMSLLYECINTVIAVLISISSGMPNHSASIQLCVQKLRILIEDSDQNLKYLGLLAMSKILKTHPKSVQAHKDLILACLDDKDESIRLRALDLLYGMVSKKNLMEIVKRLLGHMERAEGSAYRDELLYKVIEICAQSSYLYVTNFEWYLTVLVELIQLEAGSRHGRLIAEQLLDVAIRVPVVRQFAVNEMTNLLDTFTVSAQSNSMYEVLYAAAWIVGEFAGELEDAEKTLNILLRPRLLPGHIQGVYVQNVIKLFARLATTCLELQDLPGLVTLCDHVLDKLQHFNGSSDIEVQERANSACMLIEMLRNQLSTSTDAMAMDTTTEGGIPPLAIEIVQEMTLLFTGELIPVAPKAQRKVPLPDGLDLDEWINAPPPEDAASSSSSEHDKDELFVSATQAGTGADGGEKRRQSLELTPEQLERQRMARLIEQSNNPHYLKSTPTASGASNADQYDNIDDIPITELPLDMEGVAALRVGITKRSDKYLQEQQAAQGSKDGKKKHKKGKKSKKAKNKVAYNSSSESEGEPKPLHIVNTTLDMPEGVSMSDSEDKDGKYDPNDPHRALDIELDITEFEAPAVRSASKKSAADKENLKTPADLAGGGNAAKKDRKKDKDKDKERKVKREHRESKRERKEAAVQPVIDLIDADTPTPSPSHISATSNNNNTSTVLPDAPKHHKKKKNKEKTTDEAPDALATATGSSIIDVGGEEASEVASKVHKKKHKKEKSQRKEKKKASESASVSAIVSIGDYEQPLGISTPSKEIL

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
652	Phosphorylation	PPPEDAASSSSSEHD CCHHHCCCCCCCCCC	32.26	19429919
653	Phosphorylation	PPEDAASSSSSEHDK CHHHCCCCCCCCCCH	29.52	19429919
654	Phosphorylation	PEDAASSSSSEHDKD HHHCCCCCCCCCCHH	35.07	19429919
655	Phosphorylation	EDAASSSSSEHDKDE HHCCCCCCCCCCHHH	41.51	19429919
656	Phosphorylation	DAASSSSSEHDKDEL HCCCCCCCCCCHHHE	40.68	19429919
683	Phosphorylation	GGEKRRQSLELTPEQ CCHHHHHHCCCCHHH	23.23	21082442
687	Phosphorylation	RRQSLELTPEQLERQ HHHHCCCCHHHHHHH	18.53	19429919
766	Phosphorylation	EQQAAQGSKDGKKKH HHHHHHCCCCHHHHC	18.59	27794539
790	Phosphorylation	KNKVAYNSSSESEGE CCCCCCCCCCCCCCC	23.67	19429919
791	Phosphorylation	NKVAYNSSSESEGEP CCCCCCCCCCCCCCC	34.19	19429919
792	Phosphorylation	KVAYNSSSESEGEPK CCCCCCCCCCCCCCC	44.99	19429919
794	Phosphorylation	AYNSSSESEGEPKPL CCCCCCCCCCCCCCE	53.50	19429919
815	Phosphorylation	LDMPEGVSMSDSEDK CCCCCCCCCCCCCCC	24.35	19429919
817	Phosphorylation	MPEGVSMSDSEDKDG CCCCCCCCCCCCCCC	30.40	19429919
819	Phosphorylation	EGVSMSDSEDKDGKY CCCCCCCCCCCCCCC	40.15	19429919
919	Phosphorylation	IDLIDADTPTPSPSH HHHHCCCCCCCCCCC	30.68	30478224

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

Oops, there are no upstream regulatory protein records of AP3D_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AP3D_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 AP3D_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZEST_DROME	z	genetic	11962627
WHITE_DROME	w	genetic	11962627
BL1S1_DROME	Blos1	genetic	20015953

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-683 AND THR-687, ANDMASS SPECTROMETRY.
PubMed: 18327897

"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683, AND MASSSPECTROMETRY.
PubMed: 17372656