CED6_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CED6_DROME
• UniProt AC: Q7JUY7
• Protein Name: PTB domain-containing adapter protein ced-6
• Gene Name: ced-6
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 517
• Subcellular Localization: Cytoplasm.
• Protein Description: Plays a role in axon pruning in larval mushroom body neurons during metamorphosis. [PubMed: 16772168 Plays a role in the infiltration of glial cell processes into mushroom body lobes and the subsequent engulfment of degenerating axon branches]
• Protein Sequence: MPYQPANSGGTSGGSKAAAKMAQLKFWNKQNSSKQQQQDKDKDAADGGNNTSGGGTGSNSNGDAKSEAKNGKRNWLHTPEQLISGHAVYLVKFFGNLSVDQPKGIEVVKEAIRKLQFAQQMKKAETGTQEKFKKLEITISIKGVAIQEPRTHKILHQFPLYNISYCADEKGVKKFFSFIAKTVKTQDGSDPTSNGHANGNGDGSAKVEESHECFVFISNKLASDITLTIGQAFDLAYRKYMDSTEKTNLSKAQQQINHLQQTVNVYKERLREVSAKLPKAELDALLFNLGIKDILEAPTTEPQNGIEVASEALSNGKLDDDKLLIDTNSTTASTHSASPSSFLPIVPPRNNLSSQISIGGKSNSQKMDELLLNSDSDSDFDPRADETQEIGGTGRSAISNMFGFEPANSFGQHLFSNNNDHKLQNNNSSLLITSNNNSINSSGFSSELNITPPLLAPPPKIAAPRRLNSVTTGNGLNGNTDLFGSDPFELNNGPNIFKQNQLNLDDFSLESLDPLRK

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
330	Phosphorylation	LLIDTNSTTASTHSA EEEECCCCCCCCCCC	28.57	19429919
336	Phosphorylation	STTASTHSASPSSFL CCCCCCCCCCHHHCC	30.45	19429919
338	Phosphorylation	TASTHSASPSSFLPI CCCCCCCCHHHCCCC	28.47	19429919
340	Phosphorylation	STHSASPSSFLPIVP CCCCCCHHHCCCCCC	31.09	19429919
357	Phosphorylation	NNLSSQISIGGKSNS CCCCCCEEECCCCCC	13.93	19429919
362	Phosphorylation	QISIGGKSNSQKMDE CEEECCCCCCHHHHH	45.01	21082442
374	Phosphorylation	MDELLLNSDSDSDFD HHHHHHCCCCCCCCC	38.16	19429919
376	Phosphorylation	ELLLNSDSDSDFDPR HHHHCCCCCCCCCCC	38.54	19429919
378	Phosphorylation	LLNSDSDSDFDPRAD HHCCCCCCCCCCCCC	44.09	19429919
469	Phosphorylation	AAPRRLNSVTTGNGL CCCCCCCCCCCCCCC	25.98	19429919
471	Phosphorylation	PRRLNSVTTGNGLNG CCCCCCCCCCCCCCC	28.89	19429919
472	Phosphorylation	RRLNSVTTGNGLNGN CCCCCCCCCCCCCCC	26.88	19429919
480	Phosphorylation	GNGLNGNTDLFGSDP CCCCCCCCCCCCCCC	35.16	17372656
508	Phosphorylation	QLNLDDFSLESLDPL CCCCCCCCHHHCCCC	37.92	19429919
511	Phosphorylation	LDDFSLESLDPLRK- CCCCCHHHCCCCCC-	43.28	19429919

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

Oops, there are no upstream regulatory protein records of CED6_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CED6_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 CED6_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference

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-338; SER-374; SER-376AND SER-378, AND MASS 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-338; SER-469 ANDTHR-480, AND MASS SPECTROMETRY.
PubMed: 17372656