GYS_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GYS_DROME
• UniProt AC: Q9VFC8
• Protein Name: Glycogen [starch] synthase
• Gene Name: GlyS
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 709
• Subcellular Localization: Cytoplasmic vesicle, autophagosome . Isoform B colocalizes with Atg8a at autophagosomes upon starvation in larval skeletal muscle.
• Protein Description: Transfers the glycosyl residue from UDPG to the non-reducing end of alpha-1,4-glucan. In larval skeletal muscle, isoform B is required for the formation of autophagosomes during starvation and during cloroquine-induced vacuolar myopathy..
• Protein Sequence: MRRQQSYRFEDNESTSYALRMNRRFSRVESGADLKDYFDRGDIASRENRWNFEVAWEVANKVGGIYTVIRSKAYVSTEEMGEQLCMMGPYKEHCARTEMEEMEFPRGNPLLDAVNSLRSRGYKIHTGRWLVDGNPQLILFDIGSAAWKLDQFKSEMWEKCHIGIPHLDIETNDAIILGFMIAEFLEEFRNFAVTYSQNNELSAPRIVAHFHEWQAGVGLIVLRTRLVEIATVFTTHATLLGRYLCAGNTDFYNNLDKFAVDEEAGKRQIYHRYCLERGATHLAHVFTTVSEITGYEAEHLLKRKPDIITPNGLNVKKFSAIHEFQNLHAVAKEKINEFVRGHFYGHIDFDLDKTLYFFIAGRYEFGNKGADIFIEALARLNAMLKHEKPDTTVVAFLIFPTKTNNFNVDSLRGHAVIKQLRDTINNVQQAVGKRMFDTCLQGNIPNADDLLQKDDLVKIKRCMFAMQRDSMPPVTTHNVADDWNDPVLSSIRRCHLFNSRHDRVKMVFHPEFLTSTNPLFGIDYEEFVRGCHLGVFPSYYEPWGYTPAECTVMGIPSVTTNLSGFGCFMEEHISDPKSYGIYIVDRRYIGLENSVQQLSSFMMEFSRLNRRQRIIQRNRTERLSDLLDWRTLGIYYRQARVKALQAVYPDYVDELSLYGSKNNLIFSRPHSEPPSPTSSRHTTPAPSVHGSDDEDSVDEETELKELGIK

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
26	Phosphorylation	LRMNRRFSRVESGAD HHHHHHCCCCCCCCC	33.34	19429919
30	Phosphorylation	RRFSRVESGADLKDY HHCCCCCCCCCHHHH	36.10	21082442
37	Phosphorylation	SGADLKDYFDRGDIA CCCCHHHHCHHCCCC	13.04	22668510
423	Phosphorylation	VIKQLRDTINNVQQA HHHHHHHHHHHHHHH	21.12	21082442
656	Phosphorylation	PDYVDELSLYGSKNN CCHHHHEEEECCCCC	19.93	19429919
658	Phosphorylation	YVDELSLYGSKNNLI HHHHEEEECCCCCEE	18.90	19429919
660	Phosphorylation	DELSLYGSKNNLIFS HHEEEECCCCCEEEC	20.75	21082442
667	Phosphorylation	SKNNLIFSRPHSEPP CCCCEEECCCCCCCC	37.60	19429919
671	Phosphorylation	LIFSRPHSEPPSPTS EEECCCCCCCCCCCC	55.25	19429919
675	Phosphorylation	RPHSEPPSPTSSRHT CCCCCCCCCCCCCCC	52.07	19429919
677	Phosphorylation	HSEPPSPTSSRHTTP CCCCCCCCCCCCCCC	43.61	19429919
678	Phosphorylation	SEPPSPTSSRHTTPA CCCCCCCCCCCCCCC	28.85	19429919
679	Phosphorylation	EPPSPTSSRHTTPAP CCCCCCCCCCCCCCC	30.47	19429919
682	Phosphorylation	SPTSSRHTTPAPSVH CCCCCCCCCCCCCCC	33.11	19429919
683	Phosphorylation	PTSSRHTTPAPSVHG CCCCCCCCCCCCCCC	16.01	19429919
687	Phosphorylation	RHTTPAPSVHGSDDE CCCCCCCCCCCCCCC	28.93	19429919
691	Phosphorylation	PAPSVHGSDDEDSVD CCCCCCCCCCCCCCC	27.32	19429919
696	Phosphorylation	HGSDDEDSVDEETEL CCCCCCCCCCHHHHH	29.44	21082442
701	Phosphorylation	EDSVDEETELKELGI CCCCCHHHHHHHHCC	44.57	19429919

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GYS_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 GYS_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ESM8_DROME	E(spl)m8-HLH	physical	14605208

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-26; SER-30; SER-660;SER-667; SER-671; SER-675; SER-679; THR-682; THR-683; SER-687; SER-691AND SER-696, 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-30 AND SER-660, AND MASSSPECTROMETRY.
PubMed: 17372656