PYRG_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PYRG_DROME
• UniProt AC: Q9VUL1
• Protein Name: CTP synthase
• Gene Name: CTPsyn
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 627
• Subcellular Localization: Cytoplasm . Isoform 1 localizes to cytoophidium, a subcellular filamentary structure where CTP synthase is compartmentalized. Isoform 2 localizes to cytoplasm.
• Protein Description: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Constitutes the rate-limiting enzyme in the synthesis of cytosine nucleotides (By similarity). Isoform 1 is required for cytoophidium assembly in female germline cells..
• Protein Sequence: MKYILVTGGVISGVGKGVIASSFGTLLKSCGLDVTSIKIDPYINIDAGTFSPYEHGEVYVLDDGAEVDLDLGNYERFLDVTLHRDNNITTGKIYKLVIEKERTGEYLGKTVQVVPHITDAIQEWVERVAQTPVQGSSKPQVCIVELGGTIGDIEGMPFVEAFRQFQFRVKRENFCLAHVSLVPLPKATGEPKTKPTQSSVRELRGCGLSPDLIVCRSEKPIGLEVKEKISNFCHVGPDQVICIHDLNSIYHVPLLMEQNGVIEYLNERLQLNIDMSKRTKCLQQWRDLARRTETVRREVCIAVVGKYTKFTDSYASVVKALQHAALAVNRKLELVFIESCLLEEETLHSEPSKYHKEWQKLCDSHGILVPGGFGSRGMEGKIRACQWARENQKPLLGICLGLQAAVIEFARNKLGLKDANTTEIDPNTANALVIDMPEHHTGQLGGTMRLGKRITVFSDGPSVIRQLYGNPKSVQERHRHRYEVNPKYVHLLEEQGMRFVGTDVDKTRMEIIELSGHPYFVATQYHPEYLSRPLKPSPPFLGLILASVDRLNQYIQRGCRLSPRQLSDASSDEEDSVVGLAGATKSLSSLKIPITPTNGISKSCNGSISTSDSEGACGGVDPTNGHK

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
94	Phosphorylation	NITTGKIYKLVIEKE CCCCCEEEEEEEECC	11.19	27794539
468	Phosphorylation	PSVIRQLYGNPKSVQ HHHHHHHHCCCCHHH	13.40	25749252
562	Phosphorylation	IQRGCRLSPRQLSDA HHHCCCCCHHHHCCC	9.93	25749252
567	Phosphorylation	RLSPRQLSDASSDEE CCCHHHHCCCCCCCH	23.85	19429919
570	Phosphorylation	PRQLSDASSDEEDSV HHHHCCCCCCCHHHH	43.22	19429919
571	Phosphorylation	RQLSDASSDEEDSVV HHHCCCCCCCHHHHH	51.25	19429919
576	Phosphorylation	ASSDEEDSVVGLAGA CCCCCHHHHHHHCHH	23.21	28490779
586	Phosphorylation	GLAGATKSLSSLKIP HHCHHCCCHHHCCCC	29.18	21082442
588	Phosphorylation	AGATKSLSSLKIPIT CHHCCCHHHCCCCCC	40.49	22817900
589	Phosphorylation	GATKSLSSLKIPITP HHCCCHHHCCCCCCC	38.69	21082442
595	Phosphorylation	SSLKIPITPTNGISK HHCCCCCCCCCCCCC	20.78	28490779
607	Phosphorylation	ISKSCNGSISTSDSE CCCCCCCCCCCCCCC	10.20	29892262
609	Phosphorylation	KSCNGSISTSDSEGA CCCCCCCCCCCCCCC	24.45	29892262
610	Phosphorylation	SCNGSISTSDSEGAC CCCCCCCCCCCCCCC	34.58	29892262
611	Phosphorylation	CNGSISTSDSEGACG CCCCCCCCCCCCCCC	32.14	29892262
613	Phosphorylation	GSISTSDSEGACGGV CCCCCCCCCCCCCCC	37.38	29892262

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PYRG_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 PYRG_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PYRG_DROME	CTPsyn	physical	14605208
CTBP_DROME	CtBP	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-567; SER-570; SER-571;SER-588 AND THR-595, AND MASS SPECTROMETRY.
PubMed: 18327897