BTHD_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BTHD_DROME
• UniProt AC: Q9VYB0
• Protein Name: Selenoprotein BthD
• Gene Name: BthD
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 249
• Subcellular Localization: Cytoplasm . Secreted . Secreted into the salivary gland lumen.
• Protein Description: May be involved in a redox-related process. Required for survival and specifically for salivary gland morphogenesis..
• Protein Sequence: MPPKRNKKAEAPIAERDAGEELDPNAPVLYVEHCRSURVFRRRAEELHSALRERGLQQLQLQLNALGAPRRGAFELSLSAGGMGKQEQVALWSGLKRGPPRARKFPTVEEVYDQIVGILGDQQESKEQTNTQKSSKIDLPGSEAIASPKKSESTEEAQENKAPTSTSTSRKSKKEQKSEEEPTQVDSKEAKQSKELVKTKRQPKAQKKQAKASESQEEVAEDKPPSSQKRKRTTRSSTDEATAGAKRRR

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
147	Phosphorylation	PGSEAIASPKKSEST CCCHHCCCCCCCCCH	31.01	28490779
178	Phosphorylation	KSKKEQKSEEEPTQV HHHHHHCCCCCCCCC	50.35	25749252
236	Phosphorylation	KRKRTTRSSTDEATA HCCCCCCCCHHHHHH	35.18	21082442
237	Phosphorylation	RKRTTRSSTDEATAG CCCCCCCCHHHHHHH	36.27	25749252
238	Phosphorylation	KRTTRSSTDEATAGA CCCCCCCHHHHHHHH	38.82	29892262

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BTHD_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 BTHD_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WDR82_DROME	Wdr82	physical	22036573
HPF1_DROME	CG1218	physical	22036573
GMPPB_DROME	CG1129	physical	22036573

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-147, AND MASSSPECTROMETRY.
PubMed: 17372656