INAD_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: INAD_DROME
• UniProt AC: Q24008
• Protein Name: Inactivation-no-after-potential D protein
• Gene Name: inaD
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 674
• Subcellular Localization: Cell membrane ; Peripheral membrane protein .
• Protein Description: Involved in the negative feedback regulation of the light-activated signaling cascade in photoreceptors through a calcium-mediated process. Interacts with tetrapeptide ligand located in C-terminal sequence of 3 key components of the visual cascade, tethering them and forming a macromolecular signaling phototransduction complex..
• Protein Sequence: MVQFLGKQGTAGELIHMVTLDKTGKKSFGICIVRGEVKDSPNTKTTGIFIKGIVPDSPAHLCGRLKVGDRILSLNGKDVRNSTEQAVIDLIKEADFKIELEIQTFDKSDEQQAKSDPRSNGYMQAKNKFNQEQTTNNNASGGQGMGQGQGQGQGMAGMNRQQSMQKRNTTFTASMRQKHSNYADEDDEDTRDMTGRIRTEAGYEIDRASAGNCKLNKQEKDRDKEQEDEFGYTMAKINKRYNMMKDLRRIEVQRDASKPLGLALAGHKDRQKMACFVAGVDPNGALGSVDIKPGDEIVEVNGNVLKNRCHLNASAVFKNVDGDKLVMITSRRKPNDEGMCVKPIKKFPTASDETKFIFDQFPKARTVQVRKEGFLGIMVIYGKHAEVGSGIFISDLREGSNAELAGVKVGDMLLAVNQDVTLESNYDDATGLLKRAEGVVTMILLTLKSEEAIKAEKAAEEKKKEEAKKEEEKPQEPATAEIKPNKKILIELKVEKKPMGVIVCGGKNNHVTTGCVITHVYPEGQVAADKRLKIFDHICDINGTPIHVGSMTTLKVHQLFHTTYEKAVTLTVFRADPPELEKFNVDLMKKAGKELGLSLSPNEIGCTIADLIQGQYPEIDSKLQRGDIITKFNGDALEGLPFQVCYALFKGANGKVSMEVTRPKPTLRTEAPKA

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
40	Phosphorylation	VRGEVKDSPNTKTTG EECEECCCCCCEEEE	17.84	27794539
163	Phosphorylation	AGMNRQQSMQKRNTT CCCCHHHHHHHHHCC	18.16	27794539
170	Phosphorylation	SMQKRNTTFTASMRQ HHHHHHCCCCHHHHH	23.65	27794539
174	Phosphorylation	RNTTFTASMRQKHSN HHCCCCHHHHHHCCC	16.08	27794539
314	Phosphorylation	NRCHLNASAVFKNVD CCCCCCCCEEEECCC	24.72	27794539
544	Phosphorylation	HICDINGTPIHVGSM EEECCCCCCCEECCC	18.00	27794539
598	Phosphorylation	AGKELGLSLSPNEIG HCHHHCCCCCCCHHC	25.63	22817900
600	Phosphorylation	KELGLSLSPNEIGCT HHHCCCCCCCHHCCC	23.46	22817900

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of INAD_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 INAD_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRP_DROME	trp	physical	8630257
OPS1_DROME	ninaE	physical	9010208
TRP_DROME	trp	physical	9010208
KPC2_DROME	inaC	physical	9230432
PIPA_DROME	norpA	physical	9230432
TRP_DROME	trp	physical	9230432
PIPA_DROME	norpA	physical	11150331
PIPA_DROME	norpA	physical	9356510
PIPA_DROME	norpA	physical	9545241
PIPA_DROME	norpA	physical	11500369
TRPL_DROME	trpl	physical	9679151
KPC2_DROME	inaC	physical	11150331
KPC2_DROME	inaC	physical	11342563
KPC2_DROME	inaC	physical	9679151
INAD_DROME	inaD	physical	9679151
OPS1_DROME	ninaE	physical	9679151
TRP_DROME	trp	physical	26853938
TRP_DROME	trp	physical	21703451

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-598 AND SER-600, ANDMASS SPECTROMETRY.
PubMed: 17372656