NCBP1_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: NCBP1_DROME
• UniProt AC: Q7K4N3
• Protein Name: Nuclear cap-binding protein subunit 1
• Gene Name: Cbp80
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 800
• Subcellular Localization: Nucleus.
• Protein Description: Component of the cap-binding complex (CBC), which binds cotranscriptionally to the 5'-cap of pre-mRNAs and is involved in various processes such as pre-mRNA splicing and RNA-mediated gene silencing (RNAi). The CBC complex is involved in miRNA-mediated RNA interference via its interaction with Ars2 and is required for primary microRNAs (miRNAs) processing. Also involved in innate immunity via the short interfering RNAs (siRNAs) processing machinery by restricting the viral RNA production. In the CBC complex, Cbp80 does not bind directly capped RNAs (m7GpppG-capped RNA) but is required to stabilize the movement of the N-terminal loop of Cbp20 and lock the CBC into a high affinity cap-binding state with the cap structure..
• Protein Sequence: MSRRRAHDTEDEGYDHRRNKRRRVSENQEIEDRLESLILRVGERSTSSVESNLEGLVSVLEADLGTFRLKILRILSDCAVRMPEKCTVYTTLVGLLNAKNYKFGGEFVDHMVKTFKESLKMCRWDAARYSLRFLADLVNCHVISATSLLQLLDTMIDVSNEDTVPQVRRDWFVFAVLSTLPWVGRDLYEKKESALESLLLRIEVYLNKRSKKHHNALRVWSSDAPHPQEEYLDCLWAQIRKLRQDNWAEKHIPRPYLVFDSILCEALQHNLPTIVPPPHHDNFEYPMPWVVYRMFDYTDCPDGPNLPGAHSIERFLIEEHLHHIIETYHHERKDCAAQLLSFPYKHKIPLEYCIVEVVFAELFHMPTPRYLDICYGSILIELCKLQPATLPQVLAQATEILFMRIDSMNTSCFDRFVNWFSYHLSNFKFTWSWDEWDSCLLLDGEHPRPKFIQEVLQKCLRLSYHQRITEMMPTTYAKLIPLTPVPNYKYANEEAANLPGTTVAHQLVVAIRQKCTPEEVVNILKDIPNSGYSGEEMSDGSFNALKIDVFVQTLLNLGSKSFSHSFAAISKFHSVFRALAETEEAQICILHNIFELWSSHQQMMVVLIDKLLKLQIVDCSAVATWIFSKEMTGEFTKLYLWEILHLTIKKMNKHVIKLNTELSEAKEKLAKADSSSSDSEDDSSHKRKKPITHADKPSEEVVERMEEKLEAANVNQKRLFLIVFQRFIMILSEHLLRSDTDGRDPDTDWYRWTIGRLQQVFLMHHEQVQKYSSTLETLLFTSDLDTHILEVFQQFVALRA

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
9	Phosphorylation	SRRRAHDTEDEGYDH CCCCCCCCCCCCHHH	35.15	19429919
25	Phosphorylation	RNKRRRVSENQEIED HHHCCCCCCCHHHHH	29.08	19429919
36	Phosphorylation	EIEDRLESLILRVGE HHHHHHHHHHHHHHC	25.87	23607784
516	Phosphorylation	VAIRQKCTPEEVVNI HHHHHCCCHHHHHHH	40.55	22668510
530	Phosphorylation	ILKDIPNSGYSGEEM HHHCCCCCCCCCCCC	33.48	22668510
533	Phosphorylation	DIPNSGYSGEEMSDG CCCCCCCCCCCCCCC	43.16	22668510
538	Phosphorylation	GYSGEEMSDGSFNAL CCCCCCCCCCCCCHH	41.94	22668510
559	Phosphorylation	QTLLNLGSKSFSHSF HHHHHHCCCCCCCHH	28.43	22668510
708	Acetylation	VVERMEEKLEAANVN HHHHHHHHHHHCCCC	38.02	21791702

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

Oops, there are no upstream regulatory protein records of NCBP1_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of NCBP1_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 NCBP1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NCBP2_DROME	Cbp20	physical	22036573
SGF11_DROME	Sgf11	physical	22989713

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 THR-9, AND MASSSPECTROMETRY.
PubMed: 18327897