SRRT_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SRRT_DROME
• UniProt AC: Q9V9K7
• Protein Name: Serrate RNA effector molecule homolog
• Gene Name: Ars2
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 943
• Subcellular Localization: Nucleus.
• Protein Description: Acts as a mediator between the cap-binding complex (CBC) and RNA-mediated gene silencing (RNAi). Involved in innate immunity via the short interfering RNAs (siRNAs) processing machinery by restricting the viral RNA production. Also involved microRNA (miRNA)-mediated silencing by contributing to the stability and delivery of primary miRNA transcripts to the primary miRNA processing complex containing drosha and pasha..
• Protein Sequence: MGDSDDEYDRKRRDKFRGERESYRTERRDDRRPVGGSAGARDEWAERNPFRGGASAGGGGARHRPDYSDYRGPGARPRYGSPVRDLPPAKRMRPDWGDGDVRANPRFGGYDPYLMQAWNDHYQSMHSAYSHGGHAPPVRESIGGGGGDTLTQPAMLNLKQFLDTQDENISDSEVMRKYTEYKTDFKRQQLNEFFVAHKDEEWFKNKYHPEDSVKRSEEQRGFLQRRTDVFMELLENGTIGSVKVDSSQADALIRVLDTCVIKLEGGTDEDLKVLDEKPKDPVVYERKAEQMQSVKEVEKTINSPKEEMSEADPVSTQRKPVRPVNSDGENWDDDDAENSAPKKELAEDSKDSDSKPEDKQLNKKKTKKRKRNSSDDDSSSSESSSSSDEEKLKEKYDVEDGLRAEQKTEAEKDRQEATKAKQGPQSPKLDEDEGNENTEPKGLDSKINTYEEIDNTLKSPEISSNPIKNTDNGDGSKVEEDGEKPSVGKDKVVETETIDLDKVKDGQPRALHRTSSIFLRNLAPSITRSEIEAVCNRFSGYLRVAIADPLVERRWYRRGWITFMRDVNIKEICWGLNNQRLRDCEMGAIVNRDLSRRVRPANGITAHKQVVRSDIKLCAKIALNLDEKFRLWAEGPKDDSNSARANESSENGSGSTYGFNSQNPVLQNITDYLIEEASAEEEELLGLTGENKDTEGEPIERDEQLISVLDRLVLYLRIVHSVDYYNHCEYPYEDEMPNRCGIIHARGPPPVRVTNNDVQEYIKIYESKLQQFLTKTVPLSDEEIKNLGAKDAETEVEKFVQANTQELAKDKWLCPLSGKKFKGPEFIRKHIFNKHEEKVDEVRKEVQYFNNYLRDPKRPQLPEHPGTSKRPESESARGGGGGYRPPMYPPFSAMPYGFGPPMMGGGRGGRNFPPARRELPLEHQRRLIGYHDLDAPANSDMFD

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
4	Phosphorylation	----MGDSDDEYDRK ----CCCCHHHHHHH	41.03	19429919
79	Phosphorylation	GPGARPRYGSPVRDL CCCCCCCCCCCCCCC	25.33	22817900
81	Phosphorylation	GARPRYGSPVRDLPP CCCCCCCCCCCCCCC	15.99	19429919
170	Phosphorylation	DTQDENISDSEVMRK HCCCCCCCHHHHHHH	46.82	22668510
300	Phosphorylation	SVKEVEKTINSPKEE HHHHHHHHHCCCHHH	16.34	19429919
303	Phosphorylation	EVEKTINSPKEEMSE HHHHHHCCCHHHHHC	33.23	21082442
309	Phosphorylation	NSPKEEMSEADPVST CCCHHHHHCCCCCCC	32.67	19429919
326	Phosphorylation	KPVRPVNSDGENWDD CCCCCCCCCCCCCCC	47.42	21082442
339	Phosphorylation	DDDDAENSAPKKELA CCCCCCCCCCHHHHH	37.14	22668510
349	Phosphorylation	KKELAEDSKDSDSKP HHHHHHCCCCCCCCH	29.84	25749252
352	Phosphorylation	LAEDSKDSDSKPEDK HHHCCCCCCCCHHHH	47.74	19429919
354	Phosphorylation	EDSKDSDSKPEDKQL HCCCCCCCCHHHHHH	54.80	19429919
426	Phosphorylation	KAKQGPQSPKLDEDE HHHCCCCCCCCCCCC	27.43	21082442
449	Phosphorylation	GLDSKINTYEEIDNT CHHHHCCCHHHHHHC	35.46	22668510
456	Phosphorylation	TYEEIDNTLKSPEIS CHHHHHHCCCCCCCC	31.64	22817900
459	Phosphorylation	EIDNTLKSPEISSNP HHHHCCCCCCCCCCC	30.77	19429919
464	Phosphorylation	LKSPEISSNPIKNTD CCCCCCCCCCCCCCC	52.89	22668510
640	Phosphorylation	AEGPKDDSNSARANE HCCCCCCCCCCCCCC	42.70	19429919
642	Phosphorylation	GPKDDSNSARANESS CCCCCCCCCCCCCCC	24.08	19429919
794	Phosphorylation	LGAKDAETEVEKFVQ CCCCCHHHHHHHHHH	47.23	22668510
804	Phosphorylation	EKFVQANTQELAKDK HHHHHHCHHHHHCCC	26.83	22668510

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SRRT_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 SRRT_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NCBP1_DROME	Cbp80	physical	24145821

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 TYR-79; SER-81; THR-300;SER-303; SER-309; SER-349; SER-352; SER-640 AND SER-642, AND MASSSPECTROMETRY.
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-326 AND SER-426, ANDMASS SPECTROMETRY.
PubMed: 17372656