NASP_DROME - dbPTM
NASP_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NASP_DROME
UniProt AC Q9I7K6
Protein Name Protein NASP homolog
Gene Name CG8223
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 492
Subcellular Localization
Protein Description
Protein Sequence MSAEAEAIVTTATADVSSPSKTVAVEPVAADTTPDNAPAVSTEGSGKAEQERAEKILKGKELFSQGSRNFLVKSYDEAADELSQVCQLYEEVYGELADELGQPLLLYAKALIAMALDENKVIDVPDEAADDDDEDVDDDEEESAEDGAAKKEEKKDTKEAANGASSSNGKELDTIKEGSDEADSTGEAEQAQSDEKPSKKVPTGVDEVSSSNGGGGAAVNDDERPSTSNGEVTASCSNGAAPAVEEEPEEEEGVSGSLQLAWEILEAAAQIFSRQGLSGLPYLAEVQTELANIEFENGILEAAREDYEKALKIHGELPTRNRRALAELHYKIGLTYLMQQLNKEGATALRQSSVLIEEEIAEIKGKDEPSERDRNNMLDLEETKQEILAKIQEIEEMQAQTIAEVRAALDSYIKPMSSGDAAAASSSSSSSANGAASSSSSSSKGAAAASSSTISSSSAKPTDITHLIKRKKPEDPSSEAEALCSPAKRAAV
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 Orthologous
Protein Cluster
2Phosphorylation------MSAEAEAIV
------CCHHHCEEE
34.5119429919
10PhosphorylationAEAEAIVTTATADVS
HHHCEEEEECCCCCC
12.4719429919
11PhosphorylationEAEAIVTTATADVSS
HHCEEEEECCCCCCC
15.8919429919
13PhosphorylationEAIVTTATADVSSPS
CEEEEECCCCCCCCC
22.6919429919
17PhosphorylationTTATADVSSPSKTVA
EECCCCCCCCCCEEE
36.7619429919
18PhosphorylationTATADVSSPSKTVAV
ECCCCCCCCCCEEEE
32.8019429919
20PhosphorylationTADVSSPSKTVAVEP
CCCCCCCCCEEEEEE
42.7919429919
22PhosphorylationDVSSPSKTVAVEPVA
CCCCCCCEEEEEEEC
20.3128490779
32PhosphorylationVEPVAADTTPDNAPA
EEEECCCCCCCCCCC
35.1928490779
33PhosphorylationEPVAADTTPDNAPAV
EEECCCCCCCCCCCC
29.2322817900
42PhosphorylationDNAPAVSTEGSGKAE
CCCCCCCCCCCCHHH
37.4530478224
47AcetylationVSTEGSGKAEQERAE
CCCCCCCHHHHHHHH
50.9121791702
143PhosphorylationVDDDEEESAEDGAAK
CCCCHHHHHHHHHHH
39.9919429919
165PhosphorylationKEAANGASSSNGKEL
HHHHHCCCCCCCCCC
35.3822668510
166PhosphorylationEAANGASSSNGKELD
HHHHCCCCCCCCCCC
27.5622668510
170AcetylationGASSSNGKELDTIKE
CCCCCCCCCCCCCCC
60.3921791702
174PhosphorylationSNGKELDTIKEGSDE
CCCCCCCCCCCCCCC
46.7219429919
179PhosphorylationLDTIKEGSDEADSTG
CCCCCCCCCCCCCCC
33.1121082442
184PhosphorylationEGSDEADSTGEAEQA
CCCCCCCCCCHHHHH
45.4121082442
185PhosphorylationGSDEADSTGEAEQAQ
CCCCCCCCCHHHHHH
39.3219429919
193PhosphorylationGEAEQAQSDEKPSKK
CHHHHHHCCCCCCCC
51.2418327897
198PhosphorylationAQSDEKPSKKVPTGV
HHCCCCCCCCCCCCC
57.0623607784
451PhosphorylationKGAAAASSSTISSSS
HCCCHHCCCCCCCCC
27.1221082442
452PhosphorylationGAAAASSSTISSSSA
CCCHHCCCCCCCCCC
27.5421082442
455PhosphorylationAASSSTISSSSAKPT
HHCCCCCCCCCCCCC
25.0221082442
456PhosphorylationASSSTISSSSAKPTD
HCCCCCCCCCCCCCC
25.1822817900
460AcetylationTISSSSAKPTDITHL
CCCCCCCCCCCHHHH
50.8521791702
469AcetylationTDITHLIKRKKPEDP
CCHHHHHHCCCCCCC
65.6121791702
477PhosphorylationRKKPEDPSSEAEALC
CCCCCCCCHHHHHHC
53.8019429919
478PhosphorylationKKPEDPSSEAEALCS
CCCCCCCHHHHHHCC
46.3319429919
485PhosphorylationSEAEALCSPAKRAAV
HHHHHHCCHHHHHCC
28.8321082442

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

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

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NASP_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of NASP_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS27A_DROMERpS27Aphysical
24292889

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NASP_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-32; THR-33; SER-179;SER-184; THR-185; SER-193; SER-478 AND SER-485, AND MASS SPECTROMETRY.
"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-485, AND MASSSPECTROMETRY.

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