CPD1_DROME - dbPTM
CPD1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPD1_DROME
UniProt AC P22058
Protein Name Chromosomal protein D1
Gene Name D1
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 355
Subcellular Localization Nucleus. Chromosome.
Protein Description This satellite DNA-associated protein is a double-stranded DNA binding protein specific for tracts of pure at DNA. It may play a role in organizing the higher-order structure of euchromatin as well as heterochromatin..
Protein Sequence MEEVAVKKRGRPSKASVGGKSSTAAVAAISPGIKKRGRPAKNKGSSGGGGQRGRPPKASKIQNDEDPEDEGEEDGDGDGSGAELANNSSPSPTKGRGRPKSSGGAGSGSGDSVKTPGSAKKRKAGRPKKHQPSDSENEDDQDEDDDGNSSIEERRPVGRPSAGSVNLNISRTGRGLGRPKKRAVESNGDGEPQVPKKRGRPPQNKSGSGGSTGYVPTGRPRGRPKANAAPVEKHEDNDDDQDDENSGEEEHSSPEKTVVAPKKRGRPSLAAGKVSKEETTKPRSRPAKNIDDDADDADSADQGQHNSKKESNDEDRAVDGTPTKGDGLKWNSDGENDANDGYVSDNYNDSESVAA
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
1Acetylation-------MEEVAVKK
-------CCCCCCCC		10.012542275
13PhosphorylationVKKRGRPSKASVGGK
CCCCCCCCCCCCCCH		39.2225749252
16PhosphorylationRGRPSKASVGGKSST
CCCCCCCCCCCHHHH		25.6525749252
21PhosphorylationKASVGGKSSTAAVAA
CCCCCCHHHHHHHHH		35.8721082442
22PhosphorylationASVGGKSSTAAVAAI
CCCCCHHHHHHHHHH		26.0821082442
30PhosphorylationTAAVAAISPGIKKRG
HHHHHHHCCCHHHCC		16.6121082442
46PhosphorylationPAKNKGSSGGGGQRG
CCCCCCCCCCCCCCC		50.5630478224
80PhosphorylationEDGDGDGSGAELANN
CCCCCCCCCHHHCCC		39.3021082442
88PhosphorylationGAELANNSSPSPTKG
CHHHCCCCCCCCCCC		43.3523607784
89PhosphorylationAELANNSSPSPTKGR
HHHCCCCCCCCCCCC		31.3623607784
91PhosphorylationLANNSSPSPTKGRGR
HCCCCCCCCCCCCCC		47.3423607784
93PhosphorylationNNSSPSPTKGRGRPK
CCCCCCCCCCCCCCC		50.9322668510
101PhosphorylationKGRGRPKSSGGAGSG
CCCCCCCCCCCCCCC		36.5829892262
102PhosphorylationGRGRPKSSGGAGSGS
CCCCCCCCCCCCCCC		47.5829892262
107PhosphorylationKSSGGAGSGSGDSVK
CCCCCCCCCCCCCCC		29.2925749252
109PhosphorylationSGGAGSGSGDSVKTP
CCCCCCCCCCCCCCC		40.9225749252
112PhosphorylationAGSGSGDSVKTPGSA
CCCCCCCCCCCCCCH		29.1022817900
115PhosphorylationGSGDSVKTPGSAKKR
CCCCCCCCCCCHHCC		30.6325749252
118PhosphorylationDSVKTPGSAKKRKAG
CCCCCCCCHHCCCCC		37.8125749252
133PhosphorylationRPKKHQPSDSENEDD
CCCCCCCCCCCCCCC		47.3919429919
135PhosphorylationKKHQPSDSENEDDQD
CCCCCCCCCCCCCCC		46.8119429919
149PhosphorylationDEDDDGNSSIEERRP
CCCCCCCCCHHHHCC		37.9219429919
150PhosphorylationEDDDGNSSIEERRPV
CCCCCCCCHHHHCCC		37.7119429919
161PhosphorylationRRPVGRPSAGSVNLN
HCCCCCCCCCCEEEE		43.8519429919
164PhosphorylationVGRPSAGSVNLNISR
CCCCCCCCEEEECCC		13.9319429919
170PhosphorylationGSVNLNISRTGRGLG
CCEEEECCCCCCCCC		23.7919429919
186PhosphorylationPKKRAVESNGDGEPQ
CCCHHHHCCCCCCCC		39.2419429919
208PhosphorylationPPQNKSGSGGSTGYV
CCCCCCCCCCCCCCC		47.2518327897
212PhosphorylationKSGSGGSTGYVPTGR
CCCCCCCCCCCCCCC		35.4927626673
246PhosphorylationDDQDDENSGEEEHSS
CCCCCCCCCCCCCCC		45.6021082442
252PhosphorylationNSGEEEHSSPEKTVV
CCCCCCCCCCCCEEE		51.3619429919
253PhosphorylationSGEEEHSSPEKTVVA
CCCCCCCCCCCEEEC		38.7019429919
257PhosphorylationEHSSPEKTVVAPKKR
CCCCCCCEEECCCCC		20.6723607784
268PhosphorylationPKKRGRPSLAAGKVS
CCCCCCCCCCCCCCC		29.3119429919
288AcetylationKPRSRPAKNIDDDAD
CCCCCCCCCCCCCCC		58.0621791702
299PhosphorylationDDADDADSADQGQHN
CCCCCCCCCHHHHHC		35.1521082442
307PhosphorylationADQGQHNSKKESNDE
CHHHHHCCCCCCCCC		42.8719429919
308AcetylationDQGQHNSKKESNDED
HHHHHCCCCCCCCCC		66.9121791702
311PhosphorylationQHNSKKESNDEDRAV
HHCCCCCCCCCCCCC		59.4619429919
321PhosphorylationEDRAVDGTPTKGDGL
CCCCCCCCCCCCCCC		24.2621082442
323PhosphorylationRAVDGTPTKGDGLKW
CCCCCCCCCCCCCCC		47.7119429919
332PhosphorylationGDGLKWNSDGENDAN
CCCCCCCCCCCCCCC		45.9719429919
342PhosphorylationENDANDGYVSDNYND
CCCCCCCCCCCCCCC		10.3119429919
344PhosphorylationDANDGYVSDNYNDSE
CCCCCCCCCCCCCCC		16.2019429919
347PhosphorylationDGYVSDNYNDSESVA
CCCCCCCCCCCCCCC		25.9019429919
350PhosphorylationVSDNYNDSESVAA--
CCCCCCCCCCCCC--		28.2919429919
352PhosphorylationDNYNDSESVAA----
CCCCCCCCCCC----		22.4719429919
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
133SPhosphorylationKinaseCK2-Uniprot
135SPhosphorylationKinaseCK2-Uniprot
186SPhosphorylationKinaseCK2-Uniprot
311SPhosphorylationKinaseCK2-Uniprot
332SPhosphorylationKinaseCK2-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPD1_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 CPD1_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CPD1_DROME !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CPD1_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 SER-80; SER-88; SER-89;SER-107; SER-109; SER-112; THR-115; SER-118; SER-133; SER-135;SER-149; SER-150; SER-161; SER-164; SER-170; SER-208; SER-246;SER-252; SER-253; SER-299; SER-307; SER-311; THR-321 AND SER-332, ANDMASS 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-30 AND SER-246, AND MASSSPECTROMETRY.

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