dbPTM

MODU_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MODU_DROME
UniProt AC	P13469
Protein Name	DNA-binding protein modulo
Gene Name	mod
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	542
Subcellular Localization	Nucleus.
Protein Description	Its capacity to bind DNA and protein(s), and its differential expression during development suggest a role in the regulation of gene expression during Drosophila development. It could, in interaction with other factors, be required for the translation of instructions provided by pattern forming genes and controls, via chromatin changes, the activity of genes critical for the process of morphogenesis of several embryonic territories..
Protein Sequence	MAQKKAVTVKGKKATNGEEKPLAKRVTKSTKVQEEETVVPQSPSKKSRKQPVKEVPQFSEEDESDVEEQNDEQPGDDSDFETEEAAGLIDDEAEEDEEYNSDDEEDDDDDELEPGEVSKSEGADEVDESDDDEEAPVEKPVSKKSEKANSEKSEENRGIPKVKVGKIPLGTPKNQIVFVTNLPNEYLHKDLVALFAKFGRLSALQRFTNLNGNKSVLIAFDTSTGAEAVLQAKPKALTLGDNVLSVSQPRNKEENNERTVVVGLIGPNITKDDLKTFFEKVAPVEAVTISSNRLMPRAFVRLASVDDIPKALKLHSTELFSRFITVRRISQESISRTSELTLVVENVGKHESYSSDALEKIFKKFGDVEEIDVVCSKAVLAFVTFKQSDAATKALAQLDGKTVNKFEWKLHRFERSTSGRAILVTNLTSDATEADLRKVFNDSGEIESIIMLGQKAVVKFKDDEGFCKSFLANESIVNNAPIFIEPNSLLKHRLLKKRLAIGQTRAPRKFQKDTKPNFGKKPFNKRPAQENGGKSFVKRARF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
20	Acetylation	KATNGEEKPLAKRVT ECCCCCCCCHHHHHC	40.82	21791702
27	Phosphorylation	KPLAKRVTKSTKVQE CCHHHHHCCCCCCCC	24.26	22817900
42	Phosphorylation	EETVVPQSPSKKSRK CCCCCCCCCCCCCCC	25.68	21082442
44	Phosphorylation	TVVPQSPSKKSRKQP CCCCCCCCCCCCCCC	58.94	21082442
101	Phosphorylation	EEDEEYNSDDEEDDD HHCHHCCCCCCCCCC	45.60	22817900
120	Phosphorylation	EPGEVSKSEGADEVD CCCCCCCCCCCCCCC	33.48	19429919
129	Phosphorylation	GADEVDESDDDEEAP CCCCCCCCCCCCCCC	41.71	21082442
142	Phosphorylation	APVEKPVSKKSEKAN CCCCCCCCHHHHHHH	42.78	22817900
150	Phosphorylation	KKSEKANSEKSEENR HHHHHHHHHHCHHHC	51.79	19429919
153	Phosphorylation	EKANSEKSEENRGIP HHHHHHHCHHHCCCC	46.20	19429919
275	Acetylation	NITKDDLKTFFEKVA CCCHHHHHHHHHHHC	50.73	21791702
304	Phosphorylation	RAFVRLASVDDIPKA CEEEEHHCHHHHHHH	30.58	21082442
330	Phosphorylation	FITVRRISQESISRT HHHHEECCHHHHCCC	26.53	-
360	Acetylation	YSSDALEKIFKKFGD CCHHHHHHHHHHHCC	55.05	21791702
364	Acetylation	ALEKIFKKFGDVEEI HHHHHHHHHCCHHHH	43.78	21791702
405	Acetylation	LDGKTVNKFEWKLHR HCCCEECEEHHEEEE	40.08	21791702
409	Acetylation	TVNKFEWKLHRFERS EECEEHHEEEEEECC	27.50	21791702
443	Phosphorylation	LRKVFNDSGEIESII HHHHHCCCCHHEEEE	39.16	22817900
515	Acetylation	RKFQKDTKPNFGKKP HHCCCCCCCCCCCCC	48.36	21791702
520	Acetylation	DTKPNFGKKPFNKRP CCCCCCCCCCCCCCC	53.81	21791702
534	Acetylation	PAQENGGKSFVKRAR CCHHCCCCCCHHHCC	41.96	21791702

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
330	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MODU_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 MODU_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
MPIP_DROME	stg	genetic	12834864

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MODU_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-42; SER-44; SER-120;SER-129; SER-142 AND SER-443, AND MASS SPECTROMETRY.	18327897 [Abstract]
"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-42; SER-44; SER-129 ANDSER-304, AND MASS SPECTROMETRY.	17372656 [Abstract]