MMD4_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MMD4_DROME
• UniProt AC: Q86B87
• Protein Name: Modifier of mdg4
• Gene Name: mod(mdg4) {ECO:0000312|FlyBase:FBgn0002781}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 610
• Subcellular Localization: Nucleus . Chromosome . Colocalizes with other elements of the gypsy chromatin insulator complex at multiple sites on polytene chromosomes and at nuclear insulator bodies (PubMed:9491892, PubMed:11106742, PubMed:11350941, PubMed:15574329, PubMed:16209
• Protein Description: Component of the gypsy chromatin insulator complex which is required for the function of the gypsy chromatin insulator and other endogenous chromatin insulators. Chromatin insulators are regulatory elements which establish independent domains of transcriptional activity within eukaryotic genomes. Insulators have two defining properties; they can block the communication between an enhancer and a promoter when placed between them and can also buffer transgenes from position effect variegation (PEV). Insulators are proposed to structure the chromatin fiber into independent domains of differing transcriptional potential by promoting the formation of distinct chromatin loops. This chromatin looping may involve the formation of insulator bodies, where homotypic interactions between individual subunits of the insulator complex could promote the clustering of widely spaced insulators at the nuclear periphery. Within the gypsy insulator complex, this protein may control the nature of the repressive effect of su(Hw): in the absence of mod(mdg4) protein, su(Hw) exerts a bidirectional silencing effect, whereas in the presence of mod(mdg4), the silencing effect is unidirectional. Isoform H is specifically required to maintain the pairing of achiasmate homologs in male meiosis I which is mediated by the rDNA repeats on the achiasmate X-Y bivalents. Isoform H also plays a role in apoptotic regulatory pathways..
• Protein Sequence: MADDEQFSLCWNNFNTNLSAGFHESLCRGDLVDVSLAAEGQIVKAHRLVLSVCSPFFRKMFTQMPSNTHAIVFLNNVSHSALKDLIQFMYCGEVNVKQDALPAFISTAESLQIKGLTDNDPAPQPPQESSPPPAAPHVQQQQIPAQRVQRQQPRASARYKIETVDDGLGDEKQSTTQIVIQTTAAPQATIVQQQQPQQAAQQIQSQQLQTGTTTTATLVSTNKRSAQRSSLTPASSSAGVKRSKTSTSANVMDPLDSTTETGATTTAQLVPQQITVQTSVVSAAEAKLHQQSPQQVRQEEAEYIDLPMELPTKSEPDYSEDHGDAAGDAEGTYVEDDTYGDMRYDDSYFTENEDAGNQTAANTSGGGVTATTSKAVVKQQSQNYSESSFVDTSGDQGNTEAQAATSASATKIPPRKRGRPKTKVEDQTPKPKLLEKLQAATLNEEASEPAVYASTTKGGVKLIFNGHLFKFSFRKADYSVFQCCYREHGEECKVRVVCDQKRVFPYEGEHVHFMQASDKSCLPSQFMPGESGVISSLSPSKELLMKNTTKLEEADDKEDEDFEEFEIQEIDEIELDEPEKTPAKEEEVDPNDFREKIKRRLQKALQNKKK

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
129	Phosphorylation	APQPPQESSPPPAAP CCCCCCCCCCCCCCC	42.78	19429919
130	Phosphorylation	PQPPQESSPPPAAPH CCCCCCCCCCCCCCC	40.45	19429919
160	Acetylation	PRASARYKIETVDDG CCHHHEEEEEECCCC	28.63	21791702
225	Phosphorylation	LVSTNKRSAQRSSLT EEECCCCHHCHHCCC	30.29	27626673
229	Phosphorylation	NKRSAQRSSLTPASS CCCHHCHHCCCCCCC	20.02	21082442
230	Phosphorylation	KRSAQRSSLTPASSS CCHHCHHCCCCCCCC	38.15	9111355
292	Phosphorylation	EAKLHQQSPQQVRQE HHHHHCCCHHHHHHH	20.36	19429919
303	Phosphorylation	VRQEEAEYIDLPMEL HHHHHHHHCCCCCCC	13.54	23607784
314	Phosphorylation	PMELPTKSEPDYSED CCCCCCCCCCCCCCC	57.76	19429919
318	Phosphorylation	PTKSEPDYSEDHGDA CCCCCCCCCCCCCCC	25.36	19429919
319	Phosphorylation	TKSEPDYSEDHGDAA CCCCCCCCCCCCCCC	43.88	19429919
350	Phosphorylation	RYDDSYFTENEDAGN CCCCCCCCCCCCCCC	29.66	22668510
363	Phosphorylation	GNQTAANTSGGGVTA CCCCCCCCCCCCEEE	24.83	29892262
364	Phosphorylation	NQTAANTSGGGVTAT CCCCCCCCCCCEEEE	34.94	29892262
428	Phosphorylation	KTKVEDQTPKPKLLE CCCCCCCCCCHHHHH	45.67	21082442
538	Phosphorylation	SGVISSLSPSKELLM CCCCCCCCCCHHHHH	29.13	23607784
540	Phosphorylation	VISSLSPSKELLMKN CCCCCCCCHHHHHHC	35.07	23607784

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

Oops, there are no upstream regulatory protein records of MMD4_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MMD4_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 MMD4_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FLNA_DROME	cher	physical	14605208
ATPK_DROME	CG4692	physical	14605208
NPC2_DROME	Npc2a	physical	14605208
SRC64_DROME	Src64B	physical	14605208
ESM7_DROME	E(spl)m7-HLH	physical	14605208
MGN_DROME	mago	physical	14605208
TRX_DROME	trx	genetic	9491892
TRX_DROME	trx	genetic	10790390
SUHW_DROME	su(Hw)	genetic	8852842
GAGA_DROME	Trl	physical	15574329
ZEST_DROME	z	physical	23861668
FSH_DROME	fs(1)h	physical	23945939
TOP2_DROME	Top2	physical	21304601
TOPRS_DROME	Topors	physical	16209949
ACPM_DROME	mtacp1	physical	27025476
SHEP_DROME	shep	physical	23209434
SUHW_DROME	su(Hw)	physical	23209434
SUHW_DROME	su(Hw)	physical	23861668
SUHW_DROME	su(Hw)	physical	7664338
SUHW_DROME	su(Hw)	physical	11350941
SUHW_DROME	su(Hw)	physical	16209949
SUHW_DROME	su(Hw)	physical	18369369
CP190_DROME	Cp190	physical	15574329
CP190_DROME	Cp190	physical	27599504
MMD4_DROME	mod(mdg4)	physical	11350941
MMD4_DROME	mod(mdg4)	physical	18369369
MMD4_DROME	mod(mdg4)	physical	27599504

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 SER-230, AND MASSSPECTROMETRY.
PubMed: 18327897