dbPTM

Y9776_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	Y9776_DROME
UniProt AC	Q9V468
Protein Name	Zinc finger matrin-type protein CG9776
Gene Name	CG9776
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	1260
Subcellular Localization	Nucleus.
Protein Description
Protein Sequence	MDEDSATIQLGDRRLGNAVDHDLLPGPPGVDEKSGNENCEPRSSGSGKRGKSNSRRRSTSRGRSDSRNTSPSNTRRRHSLSRSLTPPRRRYDSPDYGRYSRRRFDRDRRRSPERRRSPPRRGRRYGRSRSRSMSPRRGGRWSPKKKPSSPPVPPPHGGPHPQMTPGYGAMAAHIYGSYVAPPDVYGHQYGIPPNSFPPQGPGYGIPGAPPDQSSFGSGYGPPPTSAWDVNVYGQQVWINQPISGVQPSASDSLIQPQKARETLSGKTIGEEQSVPALEGAGLTPQDAVAQEAEKQKDELKKQRANYVKKVSLLKKEMKVLKDQREDLAAGDAPPSPTTKNFIEENDRLQMQIKKKLDTIENVIDMLNGIIGYEEVEDEPSNQKSHGKTQPEQQDSRSHSSSESSADSSESSSSSSTASDSSSDNEDGEGAGGAVGSPTNRLKHRAIKSMKSKQLHGEMKAVPTQAQNYNFVFFDPEQHWCESCGVFPKSARDYLKHLHAEEHMNRETIETPWHVGIDHDPFPTFENAPARRVPVRGMQFLVPANAWFCKLCSVWIGDLHCASAHLKSRLHSNKYQQFLNQNPNYEIEWQTNRERAMNQQKDHDDAKNKKSKKDEDKASKKRKKKGGDKKKKKRKHGKKSKRSTIDANSTSSSSDSSSSEEENGQQPKKGRTEQQPICQSDKSTNAASIRVAMRKQESTPTNLKPEVPCQPVVPPPPPIIKDSTIPSERGKWTAASVEDQSKDQKNRDDTMLKQWNNVQPVISESEKKLLEQLKGRLKNKGARDQNNHKAVPTEANDEKFRRGGGRHSRSRSKRRSYSRSISRGRDRDRRDRERDRDRGRRRRSRSRGRHFSRSPIRSSRRSRSRQGRSRRSRSRSIERVERPVVKHSEFRPRTVPERKQTDIKRDKKDAESKSKSSKPSNNSLPGGKKLPFIGKMPVFKKQSVPSFNYDASAVYTNGCLEAPPPPPPPLGGATSQIAVRQQAPTAAQIQMAMMEDAFGNAPPFHPDAGMMVDYDELMPDPVQFANLMTSCPPPPPPGEGSEGDAHGPEDGDQHDNENREDVLPPGIDEAESALVPHPLDAAAQSRDGELPKDLVEALDIIFPSDVAILEASNGNSEKQEDVTITTIVEDDAVLSVIHLQDLAKEGIHLVTINEAEVPKKSHIQTSEKIEKLQDLNGKSDDGVNIKLIDAEDIPMPNSPPAEPSFDEETKSKALQKQADISEIPEPAVSPSDSEKLRRQSELDELAMLGIDRSDMAAQYAL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
34	Phosphorylation	PPGVDEKSGNENCEP CCCCCCCCCCCCCCC	44.82	22817900
64	Phosphorylation	RSTSRGRSDSRNTSP CCCCCCCCCCCCCCC	42.64	25749252
66	Phosphorylation	TSRGRSDSRNTSPSN CCCCCCCCCCCCCCH	28.77	30478224
70	Phosphorylation	RSDSRNTSPSNTRRR CCCCCCCCCCHHHHH	29.85	29892262
74	Phosphorylation	RNTSPSNTRRRHSLS CCCCCCHHHHHHHHC	29.86	27626673
79	Phosphorylation	SNTRRRHSLSRSLTP CHHHHHHHHCCCCCC	26.65	19429919
81	Phosphorylation	TRRRHSLSRSLTPPR HHHHHHHCCCCCCCC	23.88	19429919
83	Phosphorylation	RRHSLSRSLTPPRRR HHHHHCCCCCCCCCC	32.97	19429919
85	Phosphorylation	HSLSRSLTPPRRRYD HHHCCCCCCCCCCCC	32.28	19429919
93	Phosphorylation	PPRRRYDSPDYGRYS CCCCCCCCCCCCHHH	15.67	19429919
96	Phosphorylation	RRYDSPDYGRYSRRR CCCCCCCCCHHHHHC	13.59	27626673
111	Phosphorylation	FDRDRRRSPERRRSP CCHHHCCCCCHHCCC	29.33	25749252
128	Phosphorylation	RGRRYGRSRSRSMSP CHHCCCCCCCCCCCC	30.19	19429919
130	Phosphorylation	RRYGRSRSRSMSPRR HCCCCCCCCCCCCCC	29.92	19429919
132	Phosphorylation	YGRSRSRSMSPRRGG CCCCCCCCCCCCCCC	25.51	19429919
134	Phosphorylation	RSRSRSMSPRRGGRW CCCCCCCCCCCCCCC	19.26	19429919
142	Phosphorylation	PRRGGRWSPKKKPSS CCCCCCCCCCCCCCC	26.02	27626673
262	Phosphorylation	QPQKARETLSGKTIG CHHHHHHHHCCCCCC	22.22	22817900
311	Phosphorylation	ANYVKKVSLLKKEMK HHHHHHHHHHHHHHH	36.54	27626673
335	Phosphorylation	AAGDAPPSPTTKNFI HCCCCCCCCCHHHHH	33.54	19429919
337	Phosphorylation	GDAPPSPTTKNFIEE CCCCCCCCHHHHHHH	55.53	19429919
338	Phosphorylation	DAPPSPTTKNFIEEN CCCCCCCHHHHHHHC	27.63	19429919
697	Phosphorylation	VAMRKQESTPTNLKP HHHHCCCCCCCCCCC	36.87	23607784
698	Phosphorylation	AMRKQESTPTNLKPE HHHCCCCCCCCCCCC	33.12	23607784
700	Phosphorylation	RKQESTPTNLKPEVP HCCCCCCCCCCCCCC	53.95	23607784
730	Acetylation	TIPSERGKWTAASVE CCCCCCCCCEECCHH	47.82	21791702
816	Phosphorylation	SRSKRRSYSRSISRG CHHHCCCHHHHHHCC	13.29	25749252
851	Phosphorylation	RSRGRHFSRSPIRSS HHCCCCCCCCCCCCC	26.23	19429919
853	Phosphorylation	RGRHFSRSPIRSSRR CCCCCCCCCCCCCHH	24.39	19429919
871	Phosphorylation	RQGRSRRSRSRSIER HHCCHHHHHHHHHHH	33.23	22668510
873	Phosphorylation	GRSRRSRSRSIERVE CCHHHHHHHHHHHCC	31.46	22668510
875	Phosphorylation	SRRSRSRSIERVERP HHHHHHHHHHHCCCC	30.01	22668510
927	Acetylation	NNSLPGGKKLPFIGK CCCCCCCCCCCCCCC	57.99	21791702
1167	Acetylation	SHIQTSEKIEKLQDL CCCCCHHHHHHHHHH	56.80	21791702
1177	Acetylation	KLQDLNGKSDDGVNI HHHHHCCCCCCCCEE	50.03	21791702
1178	Phosphorylation	LQDLNGKSDDGVNIK HHHHCCCCCCCCEEE	42.19	22668510
1197	Phosphorylation	EDIPMPNSPPAEPSF HHCCCCCCCCCCCCC	26.79	19429919
1203	Phosphorylation	NSPPAEPSFDEETKS CCCCCCCCCCHHHHH	36.51	22668510
1228	Phosphorylation	EIPEPAVSPSDSEKL HCCCCCCCCCHHHHH	22.31	21082442
1230	Phosphorylation	PEPAVSPSDSEKLRR CCCCCCCCHHHHHHH	46.38	19429919
1232	Phosphorylation	PAVSPSDSEKLRRQS CCCCCCHHHHHHHHH	40.75	21082442
1239	Phosphorylation	SEKLRRQSELDELAM HHHHHHHHHHHHHHH	38.01	19429919

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 Y9776_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of Y9776_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 Y9776_DROME !!

Protein-Protein Interaction

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

Drug and Disease Associations

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

Regulatory Network of Y9776_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-697; THR-700; SER-1228AND SER-1232, 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-335; THR-338 ANDSER-1197, AND MASS SPECTROMETRY.	17372656 [Abstract]