INO80_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: INO80_DROME
• UniProt AC: Q9VDY1
• Protein Name: Chromatin-remodeling ATPase INO80 {ECO:0000305}
• Gene Name: Ino80 {ECO:0000303|PubMed:16618800, ECO:0000312|FlyBase:FBgn0086613}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 1638
• Subcellular Localization: Nucleus .
• Protein Description: ATPase component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and DNA repair. Binds DNA. As part of the INO80 complex, remodels chromatin by shifting nucleosomes..
• Protein Sequence: MEAKPVPAPQPRPRAMAEPLHIQRLEAALNMRPFMNMAKRSLRKPLSSDEETDDEHVVKREHDVQDSDDSSTVGVVRMKQSSKRKSRLLASKEERQSVKAQLYNFNDLTSDREWLYDLLLSDTESDDPTITEDEYVQQLLREHVREQRQRKNYYKKAANAQYAYYGSGLLSNHDIFAERQLATAGVRKRRRRTKQEILMARLAEAQAGPKPPKQRRRGRKKRDNMGSPESGEVPPSELGKYTFGDTLPNNEDDDEDGGEVDYKRELASLALDYPEEEEIEEEVDVEGGTEGQVTKVRRKRKNPAALAARRRRIWQIMSKKESGRLQRIKSNNHKEMLANCKRVAGMCAKVVRQRAINSQRIMKETVWRAKRLTREMLAYWKRYERVERDQRRKQEREAEEQRKQDVELIEVKRQQRKLNFLITQTELYAHFMSKKLGQGSEEDQLRILSQLDEETNARLAAQDDYDAGEMKLLAQENAEAAMQRDLDKTRAFDVFAKKKEKEEEEQAQESVEDIKPEPRPEMKDLPQPKMFKGTLKGYQIKGMTWLANIYDQGISGILADEMGLGKTVQSIAFLCHIAEHYGVWGPFLVISPASTLHNWQQEMSRFVPDFKVVPYWGSPAERKILRQFWDQKHLHTRDASFHVVITSYQLVVSDYKYFNRIKWQYMVLDEAQAIKSAASQRWKLLLGFSCRNRLLLSGTPIQNSMAELWALLHFIMPTLFDSHDEFNEWFSKDIESHAENKTGIDEKQISRLHMILKPFMLRRIKKDVENELSDKIEIMVYCPLTIRQKLLYRALKQKIRIEDLLHLTSGSTTTSSSSSASNLMNLVMQFRKVCNHPELFERRDARSPFFMRCAEYTIPRLIHEEGLIHRMLPSRKHLLYNRFNIFKSEYIQRSLFEDVNVNSCFGFTRLCDLSVGDMVEVTLNGLIDFLLHYRRVLEKYPLLAYRRFWWKKQPDSRYQLLEPMLENKLALDYMPPNSVLKNFIFTAMTANESSVYAFGDYFTYNMQETIEHRVIRSKILKKKTSLIEEMEDVSKQKLEIESVEVQTKSNAKSDVKVTTLLLLPEFPHRPRKPRKYVCEPLSMPRILYDLGQKVQAVHRYLYCDSRSAAWSQIRHNQCENSQGRELVSSGLALCKPHGGWSSIVVPDKETLITDAGKLFVLDNLLTRLKANGHRVLIYSQMTKMIDLLEEYMWHRKHRYMRLDGSSKISARRDMVADFQTRADIFVFLLSTRAGGLGINLTAADTVIFYDSDWNPTVDQQAMDRAHRLGQTKQVTVYRLICKGTIEERILQRAREKSEIQRMVISGGNFKPDTLKPKEVVSLLLDDEEIEMKYRQEAKLQSSSPIPAATQSERKRRHPQKDVNMGGTTIAATSATQNPDDDVPSCSSAAKRIKLETEEDFIDVGITSSASSVGTDSNHPTLSQETYVPGATCVQQTEIDSENEALVVDGDSPTMLGQNESMNFLDDLSGISPMRRRHHPRGTRRGRPRGSTRRGGGHGSIPRVLTPTQAATPAVPATASQAAAAGTGAAAGTSSPLPQQEVSGGGDNAGVPLHEEEYRTSPSGQSPGVSCKRGPGRPRSKTATPISRGTRGAPRARRPMGPLLVPLGRSPDDTPPSSSPATSRAPSPLSGSHGAVGPE

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
47	Phosphorylation	RSLRKPLSSDEETDD HHHCCCCCCCCCCCC	44.25	19429919
48	Phosphorylation	SLRKPLSSDEETDDE HHCCCCCCCCCCCCC	57.64	19429919
52	Phosphorylation	PLSSDEETDDEHVVK CCCCCCCCCCCHHHC	46.86	19429919
67	Phosphorylation	REHDVQDSDDSSTVG CHHCCCCCCCCCCEE	26.65	19429919
70	Phosphorylation	DVQDSDDSSTVGVVR CCCCCCCCCCEEEEE	32.66	19429919
71	Phosphorylation	VQDSDDSSTVGVVRM CCCCCCCCCEEEEEE	33.82	19429919
72	Phosphorylation	QDSDDSSTVGVVRMK CCCCCCCCEEEEEEC	25.82	19429919
227	Phosphorylation	KKRDNMGSPESGEVP CCCCCCCCCCCCCCC	18.09	22817900
230	Phosphorylation	DNMGSPESGEVPPSE CCCCCCCCCCCCHHH	43.57	22817900
497	Acetylation	RAFDVFAKKKEKEEE HHHHHHHHHHHHHHH	53.57	21791702
1343	Phosphorylation	EAKLQSSSPIPAATQ HHHHCCCCCCCCCCH	31.90	19060867
1351	Phosphorylation	PIPAATQSERKRRHP CCCCCCHHHHHHHCC	34.71	25749252

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

Oops, there are no upstream regulatory protein records of INO80_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of INO80_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 INO80_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PHO_DROME	pho	physical	16618800
FTZF1_DROME	ftz-f1	genetic	24468295

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-47; SER-48; THR-52;SER-67; SER-70; SER-227 AND SER-230, AND MASS SPECTROMETRY.
PubMed: 18327897