OSA_DROME - dbPTM
OSA_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OSA_DROME
UniProt AC Q8IN94
Protein Name Trithorax group protein osa
Gene Name osa
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 2716
Subcellular Localization Nucleus .
Protein Description Trithorax group (trxG) protein required for embryonic segmentation, development of the notum and wing margin, and photoreceptor differentiation. Required for the activation of genes such as Antp, Ubx and Eve. Binds to DNA without specific affinity, suggesting that it is recruited to promoters by promoter-specific proteins. Essential component of the Brahma complex, a multiprotein complex which is the equivalent of the yeast SWI/SNF complex and acts by remodeling the chromatin by catalyzing an ATP-dependent alteration in the structure of nucleosomal DNA. This complex can both serve as a transcriptional coactivator or corepressor, depending on the context. Acts as an essential coactivator for Zeste, which recruits the whole complex to specific genes. In contrast, it acts as a corepressor for Wg target genes, possibly via an interaction with Pan and Gro. It also acts as a negative regulator for proneural achaete-scute, when it is directly recruited by Pan and Chi. Also represses E2f activation..
Protein Sequence MNEKIKSPQTQQQQQGGAPAPAATPPSAGAAPGAATPPTSGPPTPNNNSNNGSDPSIQQQQQNVAPHPYGAPPPPGSGPGGPPGPDPAAVMHYHHLHQQQQQHPPPPHMQQQQHHGGPAPPPPGGAPEHAPGVKEEYTHLPPPHPHPAYGRYHADPNMDPYRYGQPLPGGKPPQQQQPHPQQQPPQQPGPGGSPNRPPQQRYIPGQPPQGPTPTLNSLLQSSNPPPPPQHRYANTYDPQQAAASAAAAAAAQQQQAGGPPPPGHGPPPPQHQPSPYGGQQGGWAPPPRPYSPQLGPSQQYRTPPPTNTSRGQSPYPPAHGQNSGSYPSSPQQQQQQQQQQQQQAGQQPGGPVPGGPPPGTGQQPPQQNTPPTSQYSPYPQRYPTPPGLPAGGSNHRTAYSTHQYPEPNRPWPGGSSPSPGSGHPLPPASPHHVPPLQQQPPPPPHVSAGGPPPSSSPGHAPSPSPQPSQASPSPHQELIGQNSNDSSSGGAHSGMGSGPPGTPNPQQVMRPTPSPTGSSGSRSMSPAVAQNHPISRPASNQSSSGGPMQQPPVGAGGPPPMPPHPGMPGGPPQQQQSQQQQASNSASSASNSPQQTPPPAPPPNQGMNNMATPPPPPQGAAGGGYPMPPHMHGGYKMGGPGQSPGAQGYPPQQPQQYPPGNYPPRPQYPPGAYATGPPPPPTSQAGAGGANSMPSGAQAGGYPGRGMPNHTGQYPPYQWVPPSPQQTVPGGAPGGAMVGNHVQGKGTPPPPVVGGPPPPQGSGSPRPLNYLKQHLQHKGGYGGSPTPPQGPQGYGNGPTGMHPGMPMGPPHHMGPPHGPTNMGPPTSTPPQSQMLQGGQPQGQGASGGPESGGPEHISQDNGISSSGPTGAAGMHAVTSVVTTGPDGTSMDEVSQQSTLSNASAASGEDPQCTTPKSRKNDPYSQSHLAPPSTSPHPVVMHPGGGPGEEYDMSSPPNWPRPAGSPQVFNHVPVPQEPFRSTITTTKKSDSLCKLYEMDDNPDRRGWLDKLRAFMEERRTPITACPTISKQPLDLYRLYIYVKERGGFVEVTKSKTWKDIAGLLGIGASSSAAYTLRKHYTKNLLTFECHFDRGDIDPLPIIQQVEAGSKKKTAKAASVPSPGGGHLDAGTTNSTGSSNSQDSFPAPPGSAPNAAIDGYPGYPGGSPYPVASGPQPDYATAGQMQRPPSQNNPQTPHPGAAAAVAAGDNISVSNPFEDPIAAGGGPGSGTGPGPGQGPGPGAASGGAGAVGAVGGGPQPHPPPPHSPHTAAQQAAGQHQQQHPQHQHPGLPGPPPPQQQQGQQGQQPPPSVGGGPPPAPQQHGPGQVPPSPQQHVRPAAGAPYPPGGSGYPTPVSRTPGSPYPSQPGAYGQYGSSDQYNATGPPGQPFGQGPGQYPPQNRNMYPPYGPEGEAPPTGANQYGPYGSRPYSQPPPGGPQPPTQTVAGGPPAGGAPGAPPSSAYPTGRPSQQDYYQPPPDQSPQPRRHPDFIKDSQPYPGYNARPQIYGAWQSGTQQYRPQYPSSPAPQNWGGAPPRGAAPPPGAPHGPPIQQPAGVAQWDQHRYPPQQGPPPPPQQQQQPQQQQQQPPYQQVAGPPGQQPPQAPPQWAQMNPGQTAQSGIAPPGSPLRPPSGPGQQNRMPGMPAQQQQSQQQGGVPQPPPQQASHGGVPSPGLPQVGPGGMVKPPYAMPPPPSQGVGQQVGQGPPGGMMSQKPPPMPGQAMQQQPLQQQPPSHQHPHPHQHPQHQHPHQMPPNQTAPGGYGPPGMPGGGAQLVKKELIFPHDSVESTTPVLYRRKRLMKADVCPVDPWRIFMAMRSGLLTECTWALDVLNVLLFDDSTVQFFGISNLPGLLTLLLEHFQKNLAEMFDERENEEQSALLAEDADDDADSGTVMCEKLRTSGRQPRCVRSISSYNRRRHYENMDRSGKDGAGNGSDSEDADEGIDLGQVRVQPNPEERSLLLSFTPNYTMVTRKGVPVRIQPAENDIFVDERQKAWDIDTNRLYEQLEPVGSDAWTYGFTEPDPLDGIIDVFKSEIVNIPFARYIRSDKKGRKRTELASSSRKPEIKTEENSTEEQTFNKKRRLVSGGSSSSGAHAEGKKSKLTSEEFAQPNAEVKKEPGTADSDCRPVDMDIEAPQQRLTNGVAPCSSTPAIFDPRTTAKDEARVLQRRRDSSFEDECYTRDEASLHLVSESQDSLARRCIALSNIFRNLTFVPGNETVLAKSTRFLAVLGRLLLLNHEHLRRTPKTRNYDREEDTDFSDSCSSLQGEREWWWDYLITIRENMLVAMANIAGHLELSRYDELIARPLIDGLLHWAVCPSAHGQDPFPSCGPNSVLSPQRLALEALCKLCVTDANVDLVIATPPFSRLEKLCAVLTRHLCRNEDQVLREFSVNLLHYLAAADSAMARTVALQSPCISYLVAFIEQAEQTALGVANQHGINYLRENPDSMGTSLDMLRRAAGTLLHLAKHPDNRSLFMQQEQRLLGLVMSHILDQQVALIISRVLYQVSRGTGPIHSVEFRLLQQRQQQQLRPGPAGKQAASAGGSATVKAETASTETSSTEAKPAPAATTAVVNDENSNSSQQLPPAATFNDVSNSSTNSNSCGTASSNQTNNSTTNSSHSSSAISSQSAITVAAPSAAATGAGSATAAAIASDQQQVSKVAAAAAAAAALSNASAAAAAAAAAAAASVGPPTSSSVSAGAAVAQPAAPPPTNAGTTTAVA
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
193PhosphorylationQQPGPGGSPNRPPQQ
CCCCCCCCCCCCCHH
25.5623607784
382PhosphorylationYSPYPQRYPTPPGLP
CCCCCCCCCCCCCCC
13.2521082442
384PhosphorylationPYPQRYPTPPGLPAG
CCCCCCCCCCCCCCC
32.9319429919
523PhosphorylationTGSSGSRSMSPAVAQ
CCCCCCCCCCHHHHH
25.8819429919
525PhosphorylationSSGSRSMSPAVAQNH
CCCCCCCCHHHHHCC
15.7919429919
747PhosphorylationNHVQGKGTPPPPVVG
CCCCCCCCCCCCCCC
35.7919429919
762PhosphorylationGPPPPQGSGSPRPLN
CCCCCCCCCCCCHHH
30.7419429919
764PhosphorylationPPPQGSGSPRPLNYL
CCCCCCCCCCHHHHH
21.3119429919
770PhosphorylationGSPRPLNYLKQHLQH
CCCCHHHHHHHHHHH
23.9819429919
964PhosphorylationNWPRPAGSPQVFNHV
CCCCCCCCCCCCCCC
17.7922817900
1478PhosphorylationYQPPPDQSPQPRRHP
CCCCCCCCCCCCCCC
32.6519429919
1905PhosphorylationRQPRCVRSISSYNRR
CCCCCCHHHHHHCHH
13.3625749252
1907PhosphorylationPRCVRSISSYNRRRH
CCCCHHHHHHCHHHH
28.1922817900
1921PhosphorylationHYENMDRSGKDGAGN
HHHHCCCCCCCCCCC
46.0323607784
1930PhosphorylationKDGAGNGSDSEDADE
CCCCCCCCCCCCCCC
41.8019429919
1932PhosphorylationGAGNGSDSEDADEGI
CCCCCCCCCCCCCCC
38.7919429919
2067PhosphorylationEIKTEENSTEEQTFN
CCCCCCCCCCHHHHH
40.2427794539
2081PhosphorylationNKKRRLVSGGSSSSG
HHCCCEECCCCCCCC
41.8719429919
2084PhosphorylationRRLVSGGSSSSGAHA
CCEECCCCCCCCCCC
30.4927626673
2085PhosphorylationRLVSGGSSSSGAHAE
CEECCCCCCCCCCCC
31.6229892262
2086PhosphorylationLVSGGSSSSGAHAEG
EECCCCCCCCCCCCC
34.1925749252
2087PhosphorylationVSGGSSSSGAHAEGK
ECCCCCCCCCCCCCC
41.7827626673
2143PhosphorylationTNGVAPCSSTPAIFD
CCCCCCCCCCCCCCC
35.8721082442
2168PhosphorylationVLQRRRDSSFEDECY
HHHHHHHCCCCCCEE
34.8119429919
2169PhosphorylationLQRRRDSSFEDECYT
HHHHHHCCCCCCEEC
36.6219429919
2176PhosphorylationSFEDECYTRDEASLH
CCCCCEECCCHHHHH
43.2118327897
2181PhosphorylationCYTRDEASLHLVSES
EECCCHHHHHHCCCC
17.8018327897

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 OSA_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OSA_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 OSA_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BRM_DROMEbrmphysical
15060132
OSA_DROMEosaphysical
15060132
BRM_DROMEbrmgenetic
10601025
BRM_DROMEbrmgenetic
12466201
CORTO_DROMEcortogenetic
11810228
MED18_DROMEMED18physical
22036573
ZEST_DROMEzphysical
10809665
ACT1_DROMEAct5Cphysical
10601025
DSH_DROMEdshphysical
22036573
BAP60_DROMEBap60physical
10601025
SCAL_DROMEsdphysical
24137538
MED23_DROMEMED23physical
22036573
MED14_DROMEMED14physical
22036573
Y1505_DROMECG11505physical
22036573
CPSF6_DROMECG7185physical
22036573
CDK8_DROMECdk8physical
22036573
BRM_DROMEbrmphysical
10601025
BRM_DROMEbrmphysical
23136390
SUHW_DROMEsu(Hw)physical
23609538
MED17_DROMEMED17physical
22036573

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OSA_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 THR-384; THR-747; SER-1930;SER-1932; SER-2081; SER-2168; SER-2169; THR-2176 AND SER-2181, ANDMASS SPECTROMETRY.

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