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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
193 | Phosphorylation | QQPGPGGSPNRPPQQ CCCCCCCCCCCCCHH | 25.56 | 23607784 | |
382 | Phosphorylation | YSPYPQRYPTPPGLP CCCCCCCCCCCCCCC | 13.25 | 21082442 | |
384 | Phosphorylation | PYPQRYPTPPGLPAG CCCCCCCCCCCCCCC | 32.93 | 19429919 | |
523 | Phosphorylation | TGSSGSRSMSPAVAQ CCCCCCCCCCHHHHH | 25.88 | 19429919 | |
525 | Phosphorylation | SSGSRSMSPAVAQNH CCCCCCCCHHHHHCC | 15.79 | 19429919 | |
747 | Phosphorylation | NHVQGKGTPPPPVVG CCCCCCCCCCCCCCC | 35.79 | 19429919 | |
762 | Phosphorylation | GPPPPQGSGSPRPLN CCCCCCCCCCCCHHH | 30.74 | 19429919 | |
764 | Phosphorylation | PPPQGSGSPRPLNYL CCCCCCCCCCHHHHH | 21.31 | 19429919 | |
770 | Phosphorylation | GSPRPLNYLKQHLQH CCCCHHHHHHHHHHH | 23.98 | 19429919 | |
964 | Phosphorylation | NWPRPAGSPQVFNHV CCCCCCCCCCCCCCC | 17.79 | 22817900 | |
1478 | Phosphorylation | YQPPPDQSPQPRRHP CCCCCCCCCCCCCCC | 32.65 | 19429919 | |
1905 | Phosphorylation | RQPRCVRSISSYNRR CCCCCCHHHHHHCHH | 13.36 | 25749252 | |
1907 | Phosphorylation | PRCVRSISSYNRRRH CCCCHHHHHHCHHHH | 28.19 | 22817900 | |
1921 | Phosphorylation | HYENMDRSGKDGAGN HHHHCCCCCCCCCCC | 46.03 | 23607784 | |
1930 | Phosphorylation | KDGAGNGSDSEDADE CCCCCCCCCCCCCCC | 41.80 | 19429919 | |
1932 | Phosphorylation | GAGNGSDSEDADEGI CCCCCCCCCCCCCCC | 38.79 | 19429919 | |
2067 | Phosphorylation | EIKTEENSTEEQTFN CCCCCCCCCCHHHHH | 40.24 | 27794539 | |
2081 | Phosphorylation | NKKRRLVSGGSSSSG HHCCCEECCCCCCCC | 41.87 | 19429919 | |
2084 | Phosphorylation | RRLVSGGSSSSGAHA CCEECCCCCCCCCCC | 30.49 | 27626673 | |
2085 | Phosphorylation | RLVSGGSSSSGAHAE CEECCCCCCCCCCCC | 31.62 | 29892262 | |
2086 | Phosphorylation | LVSGGSSSSGAHAEG EECCCCCCCCCCCCC | 34.19 | 25749252 | |
2087 | Phosphorylation | VSGGSSSSGAHAEGK ECCCCCCCCCCCCCC | 41.78 | 27626673 | |
2143 | Phosphorylation | TNGVAPCSSTPAIFD CCCCCCCCCCCCCCC | 35.87 | 21082442 | |
2168 | Phosphorylation | VLQRRRDSSFEDECY HHHHHHHCCCCCCEE | 34.81 | 19429919 | |
2169 | Phosphorylation | LQRRRDSSFEDECYT HHHHHHCCCCCCEEC | 36.62 | 19429919 | |
2176 | Phosphorylation | SFEDECYTRDEASLH CCCCCEECCCHHHHH | 43.21 | 18327897 | |
2181 | Phosphorylation | CYTRDEASLHLVSES EECCCHHHHHHCCCC | 17.80 | 18327897 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of OSA_DROME !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
BRM_DROME | brm | physical | 15060132 | |
OSA_DROME | osa | physical | 15060132 | |
BRM_DROME | brm | genetic | 10601025 | |
BRM_DROME | brm | genetic | 12466201 | |
CORTO_DROME | corto | genetic | 11810228 | |
MED18_DROME | MED18 | physical | 22036573 | |
ZEST_DROME | z | physical | 10809665 | |
ACT1_DROME | Act5C | physical | 10601025 | |
DSH_DROME | dsh | physical | 22036573 | |
BAP60_DROME | Bap60 | physical | 10601025 | |
SCAL_DROME | sd | physical | 24137538 | |
MED23_DROME | MED23 | physical | 22036573 | |
MED14_DROME | MED14 | physical | 22036573 | |
Y1505_DROME | CG11505 | physical | 22036573 | |
CPSF6_DROME | CG7185 | physical | 22036573 | |
CDK8_DROME | Cdk8 | physical | 22036573 | |
BRM_DROME | brm | physical | 10601025 | |
BRM_DROME | brm | physical | 23136390 | |
SUHW_DROME | su(Hw) | physical | 23609538 | |
MED17_DROME | MED17 | physical | 22036573 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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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 THR-384; THR-747; SER-1930;SER-1932; SER-2081; SER-2168; SER-2169; THR-2176 AND SER-2181, ANDMASS SPECTROMETRY. |