| UniProt ID | HIRA_DROME | |
|---|---|---|
| UniProt AC | O17468 | |
| Protein Name | Protein HIRA homolog | |
| Gene Name | Hira | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 1047 | |
| Subcellular Localization | Nucleus . Maternally contributed protein localizes specifically to the male nucleus in fertilized eggs. This localization persists from the initiation of sperm nucleus decondensation to the end of pronucleus formation. | |
| Protein Description | Required for the periodic repression of histone gene transcription during the cell cycle (By similarity). Required for replication-independent chromatin assembly. Promotes remodeling of sperm chromatin following fertilization via the incorporation of histone H3.3 and histone H4.. | |
| Protein Sequence | MRLLKPAWVHHDDKQIFSVDIHKDCTKFATGGQGSDCGRVVIWNLLPVLSDKAEFDADVPKMLCQMDQHLACVNCVRWSQNGQNLASGSDDKLIMIWRKSAGSSGVFGTGGMQKNHESWKCFYTLRGHDGDVLDLAWSPNDVYLASCSIDNTVIIWDAQAFPHSVATLKGHTGLVKGVSWDPLGRFLASQSDDRSIKIWNTMNWSLSHTITEPFEECGGTTHILRLSWSPDGQYLVSAHAMNGGGPTAQIIEREGWKCDKDFVGHRKAVTCVRFHNSILSRQENDGSPSKPLQYCCLAVGSRDRSLSVWMTALQRPMVVIHELFNASILDLTWGPQECLLMACSVDGSIACLKFTEEELGKAISEEEQNAIIRKMYGKNYVNGLGKSAPVLEHPQRLLLPQGDKPTKFPLSNNNEANQRPISKQTETRTKDGKRRITPMFIPLHEDGPTSLSMNIVSSSGSSTTALTSCSAAIGTLPAAAPTESAATPLMPLEPLVSKIDLGRLDSRLKTQPASQRRQSLPFDPGQSNELLRTPRLEEHQSSTCSPSNLNVTATGKSEFVKAALDYRLHVSNGHLKTQHGMLAKVTASDSKEMLWEFYVGSPLVNLNLCEKYAMLCSLDGSMRLISMETGCPVFPAISLTSSAVHCAFSPDNSLVGVLTECGLLRIWDIAKKVVSLAAGCLELLNKHGTAAQFSVTNQGMPLIGFPSGNSYSYSTSLQSWLVLATKDAIMYHGIRGTLPRDMDQMQQKFPLLSMQASSQNYFSFTGSMELRHSESWQQCAKIRFIENQIKLCEALQSLDELQHWHKMLTFQLATHGSEKRMRVFLDDLLSMPEPGISQFVPKLELMQCVLDTLKPHSEWNRLHSEYTELLKECKSERQKDIFATPAPPQQKTASSAGSSPRSGEATGEEVTEKDGATAVAAAVVAGSRMAVTTGTSTTTTTTASSSLSSSGSSSSTSGSGSSSSSSSTSSLSVPQPAPSLSPEIQTLDSPTVCIDDEILSASSSLPPLDTSPVEVSPASTSGGAASTSPAASVAGSAPVSSSKTDQT | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 289 | Phosphorylation | QENDGSPSKPLQYCC CCCCCCCCCCHHHHH | 48.91 | 25749252 | |
| 519 | Phosphorylation | PASQRRQSLPFDPGQ CHHHCCCCCCCCCCC | 35.88 | 19429919 | |
| 899 | Phosphorylation | TASSAGSSPRSGEAT CCCCCCCCCCCCCCC | 24.34 | 30478224 |
| 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 HIRA_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HIRA_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 HIRA_DROME !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| ASF1_DROME | asf1 | physical | 19782028 | |
| GAGA_DROME | Trl | physical | 19782028 | |
| ABRU_DROME | ab | physical | 19782028 | |
| RAGP1_DROME | RanGAP | physical | 19782028 | |
| HTS_DROME | hts | physical | 19782028 | |
| TCPG_DROME | Cctgamma | physical | 19782028 | |
| TCPA_DROME | T-cp1 | physical | 19782028 | |
| CHD1_DROME | Chd1 | physical | 17717186 | |
| GAGA_DROME | Trl | physical | 17344416 | |
| YEMA_DROME | yem | physical | 23408912 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "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-519, AND MASSSPECTROMETRY. | |