| UniProt ID | HMGD_DROME | |
|---|---|---|
| UniProt AC | Q05783 | |
| Protein Name | High mobility group protein D | |
| Gene Name | HmgD | |
| Organism | Drosophila melanogaster (Fruit fly). | |
| Sequence Length | 112 | |
| Subcellular Localization | Nucleus. Chromosome. | |
| Protein Description | Binds preferentially single-stranded DNA and unwinds double-stranded DNA. Prefers sites containing the sequence 5'-ttg-3'. Facilitates DNA bending. Associated with early embryonic chromatin in the absence of histone H1.. | |
| Protein Sequence | MSDKPKRPLSAYMLWLNSARESIKRENPGIKVTEVAKRGGELWRAMKDKSEWEAKAAKAKDDYDRAVKEFEANGGSSAANGGGAKKRAKPAKKVAKKSKKEESDEDDDDESE | |
| 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 |
|---|---|---|---|---|---|
| 10 | Phosphorylation | DKPKRPLSAYMLWLN CCCCCCHHHHHHHHH | 21.75 | 19429919 | |
| 12 | Phosphorylation | PKRPLSAYMLWLNSA CCCCHHHHHHHHHHH | 6.86 | 19429919 | |
| 13 | Sulfoxidation | KRPLSAYMLWLNSAR CCCHHHHHHHHHHHH | 1.85 | 9323026 | |
| 76 | Phosphorylation | EFEANGGSSAANGGG HHHHCCCCCCCCCCC | 20.43 | 30478224 | |
| 77 | Phosphorylation | FEANGGSSAANGGGA HHHCCCCCCCCCCCH | 34.37 | 27794539 | |
| 103 | Phosphorylation | KKSKKEESDEDDDDE HHHHHHCCCCCCCCC | 47.60 | 21082442 | |
| 111 | Phosphorylation | DEDDDDESE------ CCCCCCCCC------ | 56.45 | 19429919 |
| 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 HMGD_DROME !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HMGD_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 HMGD_DROME !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| YC17_DROME | CG16817 | physical | 22036573 | |
| NACA_DROME | Nacalpha | physical | 22036573 | |
| NLP_DROME | Nlp | physical | 22036573 | |
| CALR_DROME | Crc | physical | 22036573 | |
| PDI_DROME | Pdi | 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 SER-10; TYR-12; SER-103 ANDSER-111, AND MASS SPECTROMETRY. | |
| "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-103 AND SER-111, ANDMASS SPECTROMETRY. | |