UniProt ID | PSMF1_DROME | |
---|---|---|
UniProt AC | Q9V637 | |
Protein Name | Proteasome inhibitor PI31 subunit | |
Gene Name | PI31 | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 270 | |
Subcellular Localization | Cytoplasm . In the spermatid, localizes to the actin-based individualization complex. | |
Protein Description | Plays an important role in the control of proteasome function. Inhibits the hydrolysis of protein and peptide substrates by the 20S proteasome. Enhances 26S proteasome function by promoting its assembly through the interaction with the assembly chaperones PSMD9 and PMSD5. Functions together with ntc to control non-apoptotic caspase activation during sperm individualization. In testis, is required for proper protein degradation and germline cell cycle progression.. | |
Protein Sequence | MESGSTAKTGDFFYGWDLLYKTVKADVSKKSDLLIALVHFLLTKHYNFRCVGVGDDKTLPEEEGSELLPDSWNDDDTKYSLRYVHDKMLYLLLGHITEGSLLINLLDINTKKVSNICVEPETLVPEVKGGITTIMPSASEIVERYRRELLDPVFTGNSREVTTQTTNSPRPIGSDPDPLRIGEPRRGGSFIPSAFEPRPFGFPDVGRGDLDPLGRGGHGNLFSFPSRPNMGPGPVPRFDPFNPLNPNRPGQGGINPDHMRPPDWNPDYYM | |
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 |
---|---|---|---|---|---|
162 | Phosphorylation | TGNSREVTTQTTNSP CCCCCEEEEECCCCC | 14.40 | 23607784 | |
163 | Phosphorylation | GNSREVTTQTTNSPR CCCCEEEEECCCCCC | 29.15 | 23607784 | |
165 | Phosphorylation | SREVTTQTTNSPRPI CCEEEEECCCCCCCC | 26.33 | 29892262 | |
166 | Phosphorylation | REVTTQTTNSPRPIG CEEEEECCCCCCCCC | 24.71 | 28490779 | |
168 | Phosphorylation | VTTQTTNSPRPIGSD EEEECCCCCCCCCCC | 21.86 | 23607784 | |
189 | Phosphorylation | GEPRRGGSFIPSAFE CCCCCCCCCCCCCCC | 23.87 | 19429919 | |
223 | Phosphorylation | GGHGNLFSFPSRPNM CCCCCCCCCCCCCCC | 39.14 | 21082442 | |
226 | Phosphorylation | GNLFSFPSRPNMGPG CCCCCCCCCCCCCCC | 59.36 | 21082442 |
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 PSMF1_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSMF1_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 PSMF1_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TNKS_DROME | Tnks | physical | 23622245 | |
PSMD5_DROME | CG12096 | physical | 23622245 | |
PSMD9_DROME | CG9588 | physical | 23622245 |
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-168, AND MASSSPECTROMETRY. | |
"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-168 AND SER-189, ANDMASS SPECTROMETRY. |