| UniProt ID | DID4_YEAST | |
|---|---|---|
| UniProt AC | P36108 | |
| Protein Name | DOA4-independent degradation protein 4 | |
| Gene Name | DID4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 232 | |
| Subcellular Localization |
Cytoplasm . Endosome membrane Peripheral membrane protein . |
|
| Protein Description | Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Can directly stimulate VPS4 ATPase activity. The DID4/VPS2-VPS24 subcomplex is required for the VPS4-dependent dissociation of ESCRT-III.. | |
| Protein Sequence | MSLFEWVFGKNVTPQERLKKNQRALERTQRELEREKRKLELQDKKLVSEIKKSAKNGQVAAAKVQAKDLVRTRNYIQKFDNMKAQLQAISLRIQAVRSSDQMTRSMSEATGLLAGMNRTMNLPQLQRISMEFEKQSDLMGQRQEFMDEAIDNVMGDEVDEDEEADEIVNKVLDEIGVDLNSQLQSTPQNLVSNAPIAETAMGIPEPIGAGSEFHGNPDDDLQARLNTLKKQT | |
| 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 |
|---|---|---|---|---|---|
| 98 | Phosphorylation | LRIQAVRSSDQMTRS HHHHHHHCCHHHHHH | 31.50 | 28889911 | |
| 99 | Phosphorylation | RIQAVRSSDQMTRSM HHHHHHCCHHHHHHH | 22.69 | 30377154 | |
| 103 | Phosphorylation | VRSSDQMTRSMSEAT HHCCHHHHHHHHHHH | 17.60 | 30377154 | |
| 105 | Phosphorylation | SSDQMTRSMSEATGL CCHHHHHHHHHHHHH | 19.93 | 30377154 | |
| 107 | Phosphorylation | DQMTRSMSEATGLLA HHHHHHHHHHHHHHH | 25.89 | 28152593 | |
| 129 | Phosphorylation | LPQLQRISMEFEKQS HHHHHHHHHHHHHHH | 17.91 | 30377154 | |
| 211 | Phosphorylation | PEPIGAGSEFHGNPD CCCCCCCCCCCCCCC | 36.23 | 28889911 |
| 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 DID4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DID4_YEAST !! | ||||||
* 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 DID4_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 AND SER-211, ANDMASS SPECTROMETRY. | |
