| UniProt ID | DIA2_YEAST | |
|---|---|---|
| UniProt AC | Q08496 | |
| Protein Name | Protein DIA2 | |
| Gene Name | DIA2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 732 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | F-box protein component of a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins (By similarity). The SCF(DIA2) complex is specifically involved in the pheromone induced degradation of phosphorylated TEC1. The SCF(DIA2) complex binds to DNA replication origins. Involved in DNA replication, genome stability, and the control of cell cycle, probably through its association to replication origins to facilitate the ubiquitination of another origin-binding protein. Required for invasive growth and growth under alkaline conditions.. | |
| Protein Sequence | MSSPGNSGVAIDSTVLKAIELGTRLFKSGEYLQAKRIFTNALRVCDSYSQEQIMRIRNAYQLDTARPDNKRLYHPRYIKILDNICACYEKLNDLKSCLDVSQRLLKLEPGNIKCYIRCTRTLIKLKDWKRAYKTCSRGLQLCNNDSNHLRQQKQFIKNNMVQKQDGKRSYIDPLEETKIAKKKKNNNVLESLPKKKIKGSTKKTDLVGNLPIEILPIIFQRFTTKELVTLSLVCNKWRDKILYHLDCFQEFNLAPINFKNFVKFMDFLQQNFTRTYRKYILSQVKVSSRITSEELRITQLLFSKMPKCINIERLILSMPTLTTTQIFKLMVRGGTDFFTRLLELSLMITYRPDKQHELEILQTCPLLKKIELIFVNSLVPIFDGNNSVGRDGSFNVMARHTNMQISTADNDEQGIVEEKVIYSELEKITLICDKKKIKNFPLCRALLRGQFPLLQKLTITGVTFPMNNQDIMNFQWLLNFPDLKELWIEDNDNCELSKFLQLLKFSNVWKNLEKLTFRENKLYPIVNLDEDQPVTNDDEVPSMLFYKENLQNLEKLDLMGTSISGSALTRLCEQEYLDGRKLRSLNIGNCPNIQFPNNHAHTARMILDVNAVLKRLSKLEEINLSHLSSLNDSTMKSFIINVPFLENLKRLDISHNFEITGISIYEFLKKFQMDHDNEAGGQPLAYLNIDGCSQVSHITVNMIRAQNLVTQVDCVYERDVWRKFGINSYSYS | |
| 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 |
|---|---|---|---|---|---|
| 39 | Phosphorylation | LQAKRIFTNALRVCD HHHHHHHHHHHHHCC | 19.74 | 25882841 | |
| 393 | Phosphorylation | NSVGRDGSFNVMARH CCCCCCCCEEEEECC | 20.24 | 25752575 | |
| 407 | Phosphorylation | HTNMQISTADNDEQG CCCCEEECCCCCCCC | 39.39 | 18407956 |
| 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 DIA2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DIA2_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 DIA2_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-393, AND MASSSPECTROMETRY. | |
