| UniProt ID | CFD1_YEAST | |
|---|---|---|
| UniProt AC | P40558 | |
| Protein Name | Cytosolic Fe-S cluster assembly factor CFD1 {ECO:0000255|HAMAP-Rule:MF_03039} | |
| Gene Name | CFD1 {ECO:0000255|HAMAP-Rule:MF_03039} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 293 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery. Required for maturation of extramitochondrial Fe-S proteins. The NBP35-CFD1 heterotetramer forms a Fe-S scaffold complex, mediating the de novo assembly of an Fe-S cluster and its transfer to target apoproteins. Nucleotide binding/hydrolysis seems to be critcal for loading of Fe-S clusters onto CFD1 and NBP35. Required for biogenesis and export of both ribosomal subunits, which may reflect a role in assembly of the Fe/S clusters in RLI1, a protein which performs rRNA processing and ribosome export.. | |
| Protein Sequence | MEEQEIGVPAASLAGIKHIILILSGKGGVGKSSVTTQTALTLCSMGFKVGVLDIDLTGPSLPRMFGLENESIYQGPEGWQPVKVETNSTGSLSVISLGFLLGDRGNSVIWRGPKKTSMIKQFISDVAWGELDYLLIDTPPGTSDEHISIAEELRYSKPDGGIVVTTPQSVATADVKKEINFCKKVDLKILGIIENMSGFVCPHCAECTNIFSSGGGKRLSEQFSVPYLGNVPIDPKFVEMIENQVSSKKTLVEMYRESSLCPIFEEIMKKLRKQDTTTPVVDKHEQPQIESPK | |
| 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 |
|---|---|---|---|---|---|
| 107 | Phosphorylation | LLGDRGNSVIWRGPK EECCCCCCEEECCCC | 20.15 | 28889911 | |
| 276 | Phosphorylation | KKLRKQDTTTPVVDK HHHHCCCCCCCCCCC | 30.03 | 28889911 | |
| 277 | Phosphorylation | KLRKQDTTTPVVDKH HHHCCCCCCCCCCCC | 37.07 | 28889911 | |
| 278 | Phosphorylation | LRKQDTTTPVVDKHE HHCCCCCCCCCCCCC | 19.04 | 28889911 | |
| 291 | Phosphorylation | HEQPQIESPK----- CCCCCCCCCC----- | 39.35 | 25521595 |
| 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 CFD1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CFD1_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 CFD1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, AND MASSSPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, AND MASSSPECTROMETRY. | |
