| UniProt ID | UBA4_YEAST | |
|---|---|---|
| UniProt AC | P38820 | |
| Protein Name | Adenylyltransferase and sulfurtransferase UBA4 {ECO:0000255|HAMAP-Rule:MF_03049} | |
| Gene Name | UBA4 {ECO:0000255|HAMAP-Rule:MF_03049} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 440 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of sulfur carrier URM1. Its N-terminus first activates URM1 as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 to form thiocarboxylation (-COSH) of its C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards URM1. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.. | |
| Protein Sequence | MNDYHLEDTTSELEALRLENAQLREQLAKREDSSRDYPLSLEEYQRYGRQMIVEETGGVAGQVKLKNTKVLVVGAGGLGCPALPYLAGAGVGQIGIVDNDVVETSNLHRQVLHDSSRVGMLKCESARQYITKLNPHINVVTYPVRLNSSNAFDIFKGYNYILDCTDSPLTRYLVSDVAVNLGITVVSASGLGTEGQLTILNFNNIGPCYRCFYPTPPPPNAVTSCQEGGVIGPCIGLVGTMMAVETLKLILGIYTNENFSPFLMLYSGFPQQSLRTFKMRGRQEKCLCCGKNRTITKEAIEKGEINYELFCGARNYNVCEPDERISVDAFQRIYKDDEFLAKHIFLDVRPSHHYEISHFPEAVNIPIKNLRDMNGDLKKLQEKLPSVEKDSNIVILCRYGNDSQLATRLLKDKFGFSNVRDVRGGYFKYIDDIDQTIPKY | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MNDYHLED -------CCCCCCCC | 8.53 | 22814378 | |
| 4 | Phosphorylation | ----MNDYHLEDTTS ----CCCCCCCCCHH | 11.87 | 22369663 | |
| 9 | Phosphorylation | NDYHLEDTTSELEAL CCCCCCCCHHHHHHH | 23.89 | 22369663 | |
| 10 | Phosphorylation | DYHLEDTTSELEALR CCCCCCCHHHHHHHH | 32.31 | 22369663 | |
| 11 | Phosphorylation | YHLEDTTSELEALRL CCCCCCHHHHHHHHH | 42.13 | 22369663 | |
| 40 | Phosphorylation | SSRDYPLSLEEYQRY CCCCCCCCHHHHHHH | 29.27 | 25005228 | |
| 132 | Acetylation | SARQYITKLNPHINV HHHHHHHHHCCCCCE | 36.39 | 24489116 | |
| 326 | Phosphorylation | CEPDERISVDAFQRI CCCCCCCCHHHHHHH | 21.84 | 23749301 | |
| 335 | Acetylation | DAFQRIYKDDEFLAK HHHHHHHCCCHHHHH | 57.22 | 24489116 |
| 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 UBA4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UBA4_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 UBA4_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-326, AND MASSSPECTROMETRY. | |
