UniProt ID | RIB1_YEAST | |
---|---|---|
UniProt AC | P38066 | |
Protein Name | GTP cyclohydrolase-2 | |
Gene Name | RIB1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 345 | |
Subcellular Localization | ||
Protein Description | Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate.. | |
Protein Sequence | MTIDNYDNSKQDSSKYEVSGTGDGRNGDGGLPLVQCVARARIPTTQGPDIFLHLYSNNRDNKEHLAIVFGEDIRSRSLFRRRQCETQQDRMIRGAYIGKLYPGRTVADEDDRLGLALEFDDSTGELLASKATTWDAHNDTLVRIHSECYTGENAWSARCDCGEQFDRAGRLIACDHEPTSNIKGGNGHGVIVYLRQEGRGIGLGEKLKAYNLQDLGADTVQANLMLKHPVDARDFSLGKAILLDLGIGNVRLLTNNPEKIKQVDHAPYLKCVERVPMVPIHWTNSSEGIDSKEIEGYLRTKIERMGHLLTEPLKLHTNPQPTETSEAQNQNRMNSALSSTSTLAI | |
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 |
---|---|---|---|---|---|
210 | Phosphorylation | LGEKLKAYNLQDLGA HHHHHHHCCCHHCCC | 18.15 | 27017623 | |
219 | Phosphorylation | LQDLGADTVQANLML CHHCCCCCHHHHHEE | 17.62 | 27017623 | |
259 | Acetylation | LLTNNPEKIKQVDHA ECCCCHHHHHCCCCC | 57.36 | 24489116 | |
283 | Phosphorylation | PMVPIHWTNSSEGID CEECCEECCCCCCCC | 15.85 | 22369663 | |
285 | Phosphorylation | VPIHWTNSSEGIDSK ECCEECCCCCCCCHH | 23.53 | 22369663 | |
286 | Phosphorylation | PIHWTNSSEGIDSKE CCEECCCCCCCCHHH | 41.74 | 22369663 | |
291 | Phosphorylation | NSSEGIDSKEIEGYL CCCCCCCHHHHHHHH | 30.21 | 22369663 | |
335 | Phosphorylation | QNQNRMNSALSSTST HHHHHHHHHHHHCCC | 22.65 | 22369663 | |
338 | Phosphorylation | NRMNSALSSTSTLAI HHHHHHHHHCCCCCC | 31.14 | 22369663 | |
339 | Phosphorylation | RMNSALSSTSTLAI- HHHHHHHHCCCCCC- | 27.51 | 22369663 | |
340 | Phosphorylation | MNSALSSTSTLAI-- HHHHHHHCCCCCC-- | 23.50 | 22369663 | |
341 | Phosphorylation | NSALSSTSTLAI--- HHHHHHCCCCCC--- | 24.30 | 22369663 | |
342 | Phosphorylation | SALSSTSTLAI---- HHHHHCCCCCC---- | 21.94 | 22369663 |
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 RIB1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RIB1_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 RIB1_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
PDXH_YEAST | YPR172W | physical | 11283351 | |
RIB1_YEAST | RIB1 | physical | 18467557 | |
RIB1_YEAST | RIB1 | physical | 18719252 | |
RIB1_YEAST | RIB1 | physical | 22615397 |
Kegg Drug | ||||||
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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-285, AND MASSSPECTROMETRY. |