| UniProt ID | GDE1_YEAST | |
|---|---|---|
| UniProt AC | Q02979 | |
| Protein Name | Glycerophosphocholine phosphodiesterase GDE1 {ECO:0000303|PubMed:16141200} | |
| Gene Name | GDE1 {ECO:0000303|PubMed:16141200} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1223 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Glycerophosphocholine glycerophosphodiesterase responsible for the hydrolysis of intracellular glycerophosphocholine into glycerol-phosphate and choline. [PubMed: 16141200] | |
| Protein Sequence | MKFGKTFANHRIPEWSSQYVGYKSLKKMIKEITRLQEDIYRAHNKNSYDEGRPPTKMRDSSNSAQNYLDSPKIQKLLASFFFAVDRDIEKVDTFYNSQYAEYKKRFERLLSSNQFNEIKSTLVVDANKEDAVAQTLLTKDTREMNMLLKGTSQASRLSYHKDDLIEIQSILAELRKQFRNLKWYAELNKRAFGKILKKLDKKVGTNQQMSTMKTRILPLQFANDSLITKDLSLLKTIWEQVTFRINSYERVMRSTSPNANANDNTEFFKIICVFIEEDDSKGLIRELTNLYSELSLIPTRIMISVLNKAALSKSLACIDAILKVIPSLNDSEDINRRNFFHHHIIAIGKLIRKQEILSRKKKSQPSKYTNSEGEIVTDLRTLHTTLSAPAESDSITEEEKSSACTLSYILEELPIHLRPCLFQHDNYKRTPLHYSCQYGLSEVTKLIIKLMKEWNIWNEIPIDDVSAFGDAESLTPLHLCVLGAHPKTTEVLLQSLDPNVKLKSSSLLHLATEWNNYPLLHVLLSSKRFDINYQDNELHETPLYLACRLNFFEAAVCLLYNGADLEIREKLFGWTAIFVAAAEGFTDIVKLLIANNANFDIEDEGGWTPMEHAVLRGHLHIADMVQIRDELVTHPHSQLNSGSEEKEPLNEISAGELNERNENGNGGNKGSLGKLAGPIKSYGHRFLDNNESLILITLGSNDTRNKSPSISLSSEALAKVIGLETDCALSLVISCNDSIDKSSVILDLPLDDNVDAVDFKVPFKVDYSHTLYFDIVPTYGTRSLETHNRIDCQKNNNNYVMARGVSMLNKSYSSVGVNRSILNGSVTVPIIANHTLEILGTLKFEYIIITPFEHPQLPLERTETYWKSLVSTRVIGHRGLGKNNPNKSLQIGENTVESFIMAASLGASYVEFDVQLTKDNVPVVYHDFLVAETGVDIPMHELTLEQFLDLNNADKEHIQRGAGHSPHHVNGADTALQKYRGRSVDDSDVSTLRRAWDLHDNDPNGKSNNAHWSDNRMRLTKTFKKNNFKGNARGHSIASSFVTLKELFKKIPANVGFNIECKFPMLDEAEEEELGQIMMEMNHWVDTVLKVVFDNANGRDIIFSSFHPDICIMLSLKQPVIPILFLTEGGSEQMADLRASSLQNGIRFAKKWNLLGIVSAAAPILKAPRLVQVVKSNGLVCVTYGVDNNDPENASIQIEAGVDAVIVDSVLAIRRGLTKKNEK | |
| 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 |
|---|---|---|---|---|---|
| 61 | Phosphorylation | PTKMRDSSNSAQNYL CCCCCCCCCHHHHHH | 38.81 | 28889911 | |
| 70 | Phosphorylation | SAQNYLDSPKIQKLL HHHHHHCCHHHHHHH | 26.04 | 27214570 | |
| 121 | Phosphorylation | QFNEIKSTLVVDANK CCCCCCCEEEEECCH | 20.69 | 28889911 | |
| 141 | Phosphorylation | QTLLTKDTREMNMLL HHHHCCCHHHHHHHH | 30.04 | 30377154 | |
| 151 | Phosphorylation | MNMLLKGTSQASRLS HHHHHHCCCHHHHHH | 18.97 | 19823750 | |
| 152 | Phosphorylation | NMLLKGTSQASRLSY HHHHHCCCHHHHHHC | 32.20 | 19823750 | |
| 155 | Phosphorylation | LKGTSQASRLSYHKD HHCCCHHHHHHCCHH | 26.56 | 19823750 | |
| 158 | Phosphorylation | TSQASRLSYHKDDLI CCHHHHHHCCHHHHH | 24.87 | 19823750 | |
| 159 | Phosphorylation | SQASRLSYHKDDLIE CHHHHHHCCHHHHHH | 19.92 | 19823750 | |
| 213 | Ubiquitination | NQQMSTMKTRILPLQ CHHHCCCHHCCHHHH | 34.44 | 23749301 | |
| 254 | Phosphorylation | SYERVMRSTSPNANA HHHHHHHCCCCCCCC | 18.36 | 22369663 | |
| 255 | Phosphorylation | YERVMRSTSPNANAN HHHHHHCCCCCCCCC | 37.53 | 22369663 | |
| 256 | Phosphorylation | ERVMRSTSPNANAND HHHHHCCCCCCCCCC | 19.87 | 22369663 | |
| 265 | Phosphorylation | NANANDNTEFFKIIC CCCCCCCCCEEEEEE | 36.71 | 28889911 | |
| 633 | Phosphorylation | QIRDELVTHPHSQLN EHHHHHHHCCCHHCC | 42.17 | 26447709 | |
| 637 | Phosphorylation | ELVTHPHSQLNSGSE HHHHCCCHHCCCCCC | 40.59 | 26447709 | |
| 641 | Phosphorylation | HPHSQLNSGSEEKEP CCCHHCCCCCCCCCC | 52.90 | 26447709 | |
| 643 | Phosphorylation | HSQLNSGSEEKEPLN CHHCCCCCCCCCCCC | 42.26 | 26447709 | |
| 653 | Phosphorylation | KEPLNEISAGELNER CCCCCCCCHHHCCCC | 24.84 | 28889911 | |
| 725 | Phosphorylation | AKVIGLETDCALSLV HHHHCCCCCCCHHEE | 41.23 | 27017623 | |
| 738 | Phosphorylation | LVISCNDSIDKSSVI EEEECCCCCCCCCEE | 20.78 | 27017623 | |
| 767 | Phosphorylation | KVPFKVDYSHTLYFD ECCEEECCCEEEEEE | 12.82 | 30377154 | |
| 772 | Phosphorylation | VDYSHTLYFDIVPTY ECCCEEEEEEEECCC | 10.60 | 30377154 | |
| 781 | Phosphorylation | DIVPTYGTRSLETHN EEECCCCCCCCCHHC | 13.48 | 30377154 | |
| 794 | Ubiquitination | HNRIDCQKNNNNYVM HCCEECCCCCCCEEE | 68.89 | 23749301 | |
| 965 | Phosphorylation | IQRGAGHSPHHVNGA HHCCCCCCCCCCCCH | 25.63 | 17563356 | |
| 983 | Phosphorylation | LQKYRGRSVDDSDVS HHHHCCCCCCHHHHH | 32.49 | 23749301 | |
| 1105 | Phosphorylation | GRDIIFSSFHPDICI CCEEEEECCCCCEEH | 19.47 | 27017623 | |
| 1115 | Phosphorylation | PDICIMLSLKQPVIP CCEEHHHCCCCCEEE | 19.01 | 27017623 |
| 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 GDE1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GDE1_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 GDE1_YEAST !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| THG1_YEAST | THG1 | physical | 10688190 | |
| NET1_YEAST | NET1 | physical | 16554755 | |
| SSZ1_YEAST | SSZ1 | physical | 19536198 | |
| HSP72_YEAST | SSA2 | physical | 19536198 | |
| HSP71_YEAST | SSA1 | physical | 19536198 | |
| YNE0_YEAST | YNL040W | genetic | 20093466 | |
| SIW14_YEAST | SIW14 | genetic | 20093466 | |
| ADE_YEAST | AAH1 | genetic | 21623372 | |
| APT2_YEAST | APT2 | genetic | 21623372 | |
| GIT1_YEAST | GIT1 | genetic | 21623372 | |
| PGLR_YEAST | PGU1 | genetic | 21623372 | |
| RV167_YEAST | RVS167 | genetic | 27708008 | |
| SIW14_YEAST | SIW14 | genetic | 27708008 |
| 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-61; SER-254; SER-256;THR-265 AND SER-653, AND MASS SPECTROMETRY. | |
| "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-965, AND MASSSPECTROMETRY. | |