| UniProt ID | IDS2_YEAST | |
|---|---|---|
| UniProt AC | P46958 | |
| Protein Name | IME2-dependent-signaling protein | |
| Gene Name | IDS2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 469 | |
| Subcellular Localization | ||
| Protein Description | Seems to act indirectly to modify IME2 activity, thus permitting IME2 to carry out later meiotic functions.. | |
| Protein Sequence | MDNQQESISEDITGDLAAAVRKSWSESQDNPLLLNFNNSPIGTPTDRYSPEPATMMEGNAMNLSSLARGSTQQQQRLYGSSQTREKSDQQQQDYQLFKHHYSLGQETRESVSDILNDLTLGSPEPSERASPIRQPSVDVPPLTTRRSSIQDVQWIRHLLNPRSSFSGASSNEPTNSPGDFLNQSRAWITILHDSSAESLQAVIVLAESLKNVNSQYNLWVLHSSEVNAFQLAQVGIKTLIIDEYINLFMNFGTGSGFSASSQSTETKGELNFKWCKLFLFFSLIDRFELICYLSPTCLVLQNIDELLESTEVSDEIDNETCVLLSNKVNYINEDLVSVNQDQSSAENYDDDPQIIILKPNRAVAMCIKEYFTIYGNDFEGESKRSMFHQMNDLQIMKALFGDKWSYIDSVGYCAVPIASVPANRLNYKIIEFKILKPWERQNYIAAGQHRESIMNKWLDLWRDFLNQAN | |
| 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 | -------MDNQQESI -------CCCHHHHH | 11.16 | 22814378 | |
| 7 | Phosphorylation | -MDNQQESISEDITG -CCCHHHHHHHCHHH | 27.38 | 30377154 | |
| 13 | Phosphorylation | ESISEDITGDLAAAV HHHHHCHHHHHHHHH | 36.64 | 28889911 | |
| 23 | Phosphorylation | LAAAVRKSWSESQDN HHHHHHHHCCCCCCC | 25.85 | 28889911 | |
| 25 | Phosphorylation | AAVRKSWSESQDNPL HHHHHHCCCCCCCCE | 34.17 | 19779198 | |
| 27 | Phosphorylation | VRKSWSESQDNPLLL HHHHCCCCCCCCEEE | 37.00 | 23749301 | |
| 39 | Phosphorylation | LLLNFNNSPIGTPTD EEEECCCCCCCCCCC | 20.99 | 23749301 | |
| 43 | Phosphorylation | FNNSPIGTPTDRYSP CCCCCCCCCCCCCCC | 24.60 | 28889911 | |
| 45 | Phosphorylation | NSPIGTPTDRYSPEP CCCCCCCCCCCCCCC | 32.71 | 26447709 | |
| 48 | Phosphorylation | IGTPTDRYSPEPATM CCCCCCCCCCCCCCC | 31.24 | 27017623 | |
| 49 | Phosphorylation | GTPTDRYSPEPATMM CCCCCCCCCCCCCCC | 24.55 | 27017623 | |
| 64 | Phosphorylation | EGNAMNLSSLARGST CCCCCCHHHHHCCCH | 20.50 | 28889911 | |
| 65 | Phosphorylation | GNAMNLSSLARGSTQ CCCCCHHHHHCCCHH | 29.25 | 28889911 | |
| 81 | Phosphorylation | QQRLYGSSQTREKSD HHHHHCCCCCCCCCH | 31.07 | 27214570 | |
| 87 | Phosphorylation | SSQTREKSDQQQQDY CCCCCCCCHHHHHHH | 35.58 | 27017623 | |
| 94 | Phosphorylation | SDQQQQDYQLFKHHY CHHHHHHHHHHHHHH | 11.63 | 27017623 | |
| 110 | Phosphorylation | LGQETRESVSDILND CCHHHHHHHHHHHHH | 24.51 | 22369663 | |
| 112 | Phosphorylation | QETRESVSDILNDLT HHHHHHHHHHHHHCC | 28.36 | 22369663 | |
| 119 | Phosphorylation | SDILNDLTLGSPEPS HHHHHHCCCCCCCHH | 31.75 | 22369663 | |
| 122 | Phosphorylation | LNDLTLGSPEPSERA HHHCCCCCCCHHHCC | 29.24 | 22369663 | |
| 126 | Phosphorylation | TLGSPEPSERASPIR CCCCCCHHHCCCCCC | 37.74 | 19779198 | |
| 130 | Phosphorylation | PEPSERASPIRQPSV CCHHHCCCCCCCCCC | 27.38 | 15665377 | |
| 136 | Phosphorylation | ASPIRQPSVDVPPLT CCCCCCCCCCCCCCC | 23.70 | 21082442 | |
| 144 | Phosphorylation | VDVPPLTTRRSSIQD CCCCCCCCCCCHHHH | 31.59 | 19779198 | |
| 147 | Phosphorylation | PPLTTRRSSIQDVQW CCCCCCCCHHHHHHH | 28.62 | 22369663 | |
| 148 | Phosphorylation | PLTTRRSSIQDVQWI CCCCCCCHHHHHHHH | 23.58 | 22369663 | |
| 163 | Phosphorylation | RHLLNPRSSFSGASS HHHHCCCCCCCCCCC | 36.67 | 22369663 | |
| 164 | Phosphorylation | HLLNPRSSFSGASSN HHHCCCCCCCCCCCC | 25.39 | 22369663 | |
| 166 | Phosphorylation | LNPRSSFSGASSNEP HCCCCCCCCCCCCCC | 35.08 | 22369663 | |
| 169 | Phosphorylation | RSSFSGASSNEPTNS CCCCCCCCCCCCCCC | 36.90 | 22369663 | |
| 170 | Phosphorylation | SSFSGASSNEPTNSP CCCCCCCCCCCCCCC | 44.68 | 22369663 | |
| 174 | Phosphorylation | GASSNEPTNSPGDFL CCCCCCCCCCCCHHH | 41.99 | 22369663 | |
| 176 | Phosphorylation | SSNEPTNSPGDFLNQ CCCCCCCCCCHHHHH | 32.51 | 29136822 |
| 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 IDS2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IDS2_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 IDS2_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 THR-13; SER-23; SER-39;SER-122; SER-130; SER-136; SER-147; SER-148; SER-163; SER-166 ANDSER-169, AND MASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-163, ANDMASS SPECTROMETRY. | |