| UniProt ID | PDS5_YEAST | |
|---|---|---|
| UniProt AC | Q04264 | |
| Protein Name | Sister chromatid cohesion protein PDS5 | |
| Gene Name | PDS5 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1277 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Essential for the establishment and maintenance of sister chromatid cohesion at centromere proximal and distal regions during S phase. Also required for chromosomal condensation.. | |
| Protein Sequence | MAKGAVTKLKFNSPIISTSDQLISTNELLDRLKALHEELASLDQDNTDLTGLDKYRDALVSRKLLKHKDVGIRAFTACCLSDILRLYAPDAPYTDAQLTDIFKLVLSQFEQLGDQENGYHIQQTYLITKLLEYRSIVLLADLPSSNNLLIELFHIFYDPNKSFPARLFNVIGGILGEVISEFDSVPLEVLRLIFNKFLTYNPNEIPEGLNVTSDCGYEVSLILCDTYSNRMSRHLTKYYSEIIHEATNDDNNSRLLTVVVKLHKLVLRLWETVPELINAVIGFIYHELSSENELFRKEATKLIGQILTSYSDLNFVSTHSDTFKAWISKIADISPDVRVEWTESIPQIIATREDISKELNQALAKTFIDSDPRVRRTSVMIFNKVPVTEIWKNITNKAIYTSLLHLAREKHKEVRELCINTMAKFYSNSLNEIERTYQNKEIWEIIDTIPSTLYNLYYINDLNINEQVDSVIFEYLLPFEPDNDKRVHRLLTVLSHFDKKAFTSFFAFNARQIKISFAISKYIDFSKFLNNQESMSSSQGPIVMNKYNQTLQWLASGLSDSTKAIDALETIKQFNDERIFYLLNACVTNDIPFLTFKNCYNELVSKLQTPGLFKKYNISTGASIMPRDIAKVIQILLFRASPIIYNVSNISVLLNLSNNSDAKQLDLKRRILDDISKVNPTLFKDQIRTLKTIIKDLDDPDAEKNDNLSLEEALKTLYKASKTLKDQVDFDDTFFFTKLYDFAVESKPEITKYATKLIALSPKAEETLKKIKIRILPLDLQKDKYFTSHIIVLMEIFKKFPHVLNDDSTDIISYLIKEVLLSNQVVGDSKKEIDWVEDSLLSDTKYSAIGNKVFTLKLFTNKLRSIAPDVPRDELAESFTEKTMKLFFYLIASGGELISEFNKEFYPTPSNYQTKLRCVAGIQVLKLARISNLNNFIKPSDIIKLINLVEDESLPVRKTFLEQLKDYVANELISIKFLPLVFFTAYEPDVELKTTTKIWINFTFGLKSFKKGTIFERALPRLIHAIAHHPDIVGGLDSEGDAYLNALTTAIDYLLFYFDSIAAQENFSLLYYLSERVKNYQDKLVEDEIDEEEGPQKEEAPKKHRPYGQKMYIIGELSQMILLNLKEKKNWQHSAYPGKLNLPSDLFKPFATVQEAQLSFKTYIPESLTEKIQNNIKAKIGRILHTSQTQRQRLQKRLLAHENNESQKKKKKVHHARSQADDEEGDGDRESDSDDDSYSPSNKNETKKGHENIVMKKLRVRKEVDYKDDEDDDIEMT | |
| 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 |
|---|---|---|---|---|---|
| 76 | Phosphorylation | DVGIRAFTACCLSDI CCCHHHHHHHHHHHH | 20.14 | 28889911 | |
| 522 | Phosphorylation | ISFAISKYIDFSKFL HHHHHHHHHCHHHHH | 10.03 | 19779198 | |
| 534 | Phosphorylation | KFLNNQESMSSSQGP HHHCCCCCCCCCCCC | 17.75 | 30377154 | |
| 536 | Phosphorylation | LNNQESMSSSQGPIV HCCCCCCCCCCCCEE | 35.80 | 27214570 | |
| 537 | Phosphorylation | NNQESMSSSQGPIVM CCCCCCCCCCCCEEH | 20.31 | 19779198 | |
| 538 | Phosphorylation | NQESMSSSQGPIVMN CCCCCCCCCCCEEHH | 31.67 | 25752575 | |
| 547 | Phosphorylation | GPIVMNKYNQTLQWL CCEEHHHHHHHHHHH | 13.90 | 30377154 | |
| 556 | Phosphorylation | QTLQWLASGLSDSTK HHHHHHHHCCCCHHH | 37.79 | 30377154 | |
| 561 | Phosphorylation | LASGLSDSTKAIDAL HHHCCCCHHHHHHHH | 28.56 | 30377154 | |
| 562 | Phosphorylation | ASGLSDSTKAIDALE HHCCCCHHHHHHHHH | 29.50 | 30377154 | |
| 616 | Phosphorylation | TPGLFKKYNISTGAS CCCHHHCCCCCCCCC | 20.51 | 28889911 | |
| 684 | Acetylation | KVNPTLFKDQIRTLK HHCHHHHHHHHHHHH | 52.41 | 24489116 | |
| 740 | Phosphorylation | TFFFTKLYDFAVESK CHHHHHHHHHHHHCC | 15.57 | 29136822 | |
| 746 | Phosphorylation | LYDFAVESKPEITKY HHHHHHHCCHHHHHH | 47.08 | 29136822 | |
| 751 | Phosphorylation | VESKPEITKYATKLI HHCCHHHHHHHHHHH | 19.15 | 29136822 | |
| 752 | Acetylation | ESKPEITKYATKLIA HCCHHHHHHHHHHHH | 38.25 | 24489116 | |
| 753 | Phosphorylation | SKPEITKYATKLIAL CCHHHHHHHHHHHHH | 15.74 | 29136822 | |
| 755 | Phosphorylation | PEITKYATKLIALSP HHHHHHHHHHHHHCC | 24.24 | 29136822 | |
| 761 | Phosphorylation | ATKLIALSPKAEETL HHHHHHHCCCHHHHH | 18.48 | 29136822 | |
| 860 | Phosphorylation | VFTLKLFTNKLRSIA EEEHHHHHHHHHHHC | 41.71 | 27017623 | |
| 1097 | Acetylation | DEEEGPQKEEAPKKH CCCCCCCCCCCCCCC | 61.73 | 22865919 | |
| 1102 | Acetylation | PQKEEAPKKHRPYGQ CCCCCCCCCCCCCCC | 69.16 | 24489116 | |
| 1171 | Acetylation | IPESLTEKIQNNIKA CCHHHHHHHHHHHHH | 44.34 | 24489116 | |
| 1186 | Phosphorylation | KIGRILHTSQTQRQR HHHHHHCCCHHHHHH | 21.05 | 30377154 | |
| 1187 | Phosphorylation | IGRILHTSQTQRQRL HHHHHCCCHHHHHHH | 22.08 | 25752575 | |
| 1189 | Phosphorylation | RILHTSQTQRQRLQK HHHCCCHHHHHHHHH | 26.03 | 21440633 | |
| 1206 | Phosphorylation | LAHENNESQKKKKKV HHHCCCHHHHHHHHH | 49.80 | 25704821 | |
| 1218 | Phosphorylation | KKVHHARSQADDEEG HHHHHHHHHCCCCCC | 30.42 | 21551504 | |
| 1231 | Phosphorylation | EGDGDRESDSDDDSY CCCCCCCCCCCCCCC | 43.22 | 21551504 | |
| 1233 | Phosphorylation | DGDRESDSDDDSYSP CCCCCCCCCCCCCCC | 52.82 | 21551504 | |
| 1237 | Phosphorylation | ESDSDDDSYSPSNKN CCCCCCCCCCCCCCC | 34.21 | 21551504 | |
| 1238 | Phosphorylation | SDSDDDSYSPSNKNE CCCCCCCCCCCCCCC | 31.43 | 19795423 | |
| 1239 | Phosphorylation | DSDDDSYSPSNKNET CCCCCCCCCCCCCCC | 26.29 | 19795423 | |
| 1241 | Phosphorylation | DDDSYSPSNKNETKK CCCCCCCCCCCCCCC | 55.27 | 19779198 | |
| 1246 | Phosphorylation | SPSNKNETKKGHENI CCCCCCCCCCCCCCC | 47.66 | 19795423 | |
| 1256 | Acetylation | GHENIVMKKLRVRKE CCCCCHHHHHHEECC | 37.45 | 25381059 |
| 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 PDS5_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PDS5_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 PDS5_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-538; SER-1187; SER-1231;SER-1233 AND SER-1239, 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-1231 AND SER-1233, ANDMASS SPECTROMETRY. | |
