| UniProt ID | PWP2_YEAST | |
|---|---|---|
| UniProt AC | P25635 | |
| Protein Name | Periodic tryptophan protein 2 | |
| Gene Name | PWP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 923 | |
| Subcellular Localization | Nucleus, nucleolus . | |
| Protein Description | Required for bud-site selection and cell separation. Also involved in nucleolar processing of pre-18S ribosomal RNA.. | |
| Protein Sequence | MKSDFKFSNLLGTVYRQGNITFSDDGKQLLSPVGNRVSVFDLINNKSFTFEYEHRKNIAAIDLNKQGTLLISIDEDGRAILVNFKARNVLHHFNFKEKCSAVKFSPDGRLFALASGRFLQIWKTPDVNKDRQFAPFVRHRVHAGHFQDITSLTWSQDSRFILTTSKDLSAKIWSVDSEEKNLAATTFNGHRDYVMGAFFSHDQEKIYTVSKDGAVFVWEFTKRPSDDDDNESEDDDKQEEVDISKYSWRITKKHFFYANQAKVKCVTFHPATRLLAVGFTSGEFRLYDLPDFTLIQQLSMGQNPVNTVSVNQTGEWLAFGSSKLGQLLVYEWQSESYILKQQGHFDSTNSLAYSPDGSRVVTASEDGKIKVWDITSGFCLATFEEHTSSVTAVQFAKRGQVMFSSSLDGTVRAWDLIRYRNFRTFTGTERIQFNCLAVDPSGEVVCAGSLDNFDIHVWSVQTGQLLDALSGHEGPVSCLSFSQENSVLASASWDKTIRIWSIFGRSQQVEPIEVYSDVLALSMRPDGKEVAVSTLKGQISIFNIEDAKQVGNIDCRKDIISGRFNQDRFTAKNSERSKFFTTIHYSFDGMAIVAGGNNNSICLYDVPNEVLLKRFIVSRNMALNGTLEFLNSKKMTEAGSLDLIDDAGENSDLEDRIDNSLPGSQRGGDLSTRKMRPEVRVTSVQFSPTANAFAAASTEGLLIYSTNDTILFDPFDLDVDVTPHSTVEALREKQFLNALVMAFRLNEEYLINKVYEAIPIKEIPLVASNIPAIYLPRILKFIGDFAIESQHIEFNLIWIKALLSASGGYINEHKYLFSTAMRSIQRFIVRVAKEVVNTTTDNKYTYRFLVSTDGSMEDGAADDDEVLLKDDADEDNEENEENDVVMESDDEEGWIGFNGKDNKLPLSNENDSSDEEENEKELP | |
| 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 |
|---|---|---|---|---|---|
| 180 | Acetylation | WSVDSEEKNLAATTF EECCCCCCCEEEEEE | 53.89 | 24489116 | |
| 225 | Phosphorylation | WEFTKRPSDDDDNES EEEECCCCCCCCCCC | 58.67 | 22369663 | |
| 232 | Phosphorylation | SDDDDNESEDDDKQE CCCCCCCCCCCHHHH | 53.21 | 22369663 | |
| 244 | Phosphorylation | KQEEVDISKYSWRIT HHHHEEHHHHCEEEE | 22.52 | 22369663 | |
| 522 | Phosphorylation | YSDVLALSMRPDGKE ECCEEEEEECCCCCE | 13.72 | 30377154 | |
| 626 | Phosphorylation | RNMALNGTLEFLNSK CCHHHCCHHHHHHCC | 23.26 | 30377154 | |
| 632 | Phosphorylation | GTLEFLNSKKMTEAG CHHHHHHCCCCCCCC | 35.48 | 30377154 | |
| 636 | Phosphorylation | FLNSKKMTEAGSLDL HHHCCCCCCCCCCCC | 31.40 | 22369663 | |
| 640 | Phosphorylation | KKMTEAGSLDLIDDA CCCCCCCCCCCCCCC | 26.26 | 22369663 | |
| 651 | Phosphorylation | IDDAGENSDLEDRID CCCCCCCCCHHHHHH | 38.99 | 22369663 | |
| 660 | Phosphorylation | LEDRIDNSLPGSQRG HHHHHHHCCCCCCCC | 31.99 | 22369663 | |
| 664 | Phosphorylation | IDNSLPGSQRGGDLS HHHCCCCCCCCCCCC | 18.11 | 22369663 | |
| 833 | Ubiquitination | RFIVRVAKEVVNTTT HHHHHHHHHHHCCCC | 48.46 | 23749301 | |
| 843 | Ubiquitination | VNTTTDNKYTYRFLV HCCCCCCCEEEEEEE | 41.60 | 23749301 | |
| 888 | Phosphorylation | ENDVVMESDDEEGWI CCCCEECCCCCCCCE | 32.06 | 28889911 | |
| 907 | Phosphorylation | KDNKLPLSNENDSSD CCCCCCCCCCCCCCC | 39.91 | 22369663 | |
| 912 | Phosphorylation | PLSNENDSSDEEENE CCCCCCCCCCHHHHH | 51.80 | 22369663 | |
| 913 | Phosphorylation | LSNENDSSDEEENEK CCCCCCCCCHHHHHC | 52.48 | 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 PWP2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PWP2_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 PWP2_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-232; SER-651; SER-660;SER-664; SER-912 AND SER-913, 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-232 AND SER-651, ANDMASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-651; SER-912AND SER-913, AND MASS SPECTROMETRY. | |
