| UniProt ID | PSH1_YEAST | |
|---|---|---|
| UniProt AC | Q12161 | |
| Protein Name | RING finger protein PSH1 | |
| Gene Name | PSH1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 406 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | ||
| Protein Sequence | MGDELHNRLLHQNDGTKDAILYKIIESLVCSICHDYMFVPMMTPCGHNYCYGCLNTWFASNTQKELACPQCRSDITTIPALNTTLQQYLSFILEKLRDQNDESFKKLLTTKTKEENDYKNDKEKDTLFDKVFKNSALAVADDSDDGITRCSNCHWELDPDEVEDGNVCPHCNARIRNYAGGRDEFDEEEYSEGELDEIRESMRRRRENRFASTNPFANRDDVSSEDDDSSEEEPMREHIPLGRWARSHNRSIAVDAVDDEDDEEEDEEEEEEMDSDLKDFIEDDEDDEDEDGSRRNLVLSALKNRHVIITDDEEEEQRRHATEEEDRDSDFYEHNDDGFVSGDSLDEDQKEVTRIQSSSDSEDRSLSYSGSSDVKDNNDDNTEELDDPQPKRQKRFRVVLGDSDDE | |
| 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 |
|---|---|---|---|---|---|
| 135 | Phosphorylation | FDKVFKNSALAVADD HHHHHHCCCEEEECC | 25.83 | 21126336 | |
| 143 | Phosphorylation | ALAVADDSDDGITRC CEEEECCCCCCCCCC | 37.84 | 22369663 | |
| 148 | Phosphorylation | DDSDDGITRCSNCHW CCCCCCCCCCCCCCE | 31.02 | 22890988 | |
| 178 | Phosphorylation | CNARIRNYAGGRDEF CCHHHHHCCCCCCCC | 9.22 | 27017623 | |
| 190 | Phosphorylation | DEFDEEEYSEGELDE CCCCHHHHCCCCHHH | 18.46 | 22369663 | |
| 191 | Phosphorylation | EFDEEEYSEGELDEI CCCHHHHCCCCHHHH | 42.26 | 22369663 | |
| 201 | Phosphorylation | ELDEIRESMRRRREN CHHHHHHHHHHHHHH | 14.03 | 22369663 | |
| 275 | Phosphorylation | EEEEEMDSDLKDFIE HHHHHHHHHHHHHHH | 43.46 | 22369663 | |
| 293 | Phosphorylation | DDEDEDGSRRNLVLS CCCCCCCCHHHHHHH | 40.15 | 22369663 | |
| 300 | Phosphorylation | SRRNLVLSALKNRHV CHHHHHHHHHHCCCE | 24.87 | 22369663 | |
| 303 | Acetylation | NLVLSALKNRHVIIT HHHHHHHHCCCEEEC | 52.21 | 25381059 | |
| 310 | Phosphorylation | KNRHVIITDDEEEEQ HCCCEEECCCHHHHH | 26.69 | 22369663 | |
| 322 | Phosphorylation | EEQRRHATEEEDRDS HHHHHHCCCCHHCCC | 37.49 | 28889911 | |
| 329 | Phosphorylation | TEEEDRDSDFYEHND CCCHHCCCCCHHCCC | 30.43 | 17330950 | |
| 332 | Phosphorylation | EDRDSDFYEHNDDGF HHCCCCCHHCCCCCC | 22.67 | 17330950 | |
| 341 | Phosphorylation | HNDDGFVSGDSLDED CCCCCCCCCCCCCCC | 34.32 | 28889911 | |
| 344 | Phosphorylation | DGFVSGDSLDEDQKE CCCCCCCCCCCCHHH | 41.04 | 17330950 | |
| 353 | Phosphorylation | DEDQKEVTRIQSSSD CCCHHHHHEECCCCC | 24.13 | 24961812 | |
| 357 | Phosphorylation | KEVTRIQSSSDSEDR HHHHEECCCCCCCCC | 29.45 | 21440633 | |
| 358 | Phosphorylation | EVTRIQSSSDSEDRS HHHEECCCCCCCCCC | 23.07 | 28889911 | |
| 359 | Phosphorylation | VTRIQSSSDSEDRSL HHEECCCCCCCCCCC | 50.86 | 21440633 | |
| 361 | Phosphorylation | RIQSSSDSEDRSLSY EECCCCCCCCCCCCC | 43.26 | 24961812 | |
| 365 | Phosphorylation | SSDSEDRSLSYSGSS CCCCCCCCCCCCCCC | 33.71 | 24961812 | |
| 367 | Phosphorylation | DSEDRSLSYSGSSDV CCCCCCCCCCCCCCC | 20.64 | 24961812 | |
| 369 | Phosphorylation | EDRSLSYSGSSDVKD CCCCCCCCCCCCCCC | 28.90 | 24961812 | |
| 371 | Phosphorylation | RSLSYSGSSDVKDNN CCCCCCCCCCCCCCC | 19.88 | 24961812 | |
| 382 | Phosphorylation | KDNNDDNTEELDDPQ CCCCCCCCCCCCCCC | 37.52 | 22890988 | |
| 403 | Phosphorylation | FRVVLGDSDDE---- EEEECCCCCCC---- | 45.20 | 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 PSH1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PSH1_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 PSH1_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-143; SER-191 ANDTHR-310, 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-191 AND THR-310, 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-143; THR-310 ANDSER-403, AND MASS SPECTROMETRY. | |