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 | ||
|
* 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 | ||||||
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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. |