UniProt ID | HAS1_YEAST | |
---|---|---|
UniProt AC | Q03532 | |
Protein Name | ATP-dependent RNA helicase HAS1 | |
Gene Name | HAS1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 505 | |
Subcellular Localization | Nucleus, nucleolus . | |
Protein Description | ATP-dependent RNA helicase involved in 40S ribosomal subunit biogenesis. Required for the processing and cleavage of 35S pre-rRNA at sites A0, A1, and A2, leading to mature 18S rRNA.. | |
Protein Sequence | MATPSNKRSRDSESTEEPVVDEKSTSKQNNAAPEGEQTTCVEKFEELKLSQPTLKAIEKMGFTTMTSVQARTIPPLLAGRDVLGAAKTGSGKTLAFLIPAIELLHSLKFKPRNGTGIIVITPTRELALQIFGVARELMEFHSQTFGIVIGGANRRQEAEKLMKGVNMLIATPGRLLDHLQNTKGFVFKNLKALIIDEADRILEIGFEDEMRQIIKILPNEDRQSMLFSATQTTKVEDLARISLRPGPLFINVVPETDNSTADGLEQGYVVCDSDKRFLLLFSFLKRNQKKKIIVFLSSCNSVKYYAELLNYIDLPVLELHGKQKQQKRTNTFFEFCNAERGILICTDVAARGLDIPAVDWIIQFDPPDDPRDYIHRVGRTARGTKGKGKSLMFLTPNELGFLRYLKASKVPLNEYEFPENKIANVQSQLEKLIKSNYYLHQTAKDGYRSYLQAYASHSLKTVYQIDKLDLAKVAKSYGFPVPPKVNITIGASGKTPNTKRRKTHK | |
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 |
---|---|---|---|---|---|
9 | Phosphorylation | ATPSNKRSRDSESTE CCCCCCCCCCCCCCC | 41.89 | 29136822 | |
12 | Phosphorylation | SNKRSRDSESTEEPV CCCCCCCCCCCCCCC | 32.13 | 25521595 | |
14 | Phosphorylation | KRSRDSESTEEPVVD CCCCCCCCCCCCCCC | 45.10 | 19823750 | |
15 | Phosphorylation | RSRDSESTEEPVVDE CCCCCCCCCCCCCCC | 40.07 | 25752575 | |
24 | Phosphorylation | EPVVDEKSTSKQNNA CCCCCCCCCCCCCCC | 35.55 | 19779198 | |
26 | Phosphorylation | VVDEKSTSKQNNAAP CCCCCCCCCCCCCCC | 39.06 | 30377154 | |
43 | Ubiquitination | EQTTCVEKFEELKLS CCCCHHHHHHHHCCC | 37.36 | 23749301 | |
48 | Acetylation | VEKFEELKLSQPTLK HHHHHHHCCCCHHHH | 49.74 | 22865919 | |
55 | Ubiquitination | KLSQPTLKAIEKMGF CCCCHHHHHHHHCCC | 50.20 | 23749301 | |
87 | Ubiquitination | RDVLGAAKTGSGKTL CCEECCCCCCCCHHH | 53.54 | 23749301 | |
115 | Phosphorylation | KFKPRNGTGIIVITP CCCCCCCCCEEEEEC | 28.85 | 27017623 | |
121 | Phosphorylation | GTGIIVITPTRELAL CCCEEEEECCHHHHH | 14.02 | 27017623 | |
123 | Phosphorylation | GIIVITPTRELALQI CEEEEECCHHHHHHH | 28.29 | 27017623 | |
188 | Acetylation | NTKGFVFKNLKALII HCCCHHHCCCEEEEE | 56.95 | 24489116 | |
215 | Acetylation | DEMRQIIKILPNEDR HHHHHHHHHCCCCCH | 39.56 | 24489116 | |
275 | Ubiquitination | YVVCDSDKRFLLLFS EEEECCCHHHHHHHH | 49.34 | 17644757 | |
322 | Acetylation | PVLELHGKQKQQKRT HHHHHCCCHHHHHHH | 43.50 | 25381059 | |
389 | Acetylation | RGTKGKGKSLMFLTP CCCCCCCCCCEEECH | 43.85 | 24489116 | |
421 | Acetylation | EYEFPENKIANVQSQ CCCCCCHHHHHHHHH | 41.35 | 24489116 | |
427 | Phosphorylation | NKIANVQSQLEKLIK HHHHHHHHHHHHHHH | 32.24 | 19823750 | |
431 | Acetylation | NVQSQLEKLIKSNYY HHHHHHHHHHHCCCC | 65.19 | 24489116 | |
431 | Ubiquitination | NVQSQLEKLIKSNYY HHHHHHHHHHHCCCC | 65.19 | 24961812 | |
434 | Acetylation | SQLEKLIKSNYYLHQ HHHHHHHHCCCCHHH | 42.98 | 24489116 | |
444 | Succinylation | YYLHQTAKDGYRSYL CCHHHHHHHHHHHHH | 55.89 | 23954790 | |
444 | Methylation | YYLHQTAKDGYRSYL CCHHHHHHHHHHHHH | 55.89 | 20137074 | |
444 | Acetylation | YYLHQTAKDGYRSYL CCHHHHHHHHHHHHH | 55.89 | 24489116 | |
458 | Phosphorylation | LQAYASHSLKTVYQI HHHHHHCCCCEEEEE | 29.12 | 30377154 | |
460 | Ubiquitination | AYASHSLKTVYQIDK HHHHCCCCEEEEECH | 38.67 | 17644757 | |
467 | Acetylation | KTVYQIDKLDLAKVA CEEEEECHHHHHHHH | 45.59 | 24489116 | |
467 | Ubiquitination | KTVYQIDKLDLAKVA CEEEEECHHHHHHHH | 45.59 | 17644757 | |
472 | Acetylation | IDKLDLAKVAKSYGF ECHHHHHHHHHHHCC | 50.45 | 24489116 | |
472 | Ubiquitination | IDKLDLAKVAKSYGF ECHHHHHHHHHHHCC | 50.45 | 17644757 | |
492 | Phosphorylation | VNITIGASGKTPNTK EEEEECCCCCCCCCC | 35.29 | 27017623 | |
494 | Acetylation | ITIGASGKTPNTKRR EEECCCCCCCCCCCC | 59.31 | 22865919 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of HAS1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of HAS1_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 HAS1_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-12 AND SER-14, AND MASSSPECTROMETRY. | |
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY. |