UniProt ID | YSH1_YEAST | |
---|---|---|
UniProt AC | Q06224 | |
Protein Name | Endoribonuclease YSH1 | |
Gene Name | YSH1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 779 | |
Subcellular Localization | Nucleus . | |
Protein Description | Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Has endonuclease activity.. | |
Protein Sequence | MERTNTTTFKFFSLGGSNEVGRSCHILQYKGKTVMLDAGIHPAYQGLASLPFYDEFDLSKVDILLISHFHLDHAASLPYVMQRTNFQGRVFMTHPTKAIYRWLLRDFVRVTSIGSSSSSMGTKDEGLFSDEDLVDSFDKIETVDYHSTVDVNGIKFTAFHAGHVLGAAMFQIEIAGLRVLFTGDYSREVDRHLNSAEVPPLSSNVLIVESTFGTATHEPRLNRERKLTQLIHSTVMRGGRVLLPVFALGRAQEIMLILDEYWSQHADELGGGQVPIFYASNLAKKCMSVFQTYVNMMNDDIRKKFRDSQTNPFIFKNISYLRNLEDFQDFGPSVMLASPGMLQSGLSRDLLERWCPEDKNLVLITGYSIEGTMAKFIMLEPDTIPSINNPEITIPRRCQVEEISFAAHVDFQENLEFIEKISAPNIILVHGEANPMGRLKSALLSNFASLKGTDNEVHVFNPRNCVEVDLEFQGVKVAKAVGNIVNEIYKEENVEIKEEIAAKIEPIKEENEDNLDSQAEKGLVDEEEHKDIVVSGILVSDDKNFELDFLSLSDLREHHPDLSTTILRERQSVRVNCKKELIYWHILQMFGEAEVLQDDDRVTNQEPKVKEESKDNLTNTGKLILQIMGDIKLTIVNTLAVVEWTQDLMNDTVADSIIAILMNVDSAPASVKLSSHSCDDHDHNNVQSNAQGKIDEVERVKQISRLFKEQFGDCFTLFLNKDEYASNKEETITGVVTIGKSTAKIDFNNMKILECNSNPLKGRVESLLNIGGNLVTPLC | |
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 |
---|---|---|---|---|---|
365 | Phosphorylation | DKNLVLITGYSIEGT CCCEEEEEEEEEECC | 26.38 | 19795423 | |
367 | Phosphorylation | NLVLITGYSIEGTMA CEEEEEEEEEECCEE | 9.60 | 19823750 | |
368 | Phosphorylation | LVLITGYSIEGTMAK EEEEEEEEEECCEEE | 18.60 | 19823750 | |
372 | Phosphorylation | TGYSIEGTMAKFIML EEEEEECCEEEEEEE | 10.93 | 19823750 | |
517 | Phosphorylation | ENEDNLDSQAEKGLV CCCCCCHHHHHHCCC | 34.16 | 22369663 | |
521 | Acetylation | NLDSQAEKGLVDEEE CCHHHHHHCCCCHHH | 61.64 | 24489116 | |
535 | Phosphorylation | EHKDIVVSGILVSDD HHHCEEEEEEEECCC | 14.82 | 27017623 | |
540 | Phosphorylation | VVSGILVSDDKNFEL EEEEEEECCCCCEEE | 36.32 | 27017623 | |
551 | Phosphorylation | NFELDFLSLSDLREH CEEEEEECHHHHHHH | 26.31 | 28132839 | |
666 | Phosphorylation | AILMNVDSAPASVKL HHHHCCCCCCCCCCC | 31.69 | 28889911 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YSH1_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 YSH1_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-517 AND SER-666, ANDMASS 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-517, AND MASSSPECTROMETRY. |