UniProt ID | NAF1_YEAST | |
---|---|---|
UniProt AC | P53919 | |
Protein Name | H/ACA ribonucleoprotein complex non-core subunit NAF1 | |
Gene Name | NAF1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 492 | |
Subcellular Localization | Nucleus . Mostly present in the nucleoplasm. Absent from the nucleolus. | |
Protein Description | RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disappears during maturation of the complex and is replaced by GAR1 to yield mature H/ACA snoRNPs complex. Acts as a competitive binder for CBF5 probably required to prevent non-cognate RNAs from being loaded during transport of the particle by inducing a non-productive conformation of CBF5.. | |
Protein Sequence | MSDDLFSKALENPDQDLNVELPKDDVDLGLLGDGGNERKTDEPVADAERSTGLGSGSSESESDSGSDSDSDSGSSGSEDDSADQDVEGEDEGGDAIENEDEDEDPSPSGPILSKNEILEETVPELPEDYEISEKTIITPIGVLKSAFENNIIIHATMSGEKRVLKEGSIFCLEDRTLIGMLTEVFGPLQNPFYRIKLPDSKKNLFDELKVRLGEKAFIVTPDAHWIDTFELKRNKGTDASNGYDEELPEEEQEFSDDEKEALFKKMKKQQRQRKKRDNRKLANDSDNVKVKRARQPKANSLPKLVPPLGMSSNAPMQHGYKSRNARENIKRESSATSNRNGSSPVPITQHHQQQFSANNYPFPQQPNGMPYPPYSPFPQPTNFQYPPPPFGQATPAQFSNTVPYGSLPPAYNNMSPPTQQSFMPMTQSQPPLPYGVPPMNQMQNPMYIQPPPQAPPQGNGNFQQVMELHQILLQQQQQQHQYQHQHQQDPRT | |
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 |
---|---|---|---|---|---|
237 | Phosphorylation | ELKRNKGTDASNGYD EHHHCCCCCCCCCCC | 29.96 | 26447709 | |
240 | Phosphorylation | RNKGTDASNGYDEEL HCCCCCCCCCCCCCC | 33.33 | 26447709 | |
243 | Phosphorylation | GTDASNGYDEELPEE CCCCCCCCCCCCCHH | 25.16 | 26447709 | |
255 | Phosphorylation | PEEEQEFSDDEKEAL CHHHHCCCHHHHHHH | 43.32 | 22369663 | |
300 | Phosphorylation | ARQPKANSLPKLVPP HCCCCCCCCCCCCCC | 51.40 | 27017623 | |
312 | Phosphorylation | VPPLGMSSNAPMQHG CCCCCCCCCCCCCCC | 28.28 | 27017623 | |
320 | Phosphorylation | NAPMQHGYKSRNARE CCCCCCCCCCHHHHH | 12.03 | 27017623 | |
322 | Phosphorylation | PMQHGYKSRNARENI CCCCCCCCHHHHHHH | 23.45 | 27017623 | |
334 | Phosphorylation | ENIKRESSATSNRNG HHHHHHHHCCCCCCC | 30.71 | 25752575 | |
336 | Phosphorylation | IKRESSATSNRNGSS HHHHHHCCCCCCCCC | 28.60 | 28889911 |
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 NAF1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NAF1_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 NAF1_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-255, AND MASSSPECTROMETRY. | |
"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-255, AND MASSSPECTROMETRY. | |
"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-255, AND MASSSPECTROMETRY. |