| UniProt ID | PUF6_YEAST | |
|---|---|---|
| UniProt AC | Q04373 | |
| Protein Name | Pumilio homology domain family member 6 | |
| Gene Name | PUF6 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 656 | |
| Subcellular Localization | Bud tip. Nucleus, nucleolus. | |
| Protein Description | RNA-binding protein involved in post-transcriptional regulation. Component of the ASH1 mRNP which transports the ASH1 mRNA to the distal tip of the bud, where the ASH1 protein is translated and targeted to the daughter cell nucleus. Binds to the ASH1 3'-UTR containing the PUF consensus UUGU segment and represses its translation. This silencing of ASH1 mRNA is critical for asymmetric seggregation of ASH1 to the daughter cell nucleus.. | |
| Protein Sequence | MAPLTKKTNGKRSAKEVSHSEKKLAKKPRISIDSSDEESELSKKEDAVSSSSDDDDLDDLSTSDSEAEEEADELDISDDSEEHENENEEKEGKDKSEGGENGNHTEQRKLLKERKMQRKSGTQVQQIKSVWERLRVKTPPLPKQIREKLSNEIWELSKDCISDLVLKHDASRIVQTLVKYSSKDRREQIVDALKGKFYVLATSAYGKYLLVKLLHYGSRSSRQTIINELHGSLRKLMRHREGAYVVEDLFVLYATHEQRQQMIKEFWGSEYAVFRETHKDLTIEKVCESSIEKRNIIARNLIGTITASVEKGSTGFQILHAAMREYVKIANEKEISEMIELLHEQFAELVHTPEGSDVACTLVARANAKERKLILKALKNHAEKLIKNEYGNIVFITILNCVDDTVLVFKTFSPTVKEHLQEFIIDKFGRRPWLYILLGLDGKYFSPIVKNELLRYIELSKATSKKDPLQRRHELLSKFAPMFLSTISKDYSSILTENLGCQFIAEVLINDELYAQLNEKDQEKYQQVLNNILTTFKGDITEEEHPIHRAFSTRLLKALIQGGKWNNKEKKVIPLKNVQGLGVPFAEKLYDEIIDSSNLLEWINNADSSFTIVALYETLKDQKEGKPFLKDLRGVQSKITTDESNKGSQLLAKLLK | |
| 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 |
|---|---|---|---|---|---|
| 15 | Acetylation | TNGKRSAKEVSHSEK CCCCCCHHHCCHHHH | 60.95 | 25381059 | |
| 22 | Acetylation | KEVSHSEKKLAKKPR HHCCHHHHHHCCCCC | 56.98 | 25381059 | |
| 31 | Phosphorylation | LAKKPRISIDSSDEE HCCCCCEECCCCHHH | 22.94 | 22369663 | |
| 34 | Phosphorylation | KPRISIDSSDEESEL CCCEECCCCHHHHHH | 37.71 | 22369663 | |
| 35 | Phosphorylation | PRISIDSSDEESELS CCEECCCCHHHHHHH | 45.34 | 22369663 | |
| 39 | Phosphorylation | IDSSDEESELSKKED CCCCHHHHHHHHHHH | 41.61 | 22890988 | |
| 42 | Phosphorylation | SDEESELSKKEDAVS CHHHHHHHHHHHHHC | 37.32 | 22890988 | |
| 138 | Phosphorylation | WERLRVKTPPLPKQI HHHHCCCCCCCCHHH | 27.55 | 28889911 | |
| 148 | Acetylation | LPKQIREKLSNEIWE CCHHHHHHHHHHHHH | 47.57 | 24489116 | |
| 384 | Acetylation | ALKNHAEKLIKNEYG HHHHHHHHHHHCCCC | 57.19 | 24489116 | |
| 417 | Acetylation | KTFSPTVKEHLQEFI EECCHHHHHHHHHHH | 41.72 | 24489116 | |
| 427 | Acetylation | LQEFIIDKFGRRPWL HHHHHHHHHCCCCEE | 39.03 | 24489116 | |
| 450 | Acetylation | KYFSPIVKNELLRYI CCCCHHHHHHHHHHH | 45.48 | 22865919 | |
| 524 | Acetylation | LNEKDQEKYQQVLNN CCHHHHHHHHHHHHH | 42.60 | 24489116 | |
| 557 | Acetylation | AFSTRLLKALIQGGK HHHHHHHHHHHHCCC | 45.82 | 24489116 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 31 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 31 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 34 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 34 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| 35 | S | Phosphorylation | Kinase | CK2-FAMILY | - | GPS |
| 35 | S | Phosphorylation | Kinase | CK2 | - | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PUF6_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 PUF6_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Nonsense-mediated decay of ash1 nonsense transcripts in Saccharomycescerevisiae."; Zheng W., Finkel J.S., Landers S.M., Long R.M., Culbertson M.R.; Genetics 180:1391-1405(2008). Cited for: FUNCTION, INTERACTION WITH FUN12, PHOSPHORYLATION AT SER-31; SER-34AND SER-35, MASS SPECTROMETRY, AND MUTAGENESIS OF SER-31; SER-34 ANDSER-35. | |
| "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-34 AND SER-35, 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-34 AND SER-35, AND MASSSPECTROMETRY. | |
