UniProt ID | PUF2_YEAST | |
---|---|---|
UniProt AC | Q12221 | |
Protein Name | mRNA-binding protein PUF2 | |
Gene Name | PUF2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1075 | |
Subcellular Localization | Cytoplasm . Localizes to foci enriched near the periphery of the cell. | |
Protein Description | RNA-binding protein involved in post-transcriptional regulation. Negatively regulates expression of COX17 by binding to the 3'-UTR of COX17 mRNA. Promotes decay of COX17 mRNA by enhancing its rate of deadenylation and subsequent turnover. Predominantly binds to mRNAs encoding membrane-associated proteins with roles in transmembrane transport and vesicular trafficking.. | |
Protein Sequence | MDNKRLYNGNLSNIPEVIDPGITIPIYEEDIRNDTRMNTNARSVRVSDKRGRSSSTSPQKIGSYRTRAGRFSDTLTNLLPSISAKLHHSKKSTPVVVVPPTSSTPDSLNSTTYAPRVSSDSFTVATPLSLQSTTTRTRTRNNTVSSQITASSSLTTDVGNATSANIWSANAESNTSSSPLFDYPLATSYFEPLTRFKSTDNYTLPQTAQLNSFLEKNGNPNIWSSAGNSNTDHLNTPIVNRQRSQSQSTTNRVYTDAPYYQQPAQNYQVQVPPRVPKSTSISPVILDDVDPASINWITANQKVPLVNQISALLPTNTISISNVFPLQPTQQHQQNAVNLTSTSLATLCSQYGKVLSARTLRGLNMALVEFSTVESAICALEALQGKELSKVGAPSTVSFARVLPMYEQPLNVNGFNNTPKQPLLQEQLNHGVLNYQLQQSLQQPELQQQPTSFNQPNLTYCNPTQNLSHLQLSSNENEPYPFPLPPPSLSDSKKDILHTISSFKLEYDHLELNHLLQNALKNKGVSDTNYFGPLPEHNSKVPKRKDTFDAPKLRELRKQFDSNSLSTIEMEQLAIVMLDQLPELSSDYLGNTVIQKLFENSSNIIRDIMLRKCNKYLTSMGVHKNGTWVCQKIIKMANTPRQINLVTSGVSDYCTPLFNDQFGNYVIQGILKFGFPWNSFIFESVLSHFWTIVQNRYGSRAVRACLEADSIITQCQLLTITSLIIVLSPYLATDTNGTLLITWLLDTCTLPNKNLILCDKLVNKNLVKLCCHKLGSLTVLKILNLRGGEEEALSKNKIIHAIFDGPISSDSILFQILDEGNYGPTFIYKVLTSRILDNSVRDEAITKIRQLILNSNINLQSRQLLEEVGLSSAGISPKQSSKNHRKQHPQGFHSPGRARGVSVSSVRSSNSRHNSVIQMNNAGPTPALNFNPAPMSEINSYFNNQQVVYSGNQNQNQNGNSNGLDELNSQFDSFRIANGTNLSLPIVNLPNVSNNNNNYNNSGYSSQMNPLSRSVSHNNNNNTNNYNNNDNDNNNNNNNNNNNNNNNNNNNNNSNNSNNNNNNDTSLYRYRSYGY | |
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 |
---|---|---|---|---|---|
53 | Phosphorylation | VSDKRGRSSSTSPQK CCCCCCCCCCCCCHH | 31.31 | 27717283 | |
54 | Phosphorylation | SDKRGRSSSTSPQKI CCCCCCCCCCCCHHC | 35.95 | 27717283 | |
55 | Phosphorylation | DKRGRSSSTSPQKIG CCCCCCCCCCCHHCC | 33.86 | 21440633 | |
56 | Phosphorylation | KRGRSSSTSPQKIGS CCCCCCCCCCHHCCC | 46.50 | 23749301 | |
57 | Phosphorylation | RGRSSSTSPQKIGSY CCCCCCCCCHHCCCH | 27.55 | 21440633 | |
72 | Phosphorylation | RTRAGRFSDTLTNLL HHCCCCCHHHHHHHH | 28.46 | 28889911 | |
81 | Phosphorylation | TLTNLLPSISAKLHH HHHHHHHHHHHHHCC | 29.19 | 27017623 | |
83 | Phosphorylation | TNLLPSISAKLHHSK HHHHHHHHHHHCCCC | 24.56 | 27017623 | |
101 | Phosphorylation | PVVVVPPTSSTPDSL CEEEECCCCCCCCCC | 29.28 | 19779198 | |
102 | Phosphorylation | VVVVPPTSSTPDSLN EEEECCCCCCCCCCC | 37.68 | 22369663 | |
103 | Phosphorylation | VVVPPTSSTPDSLNS EEECCCCCCCCCCCC | 46.57 | 22369663 | |
104 | Phosphorylation | VVPPTSSTPDSLNST EECCCCCCCCCCCCC | 30.77 | 22369663 | |
107 | Phosphorylation | PTSSTPDSLNSTTYA CCCCCCCCCCCCCCC | 30.56 | 22369663 | |
110 | Phosphorylation | STPDSLNSTTYAPRV CCCCCCCCCCCCCCC | 27.67 | 22369663 | |
111 | Phosphorylation | TPDSLNSTTYAPRVS CCCCCCCCCCCCCCC | 23.81 | 22369663 | |
112 | Phosphorylation | PDSLNSTTYAPRVSS CCCCCCCCCCCCCCC | 19.94 | 22369663 | |
113 | Phosphorylation | DSLNSTTYAPRVSSD CCCCCCCCCCCCCCC | 18.07 | 19779198 | |
118 | Phosphorylation | TTYAPRVSSDSFTVA CCCCCCCCCCCEEEE | 29.70 | 28152593 | |
119 | Phosphorylation | TYAPRVSSDSFTVAT CCCCCCCCCCEEEEE | 34.12 | 19779198 | |
121 | Phosphorylation | APRVSSDSFTVATPL CCCCCCCCEEEEECC | 25.43 | 28889911 | |
123 | Phosphorylation | RVSSDSFTVATPLSL CCCCCCEEEEECCEE | 17.12 | 21440633 | |
126 | Phosphorylation | SDSFTVATPLSLQST CCCEEEEECCEECCC | 22.04 | 28152593 | |
198 | Phosphorylation | EPLTRFKSTDNYTLP CCCCCCCCCCCCCCC | 37.98 | 22369663 | |
199 | Phosphorylation | PLTRFKSTDNYTLPQ CCCCCCCCCCCCCCC | 28.93 | 22369663 | |
202 | Phosphorylation | RFKSTDNYTLPQTAQ CCCCCCCCCCCCHHH | 16.68 | 22369663 | |
203 | Phosphorylation | FKSTDNYTLPQTAQL CCCCCCCCCCCHHHH | 37.91 | 22369663 | |
207 | Phosphorylation | DNYTLPQTAQLNSFL CCCCCCCHHHHHHHH | 17.90 | 22369663 | |
225 | Phosphorylation | GNPNIWSSAGNSNTD CCCCCHHCCCCCCCC | 25.79 | 23749301 | |
236 | Phosphorylation | SNTDHLNTPIVNRQR CCCCCCCCHHHCCCC | 22.28 | 23749301 | |
246 | Phosphorylation | VNRQRSQSQSTTNRV HCCCCCCCCCCCCCE | 27.61 | 27214570 | |
249 | Phosphorylation | QRSQSQSTTNRVYTD CCCCCCCCCCCEECC | 22.06 | 21440633 | |
278 | Phosphorylation | VPPRVPKSTSISPVI CCCCCCCCCCCCCEE | 22.71 | 15665377 | |
280 | Phosphorylation | PRVPKSTSISPVILD CCCCCCCCCCCEECC | 28.32 | 21440633 | |
282 | Phosphorylation | VPKSTSISPVILDDV CCCCCCCCCEECCCC | 16.94 | 21551504 | |
635 | Ubiquitination | WVCQKIIKMANTPRQ HHHHHHHHHCCCCHH | 35.12 | 23749301 | |
833 | Phosphorylation | FIYKVLTSRILDNSV HHHHHHHHHHHCCCC | 17.11 | 27017623 | |
839 | Phosphorylation | TSRILDNSVRDEAIT HHHHHCCCCCHHHHH | 20.42 | 30377154 | |
871 | Phosphorylation | LLEEVGLSSAGISPK HHHHHCCCCCCCCCC | 16.53 | 22369663 | |
872 | Phosphorylation | LEEVGLSSAGISPKQ HHHHCCCCCCCCCCC | 35.24 | 22369663 | |
876 | Phosphorylation | GLSSAGISPKQSSKN CCCCCCCCCCCCCCC | 25.73 | 22369663 | |
894 | Phosphorylation | QHPQGFHSPGRARGV HCCCCCCCCCCCCCC | 27.13 | 22369663 | |
902 | Phosphorylation | PGRARGVSVSSVRSS CCCCCCCCHHHHCCC | 21.07 | 21082442 | |
904 | Phosphorylation | RARGVSVSSVRSSNS CCCCCCHHHHCCCCC | 18.66 | 19684113 | |
905 | Phosphorylation | ARGVSVSSVRSSNSR CCCCCHHHHCCCCCC | 21.28 | 19684113 | |
908 | Phosphorylation | VSVSSVRSSNSRHNS CCHHHHCCCCCCCCC | 31.54 | 19684113 | |
909 | Phosphorylation | SVSSVRSSNSRHNSV CHHHHCCCCCCCCCE | 28.41 | 30377154 | |
911 | Phosphorylation | SSVRSSNSRHNSVIQ HHHCCCCCCCCCEEE | 36.54 | 23749301 | |
980 | Phosphorylation | SFRIANGTNLSLPIV EEEECCCCCCCCEEE | 32.56 | 29136822 | |
993 | Phosphorylation | IVNLPNVSNNNNNYN EEECCCCCCCCCCCC | 40.24 | 29136822 | |
999 | Phosphorylation | VSNNNNNYNNSGYSS CCCCCCCCCCCCHHH | 20.18 | 29136822 | |
1002 | Phosphorylation | NNNNYNNSGYSSQMN CCCCCCCCCHHHCCC | 35.15 | 29136822 | |
1004 | Phosphorylation | NNYNNSGYSSQMNPL CCCCCCCHHHCCCCC | 12.64 | 29136822 | |
1005 | Phosphorylation | NYNNSGYSSQMNPLS CCCCCCHHHCCCCCC | 20.02 | 29136822 | |
1006 | Phosphorylation | YNNSGYSSQMNPLSR CCCCCHHHCCCCCCC | 25.60 | 29136822 | |
1012 | Phosphorylation | SSQMNPLSRSVSHNN HHCCCCCCCCCCCCC | 24.62 | 29136822 | |
1072 | Phosphorylation | TSLYRYRSYGY---- CHHHHHHCCCC---- | 17.61 | 21440633 |
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 PUF2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PUF2_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 PUF2_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 THR-199; SER-278; SER-280;SER-872 AND SER-876, 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-198, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198 AND SER-876, ANDMASS SPECTROMETRY. |