| UniProt ID | MPT5_YEAST | |
|---|---|---|
| UniProt AC | P39016 | |
| Protein Name | Suppressor protein MPT5 | |
| Gene Name | MPT5 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 859 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | RNA-binding protein involved in post-transcriptional regulation. Negatively regulates expression of HO by binding to the 3'-UTR of HO mRNA. Predominantly binds to mRNAs encoding chromatin modifiers and spindle pole body components. Recognizes and binds to 5'-TGTAA[CT]A[AT]TA-3' in the 3'-UTR of target mRNAs. Multicopy suppressor of POP2 mutation. Required for high temperature growth.. | |
| Protein Sequence | MINNEPFPSADSASILTTSTSNNSLMSYNHQPQLSINSVQSLLEPVTPPPLGQMNNKRNHQKAHSLDLSGFNQFISSTQSPLALMNNTSTSNSANSFSPNPNAASNSTGLSASMANPPAILPLINEFDLEMDGPRRKSSHDFTVVAPSNSGVNTSSLIMETPSSSVTPAASLRNFSNSNNAASKCGVDNSSFGLSSSTSSSMVEISALPLRDLDYIKLATDQFGCRFLQKKLETPSESNMVRDLMYEQIKPFFLDLILDPFGNYLVQKLCDYLTAEQKTLLIQTIYPNVFQISINQYGTRSLQKIIDTVDNEVQIDLIIKGFSQEFTSIEQVVTLINDLNGNHVIQKCIFKFSPSKFGFIIDAIVEQNNIITISTHKHGCCVLQKLLSVCTLQQIFKISVKIVQFLPGLINDQFGNYIIQFLLDIKELDFYLLAELFNRLSNELCQLSCLKFSSNVVEKFIKKLFRIITGFIVNNNGGASQRTAVASDDVINASMNILLTTIDIFTVNLNVLIRDNFGNYALQTLLDVKNYSPLLAYNKNSNAIGQNSSSTLNYGNFCNDFSLKIGNLIVLTKELLPSIKTTSYAKKIKLKVKAYAEATGIPFTDISPQVTAMSHNNLQTINNENKNPHNKNSHNHNHNHNHNHAHNNNNNNNQKSHTRHFSLPANAYHRRSNSSVTNNFSNQYAQDQKIHSPQQIMNFNQNAYPSMGAPSFNSQTNPPLVSHNSLQNFDNRQFANLMAHPNSAAPIHSFSSSNITNVNPNVSRGFKQPGFMMNETDKINANHFSPYSNANSQNFNESFVPRMQYQTEGANWDSSLSMKSQHIGQGPYNQVNMSRNASISNMPAMNTARTSDELQFTLP | |
| 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 |
|---|---|---|---|---|---|
| 138 | Phosphorylation | MDGPRRKSSHDFTVV CCCCCCCCCCCEEEE | 30.97 | 21440633 | |
| 139 | Phosphorylation | DGPRRKSSHDFTVVA CCCCCCCCCCEEEEC | 30.06 | 20377248 | |
| 143 | Phosphorylation | RKSSHDFTVVAPSNS CCCCCCEEEECCCCC | 21.81 | 20377248 | |
| 148 | Phosphorylation | DFTVVAPSNSGVNTS CEEEECCCCCCCCCC | 33.61 | 17330950 | |
| 150 | Phosphorylation | TVVAPSNSGVNTSSL EEECCCCCCCCCCCE | 48.75 | 17330950 | |
| 154 | Phosphorylation | PSNSGVNTSSLIMET CCCCCCCCCCEEEEC | 19.79 | 30377154 | |
| 155 | Phosphorylation | SNSGVNTSSLIMETP CCCCCCCCCEEEECC | 20.24 | 19779198 | |
| 156 | Phosphorylation | NSGVNTSSLIMETPS CCCCCCCCEEEECCC | 21.63 | 19779198 | |
| 165 | Phosphorylation | IMETPSSSVTPAASL EEECCCCCCCCHHHH | 34.06 | 19779198 | |
| 176 | Phosphorylation | AASLRNFSNSNNAAS HHHHCCCCCCCCHHH | 42.78 | 21082442 | |
| 183 | Phosphorylation | SNSNNAASKCGVDNS CCCCCHHHHCCCCCC | 26.52 | 28889911 | |
| 278 | Ubiquitination | DYLTAEQKTLLIQTI HHCCHHHHHHHEEEC | 32.42 | 17644757 | |
| 539 | Ubiquitination | SPLLAYNKNSNAIGQ CCCEEECCCCCCCCC | 49.42 | 17644757 | |
| 564 | Ubiquitination | FCNDFSLKIGNLIVL CCCCCCEEECCEEEE | 47.58 | 17644757 | |
| 573 | Ubiquitination | GNLIVLTKELLPSIK CCEEEECHHHHCCCC | 42.05 | 17644757 | |
| 662 | Phosphorylation | KSHTRHFSLPANAYH CCCCCCCCCCHHHCH | 27.58 | 17330950 | |
| 668 | Phosphorylation | FSLPANAYHRRSNSS CCCCHHHCHHCCCCC | 8.82 | 29688323 | |
| 672 | Phosphorylation | ANAYHRRSNSSVTNN HHHCHHCCCCCCCCC | 40.81 | 19684113 | |
| 674 | Phosphorylation | AYHRRSNSSVTNNFS HCHHCCCCCCCCCCC | 27.68 | 28152593 | |
| 675 | Phosphorylation | YHRRSNSSVTNNFSN CHHCCCCCCCCCCCH | 36.89 | 19684113 | |
| 677 | Phosphorylation | RRSNSSVTNNFSNQY HCCCCCCCCCCCHHH | 26.79 | 19684113 | |
| 689 | Ubiquitination | NQYAQDQKIHSPQQI HHHHHHCCCCCHHHH | 51.15 | 17644757 | |
| 743 | Phosphorylation | NLMAHPNSAAPIHSF HHHHCCCCCCCCCCC | 30.20 | 22369663 | |
| 749 | Phosphorylation | NSAAPIHSFSSSNIT CCCCCCCCCCCCCCC | 27.78 | 22369663 | |
| 751 | Phosphorylation | AAPIHSFSSSNITNV CCCCCCCCCCCCCCC | 35.55 | 21440633 | |
| 752 | Phosphorylation | APIHSFSSSNITNVN CCCCCCCCCCCCCCC | 25.95 | 22369663 | |
| 753 | Phosphorylation | PIHSFSSSNITNVNP CCCCCCCCCCCCCCC | 30.93 | 22369663 | |
| 756 | Phosphorylation | SFSSSNITNVNPNVS CCCCCCCCCCCCCCC | 37.05 | 22369663 | |
| 763 | Phosphorylation | TNVNPNVSRGFKQPG CCCCCCCCCCCCCCC | 33.07 | 22369663 | |
| 778 | Ubiquitination | FMMNETDKINANHFS CCCCCCCCCCCCCCC | 45.33 | 17644757 | |
| 819 | Ubiquitination | WDSSLSMKSQHIGQG CCCCCCHHHCCCCCC | 43.52 | 17644757 | |
| 820 | Phosphorylation | DSSLSMKSQHIGQGP CCCCCHHHCCCCCCC | 20.53 | 28889911 | |
| 834 | Phosphorylation | PYNQVNMSRNASISN CCCCCCCCCCCCCCC | 19.72 | 22369663 | |
| 838 | Phosphorylation | VNMSRNASISNMPAM CCCCCCCCCCCCCCC | 30.05 | 22369663 | |
| 840 | Phosphorylation | MSRNASISNMPAMNT CCCCCCCCCCCCCCC | 25.28 | 24909858 | |
| 850 | Phosphorylation | PAMNTARTSDELQFT CCCCCCCCCCCCCCC | 37.76 | 30377154 | |
| 851 | Phosphorylation | AMNTARTSDELQFTL CCCCCCCCCCCCCCC | 24.43 | 30377154 |
| 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 MPT5_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MPT5_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 MPT5_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-138; SER-139; SER-176;SER-662; SER-675; SER-749; SER-753; THR-756 AND SER-838, 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-834, 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-662, AND MASSSPECTROMETRY. | |
