| UniProt ID | UBP12_YEAST | |
|---|---|---|
| UniProt AC | P39538 | |
| Protein Name | Ubiquitin carboxyl-terminal hydrolase 12 | |
| Gene Name | UBP12 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1254 | |
| Subcellular Localization | ||
| Protein Description | Ubiquitin carboxyl-terminal hydrolase that recognizes ubiquitin chains that stabilize FZO1 and promote mitochondrial fusion. UBP12 deubiquitylates FZO1 only after oligomerization.. | |
| Protein Sequence | MGSSDVSSRECSLVYNEDPDFTDGTTPCDRLGVDLMNVLDDKDEIKQESVPVSDREIEDTESDASAVSSFASANELIAEPHAASETNLGTNGQDGRNVLEQQRDVVARLIEENKETQKEGDKVCIVPKVWYDKFFDPDVTDPEDIGPINTRMICRDFENFVLEDYNRCPYLSIAEPVFNFLSEIYGMTSGSYPVVTNLVINQTTGELETEYNKWFFRLHYLTEKQDGRKRRHGQDDSIMYLSMSALNLVRDLVEKSMNLFFEKADHLDVNAVDFKIWFVSEGSDIATDSNVSTFLNSSYEITPLQFLELPIKKLLIPDMFENRLDKITSNPSDLVIEIKPIEGNHHWPSNYFAYNKLEPASGTTGLVNLGNTCYMNSALQCLVHIPQLRDYFLYDGYEDEINEENPLGYHGYVARAFSDLVQKLFQNRMSIMQRNAAFPPSMFKSTIGHFNSMFSGYMQQDSQEFLAFLLDSLHEDLNRIIKKEYTEKPSLSPGDDVNDWNVVKKLADDTWEMHLKRNCSVITDLFVGMYKSTLYCPECQNVSITFDPYNDVTLPLPVDTVWDKTIKIFPMNSPPLLLEVELSKSSTYMDLKNYVGKMSGLDPNTLFGCEIFSNQIYVNYESTESNAQFLTLQELIKPADDVIFYELPVTNDNEVIVPVLNTRIEKGYKNAMLFGVPFFITLKEDELNNPGAIRMKLQNRFVHLSGGYIPFPEPVGNRTDFADAFPLLVEKYPDVEFEQYKDILQYTSIKVTDKDKSFFSIKILSVEKEQQFASNNRTGPNFWTPISQLNLDKATDIDDKLEDVVKDIYNYSSLVDCAEGVLMQVDDEGDTEGSEAKNFSKPFQSGDDEENKETVTNNENVNNTNDRDEDMELTDDVEEDASTEPELTDKPEALDKIKDSLTSTPFAILSMNDIIVCEWSELGSNEAFSDDKIYNWENPATLPNKELENAKLERSNAKERTITLDDCLQLFSKPEILGLTDSWYCPTCKEHRQATKQIQLWNTPDILLIHLKRFESQRSFSDKIDATVNFPITDLDLSRYVVYKDDPRGLIYDLYAVDNHYGGLGGGHYTAYVKNFADNKWYYFDDSRVTETAPENSIAGSAYLLFYIRRHKDGNGLGSSKLQEIIQKSRHGYDERIKKIYDEQMKLYEFNKTDEEEDVSDDMIECNEDVQAPEYSNRSLEVGHIETQDCNDEDDNDDGERTNSGRRKLRLLKKVYKNNSGLGSSSTSEISEGCPENEVADLNLKNGVTLESPE | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MGSSDVSSRE -----CCCCCCCCCC | 34.91 | 27017623 | |
| 12 | Phosphorylation | DVSSRECSLVYNEDP CCCCCCCCEEECCCC | 19.00 | 28889911 | |
| 26 | Phosphorylation | PDFTDGTTPCDRLGV CCCCCCCCCCHHHCC | 27.70 | 23749301 | |
| 49 | Phosphorylation | KDEIKQESVPVSDRE HHHHHHHCCCCCHHC | 29.27 | 28889911 | |
| 53 | Phosphorylation | KQESVPVSDREIEDT HHHCCCCCHHCCCCC | 25.53 | 28889911 | |
| 84 | Phosphorylation | IAEPHAASETNLGTN HCCCCCCCCCCCCCC | 45.82 | 28889911 | |
| 86 | Phosphorylation | EPHAASETNLGTNGQ CCCCCCCCCCCCCCC | 32.99 | 28889911 | |
| 430 | Phosphorylation | KLFQNRMSIMQRNAA HHHHHHHHHHHHHCC | 16.21 | 28889911 | |
| 445 | Phosphorylation | FPPSMFKSTIGHFNS CCHHHHHHHHHHHHH | 17.62 | 27017623 | |
| 446 | Phosphorylation | PPSMFKSTIGHFNSM CHHHHHHHHHHHHHH | 31.41 | 27017623 | |
| 520 | Phosphorylation | MHLKRNCSVITDLFV HHHHHCCHHHHHHHH | 21.80 | 25704821 | |
| 756 | Acetylation | IKVTDKDKSFFSIKI EEEECCCCCCEEEEE | 55.70 | 24489116 | |
| 845 | Phosphorylation | NFSKPFQSGDDEENK CCCCCCCCCCCCCCC | 44.56 | 21440633 | |
| 854 | Phosphorylation | DDEENKETVTNNENV CCCCCCCCCCCCCCC | 33.95 | 19823750 | |
| 856 | Phosphorylation | EENKETVTNNENVNN CCCCCCCCCCCCCCC | 39.48 | 19823750 | |
| 864 | Phosphorylation | NNENVNNTNDRDEDM CCCCCCCCCCCHHHC | 33.04 | 19823750 | |
| 874 | Phosphorylation | RDEDMELTDDVEEDA CHHHCCCCCCHHHCC | 19.49 | 19823750 | |
| 882 | Phosphorylation | DDVEEDASTEPELTD CCHHHCCCCCCHHCC | 45.70 | 19823750 | |
| 883 | Phosphorylation | DVEEDASTEPELTDK CHHHCCCCCCHHCCC | 58.23 | 19823750 | |
| 888 | Phosphorylation | ASTEPELTDKPEALD CCCCCHHCCCHHHHH | 40.07 | 19823750 | |
| 896 | Acetylation | DKPEALDKIKDSLTS CCHHHHHHHHHHCCC | 53.13 | 24489116 | |
| 1016 | Phosphorylation | IHLKRFESQRSFSDK EEHHHHCCCCCCCCC | 28.34 | 19823750 | |
| 1019 | Phosphorylation | KRFESQRSFSDKIDA HHHCCCCCCCCCCCE | 22.82 | 19823750 | |
| 1021 | Phosphorylation | FESQRSFSDKIDATV HCCCCCCCCCCCEEE | 38.96 | 19823750 | |
| 1141 | Phosphorylation | DERIKKIYDEQMKLY HHHHHHHHHHHHHHE | 23.47 | 21440633 | |
| 1148 | Phosphorylation | YDEQMKLYEFNKTDE HHHHHHHEECCCCCC | 16.98 | 21440633 | |
| 1153 | Phosphorylation | KLYEFNKTDEEEDVS HHEECCCCCCCCCCC | 50.15 | 28152593 | |
| 1160 | Phosphorylation | TDEEEDVSDDMIECN CCCCCCCCCCCEECC | 39.97 | 28152593 | |
| 1179 | Phosphorylation | APEYSNRSLEVGHIE CCCCCCCCEEECCEE | 32.88 | 23749301 | |
| 1202 | Phosphorylation | DNDDGERTNSGRRKL CCCCCCCCHHHHHHH | 29.45 | 21440633 | |
| 1204 | Phosphorylation | DDGERTNSGRRKLRL CCCCCCHHHHHHHHH | 32.82 | 19779198 | |
| 1220 | Phosphorylation | KKVYKNNSGLGSSST HHHHHCCCCCCCCCH | 44.80 | 28889911 | |
| 1224 | Phosphorylation | KNNSGLGSSSTSEIS HCCCCCCCCCHHHHC | 26.59 | 21440633 | |
| 1225 | Phosphorylation | NNSGLGSSSTSEISE CCCCCCCCCHHHHCC | 35.52 | 20377248 | |
| 1226 | Phosphorylation | NSGLGSSSTSEISEG CCCCCCCCHHHHCCC | 37.34 | 28889911 | |
| 1227 | Phosphorylation | SGLGSSSTSEISEGC CCCCCCCHHHHCCCC | 32.12 | 21440633 | |
| 1228 | Phosphorylation | GLGSSSTSEISEGCP CCCCCCHHHHCCCCC | 34.58 | 20377248 | |
| 1231 | Phosphorylation | SSSTSEISEGCPENE CCCHHHHCCCCCCCC | 24.72 | 21551504 | |
| 1249 | Phosphorylation | LNLKNGVTLESPE-- CCCCCCCEECCCC-- | 26.63 | 19823750 | |
| 1252 | Phosphorylation | KNGVTLESPE----- CCCCEECCCC----- | 37.12 | 22369663 |
| 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 UBP12_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UBP12_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 UBP12_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-12; SER-84; THR-86;SER-430; THR-1153; SER-1226 AND THR-1227, AND MASS SPECTROMETRY. | |