| UniProt ID | UBI4P_YEAST | |
|---|---|---|
| UniProt AC | P0CG63 | |
| Protein Name | Polyubiquitin | |
| Gene Name | UBI4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 381 | |
| Subcellular Localization | Cytoplasm. Nucleus. | |
| Protein Description | Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).. | |
| Protein Sequence | MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGN | |
| 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 |
|---|---|---|---|---|---|
| 6 | Ubiquitination | --MQIFVKTLTGKTI --CEEEEEECCCCEE | 27.37 | 23749301 | |
| 11 | Ubiquitination | FVKTLTGKTITLEVE EEEECCCCEEEEEEE | 31.36 | 23749301 | |
| 12 | Phosphorylation | VKTLTGKTITLEVES EEECCCCEEEEEEEC | 22.12 | 23749301 | |
| 14 | Phosphorylation | TLTGKTITLEVESSD ECCCCEEEEEEECCC | 23.30 | 23749301 | |
| 19 | Phosphorylation | TITLEVESSDTIDNV EEEEEEECCCCHHHH | 38.39 | 23749301 | |
| 22 | Phosphorylation | LEVESSDTIDNVKSK EEEECCCCHHHHHHH | 31.98 | 23749301 | |
| 27 | Ubiquitination | SDTIDNVKSKIQDKE CCCHHHHHHHCCCCC | 52.89 | 23749301 | |
| 29 | Ubiquitination | TIDNVKSKIQDKEGI CHHHHHHHCCCCCCC | 38.37 | 22817900 | |
| 33 | Ubiquitination | VKSKIQDKEGIPPDQ HHHHCCCCCCCCHHH | 41.27 | 23749301 | |
| 48 | Ubiquitination | QRLIFAGKQLEDGRT HEEEEEEEECCCCCC | 48.56 | 23749301 | |
| 55 | Phosphorylation | KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC | 35.82 | 22369663 | |
| 57 | Phosphorylation | LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH | 37.12 | 22369663 | |
| 59 | Phosphorylation | DGRTLSDYNIQKEST CCCCCCCCCCCCHHE | 15.70 | 22369663 | |
| 63 | Ubiquitination | LSDYNIQKESTLHLV CCCCCCCCHHEEEEE | 50.24 | 23749301 | |
| 65 | Phosphorylation | DYNIQKESTLHLVLR CCCCCCHHEEEEEEE | 43.22 | 23749301 | |
| 66 | Phosphorylation | YNIQKESTLHLVLRL CCCCCHHEEEEEEEE | 21.20 | 23749301 | |
| 82 | Ubiquitination | GGMQIFVKTLTGKTI CCEEEEEEECCCCEE | 27.37 | 23749301 | |
| 87 | Ubiquitination | FVKTLTGKTITLEVE EEEECCCCEEEEEEE | 31.36 | 23749301 | |
| 88 | Phosphorylation | VKTLTGKTITLEVES EEECCCCEEEEEEEC | 22.12 | 23749301 | |
| 90 | Phosphorylation | TLTGKTITLEVESSD ECCCCEEEEEEECCC | 23.30 | 23749301 | |
| 95 | Phosphorylation | TITLEVESSDTIDNV EEEEEEECCCCHHHH | 38.39 | 23749301 | |
| 98 | Phosphorylation | LEVESSDTIDNVKSK EEEECCCCHHHHHHH | 31.98 | 23749301 | |
| 103 | Ubiquitination | SDTIDNVKSKIQDKE CCCHHHHHHHCCCCC | 52.89 | 23749301 | |
| 105 | Ubiquitination | TIDNVKSKIQDKEGI CHHHHHHHCCCCCCC | 38.37 | 22817900 | |
| 109 | Ubiquitination | VKSKIQDKEGIPPDQ HHHHCCCCCCCCHHH | 41.27 | 23749301 | |
| 124 | Ubiquitination | QRLIFAGKQLEDGRT HEEEEEEEECCCCCC | 48.56 | 23749301 | |
| 131 | Phosphorylation | KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC | 35.82 | 22369663 | |
| 133 | Phosphorylation | LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH | 37.12 | 22369663 | |
| 135 | Phosphorylation | DGRTLSDYNIQKEST CCCCCCCCCCCCHHE | 15.70 | 22369663 | |
| 139 | Ubiquitination | LSDYNIQKESTLHLV CCCCCCCCHHEEEEE | 50.24 | 23749301 | |
| 141 | Phosphorylation | DYNIQKESTLHLVLR CCCCCCHHEEEEEEE | 43.22 | 23749301 | |
| 142 | Phosphorylation | YNIQKESTLHLVLRL CCCCCHHEEEEEEEE | 21.20 | 23749301 | |
| 158 | Ubiquitination | GGMQIFVKTLTGKTI CCEEEEEEECCCCEE | 27.37 | 23749301 | |
| 163 | Ubiquitination | FVKTLTGKTITLEVE EEEECCCCEEEEEEE | 31.36 | 23749301 | |
| 164 | Phosphorylation | VKTLTGKTITLEVES EEECCCCEEEEEEEC | 22.12 | 23749301 | |
| 166 | Phosphorylation | TLTGKTITLEVESSD ECCCCEEEEEEECCC | 23.30 | 23749301 | |
| 171 | Phosphorylation | TITLEVESSDTIDNV EEEEEEECCCCHHHH | 38.39 | 23749301 | |
| 174 | Phosphorylation | LEVESSDTIDNVKSK EEEECCCCHHHHHHH | 31.98 | 23749301 | |
| 179 | Ubiquitination | SDTIDNVKSKIQDKE CCCHHHHHHHCCCCC | 52.89 | 23749301 | |
| 181 | Ubiquitination | TIDNVKSKIQDKEGI CHHHHHHHCCCCCCC | 38.37 | 22817900 | |
| 185 | Ubiquitination | VKSKIQDKEGIPPDQ HHHHCCCCCCCCHHH | 41.27 | 23749301 | |
| 200 | Ubiquitination | QRLIFAGKQLEDGRT HEEEEEEEECCCCCC | 48.56 | 23749301 | |
| 207 | Phosphorylation | KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC | 35.82 | 22369663 | |
| 209 | Phosphorylation | LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH | 37.12 | 22369663 | |
| 211 | Phosphorylation | DGRTLSDYNIQKEST CCCCCCCCCCCCHHE | 15.70 | 22369663 | |
| 215 | Ubiquitination | LSDYNIQKESTLHLV CCCCCCCCHHEEEEE | 50.24 | 23749301 | |
| 217 | Phosphorylation | DYNIQKESTLHLVLR CCCCCCHHEEEEEEE | 43.22 | 23749301 | |
| 218 | Phosphorylation | YNIQKESTLHLVLRL CCCCCHHEEEEEEEE | 21.20 | 23749301 | |
| 234 | Ubiquitination | GGMQIFVKTLTGKTI CCEEEEEEECCCCEE | 27.37 | 23749301 | |
| 239 | Ubiquitination | FVKTLTGKTITLEVE EEEECCCCEEEEEEE | 31.36 | 23749301 | |
| 240 | Phosphorylation | VKTLTGKTITLEVES EEECCCCEEEEEEEC | 22.12 | 23749301 | |
| 242 | Phosphorylation | TLTGKTITLEVESSD ECCCCEEEEEEECCC | 23.30 | 23749301 | |
| 247 | Phosphorylation | TITLEVESSDTIDNV EEEEEEECCCCHHHH | 38.39 | 23749301 | |
| 250 | Phosphorylation | LEVESSDTIDNVKSK EEEECCCCHHHHHHH | 31.98 | 23749301 | |
| 255 | Ubiquitination | SDTIDNVKSKIQDKE CCCHHHHHHHCCCCC | 52.89 | 23749301 | |
| 257 | Ubiquitination | TIDNVKSKIQDKEGI CHHHHHHHCCCCCCC | 38.37 | 22817900 | |
| 261 | Ubiquitination | VKSKIQDKEGIPPDQ HHHHCCCCCCCCHHH | 41.27 | 23749301 | |
| 276 | Ubiquitination | QRLIFAGKQLEDGRT HEEEEEEEECCCCCC | 48.56 | 23749301 | |
| 283 | Phosphorylation | KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC | 35.82 | 22369663 | |
| 285 | Phosphorylation | LEDGRTLSDYNIQKE CCCCCCCCCCCCCCH | 37.12 | 22369663 | |
| 287 | Phosphorylation | DGRTLSDYNIQKEST CCCCCCCCCCCCHHE | 15.70 | 22369663 | |
| 291 | Ubiquitination | LSDYNIQKESTLHLV CCCCCCCCHHEEEEE | 50.24 | 23749301 | |
| 293 | Phosphorylation | DYNIQKESTLHLVLR CCCCCCHHEEEEEEE | 43.22 | 23749301 | |
| 294 | Phosphorylation | YNIQKESTLHLVLRL CCCCCHHEEEEEEEE | 21.20 | 23749301 | |
| 310 | Ubiquitination | GGMQIFVKTLTGKTI CCEEEEEEECCCCEE | 27.37 | 23749301 | |
| 315 | Ubiquitination | FVKTLTGKTITLEVE EEEECCCCEEEEEEE | 31.36 | 23749301 | |
| 316 | Phosphorylation | VKTLTGKTITLEVES EEECCCCEEEEEEEC | 22.12 | 23749301 | |
| 318 | Phosphorylation | TLTGKTITLEVESSD ECCCCEEEEEEECCC | 23.30 | 23749301 | |
| 323 | Phosphorylation | TITLEVESSDTIDNV EEEEEEECCCCHHHH | 38.39 | 23749301 | |
| 326 | Phosphorylation | LEVESSDTIDNVKSK EEEECCCCHHHHHHH | 31.98 | 23749301 | |
| 331 | Ubiquitination | SDTIDNVKSKIQDKE CCCHHHHHHHCCCCC | 52.89 | 23749301 | |
| 333 | Ubiquitination | TIDNVKSKIQDKEGI CHHHHHHHCCCCCCC | 38.37 | 22817900 | |
| 337 | Ubiquitination | VKSKIQDKEGIPPDQ HHHHCCCCCCCCHHH | 41.27 | 23749301 | |
| 352 | Ubiquitination | QRLIFAGKQLEDGRT HEEEEEEEECCCCCC | 48.56 | 23749301 | |
| 359 | Phosphorylation | KQLEDGRTLSDYNIQ EECCCCCCCCCCCCC | 35.82 | 22369663 | |
| 361 | Phosphorylation | LEDGRTLSDYNIQKE CCCCCCCCCCCCCCC | 37.12 | 22369663 | |
| 363 | Phosphorylation | DGRTLSDYNIQKEST CCCCCCCCCCCCCCE | 15.70 | 22369663 | |
| 367 | Ubiquitination | LSDYNIQKESTLHLV CCCCCCCCCCEEEEE | 50.24 | 23749301 | |
| 369 | Phosphorylation | DYNIQKESTLHLVLR CCCCCCCCEEEEEEE | 43.22 | 23749301 | |
| 370 | Phosphorylation | YNIQKESTLHLVLRL CCCCCCCEEEEEEEE | 21.20 | 23749301 |
| 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 UBI4P_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UBI4P_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 UBI4P_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-57, AND MASSSPECTROMETRY. | |
| "A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: PROTEIN SEQUENCE OF 43-53, PHOSPHORYLATION [LARGE SCALE ANALYSIS] ATSER-57, UBIQUITINATION AT LYS-6; LYS-11; LYS-27; LYS-29; LYS-33;LYS-48 AND LYS-63, AND MASS SPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery."; Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.; Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-48 AND LYS-63,AND MASS SPECTROMETRY. | |
| "A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: PROTEIN SEQUENCE OF 43-53, PHOSPHORYLATION [LARGE SCALE ANALYSIS] ATSER-57, UBIQUITINATION AT LYS-6; LYS-11; LYS-27; LYS-29; LYS-33;LYS-48 AND LYS-63, AND MASS SPECTROMETRY. | |
