| UniProt ID | UBP13_YEAST | |
|---|---|---|
| UniProt AC | P38187 | |
| Protein Name | Ubiquitin carboxyl-terminal hydrolase 13 | |
| Gene Name | UBP13 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 747 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MIRRWLTISKSGKKKKAVNDTITEEVEKVDFKPVNHDINDELCYSESSDNPSSSLFVSNLDTKETFLNEDNNLQISSGLDYSSETCNQGSNYSQDGIFYISNAKAINAYGGIITQGPEAPILAMKVSDSMPYGDGSNKVFGYENFGNTCYCNSVLQCLYNLSSLRENILQFPKKSRESDQPRKKEMRGKKPRIFTEASFEKSIAGTNGHLPNPKPQSVDDGKPTPVNSVNSNTAGPSEKKSKFFKSFSAKHVQDNNKKEGSPAILTTGKPSSRPQDAPPLIVETPNEPGAPSRLSFENVTDRPPDVPRKIIVGRVLNYENPSRGSSNSNNLDLKGESNSSLSTPLDKKDTRRSSSSSQISPEHRKKSALIRGPVLNIDHSLNGSDKATLYSSLRDIFECITENTYLTGVVSPSSFVDVLKRENVLFNTTMHQDAHEFFNFLLNELSEYIERENKKIAASDINSDSEPSKSKNFISDLFQGTLTNQIKCLTCDNITSRDEPFLDFPIEVQGDEETDIQEILKSYHQREMLNGSNKFYCDECCGLQEAERLVGLKQLPDTLTLHLKRFKYSEKQNCNIKLFNNIHYPLTLNVCSSINSKVCQKYELAGIVVHMGGGPQHGHYVSLCKHEKFGWLLFDDETVEAVKEETVLEFTGESPNMATAYVLFYKAMYSNAVEKNDRENMAKEQDDNIDNLIKYDDWLRTCNSGQKKKEELPIADDLDTAIDDSFVSNTPIKSSKKKSRMFSFRKS | |
| 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 |
|---|---|---|---|---|---|
| 44 | Phosphorylation | DINDELCYSESSDNP CCCCCCCCCCCCCCC | 28.26 | 20377248 | |
| 45 | Phosphorylation | INDELCYSESSDNPS CCCCCCCCCCCCCCC | 29.97 | 20377248 | |
| 47 | Phosphorylation | DELCYSESSDNPSSS CCCCCCCCCCCCCCC | 36.73 | 19779198 | |
| 48 | Phosphorylation | ELCYSESSDNPSSSL CCCCCCCCCCCCCCE | 37.04 | 21440633 | |
| 52 | Phosphorylation | SESSDNPSSSLFVSN CCCCCCCCCCEEEEC | 38.52 | 20377248 | |
| 53 | Phosphorylation | ESSDNPSSSLFVSNL CCCCCCCCCEEEECC | 32.11 | 21551504 | |
| 195 | Phosphorylation | GKKPRIFTEASFEKS CCCCCCEEHHHHHHH | 28.42 | 24961812 | |
| 198 | Phosphorylation | PRIFTEASFEKSIAG CCCEEHHHHHHHHCC | 27.92 | 17287358 | |
| 217 | Phosphorylation | LPNPKPQSVDDGKPT CCCCCCCCCCCCCCC | 35.72 | 21440633 | |
| 261 | Phosphorylation | DNNKKEGSPAILTTG CCCCCCCCCCEEECC | 16.55 | 27214570 | |
| 266 | Phosphorylation | EGSPAILTTGKPSSR CCCCCEEECCCCCCC | 27.65 | 29688323 | |
| 267 | Phosphorylation | GSPAILTTGKPSSRP CCCCEEECCCCCCCC | 39.50 | 29688323 | |
| 271 | Phosphorylation | ILTTGKPSSRPQDAP EEECCCCCCCCCCCC | 42.33 | 29688323 | |
| 272 | Phosphorylation | LTTGKPSSRPQDAPP EECCCCCCCCCCCCC | 57.41 | 29688323 | |
| 284 | Phosphorylation | APPLIVETPNEPGAP CCCEEEECCCCCCCC | 22.11 | 29688323 | |
| 292 | Phosphorylation | PNEPGAPSRLSFENV CCCCCCCCCCCEECC | 45.37 | 21551504 | |
| 295 | Phosphorylation | PGAPSRLSFENVTDR CCCCCCCCEECCCCC | 29.42 | 28889911 | |
| 300 | Phosphorylation | RLSFENVTDRPPDVP CCCEECCCCCCCCCC | 37.56 | 21440633 | |
| 318 | Phosphorylation | IVGRVLNYENPSRGS EEEEECCCCCCCCCC | 16.96 | 22369663 | |
| 322 | Phosphorylation | VLNYENPSRGSSNSN ECCCCCCCCCCCCCC | 61.94 | 22369663 | |
| 325 | Phosphorylation | YENPSRGSSNSNNLD CCCCCCCCCCCCCCC | 25.82 | 22369663 | |
| 326 | Phosphorylation | ENPSRGSSNSNNLDL CCCCCCCCCCCCCCC | 47.29 | 22369663 | |
| 328 | Phosphorylation | PSRGSSNSNNLDLKG CCCCCCCCCCCCCCC | 29.10 | 22369663 | |
| 337 | Phosphorylation | NLDLKGESNSSLSTP CCCCCCCCCCCCCCC | 51.16 | 22369663 | |
| 339 | Phosphorylation | DLKGESNSSLSTPLD CCCCCCCCCCCCCCC | 41.77 | 22369663 | |
| 340 | Phosphorylation | LKGESNSSLSTPLDK CCCCCCCCCCCCCCH | 30.50 | 22369663 | |
| 342 | Phosphorylation | GESNSSLSTPLDKKD CCCCCCCCCCCCHHH | 29.90 | 22369663 | |
| 343 | Phosphorylation | ESNSSLSTPLDKKDT CCCCCCCCCCCHHHC | 32.91 | 22369663 | |
| 350 | Phosphorylation | TPLDKKDTRRSSSSS CCCCHHHCCCCCCCC | 36.54 | 27717283 | |
| 353 | Phosphorylation | DKKDTRRSSSSSQIS CHHHCCCCCCCCCCC | 31.14 | 29136822 | |
| 354 | Phosphorylation | KKDTRRSSSSSQISP HHHCCCCCCCCCCCH | 32.21 | 21082442 | |
| 355 | Phosphorylation | KDTRRSSSSSQISPE HHCCCCCCCCCCCHH | 34.94 | 21082442 | |
| 356 | Phosphorylation | DTRRSSSSSQISPEH HCCCCCCCCCCCHHH | 28.36 | 21082442 | |
| 357 | Phosphorylation | TRRSSSSSQISPEHR CCCCCCCCCCCHHHH | 33.22 | 29136822 | |
| 360 | Phosphorylation | SSSSSQISPEHRKKS CCCCCCCCHHHHHCC | 19.32 | 30377154 | |
| 459 | Phosphorylation | ENKKIAASDINSDSE HCCCCCHHHCCCCCC | 29.96 | 29688323 | |
| 463 | Phosphorylation | IAASDINSDSEPSKS CCHHHCCCCCCCCCC | 42.73 | 22369663 | |
| 465 | Phosphorylation | ASDINSDSEPSKSKN HHHCCCCCCCCCCCC | 51.75 | 22369663 | |
| 468 | Phosphorylation | INSDSEPSKSKNFIS CCCCCCCCCCCCHHH | 45.57 | 22369663 | |
| 469 | Ubiquitination | NSDSEPSKSKNFISD CCCCCCCCCCCHHHH | 75.95 | 23749301 | |
| 475 | Phosphorylation | SKSKNFISDLFQGTL CCCCCHHHHHHHCCC | 24.91 | 21440633 | |
| 571 | Ubiquitination | KRFKYSEKQNCNIKL HHCCCCCCCCCEEEE | 40.65 | 23749301 | |
| 669 | Phosphorylation | VLFYKAMYSNAVEKN HHHHHHHHHHHHHHH | 12.02 | 27017623 | |
| 701 | Phosphorylation | KYDDWLRTCNSGQKK HHHHHHHHCCCCCCC | 17.54 | 21440633 | |
| 720 | Phosphorylation | PIADDLDTAIDDSFV CCCCCCCHHCCCCHH | 32.58 | 26447709 | |
| 725 | Phosphorylation | LDTAIDDSFVSNTPI CCHHCCCCHHCCCCC | 24.65 | 24961812 | |
| 728 | Phosphorylation | AIDDSFVSNTPIKSS HCCCCHHCCCCCCCC | 32.73 | 28889911 | |
| 730 | Phosphorylation | DDSFVSNTPIKSSKK CCCHHCCCCCCCCCC | 20.91 | 21440633 | |
| 747 | Phosphorylation | RMFSFRKS------- CCCCCCCC------- | 40.99 | 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 UBP13_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UBP13_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 UBP13_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-198; SER-340 ANDSER-356, 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-354 AND SER-355, ANDMASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND MASSSPECTROMETRY. | |
