| UniProt ID | UBX1_YEAST | |
|---|---|---|
| UniProt AC | P34223 | |
| Protein Name | UBX domain-containing protein 1 | |
| Gene Name | SHP1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 423 | |
| Subcellular Localization | Nucleus . Cytoplasm . | |
| Protein Description | Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway. Direct or indirect positive regulator of GLC7 activity.. | |
| Protein Sequence | MAEIPDETIQQFMALTNVSHNIAVQYLSEFGDLNEALNSYYASQTDDQKDRREEAHWNRQQEKALKQEAFSTNSSNKAINTEHVGGLCPKPGSSQGSNEYLKRKGSTSPEPTKGSSRSGSGNNSRFMSFSDMVRGQADDDDEDQPRNTFAGGETSGLEVTDPSDPNSLLKDLLEKARRGGQMGAENGFRDDEDHEMGANRFTGRGFRLGSTIDAADEVVEDNTSQSQRRPEKVTREITFWKEGFQVADGPLYRYDDPANSFYLSELNQGRAPLKLLDVQFGQEVEVNVYKKLDESYKAPTRKLGGFSGQGQRLGSPIPGESSPAEVPKNETPAAQEQPMPDNEPKQGDTSIQIRYANGKREVLHCNSTDTVKFLYEHVTSNANTDPSRNFTLNYAFPIKPISNDETTLKDADLLNSVVVQRWA | |
| 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 |
|---|---|---|---|---|---|
| 63 | Ubiquitination | HWNRQQEKALKQEAF HHHHHHHHHHHHHHH | 55.47 | 22817900 | |
| 66 | Acetylation | RQQEKALKQEAFSTN HHHHHHHHHHHHHCC | 51.45 | 25381059 | |
| 66 | Ubiquitination | RQQEKALKQEAFSTN HHHHHHHHHHHHHCC | 51.45 | 23749301 | |
| 71 | Phosphorylation | ALKQEAFSTNSSNKA HHHHHHHHCCCCCCC | 33.45 | 22369663 | |
| 72 | Phosphorylation | LKQEAFSTNSSNKAI HHHHHHHCCCCCCCC | 32.44 | 22369663 | |
| 74 | Phosphorylation | QEAFSTNSSNKAINT HHHHHCCCCCCCCCC | 35.06 | 22369663 | |
| 75 | Phosphorylation | EAFSTNSSNKAINTE HHHHCCCCCCCCCCC | 44.40 | 22369663 | |
| 77 | Ubiquitination | FSTNSSNKAINTEHV HHCCCCCCCCCCCCC | 53.22 | 17644757 | |
| 81 | Phosphorylation | SSNKAINTEHVGGLC CCCCCCCCCCCCCCC | 22.73 | 22369663 | |
| 90 | Ubiquitination | HVGGLCPKPGSSQGS CCCCCCCCCCCCCCH | 62.10 | 23749301 | |
| 93 | Phosphorylation | GLCPKPGSSQGSNEY CCCCCCCCCCCHHHH | 28.19 | 22369663 | |
| 94 | Phosphorylation | LCPKPGSSQGSNEYL CCCCCCCCCCHHHHH | 44.46 | 22369663 | |
| 97 | Phosphorylation | KPGSSQGSNEYLKRK CCCCCCCHHHHHHCC | 20.89 | 22369663 | |
| 100 | Phosphorylation | SSQGSNEYLKRKGST CCCCHHHHHHCCCCC | 23.05 | 22369663 | |
| 102 | Acetylation | QGSNEYLKRKGSTSP CCHHHHHHCCCCCCC | 51.68 | 24489116 | |
| 102 | Ubiquitination | QGSNEYLKRKGSTSP CCHHHHHHCCCCCCC | 51.68 | 23749301 | |
| 104 | Ubiquitination | SNEYLKRKGSTSPEP HHHHHHCCCCCCCCC | 56.47 | 22817900 | |
| 106 | Phosphorylation | EYLKRKGSTSPEPTK HHHHCCCCCCCCCCC | 28.84 | 19823750 | |
| 107 | Phosphorylation | YLKRKGSTSPEPTKG HHHCCCCCCCCCCCC | 57.90 | 19823750 | |
| 108 | Phosphorylation | LKRKGSTSPEPTKGS HHCCCCCCCCCCCCC | 29.03 | 25521595 | |
| 112 | Phosphorylation | GSTSPEPTKGSSRSG CCCCCCCCCCCCCCC | 46.50 | 22890988 | |
| 113 | Ubiquitination | STSPEPTKGSSRSGS CCCCCCCCCCCCCCC | 68.46 | 23749301 | |
| 115 | Phosphorylation | SPEPTKGSSRSGSGN CCCCCCCCCCCCCCC | 24.92 | 23749301 | |
| 116 | Phosphorylation | PEPTKGSSRSGSGNN CCCCCCCCCCCCCCC | 38.85 | 19684113 | |
| 118 | Phosphorylation | PTKGSSRSGSGNNSR CCCCCCCCCCCCCCC | 38.98 | 22369663 | |
| 120 | Phosphorylation | KGSSRSGSGNNSRFM CCCCCCCCCCCCCCC | 39.32 | 22369663 | |
| 124 | Phosphorylation | RSGSGNNSRFMSFSD CCCCCCCCCCCCHHH | 30.78 | 23749301 | |
| 128 | Phosphorylation | GNNSRFMSFSDMVRG CCCCCCCCHHHHHCC | 20.91 | 22369663 | |
| 130 | Phosphorylation | NSRFMSFSDMVRGQA CCCCCCHHHHHCCCC | 19.93 | 22369663 | |
| 148 | Phosphorylation | DEDQPRNTFAGGETS CCCCCCCCCCCCCCC | 19.01 | 28132839 | |
| 154 | Phosphorylation | NTFAGGETSGLEVTD CCCCCCCCCCCEECC | 31.22 | 22369663 | |
| 155 | Phosphorylation | TFAGGETSGLEVTDP CCCCCCCCCCEECCC | 36.76 | 22369663 | |
| 160 | Phosphorylation | ETSGLEVTDPSDPNS CCCCCEECCCCCCCH | 32.58 | 22369663 | |
| 170 | Ubiquitination | SDPNSLLKDLLEKAR CCCCHHHHHHHHHHH | 52.18 | 24961812 | |
| 175 | Ubiquitination | LLKDLLEKARRGGQM HHHHHHHHHHHHCCC | 47.35 | 23749301 | |
| 210 | Phosphorylation | GRGFRLGSTIDAADE CCCCCCCCCCCHHHH | 27.12 | 21082442 | |
| 211 | Phosphorylation | RGFRLGSTIDAADEV CCCCCCCCCCHHHHH | 22.52 | 21082442 | |
| 223 | Phosphorylation | DEVVEDNTSQSQRRP HHHHHCCCCHHHCCC | 40.23 | 22369663 | |
| 224 | Phosphorylation | EVVEDNTSQSQRRPE HHHHCCCCHHHCCCH | 33.80 | 22369663 | |
| 226 | Phosphorylation | VEDNTSQSQRRPEKV HHCCCCHHHCCCHHH | 25.97 | 22369663 | |
| 241 | Ubiquitination | TREITFWKEGFQVAD HCEEEEECCCEEECC | 43.71 | 23749301 | |
| 274 | Ubiquitination | NQGRAPLKLLDVQFG CCCCCCEEEEEECCC | 46.04 | 22817900 | |
| 295 | Phosphorylation | VYKKLDESYKAPTRK EHHHCCHHCCCCCCC | 31.44 | 25704821 | |
| 297 | Ubiquitination | KKLDESYKAPTRKLG HHCCHHCCCCCCCCC | 58.11 | 22817900 | |
| 302 | Acetylation | SYKAPTRKLGGFSGQ HCCCCCCCCCCCCCC | 54.70 | 25381059 | |
| 302 | Ubiquitination | SYKAPTRKLGGFSGQ HCCCCCCCCCCCCCC | 54.70 | 23749301 | |
| 307 | Phosphorylation | TRKLGGFSGQGQRLG CCCCCCCCCCCCCCC | 33.22 | 25521595 | |
| 315 | Phosphorylation | GQGQRLGSPIPGESS CCCCCCCCCCCCCCC | 25.01 | 22369663 | |
| 321 | Phosphorylation | GSPIPGESSPAEVPK CCCCCCCCCCCCCCC | 47.76 | 22369663 | |
| 322 | Phosphorylation | SPIPGESSPAEVPKN CCCCCCCCCCCCCCC | 24.67 | 22369663 | |
| 328 | Acetylation | SSPAEVPKNETPAAQ CCCCCCCCCCCCCCC | 73.01 | 24489116 | |
| 331 | Phosphorylation | AEVPKNETPAAQEQP CCCCCCCCCCCCCCC | 27.85 | 22369663 | |
| 367 | Phosphorylation | REVLHCNSTDTVKFL EEEEEECCCHHHHHH | 32.81 | 23749301 | |
| 372 | Ubiquitination | CNSTDTVKFLYEHVT ECCCHHHHHHHHHHH | 31.57 | 17644757 | |
| 399 | Ubiquitination | LNYAFPIKPISNDET EEEEEECCCCCCCCC | 36.21 | 17644757 | |
| 399 | Acetylation | LNYAFPIKPISNDET EEEEEECCCCCCCCC | 36.21 | 24489116 | |
| 409 | Ubiquitination | SNDETTLKDADLLNS CCCCCCHHHHHHHHH | 49.10 | 17644757 |
| 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 UBX1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UBX1_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 UBX1_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-93; SER-94; SER-97;SER-106; SER-108; SER-155; SER-210; SER-226; SER-315; SER-321 ANDSER-322, 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-108; SER-315 ANDSER-321, AND MASS SPECTROMETRY. | |
| "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-315 AND SER-322, ANDMASS SPECTROMETRY. | |
| "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-315, AND MASSSPECTROMETRY. | |
| "Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-108, ANDMASS SPECTROMETRY. | |
