| UniProt ID | CDC48_YEAST | |
|---|---|---|
| UniProt AC | P25694 | |
| Protein Name | Cell division control protein 48 {ECO:0000305|PubMed:6749598} | |
| Gene Name | CDC48 {ECO:0000303|PubMed:6749598} | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 835 | |
| Subcellular Localization | Microsome . Endoplasmic reticulum . Cytoplasm . Bound loosely to components of the microsomal fraction. | |
| Protein Description | Involved in spindle disassembly, degradation of ubiquitinated proteins and protein export from the endoplasmic reticulum to the cytoplasm. Acts as a chaperone that collects ubiquitinated substrates. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway. Required for the proteasome-dependent processing/activation of MGA2 and SPT23 transcription factors leading to the subsequent expression of OLE1. Has an additional role in the turnover of OLE1 where it targets ubiquitinated OLE1 and other proteins to the ERAD. [PubMed: 11733065] | |
| Protein Sequence | MGEEHKPLLDASGVDPREEDKTATAILRRKKKDNMLLVDDAINDDNSVIAINSNTMDKLELFRGDTVLVKGKKRKDTVLIVLIDDELEDGACRINRVVRNNLRIRLGDLVTIHPCPDIKYATRISVLPIADTIEGITGNLFDVFLKPYFVEAYRPVRKGDHFVVRGGMRQVEFKVVDVEPEEYAVVAQDTIIHWEGEPINREDEENNMNEVGYDDIGGCRKQMAQIREMVELPLRHPQLFKAIGIKPPRGVLMYGPPGTGKTLMARAVANETGAFFFLINGPEVMSKMAGESESNLRKAFEEAEKNAPAIIFIDEIDSIAPKRDKTNGEVERRVVSQLLTLMDGMKARSNVVVIAATNRPNSIDPALRRFGRFDREVDIGIPDATGRLEVLRIHTKNMKLADDVDLEALAAETHGYVGADIASLCSEAAMQQIREKMDLIDLDEDEIDAEVLDSLGVTMDNFRFALGNSNPSALRETVVESVNVTWDDVGGLDEIKEELKETVEYPVLHPDQYTKFGLSPSKGVLFYGPPGTGKTLLAKAVATEVSANFISVKGPELLSMWYGESESNIRDIFDKARAAAPTVVFLDELDSIAKARGGSLGDAGGASDRVVNQLLTEMDGMNAKKNVFVIGATNRPDQIDPAILRPGRLDQLIYVPLPDENARLSILNAQLRKTPLEPGLELTAIAKATQGFSGADLLYIVQRAAKYAIKDSIEAHRQHEAEKEVKVEGEDVEMTDEGAKAEQEPEVDPVPYITKEHFAEAMKTAKRSVSDAELRRYEAYSQQMKASRGQFSNFNFNDAPLGTTATDNANSNNSAPSGAGAAFGSNAEEDDDLYS | |
| 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 | --MGEEHKPLLDASG --CCCCCCCCCCCCC | 40.41 | 24961812 | |
| 12 | Phosphorylation | HKPLLDASGVDPREE CCCCCCCCCCCCCCC | 38.73 | 28889911 | |
| 21 | Acetylation | VDPREEDKTATAILR CCCCCCCCCHHHHHH | 43.25 | 24489116 | |
| 21 | Ubiquitination | VDPREEDKTATAILR CCCCCCCCCHHHHHH | 43.25 | 23749301 | |
| 22 | Phosphorylation | DPREEDKTATAILRR CCCCCCCCHHHHHHH | 41.38 | 21440633 | |
| 24 | Phosphorylation | REEDKTATAILRRKK CCCCCCHHHHHHHHC | 21.33 | 22369663 | |
| 70 | Ubiquitination | RGDTVLVKGKKRKDT CCCEEEECCCCCCCE | 61.93 | 22817900 | |
| 70 | 2-Hydroxyisobutyrylation | RGDTVLVKGKKRKDT CCCEEEECCCCCCCE | 61.93 | - | |
| 72 | Ubiquitination | DTVLVKGKKRKDTVL CEEEECCCCCCCEEE | 43.62 | 22817900 | |
| 73 | Ubiquitination | TVLVKGKKRKDTVLI EEEECCCCCCCEEEE | 73.65 | 22817900 | |
| 75 | Ubiquitination | LVKGKKRKDTVLIVL EECCCCCCCEEEEEE | 67.63 | 22817900 | |
| 119 | Ubiquitination | IHPCPDIKYATRISV EEECCCCCHHCEEEE | 35.89 | 23749301 | |
| 119 | Acetylation | IHPCPDIKYATRISV EEECCCCCHHCEEEE | 35.89 | 24489116 | |
| 158 | Ubiquitination | EAYRPVRKGDHFVVR HCCCCCCCCCEEEEC | 69.77 | 23749301 | |
| 221 | Ubiquitination | DDIGGCRKQMAQIRE CCCHHHHHHHHHHHH | 48.80 | 23749301 | |
| 241 | Ubiquitination | LRHPQLFKAIGIKPP CCCHHHHHHCCCCCC | 47.92 | 22817900 | |
| 241 | Acetylation | LRHPQLFKAIGIKPP CCCHHHHHHCCCCCC | 47.92 | 24489116 | |
| 246 | Ubiquitination | LFKAIGIKPPRGVLM HHHHCCCCCCCEEEE | 43.70 | 23749301 | |
| 261 | Ubiquitination | YGPPGTGKTLMARAV ECCCCCCHHHHHHHH | 38.02 | 23749301 | |
| 261 | Acetylation | YGPPGTGKTLMARAV ECCCCCCHHHHHHHH | 38.02 | 24489116 | |
| 272 | Phosphorylation | ARAVANETGAFFFLI HHHHHCCCCCEEEEE | 33.35 | 19779198 | |
| 292 | Phosphorylation | MSKMAGESESNLRKA HHHHCCCCHHHHHHH | 45.46 | 22369663 | |
| 294 | Phosphorylation | KMAGESESNLRKAFE HHCCCCHHHHHHHHH | 50.90 | 22369663 | |
| 298 | Ubiquitination | ESESNLRKAFEEAEK CCHHHHHHHHHHHHH | 61.67 | 23749301 | |
| 305 | Ubiquitination | KAFEEAEKNAPAIIF HHHHHHHHCCCEEEE | 66.51 | 24961812 | |
| 305 | Acetylation | KAFEEAEKNAPAIIF HHHHHHHHCCCEEEE | 66.51 | 24489116 | |
| 318 | Phosphorylation | IFIDEIDSIAPKRDK EEEEECHHCCCCCCC | 26.72 | 28889911 | |
| 322 | Acetylation | EIDSIAPKRDKTNGE ECHHCCCCCCCCCCH | 65.29 | 24489116 | |
| 322 | Ubiquitination | EIDSIAPKRDKTNGE ECHHCCCCCCCCCCH | 65.29 | 22106047 | |
| 336 | Phosphorylation | EVERRVVSQLLTLMD HHHHHHHHHHHHHHH | 16.56 | 19779198 | |
| 340 | Phosphorylation | RVVSQLLTLMDGMKA HHHHHHHHHHHHHHC | 28.73 | 23749301 | |
| 346 | Ubiquitination | LTLMDGMKARSNVVV HHHHHHHHCCCCEEE | 46.29 | 24961812 | |
| 423 | Phosphorylation | YVGADIASLCSEAAM CCCHHHHHHCHHHHH | 30.18 | 28889911 | |
| 472 | Phosphorylation | ALGNSNPSALRETVV HCCCCCHHHHHHHHH | 44.16 | 27214570 | |
| 515 | Acetylation | LHPDQYTKFGLSPSK CCHHHCCCCCCCCCC | 32.28 | 24489116 | |
| 515 | Ubiquitination | LHPDQYTKFGLSPSK CCHHHCCCCCCCCCC | 32.28 | 24961812 | |
| 519 | Phosphorylation | QYTKFGLSPSKGVLF HCCCCCCCCCCCEEE | 27.75 | 22369663 | |
| 521 | Phosphorylation | TKFGLSPSKGVLFYG CCCCCCCCCCEEEEC | 38.37 | 22369663 | |
| 522 | Acetylation | KFGLSPSKGVLFYGP CCCCCCCCCEEEECC | 57.32 | 24489116 | |
| 522 | Ubiquitination | KFGLSPSKGVLFYGP CCCCCCCCCEEEECC | 57.32 | 23749301 | |
| 532 | Phosphorylation | LFYGPPGTGKTLLAK EEECCCCCCHHHHHH | 41.08 | 27214570 | |
| 534 | Acetylation | YGPPGTGKTLLAKAV ECCCCCCHHHHHHHH | 35.52 | 24489116 | |
| 534 | Ubiquitination | YGPPGTGKTLLAKAV ECCCCCCHHHHHHHH | 35.52 | 23749301 | |
| 539 | Ubiquitination | TGKTLLAKAVATEVS CCHHHHHHHHHHHHC | 43.28 | 23749301 | |
| 565 | Phosphorylation | LSMWYGESESNIRDI HHHHHCCCCHHHHHH | 41.80 | 23749301 | |
| 567 | Phosphorylation | MWYGESESNIRDIFD HHHCCCCHHHHHHHH | 47.00 | 21440633 | |
| 575 | Ubiquitination | NIRDIFDKARAAAPT HHHHHHHHHHHHCCE | 29.08 | 17644757 | |
| 591 | Phosphorylation | VFLDELDSIAKARGG EEHHHHHHHHHHCCC | 36.75 | 21440633 | |
| 594 | Acetylation | DELDSIAKARGGSLG HHHHHHHHHCCCCCC | 36.63 | 24489116 | |
| 594 | Ubiquitination | DELDSIAKARGGSLG HHHHHHHHHCCCCCC | 36.63 | 23749301 | |
| 599 | Phosphorylation | IAKARGGSLGDAGGA HHHHCCCCCCCCCCC | 31.81 | 22369663 | |
| 607 | Phosphorylation | LGDAGGASDRVVNQL CCCCCCCHHHHHHHH | 29.26 | 21440633 | |
| 624 | Acetylation | EMDGMNAKKNVFVIG HCCCCCCCCCEEEEE | 39.62 | 24489116 | |
| 624 | Ubiquitination | EMDGMNAKKNVFVIG HCCCCCCCCCEEEEE | 39.62 | 23749301 | |
| 665 | Phosphorylation | PDENARLSILNAQLR CCHHHCHHHHHHHHC | 21.34 | 28889911 | |
| 673 | Ubiquitination | ILNAQLRKTPLEPGL HHHHHHCCCCCCCCC | 64.19 | 23749301 | |
| 683 | Phosphorylation | LEPGLELTAIAKATQ CCCCCHHHHHHHHHC | 13.47 | 28889911 | |
| 687 | Ubiquitination | LELTAIAKATQGFSG CHHHHHHHHHCCCCH | 45.94 | 17644757 | |
| 706 | Acetylation | YIVQRAAKYAIKDSI HHHHHHHHHHHHHHH | 33.94 | 24489116 | |
| 706 | Ubiquitination | YIVQRAAKYAIKDSI HHHHHHHHHHHHHHH | 33.94 | 22817900 | |
| 710 | Ubiquitination | RAAKYAIKDSIEAHR HHHHHHHHHHHHHHH | 36.93 | 22817900 | |
| 710 | Succinylation | RAAKYAIKDSIEAHR HHHHHHHHHHHHHHH | 36.93 | 23954790 | |
| 710 | Acetylation | RAAKYAIKDSIEAHR HHHHHHHHHHHHHHH | 36.93 | 24489116 | |
| 723 | Acetylation | HRQHEAEKEVKVEGE HHHHHHHCCEEECCC | 74.89 | 24489116 | |
| 726 | Ubiquitination | HEAEKEVKVEGEDVE HHHHCCEEECCCCCE | 35.34 | 24961812 | |
| 735 | Phosphorylation | EGEDVEMTDEGAKAE CCCCCEECCCCHHHC | 19.86 | 22369663 | |
| 740 | Ubiquitination | EMTDEGAKAEQEPEV EECCCCHHHCCCCCC | 64.41 | 23749301 | |
| 740 | Acetylation | EMTDEGAKAEQEPEV EECCCCHHHCCCCCC | 64.41 | 24489116 | |
| 755 | Acetylation | DPVPYITKEHFAEAM CCCCCCCHHHHHHHH | 39.37 | 24489116 | |
| 763 | Ubiquitination | EHFAEAMKTAKRSVS HHHHHHHHHHHHCCC | 52.99 | 23749301 | |
| 763 | Acetylation | EHFAEAMKTAKRSVS HHHHHHHHHHHHCCC | 52.99 | 22865919 | |
| 766 | Ubiquitination | AEAMKTAKRSVSDAE HHHHHHHHHCCCHHH | 50.90 | 22817900 | |
| 768 | Phosphorylation | AMKTAKRSVSDAELR HHHHHHHCCCHHHHH | 25.85 | 22369663 | |
| 770 | Phosphorylation | KTAKRSVSDAELRRY HHHHHCCCHHHHHHH | 32.14 | 22369663 | |
| 777 | Phosphorylation | SDAELRRYEAYSQQM CHHHHHHHHHHHHHH | 9.85 | 24961812 | |
| 780 | Phosphorylation | ELRRYEAYSQQMKAS HHHHHHHHHHHHHHH | 8.62 | 24961812 | |
| 781 | Phosphorylation | LRRYEAYSQQMKASR HHHHHHHHHHHHHHC | 22.45 | 24961812 | |
| 785 | Ubiquitination | EAYSQQMKASRGQFS HHHHHHHHHHCCCCC | 38.58 | 23749301 | |
| 787 | Phosphorylation | YSQQMKASRGQFSNF HHHHHHHHCCCCCCC | 31.27 | 19795423 | |
| 792 | Phosphorylation | KASRGQFSNFNFNDA HHHCCCCCCCCCCCC | 32.40 | 19823750 | |
| 803 | Phosphorylation | FNDAPLGTTATDNAN CCCCCCCCCCCCCCC | 22.42 | 19823750 | |
| 804 | Phosphorylation | NDAPLGTTATDNANS CCCCCCCCCCCCCCC | 26.26 | 19823750 | |
| 806 | Phosphorylation | APLGTTATDNANSNN CCCCCCCCCCCCCCC | 27.91 | 19823750 | |
| 811 | Phosphorylation | TATDNANSNNSAPSG CCCCCCCCCCCCCCC | 34.67 | 19823750 | |
| 814 | Phosphorylation | DNANSNNSAPSGAGA CCCCCCCCCCCCCCC | 45.89 | 19823750 | |
| 817 | Phosphorylation | NSNNSAPSGAGAAFG CCCCCCCCCCCCCCC | 40.78 | 19823750 | |
| 825 | Phosphorylation | GAGAAFGSNAEEDDD CCCCCCCCCCCCCCC | 26.81 | 19823750 | |
| 834 | Phosphorylation | AEEDDDLYS------ CCCCCCCCC------ | 21.23 | 19823750 | |
| 835 | Phosphorylation | EEDDDLYS------- CCCCCCCC------- | 40.83 | 21440633 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CDC48_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 CDC48_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-292; SER-318; SER-423;SER-472; SER-519; SER-599; THR-735 AND SER-770, 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-519; THR-735 ANDSER-770, AND MASS 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-770, 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-519 AND SER-770, 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-519, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-683, UBIQUITINATION ATLYS-594 AND LYS-673, AND MASS SPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-683, UBIQUITINATION ATLYS-594 AND LYS-673, AND MASS SPECTROMETRY. | |
