| UniProt ID | UBX2_YEAST | |
|---|---|---|
| UniProt AC | Q04228 | |
| Protein Name | UBX domain-containing protein 2 | |
| Gene Name | UBX2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 584 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
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| Protein Description | Integral endoplasmic reticulum membrane protein that coordinates the assembly of the ER-associated protein degradation (ERAD) machinery at the ER membrane. Mediates binding of CDC48 to the E3 ubiquitin ligases SSM4/DOA10 and HRD1, and to ERAD substrates. Component of the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains. ERAD-C substrates are ubiquitinated through DOA10 in conjunction with the E2 ubiquitin-conjugating enzymes UBC6 and UBC7-CUE1. Also component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M). ERAD-L substrates are ubiquitinated through HRD1 in conjunction with the E2 ubiquitin-conjugating enzymes UBC1 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex and targeted to the proteasome.. | |
| Protein Sequence | MPVVNHEDSEFHLSHTEEDKLNEFQVITNFPPEDLPDVVRLLRNHGWQLEPALSRYFDGEWKGEPDQMGEPTQTSTPMAETLVPPALGPRPLLFTASLPVVRPLPANFRNDFRTIGLNGRSNTVWSMFESFSYDGNPFLFILLLIPRIINRLSATIFTFFCTLLSLHSISGGGNSGKPKISKVPKAPTRETHIPLAEILGDTKDKDAFCELKSFKPDISFNEALRIAKEEFKFMLLILVGDTYDTDTDTVDVNSKLLLEKILLNKKTLQYLRKIDNDLIIYLKCVHELEPWLVARQLGVRNTPEIFLIANVANKASHSETLPSQRLSILGKLKVNSLNRFLQSLTNVVEKYTPELVVNKTEMHELRMSREIKKLQEDAYKKSLEMDRIKAIEKEKSLKHAQDLKLNSTARQLKWLKACIDEIQPFETTGKQATLQFRTSSGKRFVKKFPSMTTLYQIYQSIGCHIYLAVYSSDPAEWSNALQDKIRQLSADDDMLCFKEGQLETATATTIEELGHIINNELTSFDLERGKLEFDFELVSPFPKYTVHPNEHMSVDQVPQLWPNGSLLVEALDEEDEEDEENEEQ | |
| 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 |
|---|---|---|---|---|---|
| 185 | Ubiquitination | PKISKVPKAPTRETH CCCCCCCCCCCCCCC | 70.73 | 17644757 | |
| 203 | Ubiquitination | AEILGDTKDKDAFCE HHHHCCCCCHHHCHH | 68.47 | 17644757 | |
| 205 | Ubiquitination | ILGDTKDKDAFCELK HHCCCCCHHHCHHCC | 53.14 | 23749301 | |
| 212 | Ubiquitination | KDAFCELKSFKPDIS HHHCHHCCCCCCCCC | 31.39 | 17644757 | |
| 215 | Ubiquitination | FCELKSFKPDISFNE CHHCCCCCCCCCHHH | 49.20 | 23749301 | |
| 228 | Ubiquitination | NEALRIAKEEFKFML HHHHHHHHHHHCEEE | 56.24 | 23749301 | |
| 260 | Acetylation | NSKLLLEKILLNKKT CHHHHHHHHHCCHHH | 38.33 | 24489116 | |
| 266 | Ubiquitination | EKILLNKKTLQYLRK HHHHCCHHHHHHHHH | 54.09 | 23749301 | |
| 273 | Ubiquitination | KTLQYLRKIDNDLII HHHHHHHHCCCCEEE | 52.39 | 17644757 | |
| 283 | Ubiquitination | NDLIIYLKCVHELEP CCEEEEEEEHHHHCH | 19.76 | 17644757 | |
| 314 | Ubiquitination | LIANVANKASHSETL EEEECCHHCCCCCCC | 41.34 | 23749301 | |
| 316 | Phosphorylation | ANVANKASHSETLPS EECCHHCCCCCCCCH | 29.20 | 29136822 | |
| 318 | Phosphorylation | VANKASHSETLPSQR CCHHCCCCCCCCHHH | 29.76 | 23749301 | |
| 320 | Phosphorylation | NKASHSETLPSQRLS HHCCCCCCCCHHHHH | 47.16 | 19823750 | |
| 323 | Phosphorylation | SHSETLPSQRLSILG CCCCCCCHHHHHHHH | 30.92 | 19823750 | |
| 327 | Phosphorylation | TLPSQRLSILGKLKV CCCHHHHHHHHHHHH | 20.25 | 19823750 | |
| 331 | Ubiquitination | QRLSILGKLKVNSLN HHHHHHHHHHHHHHH | 41.51 | 22817900 | |
| 333 | Ubiquitination | LSILGKLKVNSLNRF HHHHHHHHHHHHHHH | 42.74 | 22817900 | |
| 350 | Ubiquitination | SLTNVVEKYTPELVV HHHHHHHHHCCHHHC | 42.70 | 24961812 | |
| 359 | Ubiquitination | TPELVVNKTEMHELR CCHHHCCHHHHHHHH | 33.96 | 24961812 | |
| 372 | Ubiquitination | LRMSREIKKLQEDAY HHHHHHHHHHHHHHH | 42.55 | 17644757 | |
| 373 | Ubiquitination | RMSREIKKLQEDAYK HHHHHHHHHHHHHHH | 62.15 | 23749301 | |
| 380 | Ubiquitination | KLQEDAYKKSLEMDR HHHHHHHHHHHHHHH | 37.29 | 23749301 | |
| 381 | Ubiquitination | LQEDAYKKSLEMDRI HHHHHHHHHHHHHHH | 47.82 | 23749301 | |
| 416 | Ubiquitination | ARQLKWLKACIDEIQ HHHHHHHHHHHHHCC | 39.85 | 17644757 | |
| 427 | Phosphorylation | DEIQPFETTGKQATL HHCCCCCCCCCCEEE | 41.02 | 28889911 | |
| 428 | Phosphorylation | EIQPFETTGKQATLQ HCCCCCCCCCCEEEE | 34.87 | 28889911 | |
| 430 | Ubiquitination | QPFETTGKQATLQFR CCCCCCCCCEEEEEE | 34.37 | 23749301 | |
| 498 | Ubiquitination | DDDMLCFKEGQLETA CCCEEEEECCCCEEC | 61.00 | 17644757 | |
| 530 | Ubiquitination | SFDLERGKLEFDFEL CCCCCCCCEEEEEEE | 51.57 | 17644757 | |
| 543 | Ubiquitination | ELVSPFPKYTVHPNE EEECCCCCCCCCCCC | 54.66 | 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 UBX2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UBX2_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 UBX2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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