| UniProt ID | HRD1_YEAST | |
|---|---|---|
| UniProt AC | Q08109 | |
| Protein Name | ERAD-associated E3 ubiquitin-protein ligase HRD1 | |
| Gene Name | HRD1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 551 | |
| Subcellular Localization |
Endoplasmic reticulum membrane Multi-pass membrane protein . |
|
| Protein Description | E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC1 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of endoplasmic reticulum proteins (ERQC), also called ER-associated degradation (ERAD). 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. ERAD-M substrates are processed by the same HRD1-HRD3 core complex, but only a subset of the other components is required for ERAD-M.. | |
| Protein Sequence | MVPENRRKQLAIFVVVTYLLTFYCVYSATKTSVSFLQVTLKLNEGFNLMVLSIFILLNSTLLWQLLTKLLFGELRLIEHEHIFERLPFTIINTLFMSSLFHERYFFTVAFFGLLLLYLKVFHWILKDRLEALLQSINDSTTMKTLIFSRFSFNLVLLAVVDYQIITRCISSIYTNQKSDIESTSLYLIQVMEFTMLLIDLLNLFLQTCLNFWEFYRSQQSLSNENNHIVHGDPTDENTVESDQSQPVLNDDDDDDDDDRQFTGLEGKFMYEKAIDVFTRFLKTALHLSMLIPFRMPMMLLKDVVWDILALYQSGTSLWKIWRNNKQLDDTLVTVTVEQLQNSANDDNICIICMDELIHSPNQQTWKNKNKKPKRLPCGHILHLSCLKNWMERSQTCPICRLPVFDEKGNVVQTTFTSNSDITTQTTVTDSTGIATDQQGFANEVDLLPTRTTSPDIRIVPTQNIDTLAMRTRSTSTPSPTWYTFPLHKTGDNSVGSSRSAYEFLITNSDEKENGIPVKLTIENHEVNSLHGDGGEQIAKKIVIPDKFIQHI | |
| 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 |
|---|---|---|---|---|---|
| 31 | Phosphorylation | CVYSATKTSVSFLQV HHHHCCCCCEEEEEE | 29.97 | 21126336 | |
| 453 | Phosphorylation | LLPTRTTSPDIRIVP CCCCCCCCCCCEEEE | 21.69 | 23749301 | |
| 471 | Phosphorylation | IDTLAMRTRSTSTPS CCEEEECCCCCCCCC | 18.84 | 28889911 | |
| 473 | Phosphorylation | TLAMRTRSTSTPSPT EEEECCCCCCCCCCC | 26.54 | 22369663 | |
| 474 | Phosphorylation | LAMRTRSTSTPSPTW EEECCCCCCCCCCCE | 33.07 | 22369663 | |
| 475 | Phosphorylation | AMRTRSTSTPSPTWY EECCCCCCCCCCCEE | 39.30 | 22369663 | |
| 476 | Phosphorylation | MRTRSTSTPSPTWYT ECCCCCCCCCCCEEE | 28.07 | 22369663 | |
| 478 | Phosphorylation | TRSTSTPSPTWYTFP CCCCCCCCCCEEEEE | 34.74 | 23749301 | |
| 480 | Phosphorylation | STSTPSPTWYTFPLH CCCCCCCCEEEEEEE | 35.13 | 21440633 | |
| 483 | Phosphorylation | TPSPTWYTFPLHKTG CCCCCEEEEEEEECC | 15.44 | 21440633 | |
| 497 | Phosphorylation | GDNSVGSSRSAYEFL CCCCCCCCCCEEEEE | 25.07 | 20377248 | |
| 499 | Phosphorylation | NSVGSSRSAYEFLIT CCCCCCCCEEEEEEC | 36.83 | 21440633 | |
| 528 | Phosphorylation | IENHEVNSLHGDGGE EECCCCCCCCCCCCH | 27.24 | 20377248 | |
| 546 | Ubiquitination | KKIVIPDKFIQHI-- HEEECCHHHHHCC-- | 38.73 | 24961812 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HRD1_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 HRD1_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-475 AND SER-528, ANDMASS SPECTROMETRY. | |
