Basic Information
Name | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1 (Oligosaccharyl transferase subunit WBP1) (Oligosaccharyl transferase subunit beta) |
Uniprot ID | P33767 |
Systematic gene name | YEL002C |
Standard gene name | WBP1 |
Gene names | WBP1 YEL002C |
Description from SGD | YEL002C WBP1 SGDID:S000000728, Chr V from 150014-148722, Genome Release 64-3-1, reverse complement, Verified ORF, "Beta subunit of the oligosaccharyl transferase glycoprotein complex; required for N-linked glycosylation of proteins in the endoplasmic reticulum; human homolog DDOST can complement yeast growth defect during down-regulation of yeast gene" |
Protein length | 430 |
Download | sequence (fasta, from Uniprot), modifications (csv format) |
Database links | Uniprot, SGD, TheCellVision.org, FungiDB |
Sequence
MRTDWNFFFC ILLQAIFVVG TQTSRTLVLY DQSTEPLEEY SVYLKDLEQR
NYKLEYLDIN STSTTVDLYD KEQRLFDNII VFPTKGGKNL ARQIPVKQLI
KFFENEGNIL CMSSPGAVPN TIRLFLNELG IYPSPKGHVI RDYFSPSSEE
LVVSSNHLLN KYVYNARKSE DFVFGESSAA LLENREQIVP ILNAPRTSFT
ESKGKCNSWT SGSQGFLVVG FQNLNNARLV WIGSSDFLKN KNQDSNQEFA
KELLKWTFNE KSVIKSVHAV HSHADGTSYD EEPYKIKDKV IYSVGFSEWN
GEEWLPHIAD DIQFELRQVD PYYRLTLSPS GNDSETQYYT TGEFILPDRH
GVFTFLTDYR KIGLSFTTDK DVKAIRHLAN DEYPRSWEIS NSWVYISAIC
GVIVAWIFFV VSFVTTSSVG KKLETFKKTN
NYKLEYLDIN STSTTVDLYD KEQRLFDNII VFPTKGGKNL ARQIPVKQLI
KFFENEGNIL CMSSPGAVPN TIRLFLNELG IYPSPKGHVI RDYFSPSSEE
LVVSSNHLLN KYVYNARKSE DFVFGESSAA LLENREQIVP ILNAPRTSFT
ESKGKCNSWT SGSQGFLVVG FQNLNNARLV WIGSSDFLKN KNQDSNQEFA
KELLKWTFNE KSVIKSVHAV HSHADGTSYD EEPYKIKDKV IYSVGFSEWN
GEEWLPHIAD DIQFELRQVD PYYRLTLSPS GNDSETQYYT TGEFILPDRH
GVFTFLTDYR KIGLSFTTDK DVKAIRHLAN DEYPRSWEIS NSWVYISAIC
GVIVAWIFFV VSFVTTSSVG KKLETFKKTN
Legend
- X Glycosylation
- X Ubiquitination
Structure
Structure visualized by GLmol written by biochem_fan. The structure was downloaded from the AlphaFold Protein Structure Database.
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References
[60, Glyc] | Poljak, K., Selevsek, N., Ngwa, E., Grossmann, J., Losfeld, M.E., Aebi, M. (2018). Quantitative Profiling of N-linked Glycosylation Machinery in Yeast Saccharomyces cerevisiae. Mol Cell Proteomics 17: 18-30. (Publication) (All modifications) |
[60, Glyc] | Zielinska, D.F., Gnad, F., Schropp, K., Wiśniewski, J.R., Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications) |
[85, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[136, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[168, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[203, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[241, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[261, Ubi] | Swaney, D.L., Beltrao, P., Starita, L., Guo, A., Rush, J., Fields, S., Krogan, N.J., Villén, J. (2013). Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Nature Methods 10(7): 676-682. (Publication) (All modifications) |
[332, Glyc] | Poljak, K., Selevsek, N., Ngwa, E., Grossmann, J., Losfeld, M.E., Aebi, M. (2018). Quantitative Profiling of N-linked Glycosylation Machinery in Yeast Saccharomyces cerevisiae. Mol Cell Proteomics 17: 18-30. (Publication) (All modifications) |
[332, Glyc] | Zielinska, D.F., Gnad, F., Schropp, K., Wiśniewski, J.R., Mann, M. (2012). Mapping N-glycosylation sites across seven evolutionarily distant species reveals a divergent substrate proteome despite a common core machinery. Mol Cell 46: 542-548. (Publication) (All modifications) |