Tag | Content |
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CPLM ID | CPLM-006342 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1 |
Protein Synonyms/Alias | Oligosaccharyl transferase subunit WBP1; Oligosaccharyl transferase subunit beta |
Gene Name | WBP1 |
Gene Synonyms/Alias | YEL002C |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
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85 | NIIVFPTKGGKNLAR | ubiquitination | [1] | 136 | LGIYPSPKGHVIRDY | ubiquitination | [1] | 168 | KYVYNARKSEDFVFG | ubiquitination | [1] | 203 | RTSFTESKGKCNSWT | ubiquitination | [1] | 241 | SSDFLKNKNQDSNQE | ubiquitination | [1] | 261 | LKWTFNEKSVIKSVH | ubiquitination | [1] |
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Reference | [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation. Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J. Nat Methods. 2013 Jul;10(7):676-82. [ PMID: 23749301] |
Functional Description | Essential subunit of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. |
Sequence Annotation | CARBOHYD 60 60 N-linked (GlcNAc...) (Potential). CARBOHYD 332 332 N-linked (GlcNAc...) (Potential). |
Keyword | Complete proteome; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane; Reference proteome; Signal; Transferase; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 430 AA |
Protein Sequence | MRTDWNFFFC ILLQAIFVVG TQTSRTLVLY DQSTEPLEEY SVYLKDLEQR NYKLEYLDIN 60 STSTTVDLYD KEQRLFDNII VFPTKGGKNL ARQIPVKQLI KFFENEGNIL CMSSPGAVPN 120 TIRLFLNELG IYPSPKGHVI RDYFSPSSEE LVVSSNHLLN KYVYNARKSE DFVFGESSAA 180 LLENREQIVP ILNAPRTSFT ESKGKCNSWT SGSQGFLVVG FQNLNNARLV WIGSSDFLKN 240 KNQDSNQEFA KELLKWTFNE KSVIKSVHAV HSHADGTSYD EEPYKIKDKV IYSVGFSEWN 300 GEEWLPHIAD DIQFELRQVD PYYRLTLSPS GNDSETQYYT TGEFILPDRH GVFTFLTDYR 360 KIGLSFTTDK DVKAIRHLAN DEYPRSWEIS NSWVYISAIC GVIVAWIFFV VSFVTTSSVG 420 KKLETFKKTN 430 |
Gene Ontology | GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0005635; C:nuclear envelope; IDA:SGD. GO:0008250; C:oligosaccharyltransferase complex; IPI:SGD. GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IPI:SGD. GO:0006487; P:protein N-linked glycosylation; IPI:SGD. GO:0018279; P:protein N-linked glycosylation via asparagine; IEA:InterPro. |
Interpro | |
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PROSITE | |
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