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rdf:type |
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lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0040676,
umls-concept:C0072354,
umls-concept:C0205250,
umls-concept:C0449432,
umls-concept:C0699493,
umls-concept:C1179435,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1705248,
umls-concept:C2348205
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pubmed:issue |
7
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pubmed:dateCreated |
1988-10-25
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pubmed:databankReference |
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pubmed:abstractText |
A 57 kd component of oligosaccharyl transferase, termed glycosylation site binding protein, specifically recognizes a photoaffinity probe containing the N-glycosylation site sequence Asn-Lys-Thr. It is present in the lumen of the ER (endoplasmic reticulum) and its release from this compartment results in a loss of N-glycosylation. Antibodies against this protein were used to identify cDNA clones from a lambda gt11 expression library. Analysis of its cDNA sequence reveals high sequence similarity to three other 57 kd luminal endoplasmic reticulum proteins: protein disulfide isomerase, the beta-subunit of prolyl hydroxylase, and thyroid hormone binding protein. This finding suggests that the capacity to recognize multiple polypeptide domains may reside in a single luminal protein that participates in co- and/or posttranslational modifications of newly synthesized proteins.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Hexosyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Procollagen-Proline Dioxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Disulfide-Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/Thyroid Hormones,
http://linkedlifedata.com/resource/pubmed/chemical/Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/dolichyl-diphosphooligosaccharide...,
http://linkedlifedata.com/resource/pubmed/chemical/thyroid hormone-binding proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
54
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1053-60
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2458190-Amino Acid Sequence,
pubmed-meshheading:2458190-Animals,
pubmed-meshheading:2458190-Base Sequence,
pubmed-meshheading:2458190-Carrier Proteins,
pubmed-meshheading:2458190-Chickens,
pubmed-meshheading:2458190-DNA,
pubmed-meshheading:2458190-Endoplasmic Reticulum,
pubmed-meshheading:2458190-Female,
pubmed-meshheading:2458190-Glycosylation,
pubmed-meshheading:2458190-Hexosyltransferases,
pubmed-meshheading:2458190-Humans,
pubmed-meshheading:2458190-Isomerases,
pubmed-meshheading:2458190-Membrane Proteins,
pubmed-meshheading:2458190-Models, Biological,
pubmed-meshheading:2458190-Molecular Sequence Data,
pubmed-meshheading:2458190-Molecular Weight,
pubmed-meshheading:2458190-Nucleic Acid Hybridization,
pubmed-meshheading:2458190-Procollagen-Proline Dioxygenase,
pubmed-meshheading:2458190-Protein Disulfide-Isomerases,
pubmed-meshheading:2458190-RNA,
pubmed-meshheading:2458190-Rats,
pubmed-meshheading:2458190-Thyroid Hormones,
pubmed-meshheading:2458190-Transferases
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pubmed:year |
1988
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pubmed:articleTitle |
Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ER.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Texas MD Anderson Cancer Center, Houston 77030.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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