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rdf:type |
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lifeskim:mentions |
umls-concept:C0015295,
umls-concept:C0019733,
umls-concept:C0019744,
umls-concept:C0031727,
umls-concept:C0041485,
umls-concept:C0086943,
umls-concept:C0178719,
umls-concept:C0205250,
umls-concept:C1514562,
umls-concept:C1533691,
umls-concept:C1709915,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2700640
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pubmed:issue |
10
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pubmed:dateCreated |
1983-7-8
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pubmed:abstractText |
HLA-A2 and -B7 antigens are phosphorylated by Rous sarcoma kinase (pp60v-src) in vitro. The phosphate group is attached to the heavy chains as determined by NaDodSO4/polyacrylamide gel electrophoresis. The site of phosphorylation was localized to the COOH-terminal intracellular domain by its susceptibility to limited trypsin proteolysis. Furthermore, the 32P-labeled amino acid is a single tyrosine residue located in the COOH terminus of the heavy chain. The protein sequences of known class I human and murine intracellular domains contain a highly conserved sequence -K-G-G-X-Y- located NH2-terminally to the single tyrosine residue of this domain. The DNA sequences that encode class I antigen intracellular domains were compared by computer with a homology matrix program. Exon 6 which encodes the conserved tyrosine-containing protein sequence in both human and mouse is 75% homologous across species and 90-100% homologous within species. The significance of the high degree of conservation within exon 6 is discussed.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-14217160,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-221907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-226956,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-228858,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-230504,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-282620,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-356051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-36738,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-565878,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6157683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6172716,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6178977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6186382,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6246443,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6246487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6253501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6254669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6254988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6273838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6278432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6290988,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6461010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-670198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6895103,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6895187,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6933473,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6934534,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6954478,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-6975122,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6304688-7058332
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
80
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2894-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:6304688-Amino Acid Sequence,
pubmed-meshheading:6304688-Avian Sarcoma Viruses,
pubmed-meshheading:6304688-Base Sequence,
pubmed-meshheading:6304688-HLA Antigens,
pubmed-meshheading:6304688-HLA-A2 Antigen,
pubmed-meshheading:6304688-HLA-B7 Antigen,
pubmed-meshheading:6304688-Humans,
pubmed-meshheading:6304688-Oncogene Protein pp60(v-src),
pubmed-meshheading:6304688-Phosphorylation,
pubmed-meshheading:6304688-Tyrosine,
pubmed-meshheading:6304688-Viral Proteins
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pubmed:year |
1983
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pubmed:articleTitle |
HLA-A2 and HLA-B7 antigens are phosphorylated in vitro by rous sarcoma virus kinase (pp60v-src) at a tyrosine residue encoded in a highly conserved exon of the intracellular domain.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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