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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
36
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pubmed:dateCreated |
1991-1-23
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pubmed:databankReference |
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pubmed:abstractText |
We have previously characterized a 65-kilodalton protein (p65) as an interleukin 2 stimulated phosphoprotein in human T cells and showed that three endopeptide sequences of p65 are present in the sequence of l-plastin [Zu et al. (1990) Biochemistry 29, 1055-1062]. In this paper, we present the complete primary structure of p65 based on the cDNA isolated from a human T lymphocyte (KUT-2) cDNA library. Analysis of p65 sequences and the amino acid composition of cleaved p65 N-terminal peptide indicated that the deduced p65 amino acid sequence exactly coincides with that of l-plastin over the C-terminal 580 residues [Lin et al. (1988) Mol. Cell. Biol. 8, 4659-4668] and has a 57-residue extension at the N-terminus to l-plastin. Computer-assisted structural analysis revealed that p65 is a multidomain molecule involving at least three intriguing functional domains: two putative calcium-binding sites along the N-terminal 80 amino acid residues; a putative calmodulin-binding site following the calcium-binding region; and two tandem repeats of putative actin-binding domains in its middle and C-terminal parts, each containing approximately 240 amino acid residues. These results suggest that p65 belongs to actin-binding proteins.
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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/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin,
http://linkedlifedata.com/resource/pubmed/chemical/Calmodulin-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/plastin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
29
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8319-24
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2252891-Actins,
pubmed-meshheading:2252891-Amino Acid Sequence,
pubmed-meshheading:2252891-Base Sequence,
pubmed-meshheading:2252891-Binding Sites,
pubmed-meshheading:2252891-Calcium,
pubmed-meshheading:2252891-Calcium-Binding Proteins,
pubmed-meshheading:2252891-Calmodulin,
pubmed-meshheading:2252891-Calmodulin-Binding Proteins,
pubmed-meshheading:2252891-DNA,
pubmed-meshheading:2252891-Humans,
pubmed-meshheading:2252891-Interleukin-2,
pubmed-meshheading:2252891-Membrane Glycoproteins,
pubmed-meshheading:2252891-Microfilament Proteins,
pubmed-meshheading:2252891-Molecular Sequence Data,
pubmed-meshheading:2252891-Phosphoproteins,
pubmed-meshheading:2252891-Sequence Alignment,
pubmed-meshheading:2252891-Sequence Homology, Nucleic Acid,
pubmed-meshheading:2252891-T-Lymphocytes
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pubmed:year |
1990
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pubmed:articleTitle |
65-kilodalton protein phosphorylated by interleukin 2 stimulation bears two putative actin-binding sites and two calcium-binding sites.
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pubmed:affiliation |
Department of Pathology, Kyoto University, Japan.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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