rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
2
|
pubmed:dateCreated |
1992-2-11
|
pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M60272,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M60273,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M60352,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M60353,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M60354,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/M62419,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S65077,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S74763,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/S74785,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X56257,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X60288
|
pubmed:abstractText |
We have cloned and sequenced mouse brain AP47, the medium chain of the trans-Golgi network clathrin-associated protein complex AP-1. The predicted protein sequence of AP47 is closely related to rat and calf brain AP50, the corresponding medium chain of the plasma-membrane clathrin-associated protein complex AP-2. We have also identified in the yeast genome an open reading frame encoding a protein of previously unknown function. Referred to here as YAP54, its predicted protein sequence displays a striking homology to AP47. We therefore propose that Yap54 is the medium chain subunit of a putative AP-1 complex in yeast. From the analyses of the optimized sequence alignments of AP47, AP50 and Yap54p, we suggest a model for the domain organization of the medium chains.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0014-2956
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
5
|
pubmed:volume |
202
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
569-74
|
pubmed:dateRevised |
2007-7-23
|
pubmed:meshHeading |
pubmed-meshheading:1761056-Adaptor Protein Complex 2,
pubmed-meshheading:1761056-Adaptor Protein Complex mu Subunits,
pubmed-meshheading:1761056-Adaptor Proteins, Vesicular Transport,
pubmed-meshheading:1761056-Amino Acid Sequence,
pubmed-meshheading:1761056-Animals,
pubmed-meshheading:1761056-Base Sequence,
pubmed-meshheading:1761056-Blotting, Southern,
pubmed-meshheading:1761056-Cattle,
pubmed-meshheading:1761056-Clathrin,
pubmed-meshheading:1761056-Cloning, Molecular,
pubmed-meshheading:1761056-DNA,
pubmed-meshheading:1761056-Fungal Proteins,
pubmed-meshheading:1761056-Molecular Sequence Data,
pubmed-meshheading:1761056-Phosphoproteins,
pubmed-meshheading:1761056-Rats,
pubmed-meshheading:1761056-Saccharomyces cerevisiae,
pubmed-meshheading:1761056-Sequence Alignment
|
pubmed:year |
1991
|
pubmed:articleTitle |
The medium chains of the mammalian clathrin-associated proteins have a homolog in yeast.
|
pubmed:affiliation |
Department of Anatomy and Cellular Biology, Harvard Medical School, Boston, MA 02115.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|