Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-3-31
pubmed:databankReference
pubmed:abstractText
Nuclear pore complexes represent the channels for the the bi-directional movement of macromolecules between the nucleus and cytoplasm, and are thought to contain upwards of 100 different polypeptide subunits. Many of these subunits belong to a growing family of polypeptides termed nucleoporins which are characterized by the presence of O-linked N-acetylglucosamine moieties and a distinctive pentapeptide repeat (XFXFG). This paper reports the primary structure of hnup153, the human homologue of the rat nucleoporin, nup153, with which it shares 82% amino acid identity. In addition to 33 copies of the XFXFG repeat, hnup153 exhibits four repeats of 37-38 amino acids each containing an apparent 'zinc finger motif'. These zinc fingers are most closely related to those found in the mouse oncoprotein mdm-2 and a product of Drosophila small optic lobes (sol) gene.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
1217
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
219-23
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Sequence analysis of a cDNA encoding a human nuclear pore complex protein, hnup153.
pubmed:affiliation
Department of Cell Biology, Harvard Medical School, Boston, MA 02115.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.