http://rdf.ncbi.nlm.nih.gov/pubchem/conserveddomain/PSSMID411837

Outgoing Links

Predicate Object
abstract fifth type I K homology (KH) RNA-binding domain found in vigilin and similar proteins. Vigilin, also called high density lipoprotein-binding protein, or HDL-binding protein, is a ubiquitous and highly conserved RNA-binding protein that shuttles between nucleus and cytoplasm presumably in contact with RNA molecules. It may be involved in chromosome partitioning at mitosis, facilitating translation and tRNA transport, and control of mRNA metabolism, including estrogen-mediated stabilization of vitellogenin mRNA. Vigilin is up-regulated by cholesterol loading of cells and functions to protect cells from over-accumulation of cholesterol. It may play a role in cell sterol metabolism. Disruption of human vigilin impairs chromosome condensation and segregation. Vigilin has a unique structure of 14-15 consecutively arranged, but non-identical K-homology (KH) domains which apparently mediate RNA-protein binding. The model corresponds to the fifth one.
title KH-I_Vigilin_rpt5
isDiscussedBy http://rdf.ncbi.nlm.nih.gov/pubchem/reference/26002083
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/28965111
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/16315294
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14591919
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4356732
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1189567
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/4091872
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/28112537
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/7037828
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24666674
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2574771
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/11333162
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/14588304
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/5077392
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/1810108
http://rdf.ncbi.nlm.nih.gov/pubchem/reference/24704999
type http://purl.obolibrary.org/obo/SO_0000417

Incoming Links

Predicate Subject
has component http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ00341
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ9Z1A6
http://rdf.ncbi.nlm.nih.gov/pubchem/protein/ACCQ8VDJ3

Total number of triples: 22.