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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2002-3-21
pubmed:abstractText
We have previously isolated and characterized a novel human gene HUEL (C4orf1) that is ubiquitously expressed in a wide range of human fetal, adult tissues and cancer cell lines. HUEL maps to region 4p12-p13 within the short arm of chromosome 4 whose deletion is frequently associated with bladder and other carcinomas. Here we present the genomic organization, sizes and boundaries of exons and introns of HUEL. The GC-rich upstream genomic region and 5' untranslated region (UTR) together constitute a CpG island, a hallmark of housekeeping genes. The 3250 bp HUEL cDNA incorporates a 1704 bp ORF that translates into a hydrophilic protein of 568-amino acids (aa), detected as a band of approximately 70 kDa by Western blotting. We have isolated the murine homolog of HUEL which exhibits 89% nucleotide and 94% amino acid identity to its human counterpart. The HUEL protein shares significant homology with the minimal DNA-binding domain (DNA-BD) of the DNA repair protein encoded by the xeroderma pigmentosum group A (XPA) gene. Other notable features within HUEL include the putative nuclear receptor interaction motif, nuclear localization and export signals, zinc finger, leucine zipper and acidic domains. Mimosine-mediated cell cycle synchronization of PLC/PRF/5 liver cancer cells clearly portrayed translocation of HUEL into the nucleus specifically during the S phase of the cell cycle. Yeast two-hybrid experiments revealed interactions of HUEL with two partner proteins (designated HIPC and HIPB) bearing similarity to a mitotically phosphorylated protein and to reverse transcriptase. Co-immunoprecipitation assays validated the interaction between HUEL and HIPC proteins in mammalian cells. HUEL is likely to be an evolutionarily conserved, housekeeping gene that plays a role intimately linked with cellular replication, DNA synthesis and/or transcriptional regulation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1357-2725
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
487-504
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11906820-Active Transport, Cell Nucleus, pubmed-meshheading:11906820-Amino Acid Sequence, pubmed-meshheading:11906820-Animals, pubmed-meshheading:11906820-Base Sequence, pubmed-meshheading:11906820-Cation Transport Proteins, pubmed-meshheading:11906820-Cell Cycle, pubmed-meshheading:11906820-Cell Cycle Proteins, pubmed-meshheading:11906820-DNA Repair, pubmed-meshheading:11906820-DNA-Binding Proteins, pubmed-meshheading:11906820-Flow Cytometry, pubmed-meshheading:11906820-Humans, pubmed-meshheading:11906820-Liver Neoplasms, pubmed-meshheading:11906820-Mice, pubmed-meshheading:11906820-Microscopy, Fluorescence, pubmed-meshheading:11906820-Molecular Sequence Data, pubmed-meshheading:11906820-Nuclear Proteins, pubmed-meshheading:11906820-RNA-Binding Proteins, pubmed-meshheading:11906820-Sequence Alignment, pubmed-meshheading:11906820-Tumor Cells, Cultured, pubmed-meshheading:11906820-Two-Hybrid System Techniques, pubmed-meshheading:11906820-Urinary Bladder Neoplasms, pubmed-meshheading:11906820-Xeroderma Pigmentosum Group A Protein
pubmed:year
2002
pubmed:articleTitle
The novel human HUEL (C4orf1) protein shares homology with the DNA-binding domain of the XPA DNA repair protein and displays nuclear translocation in a cell cycle-dependent manner.
pubmed:affiliation
Human Genome Laboratory, Department of Microbiology, Faculty of Medicine, National University of Singapore, Kent Ridge 117597, Singapore.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't