Mapping of the genes for human endoplasmic reticular heat shock protein gp96/grp94

Maki, R. G., Eddy, R. L., Byers, M., Shows, T. B., Srivastava, P. K. (January 1993) Mapping of the genes for human endoplasmic reticular heat shock protein gp96/grp94. Somat Cell Mol Genet, 19 (1). pp. 73-81. ISSN 0740-7750 (Print)0740-7750 (Linking)

URL: https://www.ncbi.nlm.nih.gov/pubmed/8460400
DOI: 10.1007/bf01233956

Abstract

The murine tumor rejection antigen gp96 (TRA1, mapped to mouse chromosome 10) is a member of the heat shock protein family. Using a fragment of the murine gp96 cDNA as a probe, three gp96-related human genes have been isolated and structurally characterized. They have been mapped to human chromosomes 1 (p22), 12 (q24.2-->q24.3), and 15 (q25-->q26) by Southern blot hybridization and in situ hybridization of gene-specific probes. Only one of the genes, designated TRA1 (human chromosome 12) is a coding gene; the other genes (TRA1P1 and TRAP2) appear to be independently derived, processed pseudogenes.

Item Type: Paper
Uncontrolled Keywords: Animals Antigens, Neoplasm/*genetics Base Sequence Chromosome Mapping *Chromosomes, Human, Pair 1 *Chromosomes, Human, Pair 12 *Chromosomes, Human, Pair 15 Dna Endoplasmic Reticulum/*metabolism Heat-Shock Proteins/*genetics Humans Hybrid Cells Membrane Glycoproteins/*genetics Mice Molecular Sequence Data Pseudogenes
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > chromosome
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > chromosomes, structure and function > chromosome

bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function
CSHL Authors:
Communities: CSHL labs > Maki lab
Depositing User: Matt Covey
Date: January 1993
Date Deposited: 26 Oct 2016 21:30
Last Modified: 26 Oct 2016 21:30
Related URLs:
URI: http://repository.cshl.edu/id/eprint/33639

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