Entry - *140575 - HEAT-SHOCK PROTEIN, 90-KD, ALPHA, CLASS A, MEMBER 2, PSEUDOGENE; HSP90AA2P - OMIM
 
* 140575

HEAT-SHOCK PROTEIN, 90-KD, ALPHA, CLASS A, MEMBER 2, PSEUDOGENE; HSP90AA2P


Alternative titles; symbols

HEAT-SHOCK PROTEIN, 90-KD, ALPHA, CLASS A, MEMBER 2; HSP90AA2
HEAT-SHOCK 90-KD PROTEIN 1, ALPHA-LIKE 3, FORMERLY; HSPCAL3, FORMERLY


HGNC Approved Gene Symbol: HSP90AA2P

Cytogenetic location: 11p14.1     Genomic coordinates (GRCh38): 11:27,888,171-27,891,092 (from NCBI)


TEXT

Description

HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90AA2 is a cytosolic HSP90 protein. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1; 191175) and mitochondria (TRAP1; 606219) (Chen et al., 2005). See HSP90AA1 (140571) for further information on HSP90 proteins.


Cloning and Expression

By database analysis, Chen et al. (2005) identified 2 HSP90AA2 variants encoding proteins of 312 and 757 amino acids. Like other HSP90 proteins, the 757-amino acid HSP90AA2 protein has a highly conserved N-terminal domain, a charged domain, a middle domain involved in ATPase activity, a second charged domain, and a C-terminal domain. It also has a 4-helical cytokine motif and a gln-rich region.


Gene Structure

Chen et al. (2005) determined that the HSP90AA2 gene contains 2 exons.


Mapping

Ozawa et al. (1992) used fluorescence in situ hybridization to map the HSPCAL3 gene to chromosome 11p14.2-14.1.

By genomic sequence analysis, Chen et al. (2005) mapped the HSP90AA2 gene to chromosome 11p14.1.


Nomenclature

Chen et al. (2005) provided a revised nomenclature system for the HSP90 gene family. Under this system, the root HSP90A indicates cytosolic HSP90, HSP90B indicates endoplasmic reticulum HSP90, and TRAP indicates mitochondrial HSP90. HSP90A was divided into 2 classes, with HSP90AA representing conventional HSP90-alpha, and HSP90AB representing HSP90-beta. The number following the root/class represents the gene in that class, and a 'P' at the end indicates a putative pseudogene.


REFERENCES

  1. Chen, B., Piel, W. H., Gui, L., Bruford, E., Monteiro, A. The HSP90 family of genes in the human genome: insights into their divergence and evolution. Genomics 86: 627-637, 2005. [PubMed: 16269234, related citations] [Full Text]

  2. Ozawa, K., Murakami, Y., Eki, T., Soeda, E., Yokoyama, K. Mapping of the gene family for human heat-shock protein 90-alpha to chromosomes 1, 4, 11, and 14. Genomics 12: 214-220, 1992. [PubMed: 1740332, related citations] [Full Text]


Matthew B. Gross - updated : 8/12/2008
Mark H. Paalman - updated : 3/4/1997
Creation Date:
Victor A. McKusick : 2/1/1992
mgross : 05/02/2023
mgross : 08/12/2008
mgross : 8/12/2008
terry : 7/24/1998
dkim : 7/21/1998
mark : 3/4/1997
mark : 3/4/1997
mark : 3/4/1997
supermim : 3/16/1992
carol : 2/1/1992

* 140575

HEAT-SHOCK PROTEIN, 90-KD, ALPHA, CLASS A, MEMBER 2, PSEUDOGENE; HSP90AA2P


Alternative titles; symbols

HEAT-SHOCK PROTEIN, 90-KD, ALPHA, CLASS A, MEMBER 2; HSP90AA2
HEAT-SHOCK 90-KD PROTEIN 1, ALPHA-LIKE 3, FORMERLY; HSPCAL3, FORMERLY


HGNC Approved Gene Symbol: HSP90AA2P

Cytogenetic location: 11p14.1     Genomic coordinates (GRCh38): 11:27,888,171-27,891,092 (from NCBI)


TEXT

Description

HSP90 proteins are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. HSP90 proteins normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress. HSP90AA2 is a cytosolic HSP90 protein. Other HSP90 proteins are found in endoplasmic reticulum (HSP90B1; 191175) and mitochondria (TRAP1; 606219) (Chen et al., 2005). See HSP90AA1 (140571) for further information on HSP90 proteins.


Cloning and Expression

By database analysis, Chen et al. (2005) identified 2 HSP90AA2 variants encoding proteins of 312 and 757 amino acids. Like other HSP90 proteins, the 757-amino acid HSP90AA2 protein has a highly conserved N-terminal domain, a charged domain, a middle domain involved in ATPase activity, a second charged domain, and a C-terminal domain. It also has a 4-helical cytokine motif and a gln-rich region.


Gene Structure

Chen et al. (2005) determined that the HSP90AA2 gene contains 2 exons.


Mapping

Ozawa et al. (1992) used fluorescence in situ hybridization to map the HSPCAL3 gene to chromosome 11p14.2-14.1.

By genomic sequence analysis, Chen et al. (2005) mapped the HSP90AA2 gene to chromosome 11p14.1.


Nomenclature

Chen et al. (2005) provided a revised nomenclature system for the HSP90 gene family. Under this system, the root HSP90A indicates cytosolic HSP90, HSP90B indicates endoplasmic reticulum HSP90, and TRAP indicates mitochondrial HSP90. HSP90A was divided into 2 classes, with HSP90AA representing conventional HSP90-alpha, and HSP90AB representing HSP90-beta. The number following the root/class represents the gene in that class, and a 'P' at the end indicates a putative pseudogene.


REFERENCES

  1. Chen, B., Piel, W. H., Gui, L., Bruford, E., Monteiro, A. The HSP90 family of genes in the human genome: insights into their divergence and evolution. Genomics 86: 627-637, 2005. [PubMed: 16269234] [Full Text: https://doi.org/10.1016/j.ygeno.2005.08.012]

  2. Ozawa, K., Murakami, Y., Eki, T., Soeda, E., Yokoyama, K. Mapping of the gene family for human heat-shock protein 90-alpha to chromosomes 1, 4, 11, and 14. Genomics 12: 214-220, 1992. [PubMed: 1740332] [Full Text: https://doi.org/10.1016/0888-7543(92)90368-3]


Contributors:
Matthew B. Gross - updated : 8/12/2008
Mark H. Paalman - updated : 3/4/1997

Creation Date:
Victor A. McKusick : 2/1/1992

Edit History:
mgross : 05/02/2023
mgross : 08/12/2008
mgross : 8/12/2008
terry : 7/24/1998
dkim : 7/21/1998
mark : 3/4/1997
mark : 3/4/1997
mark : 3/4/1997
supermim : 3/16/1992
carol : 2/1/1992