Entry - *186947 - FK506-BINDING PROTEIN 3; FKBP3 - OMIM

 
 
* 186947

FK506-BINDING PROTEIN 3; FKBP3


Alternative titles; symbols

FK506-BINDING PROTEIN, T-CELL, 25-KD; FKBP25


HGNC Approved Gene Symbol: FKBP3

Cytogenetic location: 14q21.2   Genomic coordinates (GRCh38) : 14:45,115,599-45,134,481 (from NCBI)


▼ TEXT

For background information on FK506-binding proteins (FKBPs), see FKBP1A (186945).

▼ Cloning and Expression

Hung and Schreiber (1992) isolated a cDNA for FKBP25 from a human hippocampus cDNA library by oligonucleotide screening. The deduced protein contains 224 amino acids. Human FKBP25 shares 97% amino acid identity with the bovine protein and 62% homology with human FKBP12 (186945). Wiederrecht et al. (1992) independently cloned cDNA for human FKBP25.


▼ Biochemical Features

Using nuclear magnetic resonance spectroscopy, Helander et al. (2014) determined that the N-terminal domain (amino acids 1 through 73) of human FKBP25 and the structurally homologous domain (amino acids 1879 through 1966) in human HECTD1 (618649) consisted of 5 structurally distinct core helices wrapped around a common hydrophobic core, which they termed the basic tilted helix bundle (BTHB) domain. Structural analysis of the BTHB domain suggested that the DNA-binding properties of FKBP25 were mediated by the conserved basic motif, which was also present in the BTHB domain of HECTD1.


▼ Mapping

Gross (2011) mapped the FKBP3 gene to chromosome 14q21.2 based on an alignment of the FKBP3 sequence (GenBank BT006904) with the genomic sequence (GRCh37).

▼ REFERENCES

  1. Gross, M. B. Personal Communication. Baltimore, Md. 3/3/2011.

  2. Helander, S., Montecchio, M., Lemak, A., Fares, C., Almlof, J., Li, Y., Yee, A., Arrowsmith, C. H., Dhe-Paganon, S., Sunnerhagen, M. Basic tilted helix bundle--a new protein fold in human FKBP25/FKBP3 and HectD1. Biochem. Biophys. Res. Commun. 447: 26-31, 2014. [PubMed: 24667607, related citations] [Full Text]

  3. Hung, D. T., Schreiber, S. L. cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein. Biochem. Biophys. Res. Commun. 184: 733-738, 1992. [PubMed: 1374240, related citations] [Full Text]

  4. Wiederrecht, G., Martin, M. M., Sigal, N. H., Siekierka, J. J. Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin binding protein. Biochem. Biophys. Res. Commun. 185: 298-303, 1992. [PubMed: 1376117, related citations] [Full Text]


Contributors:
Bao Lige - updated : 10/30/2019
Matthew B. Gross - updated : 3/3/2011
Creation Date:
Victor A. McKusick : 6/17/1992
Edit History:
mgross : 10/30/2019
mgross : 03/03/2011
mgross : 3/3/2011
carol : 7/24/1998
alopez : 6/3/1997
carol : 2/23/1995
carol : 8/10/1992
carol : 7/23/1992
carol : 7/7/1992
carol : 6/17/1992

* 186947

FK506-BINDING PROTEIN 3; FKBP3


Alternative titles; symbols

FK506-BINDING PROTEIN, T-CELL, 25-KD; FKBP25


HGNC Approved Gene Symbol: FKBP3

Cytogenetic location: 14q21.2   Genomic coordinates (GRCh38) : 14:45,115,599-45,134,481 (from NCBI)


TEXT

For background information on FK506-binding proteins (FKBPs), see FKBP1A (186945).

Cloning and Expression

Hung and Schreiber (1992) isolated a cDNA for FKBP25 from a human hippocampus cDNA library by oligonucleotide screening. The deduced protein contains 224 amino acids. Human FKBP25 shares 97% amino acid identity with the bovine protein and 62% homology with human FKBP12 (186945). Wiederrecht et al. (1992) independently cloned cDNA for human FKBP25.


Biochemical Features

Using nuclear magnetic resonance spectroscopy, Helander et al. (2014) determined that the N-terminal domain (amino acids 1 through 73) of human FKBP25 and the structurally homologous domain (amino acids 1879 through 1966) in human HECTD1 (618649) consisted of 5 structurally distinct core helices wrapped around a common hydrophobic core, which they termed the basic tilted helix bundle (BTHB) domain. Structural analysis of the BTHB domain suggested that the DNA-binding properties of FKBP25 were mediated by the conserved basic motif, which was also present in the BTHB domain of HECTD1.


Mapping

Gross (2011) mapped the FKBP3 gene to chromosome 14q21.2 based on an alignment of the FKBP3 sequence (GenBank BT006904) with the genomic sequence (GRCh37).

REFERENCES

  1. Gross, M. B. Personal Communication. Baltimore, Md. 3/3/2011.

  2. Helander, S., Montecchio, M., Lemak, A., Fares, C., Almlof, J., Li, Y., Yee, A., Arrowsmith, C. H., Dhe-Paganon, S., Sunnerhagen, M. Basic tilted helix bundle--a new protein fold in human FKBP25/FKBP3 and HectD1. Biochem. Biophys. Res. Commun. 447: 26-31, 2014. [PubMed: 24667607] [Full Text: https://doi.org/10.1016/j.bbrc.2014.03.068]

  3. Hung, D. T., Schreiber, S. L. cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein. Biochem. Biophys. Res. Commun. 184: 733-738, 1992. [PubMed: 1374240] [Full Text: https://doi.org/10.1016/0006-291x(92)90651-z]

  4. Wiederrecht, G., Martin, M. M., Sigal, N. H., Siekierka, J. J. Isolation of a human cDNA encoding a 25 kDa FK-506 and rapamycin binding protein. Biochem. Biophys. Res. Commun. 185: 298-303, 1992. [PubMed: 1376117] [Full Text: https://doi.org/10.1016/s0006-291x(05)80990-8]


Contributors:
Bao Lige - updated : 10/30/2019
Matthew B. Gross - updated : 3/3/2011

Creation Date:
Victor A. McKusick : 6/17/1992

Edit History:
mgross : 10/30/2019
mgross : 03/03/2011
mgross : 3/3/2011
carol : 7/24/1998
alopez : 6/3/1997
carol : 2/23/1995
carol : 8/10/1992
carol : 7/23/1992
carol : 7/7/1992
carol : 6/17/1992



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OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.

NOTE: OMIM is intended for use primarily by physicians and other professionals concerned with genetic disorders, by genetics researchers, and by advanced students in science and medicine. While the OMIM database is open to the public, users seeking information about a personal medical or genetic condition are urged to consult with a qualified physician for diagnosis and for answers to personal questions.
OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.
Printed: Nov. 16, 2024