FKBP3

Last updated
FKBP3
Protein FKBP3 PDB 1pbk.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases FKBP3 , FKBP-25, FKBP-3, FKBP25, PPIase, FK506 binding protein 3, FKBP prolyl isomerase 3
External IDs OMIM: 186947 MGI: 1353460 HomoloGene: 1525 GeneCards: FKBP3
Orthologs
SpeciesHumanMouse
Entrez

2287

30795

Ensembl

ENSG00000100442

ENSMUSG00000020949

UniProt

Q00688

Q62446

RefSeq (mRNA)

NM_002013

NM_013902

RefSeq (protein)

NP_002004

NP_038930

Location (UCSC) Chr 14: 45.12 – 45.14 Mb Chr 12: 65.11 – 65.12 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

FK506-binding protein 3 also known as FKBP25 is a protein that in humans is encoded by the FKBP3 gene. [5] [6] [7]

Contents

Function

The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. It has a higher affinity for rapamycin than for FK506 and thus may be an important target molecule for immunosuppression by rapamycin. [8] [7]

Interactions

FKBP3 has been shown to interact with YY1, [9] HDAC1, [9] Histone deacetylase 2, [9] DNA, [10] and Mdm2. [11] Both crystal structure of FKBP25 with FK506 and the NMR structure of full length FKBP25 has been published with PDB ID 5D75 and 2MPH respectively. [8] [12]

Related Research Articles

<span class="mw-page-title-main">DNA-binding protein</span> Proteins that bind with DNA, such as transcription factors, polymerases, nucleases and histones

DNA-binding proteins are proteins that have DNA-binding domains and thus have a specific or general affinity for single- or double-stranded DNA. Sequence-specific DNA-binding proteins generally interact with the major groove of B-DNA, because it exposes more functional groups that identify a base pair.

In molecular biology, immunophilins are endogenous cytosolic peptidyl-prolyl isomerases (PPI) that catalyze the interconversion between the cis and trans isomers of peptide bonds containing the amino acid proline (Pro). They are chaperone molecules that generally assist in the proper folding of diverse "client" proteins. Immunophilins are traditionally classified into two families that differ in sequence and biochemical characteristics. These two families are: "cyclosporin-binding cyclophilins (CyPs)" and "FK506-binding proteins (FKBPs)". In 2005, a group of dual-family immunophilins (DFI) has been discovered, mostly in unicellular organisms; these DFIs are natural chimera of CyP and FKBPs, fused in either order.

<span class="mw-page-title-main">FKBP</span>

The FKBPs, or FK506 binding proteins, constitute a family of proteins that have prolyl isomerase activity and are related to the cyclophilins in function, though not in amino acid sequence. FKBPs have been identified in many eukaryotes, ranging from yeast to humans, and function as protein folding chaperones for proteins containing proline residues. Along with cyclophilin, FKBPs belong to the immunophilin family.

<span class="mw-page-title-main">FKBP4</span> Protein-coding gene in humans

FK506-binding protein 4 is a protein that in humans is encoded by the FKBP4 gene.

<span class="mw-page-title-main">FKBP1A</span> Protein and coding gene in humans

Peptidyl-prolyl cis-trans isomerase FKBP1A is an enzyme that in humans is encoded by the FKBP1A gene. It is also commonly referred to as FKBP-12 or FKBP12 and is a member of a family of FK506-binding proteins (FKBPs).

<span class="mw-page-title-main">PPIB</span> Protein-coding gene in the species Homo sapiens

Peptidyl-prolyl cis-trans isomerase B is an enzyme that is encoded by the PPIB gene. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to regulate protein folding of type I collagen. Generally, PPIases are found in all eubacteria and eukaryotes, as well as in a few archaebacteria, and thus are highly conserved.

<span class="mw-page-title-main">P4HB</span> Protein-coding gene in the species Homo sapiens

Protein disulfide-isomerase, also known as the beta-subunit of prolyl 4-hydroxylase (P4HB), is an enzyme that in humans encoded by the P4HB gene. The human P4HB gene is localized in chromosome 17q25. Unlike other prolyl 4-hydroxylase family proteins, this protein is multifunctional and acts as an oxidoreductase for disulfide formation, breakage, and isomerization. The activity of P4HB is tightly regulated. Both dimer dissociation and substrate binding are likely to enhance its enzymatic activity during the catalysis process.

<span class="mw-page-title-main">FKBP5</span> Protein-coding gene in humans

FK506 binding protein 5, also known as FKBP5, is a protein which in humans is encoded by the FKBP5 gene.

<span class="mw-page-title-main">FKBP8</span> Protein-coding gene in the species Homo sapiens

FK506-binding protein 8 is a protein that in humans is encoded by the FKBP8 gene.

<span class="mw-page-title-main">FKBP1B</span> Protein-coding gene in the species Homo sapiens

Peptidyl-prolyl cis-trans isomerase FKBP1B is an enzyme that in humans is encoded by the FKBP1B gene.

<span class="mw-page-title-main">Peptidylprolyl isomerase D</span> Protein-coding gene in the species Homo sapiens

Peptidylprolyl isomerase D (cyclophilin D), also known as PPID, is an enzyme which in humans is encoded by the PPID gene on chromosome 4. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to facilitate folding or repair of proteins. In addition, PPID participates in many biological processes, including mitochondrial metabolism, apoptosis, redox, and inflammation, as well as in related diseases and conditions, such as ischemic reperfusion injury, AIDS, and cancer.

<span class="mw-page-title-main">GLMN</span> Protein-coding gene in the species Homo sapiens

Glomulin is a protein that in humans is encoded by the GLMN gene.

<span class="mw-page-title-main">FKBP2</span> Protein-coding gene in the species Homo sapiens

FK506-binding protein 2 is a protein that in humans is encoded by the FKBP2 gene.

<span class="mw-page-title-main">Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4</span> Protein-coding gene in the species Homo sapiens

Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 is an enzyme that in humans is encoded by the PIN4 gene.

<span class="mw-page-title-main">PPIH</span> Protein-coding gene in the species Homo sapiens

Peptidyl-prolyl cis-trans isomerase H is an enzyme that in humans is encoded by the PPIH gene.

<span class="mw-page-title-main">PPIC</span> Protein-coding gene in the species Homo sapiens

Peptidyl-prolyl cis-trans isomerase C (PPIC) is an enzyme that in humans is encoded by the PPIC gene on chromosome 5. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to facilitate folding or repair of proteins. In addition, PPIC participates in many biological processes, including mitochondrial metabolism, apoptosis, redox, and inflammation, as well as in related diseases and conditions, such as ischemic reperfusion injury, AIDS, and cancer.

<span class="mw-page-title-main">PPIG (gene)</span> Protein-coding gene in the species Homo sapiens

Peptidyl-prolyl cis-trans isomerase G is an enzyme that in humans is encoded by the PPIG gene.

<span class="mw-page-title-main">PPIE (gene)</span> Protein-coding gene in the species Homo sapiens

Peptidylprolyl isomerase E (cyclophilin E), also known as PPIE, is an enzyme which in humans is encoded by the PPIE gene on chromosome 1. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to facilitate folding or repair of proteins. In addition, PPIE participates in many biological processes, including mitochondrial metabolism, apoptosis, and inflammation, as well as related diseases and conditions, such as ischemic reperfusion injury, AIDS, influenza, and cancer.

<span class="mw-page-title-main">FKBP10</span> Protein-coding gene in the species Homo sapiens

FK506-binding protein 10 is a protein that in humans is encoded by the FKBP10 gene.

<span class="mw-page-title-main">FKBP6</span> Protein family

FK506 binding protein 6, also known as FKBP6, is a human gene. The encoded protein shows structural homology to FKBP immunophilins, which bind to the immunosuppressants FK506 and rapamycin.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000100442 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020949 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Hung DT, Schreiber SL (Jun 1992). "cDNA cloning of a human 25 kDa FK506 and rapamycin binding protein". Biochem. Biophys. Res. Commun. 184 (2): 733–8. doi:10.1016/0006-291X(92)90651-Z. PMID   1374240.
  6. ↑ Porat R, Poutsiaka DD, Miller LC, Granowitz EV, Dinarello CA (May 1992). "Interleukin-1 (IL-1) receptor blockade reduces endotoxin and Borrelia burgdorferi-stimulated IL-8 synthesis in human mononuclear cells". FASEB J. 6 (7): 2482–6. doi: 10.1096/fasebj.6.7.1532945 . PMID   1532945. S2CID   29899093.
  7. 1 2 "Entrez Gene: FKBP3 FK506 binding protein 3, 25kDa".
  8. 1 2 Prakash A, Rajan S, Yoon HS (April 2016). "Crystal structure of the FK506 binding domain of human FKBP25 in complex with FK506". Protein Science. 25 (4): 905–910. doi:10.1002/pro.2875. ISSN   1469-896X. PMC   4941220 . PMID   26749369.
  9. 1 2 3 Yang WM, Yao YL, Seto E (Sep 2001). "The FK506-binding protein 25 functionally associates with histone deacetylases and with transcription factor YY1". EMBO J. 20 (17): 4814–25. doi:10.1093/emboj/20.17.4814. PMC   125595 . PMID   11532945.
  10. ↑ Prakash A, Shin J, Rajan S, Yoon HS (2016). "Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin". Nucleic Acids Res. 44 (6): 2909–25. doi:10.1093/nar/gkw001. PMC   4824100 . PMID   26762975.
  11. ↑ Ochocka AM, Kampanis P, Nicol S, Allende-Vega N, Cox M, Marcar L, Milne D, Fuller-Pace F, Meek D (Feb 2009). "FKBP25, a novel regulator of the p53 pathway, induces the degradation of MDM2 and activation of p53". FEBS Lett. 583 (4): 621–6. doi:10.1016/j.febslet.2009.01.009. PMID   19166840. S2CID   6110.
  12. ↑ Prakash A, Shin J, Rajan S, Yoon HS (2016-04-07). "Structural basis of nucleic acid recognition by FK506-binding protein 25 (FKBP25), a nuclear immunophilin". Nucleic Acids Research. 44 (6): 2909–2925. doi:10.1093/nar/gkw001. ISSN   0305-1048. PMC   4824100 . PMID   26762975.

Further reading


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