HADHB
| HADHB | |||
|---|---|---|---|
Gene ontology | |||
| Molecular function |
| ||
| Cellular component | |||
| Biological process | |||
| Sources:Amigo / QuickGO | |||
Ensembl | |||||||||
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| UniProt | |||||||||
| RefSeq (mRNA) | |||||||||
| RefSeq (protein) | |||||||||
| Location (UCSC) | Chr 2: 26.24 – 26.29 Mb | Chr 5: 30.36 – 30.39 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/Edit Mouse |
Trifunctional enzyme subunit beta, mitochondrial (TP-beta) also known as 3-ketoacyl-CoA thiolase, acetyl-CoA acyltransferase, or beta-ketothiolase is an enzyme that in humans is encoded by the HADHB gene.[5]
HADHB is a subunit of the mitochondrial trifunctional protein and has thiolase activity.
Structure
The HADHB gene is located on
Function
beta-oxidation
This gene encodes the beta subunit of the mitochondrial trifunctional protein, a catalyst of mitochondrial
acyl CoA
molecule, which is two carbons shorter.
The encoded protein can also bind
mRNAs. The genes of the alpha and beta subunits of the mitochondrial trifunctional protein are located adjacent to each other in the human genome in a head-to-head orientation.[5]
Clinical significance
Mutations in this gene, along with mutations in
Charcot-Marie-tooth disease, which is a neurological disorder, which shows that mutations in this gene can result in deficiencies that present in new forms not currently described.[13]
Interactions
HADHB is a functional molecular target of ERα in the mitochondria, and the interaction may play an important role in the estrogen-mediated lipid metabolism in animals and humans.[14] Additionally, HADHB has been shown to bind to the distal 3’ untranslated region of renin mRNA, thereby regulating renin protein expression.[15]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000138029 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000059447 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ a b c d "Entrez Gene: hydroxyacyl-Coenzyme A dehydrogenase/3-ketoacyl-Coenzyme A thiolase/enoyl-Coenzyme A hydratase (trifunctional protein)".
- PMID 23965338.
- ^ "Trifunctional enzyme subunit beta, mitochondrial". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Archived from the original on 4 March 2016. Retrieved 23 March 2015.
- PMID 14630990.
- S2CID 13141165.
- S2CID 85671653.
- PMID 12838198.
- PMID 1401059.
- PMID 24314034.
- PMID 22375075.
- PMID 12933794.
Further reading
- Wang R, Yang Z, Zhu JM, et al. (2006). "[Screening for G1528C mutation in mitochondrial trifunctional protein gene in pregnant women with severe preeclampsia and new born infant]". Zhonghua Fu Chan Ke Za Zhi. 41 (10): 672–5. PMID 17199921.
- Aboulaich N, Vainonen JP, Strålfors P, Vener AV (2004). "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes". Biochem. J. 383 (Pt 2): 237–48. PMID 15242332.
- Adams DJ, Beveridge DJ, van der Weyden L, et al. (2003). "HADHB, HuR, and CP1 bind to the distal 3'-untranslated region of human renin mRNA and differentially modulate renin expression". J. Biol. Chem. 278 (45): 44894–903. PMID 12933794.
- Spiekerkoetter U, Khuchua Z, Yue Z, et al. (2004). "General mitochondrial trifunctional protein (TFP) deficiency as a result of either alpha- or beta-subunit mutations exhibits similar phenotypes because mutations in either subunit alter TFP complex expression and subunit turnover". Pediatr. Res. 55 (2): 190–6. PMID 14630990.
- Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. PMID 16344560.
- Bogenhagen DF, Rousseau D, Burke S (2008). "The layered structure of human mitochondrial DNA nucleoids". J. Biol. Chem. 283 (6): 3665–75. PMID 18063578.
- Middleton B (1994). "The mitochondrial long-chain trifunctional enzyme: 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase and 3-oxoacyl-CoA thiolase". Biochem. Soc. Trans. 22 (2): 427–31. PMID 7958339.
- Zhao Y, Meng XM, Wei YJ, et al. (2003). "Cloning and characterization of a novel cardiac-specific kinase that interacts specifically with cardiac troponin I.". J. Mol. Med. 81 (5): 297–304. S2CID 13468188.
- Behrends C, Sowa ME, Gygi SP, Harper JW (2010). "Network organization of the human autophagy system". Nature. 466 (7302): 68–76. PMID 20562859.
- Purevsuren J, Fukao T, Hasegawa Y, et al. (2009). "Clinical and molecular aspects of Japanese patients with mitochondrial trifunctional protein deficiency". Mol. Genet. Metab. 98 (4): 372–7. PMID 19699128.
- Hillier LW, Graves TA, Fulton RS, et al. (2005). "Generation and annotation of the DNA sequences of human chromosomes 2 and 4". Nature. 434 (7034): 724–31. PMID 15815621.
- Spiekerkoetter U, Sun B, Khuchua Z, et al. (2003). "Molecular and phenotypic heterogeneity in mitochondrial trifunctional protein deficiency due to beta-subunit mutations". Hum. Mutat. 21 (6): 598–607. S2CID 85671653.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. PMID 15489334.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. PMID 14702039.
- Fould B, Garlatti V, Neumann E, et al. (2010). "Structural and functional characterization of the recombinant human mitochondrial trifunctional protein". Biochemistry. 49 (39): 8608–17. PMID 20825197.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMID 12477932.
- Ibdah JA, Tein I, Dionisi-Vici C, et al. (1998). "Mild trifunctional protein deficiency is associated with progressive neuropathy and myopathy and suggests a novel genotype-phenotype correlation". J. Clin. Invest. 102 (6): 1193–9. PMID 9739053.
- Gevaert K, Goethals M, Martens L, et al. (2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. S2CID 23783563.
- Hendrickson SL, Lautenberger JA, Chinn LW, et al. (2010). "Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression". PLOS ONE. 5 (9): e12862. PMID 20877624.
- Frackowiak J, Mazur-Kolecka B, Kaczmarski W, Dickson D (2001). "Deposition of Alzheimer's vascular amyloid-beta is associated with decreased expression of brain L-3-hydroxyacyl-coenzyme A dehydrogenase (ERAB)". Brain Res. 907 (1–2): 44–53. S2CID 22800813.
External links
Media related to HADHB at Wikimedia Commons- HADHB+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
