D2HGDH

Protein-coding gene in the species Homo sapiens
D2HGDH
Identifiers
AliasesD2HGDH, D2HGD, D-2-hydroxyglutarate dehydrogenase
External IDsOMIM: 609186; MGI: 2138209; HomoloGene: 5534; GeneCards: D2HGDH; OMA:D2HGDH - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for D2HGDH
Genomic location for D2HGDH
Band2q37.3Start241,734,602 bp[1]
End241,768,816 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for D2HGDH
Genomic location for D2HGDH
Band1|1 DStart93,752,631 bp[2]
End93,780,070 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right uterine tube

  • pancreatic ductal cell

  • tendon of biceps brachii

  • left lobe of thyroid gland

  • right lobe of thyroid gland

  • anterior pituitary

  • skin of abdomen

  • right lobe of liver

  • left ovary

  • transverse colon
Top expressed in
  • left lobe of liver

  • otolith organ

  • utricle

  • interventricular septum

  • Rostral migratory stream

  • ascending aorta

  • hand

  • semi-lunar valve

  • Paneth cell

  • ciliary body
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • oxidoreductase activity
  • catalytic activity
  • flavin adenine dinucleotide binding
  • oxidoreductase activity, acting on CH-OH group of donors
  • D-lactate dehydrogenase (cytochrome) activity
  • (R)-2-hydroxyglutarate dehydrogenase activity
  • FAD binding
Cellular component
  • mitochondrial matrix
  • mitochondrion
  • extrinsic component of cytoplasmic side of plasma membrane
Biological process
  • response to calcium ion
  • response to zinc ion
  • response to magnesium ion
  • response to cobalt ion
  • response to manganese ion
  • 2-oxoglutarate metabolic process
  • lactate oxidation
  • respiratory electron transport chain
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

728294

98314

Ensembl

ENSG00000180902

ENSMUSG00000073609

UniProt

Q8N465

Q8CIM3

RefSeq (mRNA)

NM_001287249
NM_152783
NM_001352824

NM_178882
NM_001310767

RefSeq (protein)

NP_001274178
NP_689996
NP_001339753

NP_001297696
NP_849213

Location (UCSC)Chr 2: 241.73 – 241.77 MbChr 1: 93.75 – 93.78 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

D-2-hydroxyglutarate dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the D2HGDH gene.[5][6][7]

This gene encodes D-2hydroxyglutarate dehydrogenase is a mitochondrial enzyme belonging to the FAD-binding oxidoreductase/transferase type 4 family. This enzyme, which is most active in liver and kidney but also active in heart and brain, converts D-2-hydroxyglutarate to 2-ketoglutarate. Mutations in this gene are present in D-2-hydroxyglutaric aciduria, a rare recessive neurometabolic disorder causing developmental delay, epilepsy, hypotonia, and dysmorphic features.[7]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000180902 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000073609 – 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. ^ Achouri Y, Noel G, Vertommen D, Rider MH, Veiga-Da-Cunha M, Van Schaftingen E (Jun 2004). "Identification of a dehydrogenase acting on D-2-hydroxyglutarate". Biochem J. 381 (Pt 1): 35–42. doi:10.1042/BJ20031933. PMC 1133759. PMID 15070399.
  6. ^ Struys EA, Salomons GS, Achouri Y, Van Schaftingen E, Grosso S, Craigen WJ, Verhoeven NM, Jakobs C (Jan 2005). "Mutations in the D-2-hydroxyglutarate dehydrogenase gene cause D-2-hydroxyglutaric aciduria". Am J Hum Genet. 76 (2): 358–60. doi:10.1086/427890. PMC 1196381. PMID 15609246.
  7. ^ a b "Entrez Gene: D2HGDH D-2-hydroxyglutarate dehydrogenase".

Further reading

  • Gibson KM, Craigen W, Herman GE, Jakobs C (1995). "D-2-hydroxyglutaric aciduria in a newborn with neurological abnormalities: a new neurometabolic disorder?". J. Inherit. Metab. Dis. 16 (3): 497–500. doi:10.1007/BF00711664. PMID 7609436. S2CID 31099476.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • 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. doi:10.1038/ng1285. PMID 14702039.
  • 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. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • 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. Bibcode:2005Natur.434..724H. doi:10.1038/nature03466. PMID 15815621.
  • Struys EA, Korman SH, Salomons GS, et al. (2005). "Mutations in phenotypically mild D-2-hydroxyglutaric aciduria". Ann. Neurol. 58 (4): 626–30. doi:10.1002/ana.20559. PMID 16037974. S2CID 45926378.
  • Misra VK, Struys EA, O'brien W, et al. (2006). "Phenotypic heterogeneity in the presentation of D-2-hydroxyglutaric aciduria in monozygotic twins". Mol. Genet. Metab. 86 (1–2): 200–5. doi:10.1016/j.ymgme.2005.06.005. PMID 16081310.
  • 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. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Struys EA, Verhoeven NM, Salomons GS, et al. (2006). "D-2-hydroxyglutaric aciduria in three patients with proven SSADH deficiency: genetic coincidence or a related biochemical epiphenomenon?". Mol. Genet. Metab. 88 (1): 53–7. doi:10.1016/j.ymgme.2005.12.002. PMID 16442322.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.


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