GLUD2 glutamate dehydrogenase 2 [Homo sapiens (human)] - Gene

Summary

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Official Symbol: GLUD2provided by HGNC
Official Full Name: glutamate dehydrogenase 2provided by HGNC
Primary source: HGNC:4336
See related: Ensembl:ENSG00000182890; HPRD:02143; MIM:300144; Vega:OTTHUMG00000022320
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: GDH2; GLUDP1
Summary: The protein encoded by this gene is localized to the mitochondrion and acts as a homohexamer to recycle glutamate during neurotransmission. The encoded enzyme catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate. This gene is intronless.[provided by RefSeq, Jan 2010]

Genomic context

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Location :: Xq24-q25

Sequence :: Chromosome: X; NC_000023.10 (120181462..120183796)

See GLUD2 in Epigenomics, MapViewer

Chromosome X - NC_000023.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence

Go to nucleotideGraphics FASTA GenBank

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Bibliography

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GeneRIFs: Gene References Into Functions What's a GeneRIF?

first N-terminal alpha helical structure is crucial for the mitochondrial import of hGDH2 and these findings may have implications in understanding the evolutionary mechanisms that led to the large mitochondrial targeting signals of human GDHs
Title: The complex regulation of human glud1 and glud2 glutamate dehydrogenases and its implications in nerve tissue biology.
first N-terminal alpha helical structure is crucial for the mitochondrial import of hGDH2 and these findings may have implications in understanding the evolutionary mechanisms that led to the large mitochondrial targeting signals of human GDHs
Title: Alpha helical structures in the leader sequence of human GLUD2 glutamate dehydrogenase responsible for mitochondrial import.
[review] Whereas GDH2 in most mammals is encoded by a single functional GLUD1 gene expressed widely, humans have acquired through retroposition an X-linked GLUD2 gene that encodes a highly homologous isoenzyme GDH2 expressed in testis and brain.
Title: The human GLUD2 glutamate dehydrogenase and its regulation in health and disease.
Human GDH1 appears to act like bovine GDH1, but human GDH2 does not show the same enhancement of branched chain alpha-keto acid dehydrogenase complex enzyme activities.
Title: Interaction between glutamate dehydrogenase (GDH) and L-leucine catabolic enzymes: intersecting metabolic pathways.
A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
Title: Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration.
GLUD2 glutamate dehydrogenase is expressed in neural and testicular supporting cells
Title: Human GLUD2 glutamate dehydrogenase is expressed in neural and testicular supporting cells.
A gain-of-function rare polymorphism in hGDH2 hastens the onset of Parkinson's disease in hemizygous subjects.
Title: Gain-of-function variant in GLUD2 glutamate dehydrogenase modifies Parkinson's disease onset.
Observational study of gene-disease association. (HuGE Navigator)
Title: Gain-of-function variant in GLUD2 glutamate dehydrogenase modifies Parkinson's disease onset.
Hence, while most of the hGDHs translocate into the mitochondria (a process associated with cleavage of the signal sequence), part of the protein localizes to the endoplasmic reticulum, probably serving additional functions
Title: Human GLUD1 and GLUD2 glutamate dehydrogenase localize to mitochondria and endoplasmic reticulum.
GDH2 localizes mainly to mitochondria and to a lesser extent to the endoplasmic reticulum of cells
Title: The human GLUD2 glutamate dehydrogenase: localization and functional aspects.

Submit: New GeneRIF Correction See all (18)

Phenotypes

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Review eQTL and phenotype association data in this region using PheGenI

Interactions

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Products	Interactant	Other Gene	Source	Pubs	Description
P49448	P49448	GLUD2	HPRD	PubMed
P49448	O75674	TOM1L1	HPRD	PubMed
BioGRID:109009	BioGRID:107776	ATF2	BioGRID	PubMed	Affinity Capture-MS
BioGRID:109009	BioGRID:115352	TOM1L1	BioGRID	PubMed	Two-hybrid
BioGRID:109009	BioGRID:113164	UBC	BioGRID	PubMed	Affinity Capture-MS

Pathways from BioSystems

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Alanine, aspartate and glutamate metabolism, organism-specific biosystem (from KEGG)
Alanine, aspartate and glutamate metabolism, organism-specific biosystem
Alanine, aspartate and glutamate metabolism
Alanine, aspartate and glutamate metabolism, conserved biosystem (from KEGG)
Alanine, aspartate and glutamate metabolism, conserved biosystem
Alanine, aspartate and glutamate metabolism
Arginine and proline metabolism, organism-specific biosystem (from KEGG)
Arginine and proline metabolism, organism-specific biosystem
Arginine and proline metabolism
Arginine and proline metabolism, conserved biosystem (from KEGG)
Arginine and proline metabolism, conserved biosystem
Arginine and proline metabolism
D-Glutamine and D-glutamate metabolism, organism-specific biosystem (from KEGG)
D-Glutamine and D-glutamate metabolism, organism-specific biosystem
D-Glutamine and D-glutamate metabolism
D-Glutamine and D-glutamate metabolism, conserved biosystem (from KEGG)
D-Glutamine and D-glutamate metabolism, conserved biosystem
D-Glutamine and D-glutamate metabolism
Proximal tubule bicarbonate reclamation, organism-specific biosystem (from KEGG)
Proximal tubule bicarbonate reclamation, organism-specific biosystemOne of the major tasks of the renal proximal tubule (PT) is to secrete acid into the tubule lumen, thereby reabsorbing approximately 80% of the filtered bicarbonate (HCO3(-)), as well as generating "...
Proximal tubule bicarbonate reclamation, conserved biosystem (from KEGG)
Proximal tubule bicarbonate reclamation, conserved biosystemOne of the major tasks of the renal proximal tubule (PT) is to secrete acid into the tubule lumen, thereby reabsorbing approximately 80% of the filtered bicarbonate (HCO3(-)), as well as generating "...
arginine biosynthesis IV, organism-specific biosystem (from BIOCYC)
arginine biosynthesis IV, organism-specific biosystemThis pathway spans the mitochondrial and cytoplasmic compartments. Glutamate is formed from 2-oxoglutarate within the mitochondrial matrix. Glutamate is then transported to the cytosol. Conversion...
arginine biosynthesis IV, conserved biosystem (from BIOCYC)
arginine biosynthesis IV, conserved biosystemThis pathway spans the mitochondrial and cytoplasmic compartments. Glutamate is formed from 2-oxoglutarate within the mitochondrial matrix. Glutamate is then transported to the cytosol. Conversion...
glutamate and glutamine biosynthesis, conserved biosystem (from BIOCYC)
glutamate and glutamine biosynthesis, conserved biosystemPlease note: This collection of reactions does not represent the metabolism of a single organism. Rather, it is assembled from a variety of organisms. Its purpose is to provide an overview of the wa...
glutamate biosynthesis II, organism-specific biosystem (from BIOCYC)
glutamate biosynthesis II, organism-specific biosystemGlutamate is biosynthesized in the mitochondrion from the tricarboxylic acid (TCA) cycle intermediate alpha-ketoglutarate. As shown in this pathway, glutamate dehydrogenase NAD(P)+ produces glutamat...
glutamate biosynthesis II, conserved biosystem (from BIOCYC)
glutamate biosynthesis II, conserved biosystemGlutamate is biosynthesized in the mitochondrion from the tricarboxylic acid (TCA) cycle intermediate alpha-ketoglutarate. As shown in this pathway, glutamate dehydrogenase NAD(P)+ produces glutamat...
glutamate degradation X, organism-specific biosystem (from BIOCYC)
glutamate degradation X, organism-specific biosystemIn this pathway :GLT is deaminated by an NAD(P)-dependent dehydrogenase, forming :AMMONIA and :2-KETOGLUTARATE, which is then fed to the :TCA. The deamination of : GLT is a key reaction not only in t...
glutamate degradation X, conserved biosystem (from BIOCYC)
glutamate degradation X, conserved biosystemIn this pathway |FRAME:GLT| is deaminated by an NAD(P)-dependent dehydrogenase, forming |FRAME:AMMONIA| and |FRAME:2-KETOGLUTARATE|, which is then fed to the |FRAME:TCA|. The deamination of |FRAME: G...

General gene information

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Markers

GLUD1-1 (e-PCR)
- UniSTS:511772

DXS7028E (e-PCR)
- UniSTS:99109

GLUD1_1725 (e-PCR)
- UniSTS:277286

D10S2137 (e-PCR)
- UniSTS:79931

RH80866 (e-PCR)
- UniSTS:85863

L47793 (e-PCR)
- UniSTS:77672

G44300 (e-PCR)
- UniSTS:95094

GDB:193864 (e-PCR)
- UniSTS:155772

RH65005 (e-PCR)
- UniSTS:76935

RH79929 (e-PCR)
- UniSTS:88720

L77323 (e-PCR)
- UniSTS:24257

GDB:277890 (e-PCR)
- UniSTS:156370

Homology

Homologs of the GLUD2 gene: The GLUD2 gene is conserved in chimpanzee, Rhesus monkey, and zebrafish.
OrthoDB: The Hierarchical Catalog of Eukaryotic Orthologs

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
ADP binding	IDA Inferred from Direct Assay more info	PubMed
GTP binding	IDA Inferred from Direct Assay more info	PubMed
glutamate dehydrogenase (NAD+) activity	IDA Inferred from Direct Assay more info	PubMed
glutamate dehydrogenase [NAD(P)+] activity	IDA Inferred from Direct Assay more info	PubMed
leucine binding	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
glutamate biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
glutamate catabolic process	IDA Inferred from Direct Assay more info	PubMed
glutamate metabolic process	IDA Inferred from Direct Assay more info	PubMed
oxidation-reduction process	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
NOT cytoplasm	IDA Inferred from Direct Assay more info	PubMed
mitochondrion	IDA Inferred from Direct Assay more info

General protein information

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Preferred Names: glutamate dehydrogenase 2, mitochondrial

Names: glutamate dehydrogenase 2, mitochondrial; GDH 2; glutamate dehydrogenase pseudogene 1

NP_036216.2

EC 1.4.1.3

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

NG_016456.1 RefSeqGene

Range

5001..7335

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_012084.3 → NP_036216.2 glutamate dehydrogenase 2, mitochondrial precursor

Status: REVIEWED

Source sequence(s)

BC050732

Consensus CDS

CCDS14603.1

UniProtKB/Swiss-Prot

P49448

Related

ENSP00000327589, OTTHUMP00000023966, ENST00000328078, OTTHUMT00000058133

Conserved Domains (3) summary

COG0334
Location:104 – 555
Blast Score: 955

GdhA; Glutamate dehydrogenase/leucine dehydrogenase [Amino acid transport and metabolism]

cd01076
Location:263 – 548
Blast Score: 877

NAD_bind_1_Glu_DH; NAD(P) binding domain of glutamate dehydrogenase, subgroup 1

pfam02812
Location:112 – 240
Blast Score: 513

ELFV_dehydrog_N; Glu/Leu/Phe/Val dehydrogenase, dimerisation domain

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 104

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh37.p10 Primary Assembly

Genomic

NC_000023.10 Reference GRCh37.p10 Primary Assembly

Range

120181462..120183796

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GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

AC_000155.1 Alternate HuRef

Range

109559683..109562017

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GenBank, FASTA, Sequence Viewer (Graphics)

Alternate CHM1_1.0

Genomic

NC_018934.1 Alternate CHM1_1.0

Range

120135419..120137753

Download

GenBank, FASTA, Sequence Viewer (Graphics)

Nucleotide		Protein
Heading	Accession and Version	Protein
genomic	ABBA01036087.1 (684..3018)	None
genomic	AC006144.1	AAD05030.1
genomic	AMYH01022925.1 (60948..63282)	None
genomic	U08997.1	AAA20969.1
genomic	X66310.1	CAA46995.1
mRNA	AK313356.1	BAG36157.1
mRNA	BC005111.1	AAH05111.1
mRNA	BC050732.2	AAH50732.1