AGXT alanine--glyoxylate aminotransferase [Homo sapiens (human)] - Gene

Summary

Official Symbol: AGXTprovided by HGNC
Official Full Name: alanine--glyoxylate aminotransferaseprovided by HGNC
Primary source: HGNC:HGNC:341
See related: Ensembl:ENSG00000172482 MIM:604285; AllianceGenome:HGNC:341
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: AGT; PH1; SPT; AGT1; SPAT; TLH6; AGXT1; Ser-PyrAT
Summary: This gene is expressed only in the liver and the encoded protein is localized mostly in the peroxisomes, where it is involved in glyoxylate detoxification. Mutations in this gene, some of which alter subcellular targetting, have been associated with type I primary hyperoxaluria. [provided by RefSeq, Jul 2008]
Expression: Restricted expression toward liver (RPKM 387.9) See more
Orthologs: mouse all
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Genomic context

Location:: 2q37.3

Exon count:: 11

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	2	NC_000002.12 (240868824..240880500)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	2	NC_060926.1 (241367223..241379660)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	2	NC_000002.11 (241808241..241819917)

Chromosome 2 - NC_000002.12 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

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See details

Project title: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Insights into the pathogenesis of primary hyperoxaluria type I from the structural dynamics of alanine:glyoxylate aminotransferase variants.
Title: Insights into the pathogenesis of primary hyperoxaluria type I from the structural dynamics of alanine:glyoxylate aminotransferase variants.
Expanding the Genetic Spectrum of AGXT Gene Variants in Egyptian Patients with Primary Hyperoxaluria Type I.
Title: Expanding the Genetic Spectrum of AGXT Gene Variants in Egyptian Patients with Primary Hyperoxaluria Type I.
Case series and literature review of primary hyperoxaluria type 1 in Chinese patients.
Title: Case series and literature review of primary hyperoxaluria type 1 in Chinese patients.
Next-generation sequencing in identification of pathogenic variants in primary hyperoxaluria among 21 Egyptian families: Identification of two novel AGXT gene mutations.
Title: Next-generation sequencing in identification of pathogenic variants in primary hyperoxaluria among 21 Egyptian families: Identification of two novel AGXT gene mutations.
Extended genetic analysis of exome sequencing for primary hyperoxaluria in pediatric urolithiasis patients with hyperoxaluria.
Title: Extended genetic analysis of exome sequencing for primary hyperoxaluria in pediatric urolithiasis patients with hyperoxaluria.
Pharmacogenetics of advanced lung cancer: Predictive value of functional genetic polymorphism AGXT Pro11Leu in clinical outcome?
Title: Pharmacogenetics of advanced lung cancer: Predictive value of functional genetic polymorphism AGXT Pro11Leu in clinical outcome?
Characteristics of the genotype and phenotype in Chinese primary hyperoxaluria type 1 populations.
Title: Characteristics of the genotype and phenotype in Chinese primary hyperoxaluria type 1 populations.
The ILE56 mutation on different genetic backgrounds of alanine:glyoxylate aminotransferase: Clinical features and biochemical characterization.
Title: The ILE56 mutation on different genetic backgrounds of alanine:glyoxylate aminotransferase: Clinical features and biochemical characterization.
Loss of alanine-glyoxylate and serine-pyruvate aminotransferase expression accelerated the progression of hepatocellular carcinoma and predicted poor prognosis.
Title: Loss of alanine-glyoxylate and serine-pyruvate aminotransferase expression accelerated the progression of hepatocellular carcinoma and predicted poor prognosis.
two human constructs, wild-type and engineered AGT (RHEAM), were tested in Agxt(-/-) mice. Repeat dosing in Agxt(-/-) mice resulted in a 40% reduction in urinary oxalate, suggesting therapeutic benefit.
Title: Systemic Alanine Glyoxylate Aminotransferase mRNA Improves Glyoxylate Metabolism in a Mouse Model of Primary Hyperoxaluria Type 1.

Submit: New GeneRIF Correction See all GeneRIFs (79)

Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Primary hyperoxaluria, type I MedGen: C0268164 OMIM: 259900 GeneReviews: Primary Hyperoxaluria Type 1	Compare labs

EBI GWAS Catalog

Description
An atlas of genetic influences on human blood metabolites. EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D15S1477 (e-PCR)
- UniSTS:474482

RH80030 (e-PCR)
- UniSTS:87680

NoName (e-PCR)
- UniSTS:481928

RH68691 (e-PCR)
- UniSTS:14988

NoName (e-PCR)
- UniSTS:489643

NoName (e-PCR)
- UniSTS:494515

NoName (e-PCR)
- UniSTS:480444

D14S779 (e-PCR)
- UniSTS:55747

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables L-serine-pyruvate transaminase activity	IBA Inferred from Biological aspect of Ancestor more info
enables L-serine-pyruvate transaminase activity	IDA Inferred from Direct Assay more info	PubMed
enables alanine-glyoxylate transaminase activity	IBA Inferred from Biological aspect of Ancestor more info
enables alanine-glyoxylate transaminase activity	IDA Inferred from Direct Assay more info	PubMed
enables alanine-glyoxylate transaminase activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables alanine-glyoxylate transaminase activity	TAS Traceable Author Statement more info	PubMed
enables amino acid binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein homodimerization activity	IDA Inferred from Direct Assay more info	PubMed
enables pyridoxal phosphate binding	IDA Inferred from Direct Assay more info	PubMed
enables pyridoxal phosphate binding	IMP Inferred from Mutant Phenotype more info	PubMed
enables transaminase activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in L-alanine catabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in L-cysteine catabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in L-serine metabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in Notch signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in glycine biosynthetic process, by transamination of glyoxylate	IBA Inferred from Biological aspect of Ancestor more info
involved_in glycine biosynthetic process, by transamination of glyoxylate	IDA Inferred from Direct Assay more info	PubMed
involved_in glyoxylate catabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in glyoxylate metabolic process	IDA Inferred from Direct Assay more info	PubMed
involved_in glyoxylate metabolic process	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in oxalic acid secretion	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in cytosol	TAS Traceable Author Statement more info
located_in intracellular membrane-bounded organelle	IDA Inferred from Direct Assay more info
located_in peroxisomal matrix	IDA Inferred from Direct Assay more info	PubMed
located_in peroxisomal matrix	TAS Traceable Author Statement more info
is_active_in peroxisome	IBA Inferred from Biological aspect of Ancestor more info
located_in peroxisome	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: alanine--glyoxylate aminotransferase

Names: L-alanine: glyoxylate aminotransferase 1; alanine--glyoxylate and serine--pyruvate aminotransferase; hepatic peroxisomal alanine:glyoxylate aminotransferase; serine--pyruvate aminotransferase

NP_000021.1

EC 2.6.1.44

EC 2.6.1.51

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_008005.1 RefSeqGene

Range

5080..16756

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GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_000030.3 → NP_000021.1 alanine--glyoxylate aminotransferase

See identical proteins and their annotated locations for NP_000021.1

Status: REVIEWED

Source sequence(s)

AA857309, AC104809, CB156891, X53414

Consensus CDS

CCDS2543.1

UniProtKB/Swiss-Prot

P21549, Q53QU6

UniProtKB/TrEMBL

A2V838

Related

ENSP00000302620.3, ENST00000307503.4

Conserved Domains (1) summary

cd06451
Location:24 → 385

AGAT_like; Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), ...