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GOT2 glutamic-oxaloacetic transaminase 2 [ Gallus gallus (chicken) ]

Gene ID: 396533, updated on 3-Apr-2024

Summary

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Symbol
GOT2provided by CGNC
Full Name
glutamic-oxaloacetic transaminase 2provided by CGNC
Primary source
CGNC:1656
See related
Ensembl:ENSGALG00010021438
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Gallus gallus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; Phasianinae; Gallus
Orthologs
human mouse all
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Genomic context

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See GOT2 in Genome Data Viewer
Location:
chromosome: 11
Exon count:
11
Annotation release Status Assembly Chr Location
106 current bGalGal1.mat.broiler.GRCg7b (GCF_016699485.2) 11 NC_052542.1 (1495732..1506319, complement)
106 current bGalGal1.pat.whiteleghornlayer.GRCg7w (GCF_016700215.2) 11 NC_052583.1 (1667993..1678581, complement)

Chromosome 11 - NC_052542.1Genomic Context describing neighboring genes Neighboring gene CCR4-NOT transcription complex subunit 1 Neighboring gene small nucleolar RNA SNORA50 Neighboring gene uncharacterized LOC121106579 Neighboring gene solute carrier family 38 member 7 Neighboring gene calbindin 2 Neighboring gene purine nucleoside phosphorylase

Genomic regions, transcripts, and products

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Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Molecular modeling and functional confirmation of a predicted fatty acid binding site of mitochondrial aspartate aminotransferase. Bradbury MW, et al. J Mol Biol, 2011 Sep 23. PMID 21803047, Free PMC Article
  2. Crystal structures and solution studies of oxime adducts of mitochondrial aspartate aminotransferase. Marković-Housley Z, et al. Eur J Biochem, 1996 Mar 15. PMID 8665890
  3. The covalent structure of mitochondrial aspartate aminotransferase from chicken. Identification of segments of the polypeptide chain invariant specifically in the mitochondrial isoenzyme. Graf-Hausner U, et al. J Biol Chem, 1983 Jul 25. PMID 6345546
  4. The primary structure of the precursor of chicken mitochondrial aspartate aminotransferase. Cloning and sequence analysis of cDNA. Jaussi R, et al. J Biol Chem, 1985 Dec 25. PMID 3840803
  5. X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase. McPhalen CA, et al. J Mol Biol, 1992 May 20. PMID 1593633

See all (8) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The modeling and comparison with the cytosolic isoform indicated that two residues (Arg201 and Ala219) were likely to be important to the structure and function of the binding site.
    Title: Molecular modeling and functional confirmation of a predicted fatty acid binding site of mitochondrial aspartate aminotransferase.
Submit: New GeneRIF Correction

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by RefSeq

Function Evidence Code Pubs
enables L-aspartate:2-oxoglutarate aminotransferase activity IEA
Inferred from Electronic Annotation
more info
 PubMed 
enables pyridoxal phosphate binding IEA
Inferred from Electronic Annotation
more info
 PubMed 
Process Evidence Code Pubs
involved_in aspartate catabolic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
involved_in biosynthetic process IEA
Inferred from Electronic Annotation
more info
 PubMed 
Component Evidence Code Pubs
located_in mitochondrion IEA
Inferred from Electronic Annotation
more info
 PubMed 

General protein information

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Preferred Names
aspartate aminotransferase, mitochondrial
Names
glutamate oxaloacetate transaminase 2
glutamic-oxaloacetic transaminase 2, mitochondrial (aspartate aminotransferase 2)
kynurenine aminotransferase 4
kynurenine aminotransferase IV
kynurenine--oxoglutarate transaminase 4
kynurenine--oxoglutarate transaminase IV
mAspAT
transaminase A
NP_990854.2
XP_015134609.3
XP_046781332.1
XP_046781333.1

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.

mRNA and Protein(s)

  1. NM_205523.2 → NP_990854.2  aspartate aminotransferase, mitochondrial precursor

    Status: PROVISIONAL

    Source sequence(s)
    JAENSK010000247
    UniProtKB/Swiss-Prot
    P00508
    UniProtKB/TrEMBL
    F1P180
    Related
    ENSGALP00010031028.1, ENSGALT00010051983.1
    Conserved Domains (1) summary
    PLN02397
    Location:25 → 423
    PLN02397; aspartate transaminase

RefSeqs of Annotated Genomes: Gallus gallus Annotation Release 106 details...Open this link in a new tab

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

Reference bGalGal1.mat.broiler.GRCg7b Primary Assembly

Genomic

  1. NC_052542.1 Reference bGalGal1.mat.broiler.GRCg7b Primary Assembly

    Range
    1495732..1506319 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_015279123.4 → XP_015134609.3  aspartate aminotransferase, mitochondrial isoform X1

Alternate bGalGal1.pat.whiteleghornlayer.GRCg7w

Genomic

  1. NC_052583.1 Alternate bGalGal1.pat.whiteleghornlayer.GRCg7w

    Range
    1667993..1678581 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_046925377.1 → XP_046781333.1  aspartate aminotransferase, mitochondrial isoform X3

  2. XM_046925376.1 → XP_046781332.1  aspartate aminotransferase, mitochondrial isoform X2

Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P00508.2 GenPept UniProtKB/Swiss-Prot:P00508

Gene LinkOut

The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.