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P80404 (GABT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-aminobutyrate aminotransferase, mitochondrial

EC=2.6.1.19
Alternative name(s):
(S)-3-amino-2-methylpropionate transaminase
EC=2.6.1.22
GABA aminotransferase
Short name=GABA-AT
Gamma-amino-N-butyrate transaminase
Short name=GABA transaminase
Short name=GABA-T
L-AIBAT
Gene names
Name:ABAT
Synonyms:GABAT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of gamma-aminobutyrate and L-beta-aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine.

Catalytic activity

4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.

(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate.

Cofactor

Pyridoxal phosphate.

Subunit structure

Homodimer; disulfide-linked. Ref.6

Subcellular location

Mitochondrion matrix.

Tissue specificity

Liver > pancreas > brain > kidney > heart > placenta.

Involvement in disease

GABA transaminase deficiency (GABATD) [MIM:613163]: An enzymatic deficiency resulting in psychomotor retardation, hypotonia, hyperreflexia, lethargy, refractory seizures, and EEG abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
   Biological processNeurotransmitter degradation
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Transferase
   PTMAcetylation
Disulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbehavior

Non-traceable author statement PubMed 11918424. Source: UniProtKB

behavioral response to cocaine

Inferred from sequence or structural similarity. Source: UniProtKB

copulation

Inferred from electronic annotation. Source: Ensembl

gamma-aminobutyric acid catabolic process

Non-traceable author statement Ref.6. Source: UniProtKB

locomotory behavior

Inferred from electronic annotation. Source: Ensembl

negative regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

neurotransmitter catabolic process

Non-traceable author statement Ref.6. Source: UniProtKB

neurotransmitter secretion

Traceable author statement. Source: Reactome

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to iron ion

Inferred from electronic annotation. Source: Ensembl

response to nicotine

Inferred from electronic annotation. Source: Ensembl

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_component4-aminobutyrate transaminase complex

Inferred from direct assay Ref.6. Source: UniProtKB

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection

Inferred from electronic annotation. Source: Ensembl

   Molecular_function(S)-3-amino-2-methylpropionate transaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

4-aminobutyrate transaminase activity

Traceable author statement. Source: Reactome

protein homodimerization activity

Inferred from physical interaction Ref.6. Source: UniProtKB

pyridoxal phosphate binding

Inferred from direct assay PubMed 15650327. Source: UniProtKB

succinate-semialdehyde dehydrogenase binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CRKP461081EBI-1753838,EBI-886

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion
Chain29 – 5004724-aminobutyrate aminotransferase, mitochondrial
PRO_0000001249

Amino acid modifications

Modified residue2311N6-succinyllysine By similarity
Modified residue2521N6-acetyllysine; alternate By similarity
Modified residue2521N6-succinyllysine; alternate By similarity
Modified residue2791N6-acetyllysine By similarity
Modified residue3181N6-acetyllysine By similarity
Modified residue3571N6-(pyridoxal phosphate)lysine
Modified residue4131N6-acetyllysine; alternate By similarity
Modified residue4131N6-succinyllysine; alternate By similarity
Modified residue4521N6-acetyllysine By similarity
Modified residue4701N6-acetyllysine By similarity
Disulfide bond163 ↔ 166 By similarity
Disulfide bond321Interchain Ref.6

Natural variations

Natural variant561Q → R. Ref.4
Corresponds to variant rs1731017 [ dbSNP | Ensembl ].
VAR_018979
Natural variant2201R → K in GABATD; 25% reduction in activity. Ref.8
VAR_008883

Experimental info

Mutagenesis3211C → M, S, A, G or K: Loss of activity. Ref.6
Sequence conflict171S → T in AAA74449. Ref.1
Sequence conflict1091H → D in AAA74449. Ref.1
Sequence conflict1131L → V in AAA74449. Ref.1
Sequence conflict1321G → E in AAA74449. Ref.1
Sequence conflict155 – 17117MSQLI…SNENA → CPSSSPWPACPAPMKTT in AAB38510. Ref.2
Sequence conflict1911Q → K in AAA74449. Ref.1
Sequence conflict2041G → W in AAA74449. Ref.1
Sequence conflict2161A → S in AAA74449. Ref.1
Sequence conflict2471P → T in AAB38510. Ref.2
Sequence conflict2681R → G in AAA74449. Ref.1
Sequence conflict3201G → C in AAA74449. Ref.1
Sequence conflict3661H → L in AAA74449. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P80404 [UniParc].

Last modified June 7, 2004. Version 3.
Checksum: F990B0B6B77BD3F5

FASTA50056,439
        10         20         30         40         50         60 
MASMLLAQRL ACSFQHSYRL LVPGSRHISQ AAAKVDVEFD YDGPLMKTEV PGPRSQELMK 

        70         80         90        100        110        120 
QLNIIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSVPIGYSHP ALLKLIQQPQ 

       130        140        150        160        170        180 
NASMFVNRPA LGILPPENFV EKLRQSLLSV APKGMSQLIT MACGSCSNEN ALKTIFMWYR 

       190        200        210        220        230        240 
SKERGQRGFS QEELETCMIN QAPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS 

       250        260        270        280        290        300 
FDWPIAPFPR LKYPLEEFVK ENQQEEARCL EEVEDLIVKY RKKKKTVAGI IVEPIQSEGG 

       310        320        330        340        350        360 
DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA DVMTFSKKMM 

       370        380        390        400        410        420 
TGGFFHKEEF RPNAPYRIFN TWLGDPSKNL LLAEVINIIK REDLLNNAAH AGKALLTGLL 

       430        440        450        460        470        480 
DLQARYPQFI SRVRGRGTFC SFDTPDDSIR NKLILIARNK GVVLGGCGDK SIRFRPTLVF 

       490        500 
RDHHAHLFLN IFSDILADFK 

« Hide

References

« Hide 'large scale' references
[1]"Screening and sequence determination of a cDNA encoding the human brain 4-aminobutyrate aminotransferase."
Osei Y.D., Churchich J.E.
Gene 155:185-187(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]Medina-Kauwe L.K., Gibson K.M., Nyhan W.L., Tobin A.J.
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pancreatic islet.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-56.
Tissue: Brain and Eye.
[5]"Primary structure and tissue distribution of human 4-aminobutyrate aminotransferase."
de Biase D., Barra D., Simmaco M., John R.A., Bossa F.
Eur. J. Biochem. 227:476-480(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-485, PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[6]"Cysteine-321 of human brain GABA transaminase is involved in intersubunit cross-linking."
Yoon C.S., Kim D.W., Jang S.H., Lee B.R., Choi H.S., Choi S.H., Kim S.Y., An J.J., Kwon O.S., Kang T.C., Won M.H., Cho S.W., Lee K.S., Park J., Eum W.S., Choi S.Y.
Mol. Cells 18:214-219(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERCHAIN DISULFIDE BOND, MUTAGENESIS OF CYS-321.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"4-aminobutyrate aminotransferase (GABA-transaminase) deficiency."
Medina-Kauwe L.K., Tobin A.J., De Meirleir L., Jaeken J., Jakobs C., Nyhan W.L., Gibson K.M.
J. Inherit. Metab. Dis. 22:414-427(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT GABATD LYS-220.
+Additional computationally mapped references.

Web resources

GeneReviews
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L32961 mRNA. Translation: AAA74449.1.
U80226 mRNA. Translation: AAB38510.1.
AK290501 mRNA. Translation: BAF83190.1.
BC015628 mRNA. Translation: AAH15628.1.
BC031413 mRNA. Translation: AAH31413.1.
S75578 mRNA. Translation: AAD14176.1.
PIRJC4022.
S67470.
RefSeqNP_000654.2. NM_000663.4.
NP_001120920.1. NM_001127448.1.
NP_065737.2. NM_020686.5.
UniGeneHs.336768.

3D structure databases

ProteinModelPortalP80404.
SMRP80404. Positions 39-499.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106536. 1 interaction.
IntActP80404. 1 interaction.
STRING9606.ENSP00000268251.

Chemistry

BindingDBP80404.
ChEMBLCHEMBL2044.
DrugBankDB00510. Divalproex sodium.
DB00951. Isoniazid.
DB00160. L-Alanine.
DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.
DB00119. Pyruvic acid.
DB00906. Tiagabine.
DB00313. Valproic Acid.
DB01080. Vigabatrin.
GuidetoPHARMACOLOGY2464.

PTM databases

PhosphoSiteP80404.

Polymorphism databases

DMDM48429239.

Proteomic databases

PaxDbP80404.
PeptideAtlasP80404.
PRIDEP80404.

Protocols and materials databases

DNASU18.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000268251; ENSP00000268251; ENSG00000183044.
ENST00000396600; ENSP00000379845; ENSG00000183044.
ENST00000425191; ENSP00000411916; ENSG00000183044.
GeneID18.
KEGGhsa:18.
UCSCuc002czc.4. human.

Organism-specific databases

CTD18.
GeneCardsGC16P008768.
HGNCHGNC:23. ABAT.
HPAHPA041528.
HPA041690.
MIM137150. gene.
613163. phenotype.
neXtProtNX_P80404.
Orphanet2066. Gamma-aminobutyric acid transaminase deficiency.
PharmGKBPA24372.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0160.
HOVERGENHBG000634.
InParanoidP80404.
KOK13524.
OrthoDBEOG7ZPNJW.
PhylomeDBP80404.
TreeFamTF105021.

Enzyme and pathway databases

BioCycMetaCyc:HS02477-MONOMER.
ReactomeREACT_13685. Neuronal System.
SABIO-RKP80404.

Gene expression databases

ArrayExpressP80404.
BgeeP80404.
CleanExHS_ABAT.
GenevestigatorP80404.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 2 hits.
InterProIPR004631. 4NH2But_aminotransferase_euk.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PTHR11986:SF6. PTHR11986:SF6. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00699. GABAtrns_euk. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSABAT. human.
GenomeRNAi18.
NextBio45.
PROP80404.
SOURCESearch...

Entry information

Entry nameGABT_HUMAN
AccessionPrimary (citable) accession number: P80404
Secondary accession number(s): A8K386 expand/collapse secondary AC list , Q16260, Q8N5W2, Q96BG2, Q99800
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: June 7, 2004
Last modified: April 16, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM