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P80404

- GABT_HUMAN

UniProt

P80404 - GABT_HUMAN

Protein

4-aminobutyrate aminotransferase, mitochondrial

Gene

ABAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    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 activityi

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

    Cofactori

    Pyridoxal phosphate.

    GO - Molecular functioni

    1. (S)-3-amino-2-methylpropionate transaminase activity Source: UniProtKB-EC
    2. 4-aminobutyrate transaminase activity Source: Reactome
    3. protein homodimerization activity Source: UniProtKB
    4. pyridoxal phosphate binding Source: UniProtKB
    5. succinate-semialdehyde dehydrogenase binding Source: UniProtKB

    GO - Biological processi

    1. behavioral response to cocaine Source: UniProtKB
    2. copulation Source: Ensembl
    3. gamma-aminobutyric acid catabolic process Source: UniProtKB
    4. locomotory behavior Source: Ensembl
    5. negative regulation of blood pressure Source: Ensembl
    6. neurotransmitter catabolic process Source: UniProtKB
    7. neurotransmitter secretion Source: Reactome
    8. response to drug Source: Ensembl
    9. response to ethanol Source: Ensembl
    10. response to hypoxia Source: Ensembl
    11. response to iron ion Source: Ensembl
    12. response to nicotine Source: Ensembl
    13. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Biological processi

    Neurotransmitter degradation

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02477-MONOMER.
    ReactomeiREACT_23964. Degradation of GABA.
    SABIO-RKP80404.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:ABAT
    Synonyms:GABAT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:23. ABAT.

    Subcellular locationi

    GO - Cellular componenti

    1. 4-aminobutyrate transaminase complex Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt
    3. mitochondrial matrix Source: Reactome
    4. mitochondrion Source: UniProtKB
    5. neuron projection Source: Ensembl

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    GABA transaminase deficiency (GABATD) [MIM:613163]: An enzymatic deficiency resulting in psychomotor retardation, hypotonia, hyperreflexia, lethargy, refractory seizures, and EEG abnormalities.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti220 – 2201R → K in GABATD; 25% reduction in activity. 1 Publication
    VAR_008883

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi321 – 3211C → M, S, A, G or K: Loss of activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi613163. phenotype.
    Orphaneti2066. Gamma-aminobutyric acid transaminase deficiency.
    PharmGKBiPA24372.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2828MitochondrionAdd
    BLAST
    Chaini29 – 5004724-aminobutyrate aminotransferase, mitochondrialPRO_0000001249Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi163 ↔ 166By similarity
    Modified residuei231 – 2311N6-succinyllysineBy similarity
    Modified residuei252 – 2521N6-acetyllysine; alternateBy similarity
    Modified residuei252 – 2521N6-succinyllysine; alternateBy similarity
    Modified residuei279 – 2791N6-acetyllysineBy similarity
    Modified residuei318 – 3181N6-acetyllysineBy similarity
    Disulfide bondi321 – 321Interchain
    Modified residuei357 – 3571N6-(pyridoxal phosphate)lysine
    Modified residuei413 – 4131N6-acetyllysine; alternateBy similarity
    Modified residuei413 – 4131N6-succinyllysine; alternateBy similarity
    Modified residuei452 – 4521N6-acetyllysineBy similarity
    Modified residuei470 – 4701N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP80404.
    PaxDbiP80404.
    PeptideAtlasiP80404.
    PRIDEiP80404.

    PTM databases

    PhosphoSiteiP80404.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP80404.
    BgeeiP80404.
    CleanExiHS_ABAT.
    GenevestigatoriP80404.

    Organism-specific databases

    HPAiHPA041528.
    HPA041690.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CRKP461081EBI-1753838,EBI-886

    Protein-protein interaction databases

    BioGridi106536. 2 interactions.
    IntActiP80404. 1 interaction.
    STRINGi9606.ENSP00000268251.

    Structurei

    3D structure databases

    ProteinModelPortaliP80404.
    SMRiP80404. Positions 39-499.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0160.
    HOVERGENiHBG000634.
    InParanoidiP80404.
    KOiK13524.
    OrthoDBiEOG7ZPNJW.
    PhylomeDBiP80404.
    TreeFamiTF105021.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    InterProiIPR004631. 4NH2But_aminotransferase_euk.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR11986. PTHR11986. 1 hit.
    PTHR11986:SF6. PTHR11986:SF6. 1 hit.
    PfamiPF00202. Aminotran_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR00699. GABAtrns_euk. 1 hit.
    PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P80404-1 [UniParc]FASTAAdd to Basket

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    MASMLLAQRL ACSFQHSYRL LVPGSRHISQ AAAKVDVEFD YDGPLMKTEV    50
    PGPRSQELMK QLNIIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI 100
    SSVPIGYSHP ALLKLIQQPQ NASMFVNRPA LGILPPENFV EKLRQSLLSV 150
    APKGMSQLIT MACGSCSNEN ALKTIFMWYR SKERGQRGFS QEELETCMIN 200
    QAPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS FDWPIAPFPR 250
    LKYPLEEFVK ENQQEEARCL EEVEDLIVKY RKKKKTVAGI IVEPIQSEGG 300
    DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA 350
    DVMTFSKKMM TGGFFHKEEF RPNAPYRIFN TWLGDPSKNL LLAEVINIIK 400
    REDLLNNAAH AGKALLTGLL DLQARYPQFI SRVRGRGTFC SFDTPDDSIR 450
    NKLILIARNK GVVLGGCGDK SIRFRPTLVF RDHHAHLFLN IFSDILADFK 500
    Length:500
    Mass (Da):56,439
    Last modified:June 7, 2004 - v3
    Checksum:iF990B0B6B77BD3F5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 171S → T in AAA74449. (PubMed:7721088)Curated
    Sequence conflicti109 – 1091H → D in AAA74449. (PubMed:7721088)Curated
    Sequence conflicti113 – 1131L → V in AAA74449. (PubMed:7721088)Curated
    Sequence conflicti132 – 1321G → E in AAA74449. (PubMed:7721088)Curated
    Sequence conflicti155 – 17117MSQLI…SNENA → CPSSSPWPACPAPMKTT in AAB38510. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti191 – 1911Q → K in AAA74449. (PubMed:7721088)Curated
    Sequence conflicti204 – 2041G → W in AAA74449. (PubMed:7721088)Curated
    Sequence conflicti216 – 2161A → S in AAA74449. (PubMed:7721088)Curated
    Sequence conflicti247 – 2471P → T in AAB38510. 1 PublicationCurated
    Sequence conflicti268 – 2681R → G in AAA74449. (PubMed:7721088)Curated
    Sequence conflicti320 – 3201G → C in AAA74449. (PubMed:7721088)Curated
    Sequence conflicti366 – 3661H → L in AAA74449. (PubMed:7721088)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti56 – 561Q → R.1 Publication
    Corresponds to variant rs1731017 [ dbSNP | Ensembl ].
    VAR_018979
    Natural varianti220 – 2201R → K in GABATD; 25% reduction in activity. 1 Publication
    VAR_008883

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS10534.1.
    PIRiJC4022.
    S67470.
    RefSeqiNP_000654.2. NM_000663.4.
    NP_001120920.1. NM_001127448.1.
    NP_065737.2. NM_020686.5.
    UniGeneiHs.336768.

    Genome annotation databases

    EnsembliENST00000268251; ENSP00000268251; ENSG00000183044.
    ENST00000396600; ENSP00000379845; ENSG00000183044.
    ENST00000425191; ENSP00000411916; ENSG00000183044.
    GeneIDi18.
    KEGGihsa:18.
    UCSCiuc002czc.4. human.

    Polymorphism databases

    DMDMi48429239.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS10534.1.
    PIRi JC4022.
    S67470.
    RefSeqi NP_000654.2. NM_000663.4.
    NP_001120920.1. NM_001127448.1.
    NP_065737.2. NM_020686.5.
    UniGenei Hs.336768.

    3D structure databases

    ProteinModelPortali P80404.
    SMRi P80404. Positions 39-499.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106536. 2 interactions.
    IntActi P80404. 1 interaction.
    STRINGi 9606.ENSP00000268251.

    Chemistry

    BindingDBi P80404.
    ChEMBLi CHEMBL2044.
    DrugBanki DB00160. L-Alanine.
    DB00780. Phenelzine.
    DB00119. Pyruvic acid.
    DB00313. Valproic Acid.
    DB01080. Vigabatrin.
    GuidetoPHARMACOLOGYi 2464.

    PTM databases

    PhosphoSitei P80404.

    Polymorphism databases

    DMDMi 48429239.

    Proteomic databases

    MaxQBi P80404.
    PaxDbi P80404.
    PeptideAtlasi P80404.
    PRIDEi P80404.

    Protocols and materials databases

    DNASUi 18.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000268251 ; ENSP00000268251 ; ENSG00000183044 .
    ENST00000396600 ; ENSP00000379845 ; ENSG00000183044 .
    ENST00000425191 ; ENSP00000411916 ; ENSG00000183044 .
    GeneIDi 18.
    KEGGi hsa:18.
    UCSCi uc002czc.4. human.

    Organism-specific databases

    CTDi 18.
    GeneCardsi GC16P008768.
    HGNCi HGNC:23. ABAT.
    HPAi HPA041528.
    HPA041690.
    MIMi 137150. gene.
    613163. phenotype.
    neXtProti NX_P80404.
    Orphaneti 2066. Gamma-aminobutyric acid transaminase deficiency.
    PharmGKBi PA24372.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0160.
    HOVERGENi HBG000634.
    InParanoidi P80404.
    KOi K13524.
    OrthoDBi EOG7ZPNJW.
    PhylomeDBi P80404.
    TreeFami TF105021.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02477-MONOMER.
    Reactomei REACT_23964. Degradation of GABA.
    SABIO-RK P80404.

    Miscellaneous databases

    ChiTaRSi ABAT. human.
    GenomeRNAii 18.
    NextBioi 45.
    PROi P80404.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P80404.
    Bgeei P80404.
    CleanExi HS_ABAT.
    Genevestigatori P80404.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    InterProi IPR004631. 4NH2But_aminotransferase_euk.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR11986. PTHR11986. 1 hit.
    PTHR11986:SF6. PTHR11986:SF6. 1 hit.
    Pfami PF00202. Aminotran_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR00699. GABAtrns_euk. 1 hit.
    PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: VARIANT GABATD LYS-220.

    Entry informationi

    Entry nameiGABT_HUMAN
    AccessioniPrimary (citable) accession number: P80404
    Secondary accession number(s): A8K386
    , Q16260, Q8N5W2, Q96BG2, Q99800
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 143 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3