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Protein

Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

Gene

AADAT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).1 Publication

Catalytic activityi

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.
L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate.

Cofactori

pyridoxal 5'-phosphate3 Publications

Enzyme regulationi

Kynurenine transaminase activity is competitively inhibited by aminoadipate, asparagine, glutamate, histidine, cysteine, lysine, 3-hydroxy-kynurenine and phenylalanine.1 Publication

Kineticsi

  1. KM=0.9 mM for aminoadipate1 Publication
  2. KM=4.7 mM for kynurenine1 Publication
  3. KM=1.7 mM for methionine1 Publication
  4. KM=1.6 mM for glutamate1 Publication
  5. KM=1.8 mM for tyrosine1 Publication
  6. KM=1.2 mM for 2-oxoglutarate1 Publication
  7. KM=1.5 mM for 2-oxocaproic acid1 Publication
  8. KM=1.8 mM for phenylpyruvate1 Publication
  9. KM=1.4 mM for ino-3-pyruvate1 Publication

    pH dependencei

    Optimum pH is 7-9.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius.1 Publication

    Pathway: L-lysine degradation via saccharopine pathway

    This protein is involved in step 4 of the subpathway that synthesizes glutaryl-CoA from L-lysine.
    Proteins known to be involved in the 6 steps of the subpathway in this organism are:
    1. Alpha-aminoadipic semialdehyde synthase, mitochondrial (AASS)
    2. Alpha-aminoadipic semialdehyde synthase, mitochondrial (AASS)
    3. no protein annotated in this organism
    4. Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (AADAT)
    5. no protein annotated in this organism
    6. Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (DLST)
    This subpathway is part of the pathway L-lysine degradation via saccharopine pathway, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutaryl-CoA from L-lysine, the pathway L-lysine degradation via saccharopine pathway and in Amino-acid degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei20 – 201Substrate
    Binding sitei74 – 741Substrate
    Binding sitei142 – 1421Substrate
    Binding sitei202 – 2021Substrate
    Binding sitei399 – 3991Substrate

    GO - Molecular functioni

    • 2-aminoadipate transaminase activity Source: UniProtKB
    • kynurenine-oxoglutarate transaminase activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03239-MONOMER.
    BRENDAi2.6.1.39. 2681.
    2.6.1.7. 2681.
    ReactomeiREACT_1298. Lysine catabolism.
    REACT_916. Tryptophan catabolism.
    UniPathwayiUPA00868; UER00838.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
    Short name:
    KAT/AadAT
    Alternative name(s):
    2-aminoadipate aminotransferase
    2-aminoadipate transaminase (EC:2.6.1.39)
    Alpha-aminoadipate aminotransferase
    Short name:
    AadAT
    Kynurenine aminotransferase II
    Kynurenine--oxoglutarate aminotransferase II
    Kynurenine--oxoglutarate transaminase 2 (EC:2.6.1.7)
    Kynurenine--oxoglutarate transaminase II
    Gene namesi
    Name:AADAT
    Synonyms:KAT2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:17929. AADAT.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24364.

    Polymorphism and mutation databases

    BioMutaiAADAT.
    DMDMi46395904.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2929MitochondrionSequence AnalysisAdd
    BLAST
    Chaini30 – 425396Kynurenine/alpha-aminoadipate aminotransferase, mitochondrialPRO_0000020602Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei69 – 691N6-acetyllysineBy similarity
    Modified residuei179 – 1791N6-acetyllysineBy similarity
    Modified residuei263 – 2631N6-(pyridoxal phosphate)lysine; alternate
    Modified residuei263 – 2631N6-acetyllysine; alternateBy similarity
    Modified residuei263 – 2631N6-succinyllysine; alternateBy similarity
    Modified residuei339 – 3391N6-acetyllysine; alternateBy similarity
    Modified residuei339 – 3391N6-succinyllysine; alternateBy similarity
    Modified residuei367 – 3671N6-acetyllysine; alternateBy similarity
    Modified residuei367 – 3671N6-succinyllysine; alternateBy similarity
    Modified residuei422 – 4221N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ8N5Z0.
    PaxDbiQ8N5Z0.
    PRIDEiQ8N5Z0.

    PTM databases

    PhosphoSiteiQ8N5Z0.

    Expressioni

    Tissue specificityi

    Higher expression in the liver. Also found in heart, brain, kidney, pancreas, prostate, testis and ovary.

    Gene expression databases

    BgeeiQ8N5Z0.
    CleanExiHS_AADAT.
    ExpressionAtlasiQ8N5Z0. baseline and differential.
    GenevisibleiQ8N5Z0. HS.

    Organism-specific databases

    HPAiHPA037502.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    STRINGi9606.ENSP00000226840.

    Structurei

    Secondary structure

    1
    425
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 64Combined sources
    Helixi9 – 124Combined sources
    Helixi19 – 213Combined sources
    Helixi22 – 287Combined sources
    Helixi43 – 453Combined sources
    Beta strandi47 – 559Combined sources
    Turni56 – 583Combined sources
    Beta strandi61 – 633Combined sources
    Helixi65 – 717Combined sources
    Helixi81 – 9515Combined sources
    Turni98 – 1014Combined sources
    Helixi104 – 1063Combined sources
    Beta strandi109 – 1168Combined sources
    Helixi117 – 12812Combined sources
    Beta strandi134 – 1407Combined sources
    Helixi143 – 1497Combined sources
    Helixi150 – 1523Combined sources
    Beta strandi155 – 1595Combined sources
    Helixi168 – 1758Combined sources
    Helixi180 – 1823Combined sources
    Beta strandi183 – 1853Combined sources
    Helixi186 – 1883Combined sources
    Beta strandi192 – 1965Combined sources
    Turni202 – 2043Combined sources
    Helixi210 – 22213Combined sources
    Beta strandi226 – 2305Combined sources
    Helixi234 – 2363Combined sources
    Beta strandi237 – 2415Combined sources
    Helixi247 – 2493Combined sources
    Beta strandi251 – 2533Combined sources
    Beta strandi255 – 2617Combined sources
    Turni262 – 2654Combined sources
    Turni267 – 2704Combined sources
    Beta strandi272 – 2776Combined sources
    Helixi278 – 28912Combined sources
    Turni290 – 2923Combined sources
    Beta strandi293 – 2953Combined sources
    Helixi297 – 34044Combined sources
    Beta strandi342 – 3476Combined sources
    Beta strandi351 – 36010Combined sources
    Helixi367 – 3715Combined sources
    Helixi373 – 3764Combined sources
    Beta strandi381 – 3833Combined sources
    Helixi384 – 3874Combined sources
    Beta strandi388 – 3903Combined sources
    Beta strandi391 – 3933Combined sources
    Beta strandi397 – 4015Combined sources
    Turni402 – 4043Combined sources
    Helixi407 – 42418Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QLRX-ray2.30A/B/C/D1-425[»]
    2R2NX-ray1.95A/B/C/D1-425[»]
    2VGZX-ray2.30A/B2-425[»]
    2XH1X-ray2.10A/B1-425[»]
    3DC1X-ray2.50A/B/C/D1-425[»]
    3UE8X-ray3.22A/B1-425[»]
    4GDYX-ray2.89A/B1-425[»]
    4GE4X-ray2.41A/B1-425[»]
    4GE7X-ray2.10A/B1-425[»]
    4GE9X-ray2.43A/B/C/D1-425[»]
    4GEBX-ray2.15A/B1-425[»]
    ProteinModelPortaliQ8N5Z0.
    SMRiQ8N5Z0. Positions 1-425.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8N5Z0.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1167.
    GeneTreeiENSGT00390000004594.
    HOGENOMiHOG000223057.
    HOVERGENiHBG050429.
    InParanoidiQ8N5Z0.
    KOiK00825.
    OMAiEWKLDND.
    OrthoDBiEOG7ZKSBF.
    PhylomeDBiQ8N5Z0.
    TreeFamiTF328598.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q8N5Z0-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MNYARFITAA SAARNPSPIR TMTDILSRGP KSMISLAGGL PNPNMFPFKT
    60 70 80 90 100
    AVITVENGKT IQFGEEMMKR ALQYSPSAGI PELLSWLKQL QIKLHNPPTI
    110 120 130 140 150
    HYPPSQGQMD LCVTSGSQQG LCKVFEMIIN PGDNVLLDEP AYSGTLQSLH
    160 170 180 190 200
    PLGCNIINVA SDESGIVPDS LRDILSRWKP EDAKNPQKNT PKFLYTVPNG
    210 220 230 240 250
    NNPTGNSLTS ERKKEIYELA RKYDFLIIED DPYYFLQFNK FRVPTFLSMD
    260 270 280 290 300
    VDGRVIRADS FSKIISSGLR IGFLTGPKPL IERVILHIQV STLHPSTFNQ
    310 320 330 340 350
    LMISQLLHEW GEEGFMAHVD RVIDFYSNQK DAILAAADKW LTGLAEWHVP
    360 370 380 390 400
    AAGMFLWIKV KGINDVKELI EEKAVKMGVL MLPGNAFYVD SSAPSPYLRA
    410 420
    SFSSASPEQM DVAFQVLAQL IKESL
    Note: May be due to a competing donor splice site.
    Length:425
    Mass (Da):47,352
    Last modified:April 13, 2004 - v2
    Checksum:i448CCAAB2173A7BA
    GO
    Isoform 2 (identifier: Q8N5Z0-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         23-23: T → SEKRA

    Show »
    Length:429
    Mass (Da):47,822
    Checksum:i0C5A6E51F1BD6F53
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti103 – 1031P → Q in AAH31068 (PubMed:15489334).Curated
    Sequence conflicti380 – 3801L → S in BAG51596 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti243 – 2431V → I.
    Corresponds to variant rs56350236 [ dbSNP | Ensembl ].
    VAR_061005

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei23 – 231T → SEKRA in isoform 2. 1 PublicationVSP_009874

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF097994 mRNA. Translation: AAF04623.1.
    AF481738 mRNA. Translation: AAM09683.1.
    AK055952 mRNA. Translation: BAG51596.1.
    BC031068 mRNA. Translation: AAH31068.1.
    CCDSiCCDS3814.1. [Q8N5Z0-1]
    CCDS75209.1. [Q8N5Z0-2]
    RefSeqiNP_001273611.1. NM_001286682.1. [Q8N5Z0-2]
    NP_001273612.1. NM_001286683.1. [Q8N5Z0-1]
    NP_057312.1. NM_016228.3. [Q8N5Z0-1]
    NP_872603.1. NM_182662.1. [Q8N5Z0-1]
    UniGeneiHs.529735.

    Genome annotation databases

    EnsembliENST00000337664; ENSP00000336808; ENSG00000109576. [Q8N5Z0-1]
    ENST00000353187; ENSP00000226840; ENSG00000109576. [Q8N5Z0-1]
    ENST00000509167; ENSP00000423190; ENSG00000109576. [Q8N5Z0-2]
    ENST00000515480; ENSP00000423341; ENSG00000109576. [Q8N5Z0-1]
    GeneIDi51166.
    KEGGihsa:51166.
    UCSCiuc003isr.3. human. [Q8N5Z0-1]
    uc003ist.3. human. [Q8N5Z0-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF097994 mRNA. Translation: AAF04623.1.
    AF481738 mRNA. Translation: AAM09683.1.
    AK055952 mRNA. Translation: BAG51596.1.
    BC031068 mRNA. Translation: AAH31068.1.
    CCDSiCCDS3814.1. [Q8N5Z0-1]
    CCDS75209.1. [Q8N5Z0-2]
    RefSeqiNP_001273611.1. NM_001286682.1. [Q8N5Z0-2]
    NP_001273612.1. NM_001286683.1. [Q8N5Z0-1]
    NP_057312.1. NM_016228.3. [Q8N5Z0-1]
    NP_872603.1. NM_182662.1. [Q8N5Z0-1]
    UniGeneiHs.529735.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QLRX-ray2.30A/B/C/D1-425[»]
    2R2NX-ray1.95A/B/C/D1-425[»]
    2VGZX-ray2.30A/B2-425[»]
    2XH1X-ray2.10A/B1-425[»]
    3DC1X-ray2.50A/B/C/D1-425[»]
    3UE8X-ray3.22A/B1-425[»]
    4GDYX-ray2.89A/B1-425[»]
    4GE4X-ray2.41A/B1-425[»]
    4GE7X-ray2.10A/B1-425[»]
    4GE9X-ray2.43A/B/C/D1-425[»]
    4GEBX-ray2.15A/B1-425[»]
    ProteinModelPortaliQ8N5Z0.
    SMRiQ8N5Z0. Positions 1-425.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi9606.ENSP00000226840.

    Chemistry

    BindingDBiQ8N5Z0.
    ChEMBLiCHEMBL2046259.

    PTM databases

    PhosphoSiteiQ8N5Z0.

    Polymorphism and mutation databases

    BioMutaiAADAT.
    DMDMi46395904.

    Proteomic databases

    MaxQBiQ8N5Z0.
    PaxDbiQ8N5Z0.
    PRIDEiQ8N5Z0.

    Protocols and materials databases

    DNASUi51166.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000337664; ENSP00000336808; ENSG00000109576. [Q8N5Z0-1]
    ENST00000353187; ENSP00000226840; ENSG00000109576. [Q8N5Z0-1]
    ENST00000509167; ENSP00000423190; ENSG00000109576. [Q8N5Z0-2]
    ENST00000515480; ENSP00000423341; ENSG00000109576. [Q8N5Z0-1]
    GeneIDi51166.
    KEGGihsa:51166.
    UCSCiuc003isr.3. human. [Q8N5Z0-1]
    uc003ist.3. human. [Q8N5Z0-2]

    Organism-specific databases

    CTDi51166.
    GeneCardsiGC04M170981.
    HGNCiHGNC:17929. AADAT.
    HPAiHPA037502.
    MIMi611754. gene.
    neXtProtiNX_Q8N5Z0.
    PharmGKBiPA24364.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1167.
    GeneTreeiENSGT00390000004594.
    HOGENOMiHOG000223057.
    HOVERGENiHBG050429.
    InParanoidiQ8N5Z0.
    KOiK00825.
    OMAiEWKLDND.
    OrthoDBiEOG7ZKSBF.
    PhylomeDBiQ8N5Z0.
    TreeFamiTF328598.

    Enzyme and pathway databases

    UniPathwayiUPA00868; UER00838.
    BioCyciMetaCyc:HS03239-MONOMER.
    BRENDAi2.6.1.39. 2681.
    2.6.1.7. 2681.
    ReactomeiREACT_1298. Lysine catabolism.
    REACT_916. Tryptophan catabolism.

    Miscellaneous databases

    ChiTaRSiAADAT. human.
    EvolutionaryTraceiQ8N5Z0.
    GenomeRNAii51166.
    NextBioi54097.
    PROiQ8N5Z0.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ8N5Z0.
    CleanExiHS_AADAT.
    ExpressionAtlasiQ8N5Z0. baseline and differential.
    GenevisibleiQ8N5Z0. HS.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning of human L-kynurenine/alpha-aminoadipate aminotransferase cDNA from brain tissue."
      Gatti S., Breton J., Mostardini M., Mosca M., Tarroni P., Schwarcz R., Speciale C., Okuno E., Toma S., Benatti L.
      Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT)."
      Goh D.L.M., Patel A., Thomas G.H., Salomons G.S., Schor D.S.M., Jakobs C., Geraghty M.T.
      Mol. Genet. Metab. 76:172-180(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, COFACTOR.
    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] (ISOFORM 1).
    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] (ISOFORM 2).
      Tissue: Brain.
    5. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "Substrate specificity and structure of human aminoadipate aminotransferase/kynurenine aminotransferase II."
      Han Q., Cai T., Tagle D.A., Robinson H., Li J.
      Biosci. Rep. 28:205-215(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH 2-OXOGLUTARATE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, FUNCTION.
    7. "Crystal structure of human kynurenine aminotransferase II."
      Han Q., Robinson H., Li J.
      J. Biol. Chem. 283:3567-3573(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND KYRUNENINE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT.
    8. "Crystal structure of human kynurenine aminotransferase II, a drug target for the treatment of schizophrenia."
      Rossi F., Garavaglia S., Montalbano V., Walsh M.A., Rizzi M.
      J. Biol. Chem. 283:3559-3566(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, SUBUNIT, COFACTOR.

    Entry informationi

    Entry nameiAADAT_HUMAN
    AccessioniPrimary (citable) accession number: Q8N5Z0
    Secondary accession number(s): B3KP84, Q9UL02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: April 13, 2004
    Last modified: June 24, 2015
    This is version 120 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.