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Q8N5Z0

- AADAT_HUMAN

UniProt

Q8N5Z0 - AADAT_HUMAN

Protein

Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial

Gene

AADAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (13 Apr 2004)
      Previous versions | rss
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    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 phosphate.3 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

    Pathwayi

    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

    1. 2-aminoadipate transaminase activity Source: UniProtKB
    2. kynurenine-oxoglutarate transaminase activity Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB
    4. pyridoxal phosphate binding Source: Ensembl

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: UniProtKB
    2. biosynthetic process Source: InterPro
    3. cellular nitrogen compound metabolic process Source: Reactome
    4. glutamate metabolic process Source: UniProtKB
    5. kynurenine metabolic process Source: UniProtKB
    6. L-kynurenine metabolic process Source: GOC
    7. L-lysine catabolic process to acetyl-CoA via saccharopine Source: UniProtKB-UniPathway
    8. lysine catabolic process Source: Reactome
    9. small molecule metabolic process Source: Reactome
    10. tryptophan catabolic process Source: Reactome
    11. tryptophan catabolic process to kynurenine Source: Ensembl

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03239-MONOMER.
    BRENDAi2.6.1.7. 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: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:17929. AADAT.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24364.

    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

    ArrayExpressiQ8N5Z0.
    BgeeiQ8N5Z0.
    CleanExiHS_AADAT.
    GenevestigatoriQ8N5Z0.

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000223057.
    HOVERGENiHBG050429.
    InParanoidiQ8N5Z0.
    KOiK00825.
    OMAiKPLGCNI.
    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. Align

    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

    MNYARFITAA SAARNPSPIR TMTDILSRGP KSMISLAGGL PNPNMFPFKT    50
    AVITVENGKT IQFGEEMMKR ALQYSPSAGI PELLSWLKQL QIKLHNPPTI 100
    HYPPSQGQMD LCVTSGSQQG LCKVFEMIIN PGDNVLLDEP AYSGTLQSLH 150
    PLGCNIINVA SDESGIVPDS LRDILSRWKP EDAKNPQKNT PKFLYTVPNG 200
    NNPTGNSLTS ERKKEIYELA RKYDFLIIED DPYYFLQFNK FRVPTFLSMD 250
    VDGRVIRADS FSKIISSGLR IGFLTGPKPL IERVILHIQV STLHPSTFNQ 300
    LMISQLLHEW GEEGFMAHVD RVIDFYSNQK DAILAAADKW LTGLAEWHVP 350
    AAGMFLWIKV KGINDVKELI EEKAVKMGVL MLPGNAFYVD SSAPSPYLRA 400
    SFSSASPEQM DVAFQVLAQL IKESL 425

    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:
    EMBL
    GenBank
    DDBJ
    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]
    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]

    Polymorphism databases

    DMDMi46395904.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF097994 mRNA. Translation: AAF04623.1 .
    AF481738 mRNA. Translation: AAM09683.1 .
    AK055952 mRNA. Translation: BAG51596.1 .
    BC031068 mRNA. Translation: AAH31068.1 .
    CCDSi CCDS3814.1. [Q8N5Z0-1 ]
    RefSeqi NP_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 ]
    UniGenei Hs.529735.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QLR X-ray 2.30 A/B/C/D 1-425 [» ]
    2R2N X-ray 1.95 A/B/C/D 1-425 [» ]
    2VGZ X-ray 2.30 A/B 2-425 [» ]
    2XH1 X-ray 2.10 A/B 1-425 [» ]
    3DC1 X-ray 2.50 A/B/C/D 1-425 [» ]
    3UE8 X-ray 3.22 A/B 1-425 [» ]
    4GDY X-ray 2.89 A/B 1-425 [» ]
    4GE4 X-ray 2.41 A/B 1-425 [» ]
    4GE7 X-ray 2.10 A/B 1-425 [» ]
    4GE9 X-ray 2.43 A/B/C/D 1-425 [» ]
    4GEB X-ray 2.15 A/B 1-425 [» ]
    ProteinModelPortali Q8N5Z0.
    SMRi Q8N5Z0. Positions 1-425.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000226840.

    Chemistry

    ChEMBLi CHEMBL2046259.

    PTM databases

    PhosphoSitei Q8N5Z0.

    Polymorphism databases

    DMDMi 46395904.

    Proteomic databases

    MaxQBi Q8N5Z0.
    PaxDbi Q8N5Z0.
    PRIDEi Q8N5Z0.

    Protocols and materials databases

    DNASUi 51166.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000337664 ; ENSP00000336808 ; ENSG00000109576 . [Q8N5Z0-1 ]
    ENST00000353187 ; ENSP00000226840 ; ENSG00000109576 . [Q8N5Z0-1 ]
    ENST00000509167 ; ENSP00000423190 ; ENSG00000109576 . [Q8N5Z0-2 ]
    ENST00000515480 ; ENSP00000423341 ; ENSG00000109576 . [Q8N5Z0-1 ]
    GeneIDi 51166.
    KEGGi hsa:51166.
    UCSCi uc003isr.3. human. [Q8N5Z0-1 ]
    uc003ist.3. human. [Q8N5Z0-2 ]

    Organism-specific databases

    CTDi 51166.
    GeneCardsi GC04M170981.
    HGNCi HGNC:17929. AADAT.
    HPAi HPA037502.
    MIMi 611754. gene.
    neXtProti NX_Q8N5Z0.
    PharmGKBi PA24364.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1167.
    HOGENOMi HOG000223057.
    HOVERGENi HBG050429.
    InParanoidi Q8N5Z0.
    KOi K00825.
    OMAi KPLGCNI.
    OrthoDBi EOG7ZKSBF.
    PhylomeDBi Q8N5Z0.
    TreeFami TF328598.

    Enzyme and pathway databases

    UniPathwayi UPA00868 ; UER00838 .
    BioCyci MetaCyc:HS03239-MONOMER.
    BRENDAi 2.6.1.7. 2681.
    Reactomei REACT_1298. Lysine catabolism.
    REACT_916. Tryptophan catabolism.

    Miscellaneous databases

    ChiTaRSi AADAT. human.
    EvolutionaryTracei Q8N5Z0.
    GenomeRNAii 51166.
    NextBioi 54097.
    PROi Q8N5Z0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8N5Z0.
    Bgeei Q8N5Z0.
    CleanExi HS_AADAT.
    Genevestigatori Q8N5Z0.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR004839. Aminotransferase_I/II.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    Pfami PF00155. Aminotran_1_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. "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.
    6. "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.
    7. "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: October 1, 2014
    This is version 113 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