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Protein

Kynureninase

Gene

KYNU

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

Functioni

Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.

Catalytic activityi

L-kynurenine + H2O = anthranilate + L-alanine.UniRule annotation
L-3-hydroxykynurenine + H2O = 3-hydroxyanthranilate + L-alanine.UniRule annotation

Cofactori

Enzyme regulationi

Inhibited by o-methoxybenzoylalanine (OMBA).2 Publications

Kineticsi

  1. KM=493 µM for L-kynurenine (at pH 7.0)4 Publications
  2. KM=28.3 µM for DL-3-hydroxykynurenine (at pH 7.0)4 Publications
  3. KM=3.0 µM for DL-3-hydroxykynurenine (at pH 7.9)4 Publications

    pH dependencei

    Optimum pH is 8.25 with DL-3-hydroxykynurenine as substrate.4 Publications

    Pathway:iL-kynurenine degradation

    This protein is involved in step 1 of the subpathway that synthesizes L-alanine and anthranilate from L-kynurenine.UniRule annotation
    Proteins known to be involved in this subpathway in this organism are:
    1. Kynureninase (KYNU), Kynureninase (KYNU), Kynureninase (KYNU)
    This subpathway is part of the pathway L-kynurenine degradation, 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 L-alanine and anthranilate from L-kynurenine, the pathway L-kynurenine degradation and in Amino-acid degradation.

    Pathway:iNAD(+) biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Kynurenine 3-monooxygenase (KMO), Kynurenine 3-monooxygenase (KMO), Kynurenine 3-monooxygenase (KMO), Kynurenine 3-monooxygenase (KMO)
    2. Kynureninase (KYNU), Kynureninase (KYNU), Kynureninase (KYNU)
    3. 3-hydroxyanthranilate 3,4-dioxygenase (HAAO)
    This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei137 – 1371Pyridoxal phosphate; via amide nitrogenUniRule annotation
    Binding sitei138 – 1381Pyridoxal phosphateUniRule annotation1 Publication
    Binding sitei221 – 2211Pyridoxal phosphateUniRule annotation
    Binding sitei250 – 2501Pyridoxal phosphateUniRule annotation1 Publication
    Binding sitei253 – 2531Pyridoxal phosphateUniRule annotation1 Publication
    Binding sitei275 – 2751Pyridoxal phosphateUniRule annotation1 Publication
    Binding sitei305 – 3051Pyridoxal phosphateUniRule annotation1 Publication
    Binding sitei333 – 3331Pyridoxal phosphateUniRule annotation1 Publication

    GO - Molecular functioni

    • kynureninase activity Source: UniProtKB
    • protein homodimerization activity Source: UniProtKB
    • pyridoxal phosphate binding Source: UniProtKB-HAMAP

    GO - Biological processi

    • 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
    • anthranilate metabolic process Source: UniProtKB
    • cellular nitrogen compound metabolic process Source: Reactome
    • L-kynurenine catabolic process Source: UniProtKB-UniPathway
    • quinolinate biosynthetic process Source: UniProtKB
    • response to interferon-gamma Source: UniProtKB
    • response to vitamin B6 Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    • tryptophan catabolic process Source: UniProtKB
    • tryptophan catabolic process to acetyl-CoA Source: Ensembl
    • tryptophan catabolic process to kynurenine Source: Ensembl
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03952-MONOMER.
    BRENDAi3.7.1.3. 2681.
    ReactomeiREACT_916. Tryptophan catabolism.
    UniPathwayiUPA00253; UER00329.
    UPA00334; UER00455.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    KynureninaseUniRule annotation (EC:3.7.1.3UniRule annotation)
    Alternative name(s):
    L-kynurenine hydrolaseUniRule annotation
    Gene namesi
    Name:KYNUUniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6469. KYNU.

    Subcellular locationi

    • Cytoplasm UniRule annotation1 Publication

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • cytosol Source: UniProtKB
    • mitochondrion Source: UniProtKB
    • nucleoplasm Source: HPA
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Hydroxykynureninuria (HYXKY)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionAn inborn error of amino acid metabolism characterized by massive urinary excretion of large amounts of kynurenine, 3-hydroxykynurenine and xanthurenic acid. Affected individuals manifest renal tubular dysfunction, metabolic acidosis, psychomotor retardation, non-progressive encephalopathy, and muscular hypertonia.

    See also OMIM:236800
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti198 – 1981T → A in HYXKY. 1 Publication
    VAR_054401

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi236800. phenotype.
    Orphaneti79155. Encephalopathy due to hydroxykynureninuria.
    PharmGKBiPA30258.

    Chemistry

    DrugBankiDB00160. L-Alanine.

    Polymorphism and mutation databases

    BioMutaiKYNU.
    DMDMi3913982.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 465465KynureninasePRO_0000218657Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei276 – 2761N6-(pyridoxal phosphate)lysine

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ16719.
    PaxDbiQ16719.
    PeptideAtlasiQ16719.
    PRIDEiQ16719.

    PTM databases

    PhosphoSiteiQ16719.

    Expressioni

    Tissue specificityi

    Expressed in all tissues tested (heart, brain placenta, lung, liver, skeletal muscle, kidney and pancreas). Highest levels found in placenta, liver and lung. Expressed in all brain regions.2 Publications

    Inductioni

    Increased levels in several cerebral and systemic inflammatory conditions.

    Gene expression databases

    BgeeiQ16719.
    CleanExiHS_KYNU.
    ExpressionAtlasiQ16719. baseline and differential.
    GenevisibleiQ16719. HS.

    Organism-specific databases

    HPAiHPA031686.

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    BioGridi114454. 31 interactions.
    IntActiQ16719. 1 interaction.
    STRINGi9606.ENSP00000264170.

    Structurei

    Secondary structure

    1
    465
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 2012Combined sources
    Helixi27 – 359Combined sources
    Helixi40 – 456Combined sources
    Helixi51 – 533Combined sources
    Helixi59 – 613Combined sources
    Turni73 – 753Combined sources
    Helixi83 – 9715Combined sources
    Helixi98 – 1025Combined sources
    Beta strandi104 – 1074Combined sources
    Helixi109 – 1113Combined sources
    Helixi114 – 1174Combined sources
    Helixi118 – 1203Combined sources
    Helixi121 – 1244Combined sources
    Helixi128 – 1303Combined sources
    Beta strandi131 – 1333Combined sources
    Helixi137 – 14812Combined sources
    Beta strandi153 – 1553Combined sources
    Beta strandi157 – 1615Combined sources
    Helixi166 – 17813Combined sources
    Helixi183 – 1864Combined sources
    Beta strandi187 – 1904Combined sources
    Helixi201 – 21111Combined sources
    Helixi212 – 2143Combined sources
    Beta strandi215 – 2239Combined sources
    Turni225 – 2273Combined sources
    Helixi233 – 24210Combined sources
    Beta strandi246 – 2505Combined sources
    Turni252 – 2576Combined sources
    Helixi262 – 2654Combined sources
    Beta strandi269 – 2724Combined sources
    Beta strandi274 – 2763Combined sources
    Beta strandi287 – 2904Combined sources
    Helixi292 – 2943Combined sources
    Turni295 – 2973Combined sources
    Helixi305 – 3073Combined sources
    Helixi310 – 3134Combined sources
    Helixi326 – 3294Combined sources
    Helixi336 – 35217Combined sources
    Helixi354 – 37522Combined sources
    Beta strandi388 – 3903Combined sources
    Helixi396 – 3983Combined sources
    Beta strandi403 – 4075Combined sources
    Helixi414 – 4196Combined sources
    Turni420 – 4223Combined sources
    Beta strandi426 – 4283Combined sources
    Turni429 – 4313Combined sources
    Beta strandi432 – 4365Combined sources
    Turni439 – 4413Combined sources
    Helixi444 – 45815Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HZPX-ray2.00A1-465[»]
    3E9KX-ray1.70A1-465[»]
    ProteinModelPortaliQ16719.
    SMRiQ16719. Positions 6-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16719.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni165 – 1684Pyridoxal phosphate binding

    Sequence similaritiesi

    Belongs to the kynureninase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG3844.
    GeneTreeiENSGT00390000008033.
    HOGENOMiHOG000242438.
    HOVERGENiHBG001170.
    InParanoidiQ16719.
    KOiK01556.
    OMAiGWYGGDK.
    OrthoDBiEOG7D2FDV.
    PhylomeDBiQ16719.
    TreeFamiTF300707.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_01970. Kynureninase.
    InterProiIPR000192. Aminotrans_V_dom.
    IPR010111. Kynureninase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR14084. PTHR14084. 1 hit.
    PfamiPF00266. Aminotran_5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038800. KYNU. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR01814. kynureninase. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    Isoform 1 (identifier: Q16719-1) [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
    MEPSSLELPA DTVQRIAAEL KCHPTDERVA LHLDEEDKLR HFRECFYIPK
    60 70 80 90 100
    IQDLPPVDLS LVNKDENAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIAAY
    110 120 130 140 150
    GHEVGKRPWI TGDESIVGLM KDIVGANEKE IALMNALTVN LHLLMLSFFK
    160 170 180 190 200
    PTPKRYKILL EAKAFPSDHY AIESQLQLHG LNIEESMRMI KPREGEETLR
    210 220 230 240 250
    IEDILEVIEK EGDSIAVILF SGVHFYTGQH FNIPAITKAG QAKGCYVGFD
    260 270 280 290 300
    LAHAVGNVEL YLHDWGVDFA CWCSYKYLNA GAGGIAGAFI HEKHAHTIKP
    310 320 330 340 350
    ALVGWFGHEL STRFKMDNKL QLIPGVCGFR ISNPPILLVC SLHASLEIFK
    360 370 380 390 400
    QATMKALRKK SVLLTGYLEY LIKHNYGKDK AATKKPVVNI ITPSHVEERG
    410 420 430 440 450
    CQLTITFSVP NKDVFQELEK RGVVCDKRNP NGIRVAPVPL YNSFHDVYKF
    460
    TNLLTSILDS AETKN
    Length:465
    Mass (Da):52,352
    Last modified:November 1, 1996 - v1
    Checksum:iBDD136BE18C79EBB
    GO
    Isoform 2 (identifier: Q16719-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         302-307: LVGWFG → RSEFFN
         308-465: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:307
    Mass (Da):34,635
    Checksum:i9219F37B19D2163E
    GO

    Mass spectrometryi

    Molecular mass is 52400 Da from positions 1 - 465. Determined by MALDI. The reported mass is given to only three significant figures.1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti188 – 1881R → Q.
    Corresponds to variant rs2304705 [ dbSNP | Ensembl ].
    VAR_049724
    Natural varianti198 – 1981T → A in HYXKY. 1 Publication
    VAR_054401
    Natural varianti412 – 4121K → E.1 Publication
    Corresponds to variant rs9013 [ dbSNP | Ensembl ].
    VAR_022092

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei302 – 3076LVGWFG → RSEFFN in isoform 2. CuratedVSP_042739
    Alternative sequencei308 – 465158Missing in isoform 2. CuratedVSP_042740Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U57721 mRNA. Translation: AAC50650.1.
    AK315343 mRNA. Translation: BAG37742.1.
    CR457423 mRNA. Translation: CAG33704.1.
    AC013437 Genomic DNA. No translation available.
    AC013444 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11599.1.
    CH471058 Genomic DNA. Translation: EAX11600.1.
    CH471058 Genomic DNA. Translation: EAX11601.1.
    BC000879 mRNA. Translation: AAH00879.1.
    CCDSiCCDS2183.1. [Q16719-1]
    CCDS33299.1. [Q16719-2]
    PIRiG02652.
    RefSeqiNP_001028170.1. NM_001032998.1. [Q16719-2]
    NP_001186170.1. NM_001199241.1. [Q16719-1]
    NP_003928.1. NM_003937.2. [Q16719-1]
    XP_011510403.1. XM_011512101.1. [Q16719-1]
    UniGeneiHs.470126.

    Genome annotation databases

    EnsembliENST00000264170; ENSP00000264170; ENSG00000115919.
    ENST00000375773; ENSP00000364928; ENSG00000115919. [Q16719-2]
    ENST00000409512; ENSP00000386731; ENSG00000115919.
    GeneIDi8942.
    KEGGihsa:8942.
    UCSCiuc002tvk.3. human. [Q16719-2]
    uc002tvl.3. human. [Q16719-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U57721 mRNA. Translation: AAC50650.1.
    AK315343 mRNA. Translation: BAG37742.1.
    CR457423 mRNA. Translation: CAG33704.1.
    AC013437 Genomic DNA. No translation available.
    AC013444 Genomic DNA. No translation available.
    CH471058 Genomic DNA. Translation: EAX11599.1.
    CH471058 Genomic DNA. Translation: EAX11600.1.
    CH471058 Genomic DNA. Translation: EAX11601.1.
    BC000879 mRNA. Translation: AAH00879.1.
    CCDSiCCDS2183.1. [Q16719-1]
    CCDS33299.1. [Q16719-2]
    PIRiG02652.
    RefSeqiNP_001028170.1. NM_001032998.1. [Q16719-2]
    NP_001186170.1. NM_001199241.1. [Q16719-1]
    NP_003928.1. NM_003937.2. [Q16719-1]
    XP_011510403.1. XM_011512101.1. [Q16719-1]
    UniGeneiHs.470126.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HZPX-ray2.00A1-465[»]
    3E9KX-ray1.70A1-465[»]
    ProteinModelPortaliQ16719.
    SMRiQ16719. Positions 6-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114454. 31 interactions.
    IntActiQ16719. 1 interaction.
    STRINGi9606.ENSP00000264170.

    Chemistry

    BindingDBiQ16719.
    ChEMBLiCHEMBL5100.
    DrugBankiDB00160. L-Alanine.

    PTM databases

    PhosphoSiteiQ16719.

    Polymorphism and mutation databases

    BioMutaiKYNU.
    DMDMi3913982.

    Proteomic databases

    MaxQBiQ16719.
    PaxDbiQ16719.
    PeptideAtlasiQ16719.
    PRIDEiQ16719.

    Protocols and materials databases

    DNASUi8942.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000264170; ENSP00000264170; ENSG00000115919.
    ENST00000375773; ENSP00000364928; ENSG00000115919. [Q16719-2]
    ENST00000409512; ENSP00000386731; ENSG00000115919.
    GeneIDi8942.
    KEGGihsa:8942.
    UCSCiuc002tvk.3. human. [Q16719-2]
    uc002tvl.3. human. [Q16719-1]

    Organism-specific databases

    CTDi8942.
    GeneCardsiGC02P143657.
    HGNCiHGNC:6469. KYNU.
    HPAiHPA031686.
    MIMi236800. phenotype.
    605197. gene.
    neXtProtiNX_Q16719.
    Orphaneti79155. Encephalopathy due to hydroxykynureninuria.
    PharmGKBiPA30258.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG3844.
    GeneTreeiENSGT00390000008033.
    HOGENOMiHOG000242438.
    HOVERGENiHBG001170.
    InParanoidiQ16719.
    KOiK01556.
    OMAiGWYGGDK.
    OrthoDBiEOG7D2FDV.
    PhylomeDBiQ16719.
    TreeFamiTF300707.

    Enzyme and pathway databases

    UniPathwayiUPA00253; UER00329.
    UPA00334; UER00455.
    BioCyciMetaCyc:HS03952-MONOMER.
    BRENDAi3.7.1.3. 2681.
    ReactomeiREACT_916. Tryptophan catabolism.

    Miscellaneous databases

    ChiTaRSiKYNU. human.
    EvolutionaryTraceiQ16719.
    GeneWikiiKynureninase.
    GenomeRNAii8942.
    NextBioi33630.
    PROiQ16719.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ16719.
    CleanExiHS_KYNU.
    ExpressionAtlasiQ16719. baseline and differential.
    GenevisibleiQ16719. HS.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_01970. Kynureninase.
    InterProiIPR000192. Aminotrans_V_dom.
    IPR010111. Kynureninase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR14084. PTHR14084. 1 hit.
    PfamiPF00266. Aminotran_5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038800. KYNU. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR01814. kynureninase. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Hepatoma.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Liver.
    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), VARIANT GLU-412.
      Tissue: Synovium.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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 1).
      Tissue: Cervix.
    8. "Purification and biochemical characterization of some of the properties of recombinant human kynureninase."
      Walsh H.A., Botting N.P.
      Eur. J. Biochem. 269:2069-2074(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, HOMODIMERIZATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    13. "Xanthurenic aciduria due to a mutation in KYNU encoding kynureninase."
      Christensen M., Duno M., Lund A.M., Skovby F., Christensen E.
      J. Inherit. Metab. Dis. 30:248-255(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HYXKY, VARIANT HYXKY ALA-198.

    Entry informationi

    Entry nameiKYNU_HUMAN
    AccessioniPrimary (citable) accession number: Q16719
    Secondary accession number(s): B2RCZ5
    , D3DP79, Q6I9T2, Q9BVW3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 1, 1996
    Last modified: July 22, 2015
    This is version 144 of the entry and version 1 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

    Caution

    It has been reported that this enzyme possesses no measurable activity against L-kynurenine and is subject to inhibition by both L-kynurenine and D-kynurenine at pH 7.9.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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.