Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q16719

- KYNU_HUMAN

UniProt

Q16719 - KYNU_HUMAN

Protein

Kynureninase

Gene

KYNU

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Pyridoxal phosphate.

    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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei137 – 1371Pyridoxal phosphate; via amide nitrogenUniRule annotation
    Binding sitei138 – 1381Pyridoxal phosphate1 PublicationUniRule annotation
    Binding sitei221 – 2211Pyridoxal phosphateUniRule annotation
    Binding sitei250 – 2501Pyridoxal phosphate1 PublicationUniRule annotation
    Binding sitei253 – 2531Pyridoxal phosphate1 PublicationUniRule annotation
    Binding sitei275 – 2751Pyridoxal phosphate1 PublicationUniRule annotation
    Binding sitei305 – 3051Pyridoxal phosphate1 PublicationUniRule annotation
    Binding sitei333 – 3331Pyridoxal phosphate1 PublicationUniRule annotation

    GO - Molecular functioni

    1. kynureninase activity Source: UniProtKB
    2. protein homodimerization activity Source: UniProtKB
    3. pyridoxal phosphate binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
    2. anthranilate metabolic process Source: UniProtKB
    3. cellular nitrogen compound metabolic process Source: Reactome
    4. L-kynurenine catabolic process Source: UniProtKB-UniPathway
    5. quinolinate biosynthetic process Source: UniProtKB
    6. response to interferon-gamma Source: UniProtKB
    7. response to vitamin B6 Source: UniProtKB
    8. small molecule metabolic process Source: Reactome
    9. tryptophan catabolic process Source: UniProtKB
    10. tryptophan catabolic process to acetyl-CoA Source: Ensembl
    11. tryptophan catabolic process to kynurenine Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03952-MONOMER.
    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: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6469. KYNU.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Xanthurenic aciduria manifesting as massive urinary excretion of large amounts of kynurenine, 3-hydroxykynurenine and xanthurenic acid has been observed in an individual carrying a homozygous missense change in KYNU (PubMed:17334708). The urinary pattern in the patient suggests kynureninase deficiency and a block in the conversion of kynurenine and 3-hydroxykynurenine to anthranilate and 3-hydroxyanthranilate, respectively.1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    Orphaneti79155. Encephalopathy due to hydroxykynureninuria.
    PharmGKBiPA30258.

    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 PublicationUniRule annotation
    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

    ArrayExpressiQ16719.
    BgeeiQ16719.
    CleanExiHS_KYNU.
    GenevestigatoriQ16719.

    Organism-specific databases

    HPAiHPA031686.

    Interactioni

    Subunit structurei

    Homodimer.1 PublicationUniRule annotation

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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/Cys_dSase.
    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. Align

    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

    MEPSSLELPA DTVQRIAAEL KCHPTDERVA LHLDEEDKLR HFRECFYIPK    50
    IQDLPPVDLS LVNKDENAIY FLGNSLGLQP KMVKTYLEEE LDKWAKIAAY 100
    GHEVGKRPWI TGDESIVGLM KDIVGANEKE IALMNALTVN LHLLMLSFFK 150
    PTPKRYKILL EAKAFPSDHY AIESQLQLHG LNIEESMRMI KPREGEETLR 200
    IEDILEVIEK EGDSIAVILF SGVHFYTGQH FNIPAITKAG QAKGCYVGFD 250
    LAHAVGNVEL YLHDWGVDFA CWCSYKYLNA GAGGIAGAFI HEKHAHTIKP 300
    ALVGWFGHEL STRFKMDNKL QLIPGVCGFR ISNPPILLVC SLHASLEIFK 350
    QATMKALRKK SVLLTGYLEY LIKHNYGKDK AATKKPVVNI ITPSHVEERG 400
    CQLTITFSVP NKDVFQELEK RGVVCDKRNP NGIRVAPVPL YNSFHDVYKF 450
    TNLLTSILDS AETKN 465
    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 Detected in a boy with xanthurenic aciduria. 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:
    EMBL
    GenBank
    DDBJ
    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]
    UniGeneiHs.470126.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi3913982.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS2183.1. [Q16719-1 ]
    CCDS33299.1. [Q16719-2 ]
    PIRi G02652.
    RefSeqi NP_001028170.1. NM_001032998.1. [Q16719-2 ]
    NP_001186170.1. NM_001199241.1. [Q16719-1 ]
    NP_003928.1. NM_003937.2. [Q16719-1 ]
    UniGenei Hs.470126.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HZP X-ray 2.00 A 1-465 [» ]
    3E9K X-ray 1.70 A 1-465 [» ]
    ProteinModelPortali Q16719.
    SMRi Q16719. Positions 6-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114454. 31 interactions.
    IntActi Q16719. 1 interaction.
    STRINGi 9606.ENSP00000264170.

    Chemistry

    BindingDBi Q16719.
    ChEMBLi CHEMBL5100.
    DrugBanki DB00160. L-Alanine.
    DB00114. Pyridoxal Phosphate.

    PTM databases

    PhosphoSitei Q16719.

    Polymorphism databases

    DMDMi 3913982.

    Proteomic databases

    MaxQBi Q16719.
    PaxDbi Q16719.
    PeptideAtlasi Q16719.
    PRIDEi Q16719.

    Protocols and materials databases

    DNASUi 8942.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264170 ; ENSP00000264170 ; ENSG00000115919 . [Q16719-1 ]
    ENST00000375773 ; ENSP00000364928 ; ENSG00000115919 . [Q16719-2 ]
    ENST00000409512 ; ENSP00000386731 ; ENSG00000115919 . [Q16719-1 ]
    GeneIDi 8942.
    KEGGi hsa:8942.
    UCSCi uc002tvk.3. human. [Q16719-2 ]
    uc002tvl.3. human. [Q16719-1 ]

    Organism-specific databases

    CTDi 8942.
    GeneCardsi GC02P143657.
    HGNCi HGNC:6469. KYNU.
    HPAi HPA031686.
    MIMi 605197. gene.
    neXtProti NX_Q16719.
    Orphaneti 79155. Encephalopathy due to hydroxykynureninuria.
    PharmGKBi PA30258.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3844.
    HOGENOMi HOG000242438.
    HOVERGENi HBG001170.
    InParanoidi Q16719.
    KOi K01556.
    OMAi GWYGGDK.
    OrthoDBi EOG7D2FDV.
    PhylomeDBi Q16719.
    TreeFami TF300707.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00329 .
    UPA00334 ; UER00455 .
    BioCyci MetaCyc:HS03952-MONOMER.
    Reactomei REACT_916. Tryptophan catabolism.

    Miscellaneous databases

    ChiTaRSi KYNU. human.
    EvolutionaryTracei Q16719.
    GeneWikii Kynureninase.
    GenomeRNAii 8942.
    NextBioi 33630.
    PROi Q16719.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16719.
    Bgeei Q16719.
    CleanExi HS_KYNU.
    Genevestigatori Q16719.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPi MF_01970. Kynureninase.
    InterProi IPR000192. Aminotrans_V/Cys_dSase.
    IPR010111. Kynureninase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR14084. PTHR14084. 1 hit.
    Pfami PF00266. Aminotran_5. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038800. KYNU. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01814. kynureninase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE, HOMODIMERIZATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    12. "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: VARIANT ALA-198, POSSIBLE INVOLVEMENT IN XANTHURENIC ACIDURIA.

    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: October 1, 2014
    This is version 135 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

    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