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Q16719

- KYNU_HUMAN

UniProt

Q16719 - KYNU_HUMAN

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Protein

Kynureninase

Gene

KYNU

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ16719.
CleanExiHS_KYNU.
ExpressionAtlasiQ16719. baseline and differential.
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.
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. 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

        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 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.

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.
GeneTreei ENSGT00390000008033.
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

Bgeei Q16719.
CleanExi HS_KYNU.
ExpressionAtlasi Q16719. baseline and differential.
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_dom.
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

« 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. 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 29, 2014
This is version 136 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