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Q8N5Z0

- AADAT_HUMAN

UniProt

Q8N5Z0 - AADAT_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ8N5Z0.
CleanExiHS_AADAT.
ExpressionAtlasiQ8N5Z0. baseline and differential.
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.
GeneTreeiENSGT00390000004594.
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

        10         20         30         40         50
MNYARFITAA SAARNPSPIR TMTDILSRGP KSMISLAGGL PNPNMFPFKT
60 70 80 90 100
AVITVENGKT IQFGEEMMKR ALQYSPSAGI PELLSWLKQL QIKLHNPPTI
110 120 130 140 150
HYPPSQGQMD LCVTSGSQQG LCKVFEMIIN PGDNVLLDEP AYSGTLQSLH
160 170 180 190 200
PLGCNIINVA SDESGIVPDS LRDILSRWKP EDAKNPQKNT PKFLYTVPNG
210 220 230 240 250
NNPTGNSLTS ERKKEIYELA RKYDFLIIED DPYYFLQFNK FRVPTFLSMD
260 270 280 290 300
VDGRVIRADS FSKIISSGLR IGFLTGPKPL IERVILHIQV STLHPSTFNQ
310 320 330 340 350
LMISQLLHEW GEEGFMAHVD RVIDFYSNQK DAILAAADKW LTGLAEWHVP
360 370 380 390 400
AAGMFLWIKV KGINDVKELI EEKAVKMGVL MLPGNAFYVD SSAPSPYLRA
410 420
SFSSASPEQM DVAFQVLAQL IKESL

Note: May be due to a competing donor splice site.

Length:425
Mass (Da):47,352
Last modified:April 13, 2004 - v2
Checksum:i448CCAAB2173A7BA
GO
Isoform 2 (identifier: Q8N5Z0-2) [UniParc]FASTAAdd to Basket

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

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

Experimental Info

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

Natural variant

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

Alternative sequence

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

Sequence databases

Select the link destinations:
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]
CCDS75209.1. [Q8N5Z0-2]
RefSeqiNP_001273611.1. NM_001286682.1. [Q8N5Z0-2]
NP_001273612.1. NM_001286683.1. [Q8N5Z0-1]
NP_057312.1. NM_016228.3. [Q8N5Z0-1]
NP_872603.1. NM_182662.1. [Q8N5Z0-1]
UniGeneiHs.529735.

Genome annotation databases

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

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 ]
CCDS75209.1. [Q8N5Z0-2 ]
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.
GeneTreei ENSGT00390000004594.
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

Bgeei Q8N5Z0.
CleanExi HS_AADAT.
ExpressionAtlasi Q8N5Z0. baseline and differential.
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

« Hide 'large scale' publications
  1. "Cloning of human L-kynurenine/alpha-aminoadipate aminotransferase cDNA from brain tissue."
    Gatti S., Breton J., Mostardini M., Mosca M., Tarroni P., Schwarcz R., Speciale C., Okuno E., Toma S., Benatti L.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "Characterization of the human gene encoding alpha-aminoadipate aminotransferase (AADAT)."
    Goh D.L.M., Patel A., Thomas G.H., Salomons G.S., Schor D.S.M., Jakobs C., Geraghty M.T.
    Mol. Genet. Metab. 76:172-180(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, COFACTOR.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  5. "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 29, 2014
This is version 114 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