Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6YP21 (KAT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kynurenine--oxoglutarate transaminase 3

EC=2.6.1.7
Alternative name(s):
Cysteine-S-conjugate beta-lyase 2
EC=4.4.1.13
Kynurenine aminotransferase III
Short name=KATIII
Kynurenine--glyoxylate transaminase
EC=2.6.1.63
Kynurenine--oxoglutarate transaminase III
Gene names
Name:CCBL2
Synonyms:KAT3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond By similarity. Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro) By similarity.

Catalytic activity

L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate.

RS-CH(2)-CH(NH3+)COO- + H2O = RSH + NH3 + pyruvate.

L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + glycine.

Cofactor

Pyridoxal phosphate By similarity.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Caution

The first non-coding exon of CCBL2 is in common with that of RBMXL1.

Sequence caution

The sequence AAC72959.1 differs from that shown. Reason: Frameshift at position 336.

The sequence AAH00819.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAG29278.1 differs from that shown. Reason: Frameshift at position 336.

The sequence CAI21695.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI21696.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI41339.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI41340.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandPyridoxal phosphate
   Molecular functionAminotransferase
Lyase
Transferase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_process2-oxoglutarate metabolic process

Inferred from electronic annotation. Source: Ensembl

L-kynurenine metabolic process

Inferred from sequence or structural similarity. Source: GOC

biosynthetic process

Inferred from electronic annotation. Source: InterPro

cellular amino acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

kynurenine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

tryptophan catabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncysteine-S-conjugate beta-lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

kynurenine-glyoxylate transaminase activity

Inferred from sequence or structural similarity. Source: UniProtKB

kynurenine-oxoglutarate transaminase activity

Inferred from sequence or structural similarity. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

pyridoxal phosphate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6YP21-1)

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.
Isoform 2 (identifier: Q6YP21-2)

The sequence of this isoform differs from the canonical sequence as follows:
     152-167: VILIVPFYDCYEPMVR → YNACTVKFTNLKCTAG
     168-454: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q6YP21-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-34: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Kynurenine--oxoglutarate transaminase 3
PRO_0000287704

Sites

Binding site531Substrate By similarity
Binding site711Substrate; via amide nitrogen By similarity
Binding site2181Substrate By similarity
Binding site4291Substrate By similarity

Amino acid modifications

Modified residue1161N6-acetyllysine; alternate Ref.8
Modified residue1161N6-succinyllysine; alternate By similarity
Modified residue2801N6-(pyridoxal phosphate)lysine By similarity

Natural variations

Alternative sequence1 – 3434Missing in isoform 3.
VSP_042841
Alternative sequence152 – 16716VILIV…EPMVR → YNACTVKFTNLKCTAG in isoform 2.
VSP_025603
Alternative sequence168 – 454287Missing in isoform 2.
VSP_025604
Natural variant2061S → P. Ref.6 Ref.7
Corresponds to variant rs1059370 [ dbSNP | Ensembl ].
VAR_032352

Experimental info

Sequence conflict2511W → R in CAG29278. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 2059D4646058BBB3

FASTA45451,400
        10         20         30         40         50         60 
MFLAQRSLCS LSGRAKFLKT ISSSKILGFS TSAKMSLKFT NAKRIEGLDS NVWIEFTKLA 

        70         80         90        100        110        120 
ADPSVVNLGQ GFPDISPPTY VKEELSKIAA IDSLNQYTRG FGHPSLVKAL SYLYEKLYQK 

       130        140        150        160        170        180 
QIDSNKEILV TVGAYGSLFN TIQALIDEGD EVILIVPFYD CYEPMVRMAG ATPVFIPLRS 

       190        200        210        220        230        240 
KPVYGKRWSS SDWTLDPQEL ESKFNSKTKA IILNTPHNPL GKVYNREELQ VIADLCIKYD 

       250        260        270        280        290        300 
TLCISDEVYE WLVYSGNKHL KIATFPGMWE RTITIGSAGK TFSVTGWKLG WSIGPNHLIK 

       310        320        330        340        350        360 
HLQTVQQNTI YTCATPLQEA LAQAFWIDIK RMDDPECYFN SLPKELEVKR DRMVRLLESV 

       370        380        390        400        410        420 
GLKPIVPDGG YFIIADVSLL DPDLSDMKNN EPYDYKFVKW MTKHKKLSAI PVSAFCNSET 

       430        440        450 
KSQFEKFVRF CFIKKDSTLD AAEEIIKAWS VQKS 

« Hide

Isoform 2 [UniParc].

Checksum: 6CA0C2A9BC6BA211
Show »

FASTA16718,352
Isoform 3 [UniParc].

Checksum: 1BB37BC0D96DB2EE
Show »

FASTA42047,753

References

« Hide 'large scale' references
[1]"Characterization of kynurenine aminotransferase III, a novel member of a phylogenetically conserved KAT family."
Yu P., Li Z., Zhang L., Tagle D.A., Cai T.
Gene 365:111-118(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal kidney.
[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. expand/collapse author list , 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 3).
Tissue: Stomach.
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] OF 85-454 (ISOFORM 1).
Tissue: Placenta.
[6]"Full-insert sequence of mapped XREF EST."
Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-454, VARIANT PRO-206.
[7]"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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-338, VARIANT PRO-206.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY028624 mRNA. Translation: AAK26163.1.
CR627392 mRNA. Translation: CAH10487.1.
AK057176 mRNA. Translation: BAG51875.1.
AL445991 Genomic DNA. Translation: CAI41345.1.
AL139416, AL445991 Genomic DNA. Translation: CAI21695.1. Sequence problems.
AL445991, AL139416 Genomic DNA. Translation: CAI41339.1. Sequence problems.
AL139416, AL445991 Genomic DNA. Translation: CAI21696.1. Sequence problems.
AL445991, AL139416 Genomic DNA. Translation: CAI41340.1. Sequence problems.
BC000819 mRNA. Translation: AAH00819.1. Different initiation.
AF091090 mRNA. Translation: AAC72959.1. Frameshift.
CR450282 mRNA. Translation: CAG29278.1. Frameshift.
CCDSCCDS30766.1. [Q6YP21-1]
CCDS30767.1. [Q6YP21-3]
RefSeqNP_001008661.1. NM_001008661.2. [Q6YP21-1]
NP_001008662.1. NM_001008662.2. [Q6YP21-3]
UniGeneHs.481898.

3D structure databases

ProteinModelPortalQ6YP21.
SMRQ6YP21. Positions 41-450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121128. 6 interactions.
IntActQ6YP21. 6 interactions.
MINTMINT-1402454.
STRING9606.ENSP00000260508.

Chemistry

ChEMBLCHEMBL2046260.
DrugBankDB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.

PTM databases

PhosphoSiteQ6YP21.

Polymorphism databases

DMDM74710502.

Proteomic databases

MaxQBQ6YP21.
PaxDbQ6YP21.
PRIDEQ6YP21.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260508; ENSP00000260508; ENSG00000137944. [Q6YP21-1]
ENST00000370485; ENSP00000359516; ENSG00000137944. [Q6YP21-2]
ENST00000370491; ENSP00000359522; ENSG00000137944. [Q6YP21-3]
GeneID56267.
KEGGhsa:56267.
UCSCuc001dmp.2. human. [Q6YP21-1]

Organism-specific databases

CTD56267.
GeneCardsGC01M089401.
HGNCHGNC:33238. CCBL2.
HPAHPA026538.
HPA027168.
MIM610656. gene.
neXtProtNX_Q6YP21.
PharmGKBPA162381274.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0436.
HOGENOMHOG000223045.
HOVERGENHBG008391.
InParanoidQ6YP21.
KOK00816.
OMAGWSIGPN.
OrthoDBEOG76DTSB.
PhylomeDBQ6YP21.
TreeFamTF352342.

Enzyme and pathway databases

BioCycMetaCyc:HS06422-MONOMER.
BRENDA2.6.1.7. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ6YP21.
BgeeQ6YP21.
CleanExHS_CCBL2.
GenevestigatorQ6YP21.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMSSF53383. SSF53383. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi56267.
NextBio61929.
PROQ6YP21.
SOURCESearch...

Entry information

Entry nameKAT3_HUMAN
AccessionPrimary (citable) accession number: Q6YP21
Secondary accession number(s): B3KQ13 expand/collapse secondary AC list , O95335, Q5JS27, Q5T9T7, Q5T9T8, Q6AI27, Q6ICW1, Q9BVY5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM