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Q6YP21

- KAT3_HUMAN

UniProt

Q6YP21 - KAT3_HUMAN

Protein

Kynurenine--oxoglutarate transaminase 3

Gene

CCBL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    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.

    Cofactori

    Pyridoxal phosphate.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei53 – 531SubstrateBy similarity
    Binding sitei71 – 711Substrate; via amide nitrogenBy similarity
    Binding sitei218 – 2181SubstrateBy similarity
    Binding sitei429 – 4291SubstrateBy similarity

    GO - Molecular functioni

    1. cysteine-S-conjugate beta-lyase activity Source: UniProtKB-EC
    2. kynurenine-glyoxylate transaminase activity Source: UniProtKB
    3. kynurenine-oxoglutarate transaminase activity Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB
    5. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. 2-oxoglutarate metabolic process Source: Ensembl
    2. biosynthetic process Source: InterPro
    3. cellular amino acid metabolic process Source: UniProtKB
    4. cellular nitrogen compound metabolic process Source: Reactome
    5. kynurenine metabolic process Source: UniProtKB
    6. L-kynurenine metabolic process Source: GOC
    7. small molecule metabolic process Source: Reactome
    8. tryptophan catabolic process Source: Reactome

    Keywords - Molecular functioni

    Aminotransferase, Lyase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06422-MONOMER.
    BRENDAi2.6.1.7. 2681.
    ReactomeiREACT_916. Tryptophan catabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:CCBL2
    Synonyms:KAT3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:33238. CCBL2.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162381274.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 454454Kynurenine--oxoglutarate transaminase 3PRO_0000287704Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei116 – 1161N6-acetyllysine; alternate1 Publication
    Modified residuei116 – 1161N6-succinyllysine; alternateBy similarity
    Modified residuei280 – 2801N6-(pyridoxal phosphate)lysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ6YP21.
    PaxDbiQ6YP21.
    PRIDEiQ6YP21.

    PTM databases

    PhosphoSiteiQ6YP21.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6YP21.
    BgeeiQ6YP21.
    CleanExiHS_CCBL2.
    GenevestigatoriQ6YP21.

    Organism-specific databases

    HPAiHPA026538.
    HPA027168.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi121128. 7 interactions.
    IntActiQ6YP21. 6 interactions.
    MINTiMINT-1402454.
    STRINGi9606.ENSP00000260508.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6YP21.
    SMRiQ6YP21. Positions 41-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0436.
    HOGENOMiHOG000223045.
    HOVERGENiHBG008391.
    InParanoidiQ6YP21.
    KOiK00816.
    OMAiGWSIGPN.
    OrthoDBiEOG76DTSB.
    PhylomeDBiQ6YP21.
    TreeFamiTF352342.

    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6YP21-1) [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

    MFLAQRSLCS LSGRAKFLKT ISSSKILGFS TSAKMSLKFT NAKRIEGLDS    50
    NVWIEFTKLA ADPSVVNLGQ GFPDISPPTY VKEELSKIAA IDSLNQYTRG 100
    FGHPSLVKAL SYLYEKLYQK QIDSNKEILV TVGAYGSLFN TIQALIDEGD 150
    EVILIVPFYD CYEPMVRMAG ATPVFIPLRS KPVYGKRWSS SDWTLDPQEL 200
    ESKFNSKTKA IILNTPHNPL GKVYNREELQ VIADLCIKYD TLCISDEVYE 250
    WLVYSGNKHL KIATFPGMWE RTITIGSAGK TFSVTGWKLG WSIGPNHLIK 300
    HLQTVQQNTI YTCATPLQEA LAQAFWIDIK RMDDPECYFN SLPKELEVKR 350
    DRMVRLLESV GLKPIVPDGG YFIIADVSLL DPDLSDMKNN EPYDYKFVKW 400
    MTKHKKLSAI PVSAFCNSET KSQFEKFVRF CFIKKDSTLD AAEEIIKAWS 450
    VQKS 454
    Length:454
    Mass (Da):51,400
    Last modified:July 5, 2004 - v1
    Checksum:i2059D4646058BBB3
    GO
    Isoform 2 (identifier: Q6YP21-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         152-167: VILIVPFYDCYEPMVR → YNACTVKFTNLKCTAG
         168-454: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:167
    Mass (Da):18,352
    Checksum:i6CA0C2A9BC6BA211
    GO
    Isoform 3 (identifier: Q6YP21-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:420
    Mass (Da):47,753
    Checksum:i1BB37BC0D96DB2EE
    GO

    Sequence cautioni

    The sequence AAC72959.1 differs from that shown. Reason: Frameshift at position 336.
    The sequence CAG29278.1 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 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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti251 – 2511W → R in CAG29278. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti206 – 2061S → P.2 Publications
    Corresponds to variant rs1059370 [ dbSNP | Ensembl ].
    VAR_032352

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 3434Missing in isoform 3. 1 PublicationVSP_042841Add
    BLAST
    Alternative sequencei152 – 16716VILIV…EPMVR → YNACTVKFTNLKCTAG in isoform 2. 1 PublicationVSP_025603Add
    BLAST
    Alternative sequencei168 – 454287Missing in isoform 2. 1 PublicationVSP_025604Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS30766.1. [Q6YP21-1]
    CCDS30767.1. [Q6YP21-3]
    RefSeqiNP_001008661.1. NM_001008661.2. [Q6YP21-1]
    NP_001008662.1. NM_001008662.2. [Q6YP21-3]
    UniGeneiHs.481898.

    Genome annotation databases

    EnsembliENST00000260508; ENSP00000260508; ENSG00000137944. [Q6YP21-1]
    ENST00000370485; ENSP00000359516; ENSG00000137944. [Q6YP21-2]
    ENST00000370491; ENSP00000359522; ENSG00000137944. [Q6YP21-3]
    GeneIDi56267.
    KEGGihsa:56267.
    UCSCiuc001dmp.2. human. [Q6YP21-1]

    Polymorphism databases

    DMDMi74710502.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS30766.1. [Q6YP21-1 ]
    CCDS30767.1. [Q6YP21-3 ]
    RefSeqi NP_001008661.1. NM_001008661.2. [Q6YP21-1 ]
    NP_001008662.1. NM_001008662.2. [Q6YP21-3 ]
    UniGenei Hs.481898.

    3D structure databases

    ProteinModelPortali Q6YP21.
    SMRi Q6YP21. Positions 41-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121128. 7 interactions.
    IntActi Q6YP21. 6 interactions.
    MINTi MINT-1402454.
    STRINGi 9606.ENSP00000260508.

    Chemistry

    ChEMBLi CHEMBL2046260.

    PTM databases

    PhosphoSitei Q6YP21.

    Polymorphism databases

    DMDMi 74710502.

    Proteomic databases

    MaxQBi Q6YP21.
    PaxDbi Q6YP21.
    PRIDEi Q6YP21.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260508 ; ENSP00000260508 ; ENSG00000137944 . [Q6YP21-1 ]
    ENST00000370485 ; ENSP00000359516 ; ENSG00000137944 . [Q6YP21-2 ]
    ENST00000370491 ; ENSP00000359522 ; ENSG00000137944 . [Q6YP21-3 ]
    GeneIDi 56267.
    KEGGi hsa:56267.
    UCSCi uc001dmp.2. human. [Q6YP21-1 ]

    Organism-specific databases

    CTDi 56267.
    GeneCardsi GC01M089401.
    HGNCi HGNC:33238. CCBL2.
    HPAi HPA026538.
    HPA027168.
    MIMi 610656. gene.
    neXtProti NX_Q6YP21.
    PharmGKBi PA162381274.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0436.
    HOGENOMi HOG000223045.
    HOVERGENi HBG008391.
    InParanoidi Q6YP21.
    KOi K00816.
    OMAi GWSIGPN.
    OrthoDBi EOG76DTSB.
    PhylomeDBi Q6YP21.
    TreeFami TF352342.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06422-MONOMER.
    BRENDAi 2.6.1.7. 2681.
    Reactomei REACT_916. Tryptophan catabolism.

    Miscellaneous databases

    GenomeRNAii 56267.
    NextBioi 61929.
    PROi Q6YP21.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6YP21.
    Bgeei Q6YP21.
    CleanExi HS_CCBL2.
    Genevestigatori Q6YP21.

    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

    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. 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.
      , 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.
      , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiKAT3_HUMAN
    AccessioniPrimary (citable) accession number: Q6YP21
    Secondary accession number(s): B3KQ13
    , O95335, Q5JS27, Q5T9T7, Q5T9T8, Q6AI27, Q6ICW1, Q9BVY5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 95 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3