KAT3_HUMAN
ID KAT3_HUMAN Reviewed; 454 AA.
AC Q6YP21; B3KQ13; O95335; Q5JS27; Q5T9T7; Q5T9T8; Q6AI27; Q6ICW1; Q9BVY5;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Kynurenine--oxoglutarate transaminase 3 {ECO:0000250|UniProtKB:Q71RI9};
DE EC=2.6.1.7 {ECO:0000250|UniProtKB:Q71RI9};
DE AltName: Full=Cysteine-S-conjugate beta-lyase 2 {ECO:0000250|UniProtKB:Q71RI9};
DE EC=4.4.1.13 {ECO:0000250|UniProtKB:Q71RI9};
DE AltName: Full=Kynurenine aminotransferase 3 {ECO:0000312|HGNC:HGNC:33238};
DE AltName: Full=Kynurenine aminotransferase III;
DE Short=KATIII;
DE AltName: Full=Kynurenine--glyoxylate transaminase {ECO:0000250|UniProtKB:Q71RI9};
DE EC=2.6.1.63 {ECO:0000250|UniProtKB:Q71RI9};
DE AltName: Full=Kynurenine--oxoglutarate transaminase III;
GN Name=KYAT3 {ECO:0000312|HGNC:HGNC:33238}; Synonyms=CCBL2, KAT3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=16376499; DOI=10.1016/j.gene.2005.09.034;
RA Yu P., Li Z., Zhang L., Tagle D.A., Cai T.;
RT "Characterization of kynurenine aminotransferase III, a novel member of a
RT phylogenetically conserved KAT family.";
RL Gene 365:111-118(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Stomach;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-454 (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 144-454, AND VARIANT PRO-206.
RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.;
RT "Full-insert sequence of mapped XREF EST.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-338, AND VARIANT PRO-206.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2 (ISOFORM 3), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 3), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the irreversible transamination of the L-tryptophan
CC metabolite L-kynurenine to form kynurenic acid (KA), an intermediate in
CC the tryptophan catabolic pathway which is also a broad spectrum
CC antagonist of the three ionotropic excitatory amino acid receptors
CC among others. May catalyze the beta-elimination of S-conjugates and Se-
CC conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S
CC or C-Se bond. Has transaminase activity towards L-kynurenine,
CC tryptophan, phenylalanine, serine, cysteine, methionine, histidine,
CC glutamine and asparagine with glyoxylate as an amino group acceptor (in
CC vitro). Has lower activity with 2-oxoglutarate as amino group acceptor
CC (in vitro). {ECO:0000250|UniProtKB:Q71RI9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-kynurenine = H2O + kynurenate + L-
CC glutamate; Xref=Rhea:RHEA:65560, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57959,
CC ChEBI:CHEBI:58454; EC=2.6.1.7;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65561;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glyoxylate + L-kynurenine = glycine + H2O + kynurenate;
CC Xref=Rhea:RHEA:65896, ChEBI:CHEBI:15377, ChEBI:CHEBI:36655,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57959, ChEBI:CHEBI:58454; EC=2.6.1.63;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65897;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-hydroxy-L-kynurenine + glyoxylate = glycine + H2O +
CC xanthurenate; Xref=Rhea:RHEA:65900, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:36655, ChEBI:CHEBI:57305, ChEBI:CHEBI:58125,
CC ChEBI:CHEBI:71201; EC=2.6.1.63;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65901;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteine + H2O = a thiol + NH4(+) +
CC pyruvate; Xref=Rhea:RHEA:18121, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29256, ChEBI:CHEBI:58717; EC=4.4.1.13;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18122;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:Q71RI9};
CC -!- PATHWAY: Amino-acid degradation; L-kynurenine degradation; kynurenate
CC from L-kynurenine: step 1/2. {ECO:0000250|UniProtKB:Q71RI9}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q71RI9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6YP21-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6YP21-2; Sequence=VSP_025603, VSP_025604;
CC Name=3;
CC IsoId=Q6YP21-3; Sequence=VSP_042841;
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: The first non-coding exon of CCBL2 is in common with that of
CC RBMXL1. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72959.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH00819.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAG29278.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY028624; AAK26163.1; -; mRNA.
DR EMBL; CR627392; CAH10487.1; -; mRNA.
DR EMBL; AK057176; BAG51875.1; -; mRNA.
DR EMBL; AL139416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000819; AAH00819.1; ALT_INIT; mRNA.
DR EMBL; AF091090; AAC72959.1; ALT_FRAME; mRNA.
DR EMBL; CR450282; CAG29278.1; ALT_FRAME; mRNA.
DR CCDS; CCDS30766.1; -. [Q6YP21-1]
DR CCDS; CCDS30767.1; -. [Q6YP21-3]
DR RefSeq; NP_001008661.1; NM_001008661.2. [Q6YP21-1]
DR RefSeq; NP_001008662.1; NM_001008662.2. [Q6YP21-3]
DR AlphaFoldDB; Q6YP21; -.
DR SMR; Q6YP21; -.
DR BioGRID; 121128; 41.
DR IntAct; Q6YP21; 10.
DR STRING; 9606.ENSP00000260508; -.
DR BindingDB; Q6YP21; -.
DR ChEMBL; CHEMBL2046260; -.
DR DrugBank; DB00114; Pyridoxal phosphate.
DR GlyGen; Q6YP21; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6YP21; -.
DR PhosphoSitePlus; Q6YP21; -.
DR BioMuta; KYAT3; -.
DR DMDM; 74710502; -.
DR EPD; Q6YP21; -.
DR jPOST; Q6YP21; -.
DR MassIVE; Q6YP21; -.
DR MaxQB; Q6YP21; -.
DR PaxDb; Q6YP21; -.
DR PeptideAtlas; Q6YP21; -.
DR PRIDE; Q6YP21; -.
DR ProteomicsDB; 67858; -. [Q6YP21-1]
DR ProteomicsDB; 67859; -. [Q6YP21-2]
DR ProteomicsDB; 67860; -. [Q6YP21-3]
DR Antibodypedia; 19822; 90 antibodies from 20 providers.
DR DNASU; 56267; -.
DR Ensembl; ENST00000260508.9; ENSP00000260508.4; ENSG00000137944.18. [Q6YP21-1]
DR Ensembl; ENST00000370491.7; ENSP00000359522.3; ENSG00000137944.18. [Q6YP21-3]
DR GeneID; 56267; -.
DR KEGG; hsa:56267; -.
DR MANE-Select; ENST00000260508.9; ENSP00000260508.4; NM_001008661.3; NP_001008661.1.
DR UCSC; uc001dmp.3; human. [Q6YP21-1]
DR CTD; 56267; -.
DR DisGeNET; 56267; -.
DR GeneCards; KYAT3; -.
DR HGNC; HGNC:33238; KYAT3.
DR HPA; ENSG00000137944; Low tissue specificity.
DR MIM; 610656; gene.
DR neXtProt; NX_Q6YP21; -.
DR OpenTargets; ENSG00000137944; -.
DR PharmGKB; PA162381274; -.
DR VEuPathDB; HostDB:ENSG00000137944; -.
DR eggNOG; KOG0257; Eukaryota.
DR GeneTree; ENSGT00940000155827; -.
DR HOGENOM; CLU_017584_4_0_1; -.
DR InParanoid; Q6YP21; -.
DR OMA; SVAMTGW; -.
DR PhylomeDB; Q6YP21; -.
DR TreeFam; TF352342; -.
DR BioCyc; MetaCyc:HS06422-MON; -.
DR BRENDA; 2.6.1.7; 2681.
DR BRENDA; 4.4.1.13; 2681.
DR PathwayCommons; Q6YP21; -.
DR Reactome; R-HSA-71240; Tryptophan catabolism.
DR SignaLink; Q6YP21; -.
DR UniPathway; UPA00334; UER00726.
DR BioGRID-ORCS; 56267; 7 hits in 1084 CRISPR screens.
DR ChiTaRS; KYAT3; human.
DR GenomeRNAi; 56267; -.
DR Pharos; Q6YP21; Tbio.
DR PRO; PR:Q6YP21; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6YP21; protein.
DR Bgee; ENSG00000137944; Expressed in parotid gland and 205 other tissues.
DR ExpressionAtlas; Q6YP21; baseline and differential.
DR Genevisible; Q6YP21; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0047804; F:cysteine-S-conjugate beta-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0047315; F:kynurenine-glyoxylate transaminase activity; ISS:UniProtKB.
DR GO; GO:0016212; F:kynurenine-oxoglutarate transaminase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; IEA:Ensembl.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; ISS:UniProtKB.
DR GO; GO:0070189; P:kynurenine metabolic process; ISS:UniProtKB.
DR GO; GO:0097053; P:L-kynurenine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR034612; KAT_III.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43807:SF6; PTHR43807:SF6; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Aminotransferase; Lyase;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..454
FT /note="Kynurenine--oxoglutarate transaminase 3"
FT /id="PRO_0000287704"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT BINDING 218
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT BINDING 429
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT MOD_RES 116
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 116
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q71RI9"
FT MOD_RES 280
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q16773"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042841"
FT VAR_SEQ 152..167
FT /note="VILIVPFYDCYEPMVR -> YNACTVKFTNLKCTAG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025603"
FT VAR_SEQ 168..454
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025604"
FT VARIANT 206
FT /note="S -> P (in dbSNP:rs1059370)"
FT /evidence="ECO:0000269|Ref.6, ECO:0000269|Ref.7"
FT /id="VAR_032352"
FT CONFLICT 251
FT /note="W -> R (in Ref. 7; CAG29278)"
FT /evidence="ECO:0000305"
FT INIT_MET Q6YP21-3:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q6YP21-3:2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 454 AA; 51400 MW; 2059D4646058BBB3 CRC64;
MFLAQRSLCS LSGRAKFLKT ISSSKILGFS TSAKMSLKFT NAKRIEGLDS NVWIEFTKLA
ADPSVVNLGQ GFPDISPPTY VKEELSKIAA IDSLNQYTRG FGHPSLVKAL SYLYEKLYQK
QIDSNKEILV TVGAYGSLFN TIQALIDEGD EVILIVPFYD CYEPMVRMAG ATPVFIPLRS
KPVYGKRWSS SDWTLDPQEL ESKFNSKTKA IILNTPHNPL GKVYNREELQ VIADLCIKYD
TLCISDEVYE WLVYSGNKHL KIATFPGMWE RTITIGSAGK TFSVTGWKLG WSIGPNHLIK
HLQTVQQNTI YTCATPLQEA LAQAFWIDIK RMDDPECYFN SLPKELEVKR DRMVRLLESV
GLKPIVPDGG YFIIADVSLL DPDLSDMKNN EPYDYKFVKW MTKHKKLSAI PVSAFCNSET
KSQFEKFVRF CFIKKDSTLD AAEEIIKAWS VQKS
