GLO2_HUMAN
ID GLO2_HUMAN Reviewed; 308 AA.
AC Q16775; A8K290; B4DP33; B4DRA7; E7EN93;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Hydroxyacylglutathione hydrolase, mitochondrial {ECO:0000303|PubMed:15117945};
DE EC=3.1.2.6 {ECO:0000269|PubMed:8550579};
DE AltName: Full=Glyoxalase II;
DE Short=Glx II;
DE Flags: Precursor;
GN Name=HAGH; Synonyms=GLO2, HAGH1;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Thalamus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-308 (ISOFORMS 1/2), PROTEIN SEQUENCE,
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC TISSUE=Liver;
RX PubMed=8550579; DOI=10.1074/jbc.271.1.319;
RA Ridderstroem M., Saccucci F., Hellman U., Bergman T., Principato G.,
RA Mannervik B.;
RT "Molecular cloning, heterologous expression, and characterization of human
RT glyoxalase II.";
RL J. Biol. Chem. 271:319-323(1996).
RN [6]
RP SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, ALTERNATIVE SPLICING
RP (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX PubMed=15117945; DOI=10.1074/jbc.m403470200;
RA Cordell P.A., Futers T.S., Grant P.J., Pease R.J.;
RT "The human hydroxyacylglutathione hydrolase (HAGH) gene encodes both
RT cytosolic and mitochondrial forms of glyoxalase II.";
RL J. Biol. Chem. 279:28653-28661(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-229, 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 [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 49-308 IN COMPLEX WITH SUBSTRATE
RP ANALOGS AND ZINC IONS, COFACTOR, SUBUNIT, AND ZINC-BINDING SITES.
RC TISSUE=Liver;
RX PubMed=10508780; DOI=10.1016/s0969-2126(99)80174-9;
RA Cameron A.D., Ridderstroem M., Olin B., Mannervik B.;
RT "Crystal structure of human glyoxalase II and its complex with a
RT glutathione thiolester substrate analogue.";
RL Structure 7:1067-1077(1999).
CC -!- FUNCTION: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-
CC glutathione to form glutathione and D-lactic acid.
CC {ECO:0000269|PubMed:8550579}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy
CC carboxylate + glutathione + H(+); Xref=Rhea:RHEA:21864,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:58896, ChEBI:CHEBI:71261; EC=3.1.2.6;
CC Evidence={ECO:0000269|PubMed:8550579};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21865;
CC Evidence={ECO:0000305|PubMed:8550579};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-S-lactoylglutathione + H2O = (R)-lactate + glutathione +
CC H(+); Xref=Rhea:RHEA:25245, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16004, ChEBI:CHEBI:57474, ChEBI:CHEBI:57925; EC=3.1.2.6;
CC Evidence={ECO:0000269|PubMed:8550579};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25246;
CC Evidence={ECO:0000305|PubMed:8550579};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10508780};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:10508780};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=187 uM for S-D-lactoylglutathione {ECO:0000269|PubMed:8550579};
CC KM=29 uM for S-D-mandeloylglutathione {ECO:0000269|PubMed:8550579};
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal degradation;
CC (R)-lactate from methylglyoxal: step 2/2.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10508780}.
CC -!- INTERACTION:
CC Q16775; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-3905342, EBI-750109;
CC Q16775-2; P31941: APOBEC3A; NbExp=3; IntAct=EBI-17557678, EBI-13050366;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion matrix
CC {ECO:0000269|PubMed:15117945}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:15117945}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=1;
CC IsoId=Q16775-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16775-2; Sequence=VSP_037929;
CC Name=3;
CC IsoId=Q16775-3; Sequence=VSP_055199, VSP_055200;
CC -!- TISSUE SPECIFICITY: Expressed in liver and kidney.
CC {ECO:0000269|PubMed:15117945}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing. Also
CC produced by alternative initiation at Met-49 of isoform 1.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family. {ECO:0000305}.
CC -!- CAUTION: Only one single gene encoding glyoxalase II has been
CC identified in vertebrates. In yeast and higher plants, separate genes
CC encode the cytosolic and mitochondrial forms of glyoxalase II.
CC {ECO:0000305|PubMed:15117945}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00840.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA62483.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK290155; BAF82844.1; -; mRNA.
DR EMBL; AK298174; BAG60445.1; -; mRNA.
DR EMBL; AK299173; BAG61219.1; -; mRNA.
DR EMBL; AE006639; AAK61294.1; -; Genomic_DNA.
DR EMBL; AC012180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000840; AAH00840.1; ALT_INIT; mRNA.
DR EMBL; BC002627; AAH02627.2; -; mRNA.
DR EMBL; X90999; CAA62483.1; ALT_INIT; mRNA.
DR CCDS; CCDS10447.2; -. [Q16775-1]
DR CCDS; CCDS32366.1; -. [Q16775-2]
DR CCDS; CCDS66900.1; -. [Q16775-3]
DR RefSeq; NP_001035517.1; NM_001040427.1. [Q16775-2]
DR RefSeq; NP_001273178.1; NM_001286249.1. [Q16775-3]
DR RefSeq; NP_005317.2; NM_005326.4. [Q16775-1]
DR RefSeq; XP_011520772.1; XM_011522470.2. [Q16775-3]
DR PDB; 1QH3; X-ray; 1.90 A; A/B=49-308.
DR PDB; 1QH5; X-ray; 1.45 A; A/B=49-308.
DR PDBsum; 1QH3; -.
DR PDBsum; 1QH5; -.
DR AlphaFoldDB; Q16775; -.
DR SMR; Q16775; -.
DR BioGRID; 109279; 69.
DR IntAct; Q16775; 33.
DR MINT; Q16775; -.
DR STRING; 9606.ENSP00000380514; -.
DR BindingDB; Q16775; -.
DR ChEMBL; CHEMBL2261; -.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB03889; S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione.
DR iPTMnet; Q16775; -.
DR MetOSite; Q16775; -.
DR PhosphoSitePlus; Q16775; -.
DR BioMuta; HAGH; -.
DR DMDM; 257051015; -.
DR EPD; Q16775; -.
DR jPOST; Q16775; -.
DR MassIVE; Q16775; -.
DR MaxQB; Q16775; -.
DR PaxDb; Q16775; -.
DR PeptideAtlas; Q16775; -.
DR PRIDE; Q16775; -.
DR ProteomicsDB; 17109; -.
DR ProteomicsDB; 61064; -. [Q16775-1]
DR ProteomicsDB; 61065; -. [Q16775-2]
DR Antibodypedia; 23273; 235 antibodies from 31 providers.
DR DNASU; 3029; -.
DR Ensembl; ENST00000397353.6; ENSP00000380511.2; ENSG00000063854.13. [Q16775-2]
DR Ensembl; ENST00000397356.8; ENSP00000380514.3; ENSG00000063854.13. [Q16775-1]
DR Ensembl; ENST00000455446.6; ENSP00000406552.2; ENSG00000063854.13. [Q16775-3]
DR GeneID; 3029; -.
DR KEGG; hsa:3029; -.
DR MANE-Select; ENST00000397356.8; ENSP00000380514.3; NM_005326.6; NP_005317.2.
DR UCSC; uc002cmz.4; human. [Q16775-1]
DR CTD; 3029; -.
DR DisGeNET; 3029; -.
DR GeneCards; HAGH; -.
DR HGNC; HGNC:4805; HAGH.
DR HPA; ENSG00000063854; Low tissue specificity.
DR MalaCards; HAGH; -.
DR MIM; 138760; gene+phenotype.
DR neXtProt; NX_Q16775; -.
DR OpenTargets; ENSG00000063854; -.
DR PharmGKB; PA29179; -.
DR VEuPathDB; HostDB:ENSG00000063854; -.
DR eggNOG; KOG0813; Eukaryota.
DR GeneTree; ENSGT00940000159176; -.
DR HOGENOM; CLU_1175103_0_0_1; -.
DR InParanoid; Q16775; -.
DR OMA; NYIWLLQ; -.
DR OrthoDB; 961826at2759; -.
DR PhylomeDB; Q16775; -.
DR TreeFam; TF105273; -.
DR BRENDA; 3.1.2.6; 2681.
DR PathwayCommons; Q16775; -.
DR Reactome; R-HSA-70268; Pyruvate metabolism. [Q16775-2]
DR SABIO-RK; Q16775; -.
DR SignaLink; Q16775; -.
DR UniPathway; UPA00619; UER00676.
DR BioGRID-ORCS; 3029; 13 hits in 1081 CRISPR screens.
DR ChiTaRS; HAGH; human.
DR EvolutionaryTrace; Q16775; -.
DR GeneWiki; HAGH; -.
DR GenomeRNAi; 3029; -.
DR Pharos; Q16775; Tbio.
DR PRO; PR:Q16775; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q16775; protein.
DR Bgee; ENSG00000063854; Expressed in apex of heart and 205 other tissues.
DR ExpressionAtlas; Q16775; baseline and differential.
DR Genevisible; Q16775; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006750; P:glutathione biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IEA:InterPro.
DR CDD; cd07723; hydroxyacylglutathione_hydrolase_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR HAMAP; MF_01374; Glyoxalase_2; 1.
DR InterPro; IPR035680; Clx_II_MBL.
DR InterPro; IPR032282; HAGH_C.
DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF16123; HAGH_C; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR PIRSF; PIRSF005457; Glx; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
DR TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing;
KW Cytoplasm; Direct protein sequencing; Hydrolase; Metal-binding;
KW Mitochondrion; Reference proteome; Transit peptide; Zinc.
FT TRANSIT 1..13
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 14..308
FT /note="Hydroxyacylglutathione hydrolase, mitochondrial"
FT /id="PRO_0000192342"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10508780"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10508780"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10508780"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10508780"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10508780"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10508780"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10508780"
FT BINDING 191..193
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10508780"
FT BINDING 221..223
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10508780"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10508780"
FT BINDING 297..300
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10508780"
FT MOD_RES 116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99KB8"
FT MOD_RES 229
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 229
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99KB8"
FT VAR_SEQ 1..48
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037929"
FT VAR_SEQ 146..236
FT /note="GSLNVKCLATPCHTSGHICYFVSKPGGSEPPAVFTGDTLFVAGCGKFYEGTA
FT DEMCKALLEVLGRLPPDTRVYCGHEYTINNLKFARHVEP -> TPCLWLAAGSSMKGLR
FT MRCVKLCWRSWAGSPRTQESTVATSTPSTTSSLHATWSPAMPPSGRSWPGPRRSTASGS
FT PQCHPPWQRSLPTTPS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055199"
FT VAR_SEQ 237..308
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055200"
FT CONFLICT 67
FT /note="D -> G (in Ref. 1; BAG60445)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="L -> P (in Ref. 1; BAG61219)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="K -> E (in Ref. 1; BAF82844)"
FT /evidence="ECO:0000305"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:1QH5"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:1QH5"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:1QH5"
FT TURN 68..71
FT /evidence="ECO:0007829|PDB:1QH5"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1QH5"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:1QH5"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1QH5"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:1QH5"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:1QH5"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:1QH5"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1QH5"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1QH5"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:1QH5"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1QH5"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:1QH5"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1QH5"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1QH5"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:1QH5"
FT TURN 206..210
FT /evidence="ECO:0007829|PDB:1QH5"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:1QH5"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:1QH5"
FT HELIX 239..254
FT /evidence="ECO:0007829|PDB:1QH5"
FT HELIX 263..269
FT /evidence="ECO:0007829|PDB:1QH5"
FT TURN 271..276
FT /evidence="ECO:0007829|PDB:1QH5"
FT HELIX 278..284
FT /evidence="ECO:0007829|PDB:1QH5"
FT HELIX 289..302
FT /evidence="ECO:0007829|PDB:1QH5"
SQ SEQUENCE 308 AA; 33806 MW; 64E5C214B6EC61CB CRC64;
MVVGRGLLGR RSLAALGAAC ARRGLGPALL GVFCHTDLRK NLTVDEGTMK VEVLPALTDN
YMYLVIDDET KEAAIVDPVQ PQKVVDAARK HGVKLTTVLT THHHWDHAGG NEKLVKLESG
LKVYGGDDRI GALTHKITHL STLQVGSLNV KCLATPCHTS GHICYFVSKP GGSEPPAVFT
GDTLFVAGCG KFYEGTADEM CKALLEVLGR LPPDTRVYCG HEYTINNLKF ARHVEPGNAA
IREKLAWAKE KYSIGEPTVP STLAEEFTYN PFMRVREKTV QQHAGETDPV TTMRAVRREK
DQFKMPRD
