Full text data of HAGH
HAGH
(GLO2, HAGH1)
[Confidence: high (present in two of the MS resources)]
Hydroxyacylglutathione hydrolase, mitochondrial; 3.1.2.6 (Glyoxalase II; Glx II; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Hydroxyacylglutathione hydrolase, mitochondrial; 3.1.2.6 (Glyoxalase II; Glx II; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00003933
IPI00003933 Hydroxyacylglutathione hydrolase Hydroxyacylglutathione hydrolase membrane n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 3 n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00003933 Hydroxyacylglutathione hydrolase Hydroxyacylglutathione hydrolase membrane n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 3 n/a not mentioned n/a found at its expected molecular weight found at molecular weight
Comments
Isoform Q16775-2 was detected.
Isoform Q16775-2 was detected.
UniProt
Q16775
ID GLO2_HUMAN Reviewed; 308 AA.
AC Q16775; A8K290; B4DRA7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-SEP-2009, sequence version 2.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Hydroxyacylglutathione hydrolase, mitochondrial;
DE EC=3.1.2.6;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
RA Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2
RT Mb of 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.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA 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.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA 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] (ISOFORMS 1 AND 2).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-308 (ISOFORMS 1/2).
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
RT human 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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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 X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 49-308 IN COMPLEX WITH
RP SUBSTRATE ANALOGS AND ZINC IONS.
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-
CC lactoyl-glutathione to form glutathione and D-lactic acid.
CC -!- CATALYTIC ACTIVITY: S-(2-hydroxyacyl)glutathione + H(2)O =
CC glutathione + a 2-hydroxy carboxylate.
CC -!- COFACTOR: Binds 2 zinc ions per subunit.
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal
CC degradation; (R)-lactate from methylglyoxal: step 2/2.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion matrix.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q16775-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16775-2; Sequence=VSP_037929;
CC Note=Produced by alternative splicing. Also produced by
CC alternative initiation at Met-49 of isoform 1;
CC -!- TISSUE SPECIFICITY: Expressed in liver and kidney.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family.
CC -!- CAUTION: Only one single gene encoding glyoxalase II has been
CC identified in vertebrates. In yeast and higher plants, separate
CC genes encode the cytosolic and mitochondrial forms of glyoxalase
CC II.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00840.1; Type=Erroneous initiation;
CC Sequence=CAA62483.1; Type=Erroneous initiation;
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DR EMBL; AK290155; BAF82844.1; -; 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 RefSeq; NP_001035517.1; NM_001040427.1.
DR RefSeq; NP_001273178.1; NM_001286249.1.
DR RefSeq; NP_005317.2; NM_005326.4.
DR UniGene; Hs.157394; -.
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 PDB; 2F50; Model; -; A=64-225.
DR PDBsum; 1QH3; -.
DR PDBsum; 1QH5; -.
DR PDBsum; 2F50; -.
DR ProteinModelPortal; Q16775; -.
DR SMR; Q16775; 49-308.
DR IntAct; Q16775; 1.
DR STRING; 9606.ENSP00000380514; -.
DR BindingDB; Q16775; -.
DR ChEMBL; CHEMBL2261; -.
DR DrugBank; DB00143; Glutathione.
DR PhosphoSite; Q16775; -.
DR DMDM; 257051015; -.
DR PaxDb; Q16775; -.
DR PRIDE; Q16775; -.
DR DNASU; 3029; -.
DR Ensembl; ENST00000397353; ENSP00000380511; ENSG00000063854.
DR Ensembl; ENST00000397356; ENSP00000380514; ENSG00000063854.
DR GeneID; 3029; -.
DR KEGG; hsa:3029; -.
DR UCSC; uc002cmz.3; human.
DR CTD; 3029; -.
DR GeneCards; GC16M001845; -.
DR HGNC; HGNC:4805; HAGH.
DR HPA; CAB033531; -.
DR MIM; 138760; gene+phenotype.
DR neXtProt; NX_Q16775; -.
DR PharmGKB; PA29179; -.
DR eggNOG; COG0491; -.
DR HOGENOM; HOG000058041; -.
DR HOVERGEN; HBG001152; -.
DR InParanoid; Q16775; -.
DR KO; K01069; -.
DR OMA; IGDEKEW; -.
DR BRENDA; 3.1.2.6; 5596.
DR SABIO-RK; Q16775; -.
DR UniPathway; UPA00619; UER00676.
DR EvolutionaryTrace; Q16775; -.
DR GeneWiki; HAGH; -.
DR GenomeRNAi; 3029; -.
DR NextBio; 11990; -.
DR PRO; PR:Q16775; -.
DR ArrayExpress; Q16775; -.
DR Bgee; Q16775; -.
DR CleanEx; HS_HAGH; -.
DR Genevestigator; Q16775; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006750; P:glutathione biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Beta-lactamas-like.
DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR PANTHER; PTHR11935:SF7; PTHR11935:SF7; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR PIRSF; PIRSF005457; Glx; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation;
KW Alternative splicing; Complete proteome; Cytoplasm; Hydrolase;
KW Metal-binding; Mitochondrion; Reference proteome; Transit peptide;
KW Zinc.
FT TRANSIT 1 13 Mitochondrion (Potential).
FT CHAIN 14 308 Hydroxyacylglutathione hydrolase,
FT mitochondrial.
FT /FTId=PRO_0000192342.
FT REGION 191 193 Substrate.
FT REGION 221 223 Substrate.
FT REGION 297 300 Substrate.
FT METAL 102 102 Zinc 1.
FT METAL 104 104 Zinc 1.
FT METAL 106 106 Zinc 2.
FT METAL 107 107 Zinc 2.
FT METAL 158 158 Zinc 1.
FT METAL 182 182 Zinc 1.
FT METAL 182 182 Zinc 2.
FT METAL 221 221 Zinc 2.
FT MOD_RES 116 116 N6-acetyllysine (By similarity).
FT MOD_RES 229 229 N6-acetyllysine.
FT VAR_SEQ 1 48 Missing (in isoform 2).
FT /FTId=VSP_037929.
FT CONFLICT 121 121 L -> P (in Ref. 1; BAG61219).
FT CONFLICT 202 202 K -> E (in Ref. 1; BAF82844).
FT STRAND 50 56
FT TURN 57 59
FT STRAND 60 67
FT TURN 68 71
FT STRAND 72 77
FT HELIX 81 91
FT STRAND 94 99
FT HELIX 105 108
FT HELIX 111 117
FT STRAND 122 126
FT STRAND 134 136
FT STRAND 142 145
FT STRAND 148 154
FT STRAND 157 159
FT STRAND 163 168
FT STRAND 170 174
FT STRAND 177 181
FT HELIX 197 205
FT TURN 206 210
FT STRAND 216 221
FT HELIX 224 234
FT HELIX 239 254
FT HELIX 263 269
FT TURN 271 276
FT HELIX 278 284
FT HELIX 289 302
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
//
ID GLO2_HUMAN Reviewed; 308 AA.
AC Q16775; A8K290; B4DRA7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-SEP-2009, sequence version 2.
DT 22-JAN-2014, entry version 126.
DE RecName: Full=Hydroxyacylglutathione hydrolase, mitochondrial;
DE EC=3.1.2.6;
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J.,
RA Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2
RT Mb of 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.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA 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.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA 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] (ISOFORMS 1 AND 2).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-308 (ISOFORMS 1/2).
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
RT human 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 MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
RA Buerckstuemmer T., 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 X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 49-308 IN COMPLEX WITH
RP SUBSTRATE ANALOGS AND ZINC IONS.
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-
CC lactoyl-glutathione to form glutathione and D-lactic acid.
CC -!- CATALYTIC ACTIVITY: S-(2-hydroxyacyl)glutathione + H(2)O =
CC glutathione + a 2-hydroxy carboxylate.
CC -!- COFACTOR: Binds 2 zinc ions per subunit.
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal
CC degradation; (R)-lactate from methylglyoxal: step 2/2.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion matrix.
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=2;
CC Name=1;
CC IsoId=Q16775-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16775-2; Sequence=VSP_037929;
CC Note=Produced by alternative splicing. Also produced by
CC alternative initiation at Met-49 of isoform 1;
CC -!- TISSUE SPECIFICITY: Expressed in liver and kidney.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC Glyoxalase II family.
CC -!- CAUTION: Only one single gene encoding glyoxalase II has been
CC identified in vertebrates. In yeast and higher plants, separate
CC genes encode the cytosolic and mitochondrial forms of glyoxalase
CC II.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00840.1; Type=Erroneous initiation;
CC Sequence=CAA62483.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AK290155; BAF82844.1; -; 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 RefSeq; NP_001035517.1; NM_001040427.1.
DR RefSeq; NP_001273178.1; NM_001286249.1.
DR RefSeq; NP_005317.2; NM_005326.4.
DR UniGene; Hs.157394; -.
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 PDB; 2F50; Model; -; A=64-225.
DR PDBsum; 1QH3; -.
DR PDBsum; 1QH5; -.
DR PDBsum; 2F50; -.
DR ProteinModelPortal; Q16775; -.
DR SMR; Q16775; 49-308.
DR IntAct; Q16775; 1.
DR STRING; 9606.ENSP00000380514; -.
DR BindingDB; Q16775; -.
DR ChEMBL; CHEMBL2261; -.
DR DrugBank; DB00143; Glutathione.
DR PhosphoSite; Q16775; -.
DR DMDM; 257051015; -.
DR PaxDb; Q16775; -.
DR PRIDE; Q16775; -.
DR DNASU; 3029; -.
DR Ensembl; ENST00000397353; ENSP00000380511; ENSG00000063854.
DR Ensembl; ENST00000397356; ENSP00000380514; ENSG00000063854.
DR GeneID; 3029; -.
DR KEGG; hsa:3029; -.
DR UCSC; uc002cmz.3; human.
DR CTD; 3029; -.
DR GeneCards; GC16M001845; -.
DR HGNC; HGNC:4805; HAGH.
DR HPA; CAB033531; -.
DR MIM; 138760; gene+phenotype.
DR neXtProt; NX_Q16775; -.
DR PharmGKB; PA29179; -.
DR eggNOG; COG0491; -.
DR HOGENOM; HOG000058041; -.
DR HOVERGEN; HBG001152; -.
DR InParanoid; Q16775; -.
DR KO; K01069; -.
DR OMA; IGDEKEW; -.
DR BRENDA; 3.1.2.6; 5596.
DR SABIO-RK; Q16775; -.
DR UniPathway; UPA00619; UER00676.
DR EvolutionaryTrace; Q16775; -.
DR GeneWiki; HAGH; -.
DR GenomeRNAi; 3029; -.
DR NextBio; 11990; -.
DR PRO; PR:Q16775; -.
DR ArrayExpress; Q16775; -.
DR Bgee; Q16775; -.
DR CleanEx; HS_HAGH; -.
DR Genevestigator; Q16775; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006750; P:glutathione biosynthetic process; IDA:UniProtKB.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Beta-lactamas-like.
DR InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR PANTHER; PTHR11935:SF7; PTHR11935:SF7; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR PIRSF; PIRSF005457; Glx; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation;
KW Alternative splicing; Complete proteome; Cytoplasm; Hydrolase;
KW Metal-binding; Mitochondrion; Reference proteome; Transit peptide;
KW Zinc.
FT TRANSIT 1 13 Mitochondrion (Potential).
FT CHAIN 14 308 Hydroxyacylglutathione hydrolase,
FT mitochondrial.
FT /FTId=PRO_0000192342.
FT REGION 191 193 Substrate.
FT REGION 221 223 Substrate.
FT REGION 297 300 Substrate.
FT METAL 102 102 Zinc 1.
FT METAL 104 104 Zinc 1.
FT METAL 106 106 Zinc 2.
FT METAL 107 107 Zinc 2.
FT METAL 158 158 Zinc 1.
FT METAL 182 182 Zinc 1.
FT METAL 182 182 Zinc 2.
FT METAL 221 221 Zinc 2.
FT MOD_RES 116 116 N6-acetyllysine (By similarity).
FT MOD_RES 229 229 N6-acetyllysine.
FT VAR_SEQ 1 48 Missing (in isoform 2).
FT /FTId=VSP_037929.
FT CONFLICT 121 121 L -> P (in Ref. 1; BAG61219).
FT CONFLICT 202 202 K -> E (in Ref. 1; BAF82844).
FT STRAND 50 56
FT TURN 57 59
FT STRAND 60 67
FT TURN 68 71
FT STRAND 72 77
FT HELIX 81 91
FT STRAND 94 99
FT HELIX 105 108
FT HELIX 111 117
FT STRAND 122 126
FT STRAND 134 136
FT STRAND 142 145
FT STRAND 148 154
FT STRAND 157 159
FT STRAND 163 168
FT STRAND 170 174
FT STRAND 177 181
FT HELIX 197 205
FT TURN 206 210
FT STRAND 216 221
FT HELIX 224 234
FT HELIX 239 254
FT HELIX 263 269
FT TURN 271 276
FT HELIX 278 284
FT HELIX 289 302
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
//
MIM
138760
*RECORD*
*FIELD* NO
138760
*FIELD* TI
*138760 HYDROXYACYL GLUTATHIONE HYDROLASE; HAGH
;;GLYOXALASE II; GLO2
*FIELD* TX
DESCRIPTION
read more
Glyoxalase II (EC 3.1.2.6), otherwise known as hydroxyacyl-glutathione
hydrolase, converts the intermediate substrate S-lactoyl-glutathione to
reduced glutathione and D-lactate (summary by Honey and Shows, 1981).
CLONING
Ridderstrom et al. (1996) cloned a cDNA coding for glyoxalase II from
human liver. The 1,011-bp sequence contains a full-length coding region
of 780 basepairs, corresponding to a 260-amino acid polypeptide. The
calculated molecular mass of the protein is 28,861 Da. They expressed
the gene in bacteria and the recombinant enzyme showed a kinetic
behavior indistinguishable from that of the native enzyme.
MAPPING
By study of somatic cell hybrids, Honey and Shows (1981) concluded that
the gene for glyoxalase II is on chromosome 16. Mulley and Callen (1986)
confirmed the assignment of HAGH to chromosome 16 by studies of a
human-mouse hybrid panel. They found that both HAGH and phosphoglycolate
phosphatase (PGP; 172280) were present only in those cell lines
containing 16p13.
Mulley et al. (1990) assigned the HAGH locus to 16p13.3 by
electrophoretic detection of enzymes from a mouse/human somatic cell
panel, the members of which carried portions of human chromosome 16 with
precisely defined breakpoints.
MOLECULAR GENETICS
Board (1980) described rare polymorphism of glyoxalase II, observed only
in a Micronesian population, in which a new variant allele had a
frequency of 0.016. In the heterozygotes, the electrophoretic pattern
was a double band, suggesting that the structure of glyoxalase II is
monomeric. The enzyme shows a high degree of polymorphism in anthropoid
primates (Board et al., 1981).
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
*FIELD* SA
Ball and Vander Jagt (1979)
*FIELD* RF
1. Ball, J. C.; Vander Jagt, D. L.: Purification of S-2-hydroxyacylglutathione
hydrolase (glyoxalase II) from rat erythrocytes. Anal. Biochem. 98:
472-477, 1979.
2. Board, P. G.: Genetic polymorphism of human erythrocyte glyoxalase
II. Am. J. Hum. Genet. 32: 690-694, 1980.
3. Board, P. G.; Gibbs, C. J., Jr.; Gajdusek, D. C.: Polymorphism
of erythrocyte glyoxalase II in anthropoid primates. Folia Primatol. 36:
138-143, 1981.
4. Honey, N. K.; Shows, T. B.: Assignment of the glyoxalase II gene
(HAGH) to human chromosome 16. Hum. Genet. 58: 358-361, 1981.
5. Mulley, J. C.; Barton, N.; Callen, D. F.: Localisation of human
PGP and HAGH genes to 16p13.3. Cytogenet. Cell Genet. 53: 175-176,
1990.
6. Mulley, J. C.; Callen, D. F.: New regional localisations for HAGH
and PGP on human chromosome 16. Hum. Genet. 74: 423-424, 1986.
7. Ridderstrom, M.; Saccucci, F.; Hellman, U.; Bergman, T.; Principato,
G.; Mannervik, B.: Molecular cloning, heterologous expression, and
characterization of human glyoxalase II. J. Biol. Chem. 271: 319-323,
1996.
8. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World Distribution.
New York: Oxford Univ. Press (pub.) 1988.
*FIELD* CN
Lori M. Kelman - updated: 8/22/1996
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 06/13/2011
carol: 6/9/2011
mgross: 3/17/2004
mark: 8/22/1996
terry: 8/22/1996
mark: 8/21/1996
mimadm: 9/24/1994
pfoster: 2/18/1994
carol: 3/26/1992
supermim: 3/16/1992
carol: 2/26/1991
carol: 2/8/1991
*RECORD*
*FIELD* NO
138760
*FIELD* TI
*138760 HYDROXYACYL GLUTATHIONE HYDROLASE; HAGH
;;GLYOXALASE II; GLO2
*FIELD* TX
DESCRIPTION
read more
Glyoxalase II (EC 3.1.2.6), otherwise known as hydroxyacyl-glutathione
hydrolase, converts the intermediate substrate S-lactoyl-glutathione to
reduced glutathione and D-lactate (summary by Honey and Shows, 1981).
CLONING
Ridderstrom et al. (1996) cloned a cDNA coding for glyoxalase II from
human liver. The 1,011-bp sequence contains a full-length coding region
of 780 basepairs, corresponding to a 260-amino acid polypeptide. The
calculated molecular mass of the protein is 28,861 Da. They expressed
the gene in bacteria and the recombinant enzyme showed a kinetic
behavior indistinguishable from that of the native enzyme.
MAPPING
By study of somatic cell hybrids, Honey and Shows (1981) concluded that
the gene for glyoxalase II is on chromosome 16. Mulley and Callen (1986)
confirmed the assignment of HAGH to chromosome 16 by studies of a
human-mouse hybrid panel. They found that both HAGH and phosphoglycolate
phosphatase (PGP; 172280) were present only in those cell lines
containing 16p13.
Mulley et al. (1990) assigned the HAGH locus to 16p13.3 by
electrophoretic detection of enzymes from a mouse/human somatic cell
panel, the members of which carried portions of human chromosome 16 with
precisely defined breakpoints.
MOLECULAR GENETICS
Board (1980) described rare polymorphism of glyoxalase II, observed only
in a Micronesian population, in which a new variant allele had a
frequency of 0.016. In the heterozygotes, the electrophoretic pattern
was a double band, suggesting that the structure of glyoxalase II is
monomeric. The enzyme shows a high degree of polymorphism in anthropoid
primates (Board et al., 1981).
Data on gene frequencies of allelic variants were tabulated by
Roychoudhury and Nei (1988).
*FIELD* SA
Ball and Vander Jagt (1979)
*FIELD* RF
1. Ball, J. C.; Vander Jagt, D. L.: Purification of S-2-hydroxyacylglutathione
hydrolase (glyoxalase II) from rat erythrocytes. Anal. Biochem. 98:
472-477, 1979.
2. Board, P. G.: Genetic polymorphism of human erythrocyte glyoxalase
II. Am. J. Hum. Genet. 32: 690-694, 1980.
3. Board, P. G.; Gibbs, C. J., Jr.; Gajdusek, D. C.: Polymorphism
of erythrocyte glyoxalase II in anthropoid primates. Folia Primatol. 36:
138-143, 1981.
4. Honey, N. K.; Shows, T. B.: Assignment of the glyoxalase II gene
(HAGH) to human chromosome 16. Hum. Genet. 58: 358-361, 1981.
5. Mulley, J. C.; Barton, N.; Callen, D. F.: Localisation of human
PGP and HAGH genes to 16p13.3. Cytogenet. Cell Genet. 53: 175-176,
1990.
6. Mulley, J. C.; Callen, D. F.: New regional localisations for HAGH
and PGP on human chromosome 16. Hum. Genet. 74: 423-424, 1986.
7. Ridderstrom, M.; Saccucci, F.; Hellman, U.; Bergman, T.; Principato,
G.; Mannervik, B.: Molecular cloning, heterologous expression, and
characterization of human glyoxalase II. J. Biol. Chem. 271: 319-323,
1996.
8. Roychoudhury, A. K.; Nei, M.: Human Polymorphic Genes: World Distribution.
New York: Oxford Univ. Press (pub.) 1988.
*FIELD* CN
Lori M. Kelman - updated: 8/22/1996
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
carol: 06/13/2011
carol: 6/9/2011
mgross: 3/17/2004
mark: 8/22/1996
terry: 8/22/1996
mark: 8/21/1996
mimadm: 9/24/1994
pfoster: 2/18/1994
carol: 3/26/1992
supermim: 3/16/1992
carol: 2/26/1991
carol: 2/8/1991