ID LGUL_HUMAN Reviewed; 184 AA.
AC Q04760; B2R6P7; B4DDV0; P78375; Q59EL0; Q5TZW3; Q96FC0; Q96J41;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 4.
DT 01-MAY-2013, entry version 144.
DE RecName: Full=Lactoylglutathione lyase;
DE EC=4.4.1.5;
DE AltName: Full=Aldoketomutase;
DE AltName: Full=Glyoxalase I;
DE Short=Glx I;
DE AltName: Full=Ketone-aldehyde mutase;
DE AltName: Full=Methylglyoxalase;
DE AltName: Full=S-D-lactoylglutathione methylglyoxal lyase;
GN Name=GLO1;
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 [MRNA] (ISOFORM 1), AND VARIANT ALA-111.
RX PubMed=7684374;
RA Kim N.-S., Umezawa Y., Ohmura S., Kato S.;
RT "Human glyoxalase I. cDNA cloning, expression, and sequence similarity
RT to glyoxalase I from Pseudomonas putida.";
RL J. Biol. Chem. 268:11217-11221(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-111.
RC TISSUE=Colon;
RX PubMed=8449929;
RA Ranganathan S., Walsh E.S., Godwin A.K., Tew K.D.;
RT "Cloning and characterization of human colon glyoxalase-I.";
RL J. Biol. Chem. 268:5661-5667(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8670058;
RA Ridderstroem M., Mannervik B.;
RT "Optimized heterologous expression of the human zinc enzyme glyoxalase
RT I.";
RL Biochem. J. 314:463-467(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-111.
RX PubMed=10564821; DOI=10.1016/S0378-1119(99)00420-5;
RA Ranganathan S., Ciaccio P.J., Walsh E.S., Tew K.D.;
RT "Genomic sequence of human glyoxalase-I: analysis of promoter activity
RT and its regulation.";
RL Gene 240:149-155(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP VARIANTS TYR-19 AND ALA-111.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP TYR-19 AND ALA-111.
RC TISSUE=Brain, Eye, 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 [10]
RP PROTEIN SEQUENCE OF 13-18 AND 128-135, ENZYME REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, GLUTATHIONYLATION AT
RP CYS-139, AND DISULFIDE BONDS.
RC TISSUE=Erythrocyte;
RX PubMed=20454679; DOI=10.1371/journal.pone.0010399;
RA Birkenmeier G., Stegemann C., Hoffmann R., Gunther R., Huse K.,
RA Birkemeyer C.;
RT "Posttranslational modification of human glyoxalase 1 indicates redox-
RT dependent regulation.";
RL PLoS ONE 5:E10399-E10399(2010).
RN [11]
RP IDENTIFICATION OF NITRIC OXIDE-MODIFIED FORM, PHOSPHORYLATION, AND
RP MUTAGENESIS OF CYS-19; CYS-20; CYS-61 AND CYS-139.
RX PubMed=17576200; DOI=10.1042/BJ20070379;
RA de Hemptinne V., Rondas D., Vandekerckhove J., Vancompernolle K.;
RT "Tumour necrosis factor induces phosphorylation primarily of the
RT nitric-oxide-responsive form of glyoxalase I.";
RL Biochem. J. 407:121-128(2007).
RN [12]
RP FUNCTION, PHOSPHORYLATION AT THR-107, AND MUTAGENESIS OF CYS-19;
RP CYS-20; SER-45; SER-69; SER-94; THR-98; THR-102; THR-107 AND CYS-139.
RX PubMed=19199007; DOI=10.1007/s11010-009-0031-7;
RA de Hemptinne V., Rondas D., Toepoel M., Vancompernolle K.;
RT "Phosphorylation on Thr-106 and NO-modification of glyoxalase I
RT suppress the TNF-induced transcriptional activity of NF-kappaB.";
RL Mol. Cell. Biochem. 325:169-178(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, 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 [14]
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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=9218781; DOI=10.1093/emboj/16.12.3386;
RA Cameron A.D., Olin B., Ridderstroem M., Mannervik B., Jones T.A.;
RT "Crystal structure of human glyoxalase I -- evidence for gene
RT duplication and 3D domain swapping.";
RL EMBO J. 16:3386-3395(1997).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=9705294; DOI=10.1074/jbc.273.34.21623;
RA Ridderstroem M., Cameron A.D., Jones T.A., Mannervik B.;
RT "Involvement of an active-site Zn2+ ligand in the catalytic mechanism
RT of human glyoxalase I.";
RL J. Biol. Chem. 273:21623-21628(1998).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10521255; DOI=10.1021/bi990696c;
RA Cameron A.D., Ridderstroem M., Olin B., Kavarana M.J., Creighton D.J.,
RA Mannervik B.;
RT "Reaction mechanism of glyoxalase I explored by an X-ray
RT crystallographic analysis of the human enzyme in complex with a
RT transition state analogue.";
RL Biochemistry 38:13480-13490(1999).
CC -!- FUNCTION: Catalyzes the conversion of hemimercaptal, formed from
CC methylglyoxal and glutathione, to S-lactoylglutathione. Involved
CC in the regulation of TNF-induced transcriptional activity of NF-
CC kappa-B.
CC -!- CATALYTIC ACTIVITY: (R)-S-lactoylglutathione = glutathione +
CC methylglyoxal.
CC -!- COFACTOR: Binds 1 zinc ion per subunit.
CC -!- ENZYME REGULATION: Regulated by oxidation of Cys-139 in response
CC to the redox state of the cell. Results in the alternative
CC formation of cystine or glutathione-bound cysteine, the latter
CC modification leading to reduced enzyme activity.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for methylglyoxal/glutathione (native form);
CC KM=0.7 mM for methylglyoxal/glutathione (reduced form);
CC Vmax=0.335 umol/min/mg enzyme with methylglyoxal/glutathione as
CC substrate (native form);
CC Vmax=0.7 umol/min/mg enzyme with methylglyoxal/glutathione as
CC substrate (reduced form);
CC Note=Reduction of GLO1 was carried out by incubation with 20 mM
CC betamercaptoethanol prior to kinetic analysis;
CC -!- PATHWAY: Secondary metabolite metabolism; methylglyoxal
CC degradation; (R)-lactate from methylglyoxal: step 1/2.
CC -!- SUBUNIT: Homodimer.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q04760-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q04760-2; Sequence=VSP_041632;
CC Note=No experimental confirmation available;
CC -!- PTM: Glutathionylation at Cys-139 inhibits enzyme activity.
CC -!- PTM: Phosphorylated at Thr-107 in the presence of CaMK2. However,
CC this is a consensus site for phosphorylation by CK2 so
CC phosphorylation may be mediated by CK2 rather than CaMK2.
CC Phosphorylation is induced by TNF and suppresses the TNF-induced
CC transcriptional activity of NF-kappa-B.
CC -!- PTM: Exists in a nitric oxide (NO)-modified form. The exact nature
CC of the modification is unknown, but it suppresses the TNF-induced
CC transcriptional activity of NF-kappa-B.
CC -!- MASS SPECTROMETRY: Mass=20687.4; Method=Electrospray; Range=2-184
CC (Q04760-1); Note=Variant Glu-111; Source=PubMed:20454679;
CC -!- MASS SPECTROMETRY: Mass=20629.7; Method=Electrospray; Range=2-184
CC (Q04760-1); Note=Variant Ala-111; Source=PubMed:20454679;
CC -!- POLYMORPHISM: Exists in three separable isoforms which originate
CC from two alleles in the genome. These correspond to two homodimers
CC and one heterodimer composed of two subunits showing different
CC electrophoretic properties.
CC -!- SIMILARITY: Belongs to the glyoxalase I family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93038.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; D13315; BAA02572.1; -; mRNA.
DR EMBL; L07837; AAA52565.1; -; mRNA.
DR EMBL; S83285; AAB49495.1; -; mRNA.
DR EMBL; AF146651; AAD38008.1; -; Genomic_DNA.
DR EMBL; AB209801; BAD93038.1; ALT_INIT; mRNA.
DR EMBL; AK293345; BAG56861.1; -; mRNA.
DR EMBL; AK312662; BAG35544.1; -; mRNA.
DR EMBL; BT019987; AAV38790.1; -; mRNA.
DR EMBL; BT019988; AAV38791.1; -; mRNA.
DR EMBL; AL391415; CAI21586.1; -; Genomic_DNA.
DR EMBL; BC001741; AAH01741.1; -; mRNA.
DR EMBL; BC011365; AAH11365.1; -; mRNA.
DR EMBL; BC015934; AAH15934.1; -; mRNA.
DR IPI; IPI00220766; -.
DR IPI; IPI01021703; -.
DR PIR; A46714; A46714.
DR PIR; S63603; S63603.
DR RefSeq; NP_006699.2; NM_006708.2.
DR UniGene; Hs.268849; -.
DR PDB; 1BH5; X-ray; 2.20 A; A/B/C/D=2-184.
DR PDB; 1FRO; X-ray; 2.20 A; A/B/C/D=2-184.
DR PDB; 1QIN; X-ray; 2.00 A; A/B=2-184.
DR PDB; 1QIP; X-ray; 1.72 A; A/B/C/D=2-184.
DR PDB; 3VW9; X-ray; 1.47 A; A/B=1-184.
DR PDBsum; 1BH5; -.
DR PDBsum; 1FRO; -.
DR PDBsum; 1QIN; -.
DR PDBsum; 1QIP; -.
DR PDBsum; 3VW9; -.
DR ProteinModelPortal; Q04760; -.
DR IntAct; Q04760; 3.
DR STRING; 9606.ENSP00000362463; -.
DR PhosphoSite; Q04760; -.
DR DMDM; 134039205; -.
DR OGP; Q04760; -.
DR REPRODUCTION-2DPAGE; IPI00220766; -.
DR REPRODUCTION-2DPAGE; Q04760; -.
DR PaxDb; Q04760; -.
DR PRIDE; Q04760; -.
DR DNASU; 2739; -.
DR Ensembl; ENST00000373365; ENSP00000362463; ENSG00000124767.
DR GeneID; 2739; -.
DR KEGG; hsa:2739; -.
DR UCSC; uc003ooc.3; human.
DR CTD; 2739; -.
DR GeneCards; GC06M038690; -.
DR HGNC; HGNC:4323; GLO1.
DR HPA; CAB040541; -.
DR HPA; CAB040542; -.
DR MIM; 138750; gene.
DR neXtProt; NX_Q04760; -.
DR PharmGKB; PA28724; -.
DR eggNOG; COG0346; -.
DR HOVERGEN; HBG025852; -.
DR InParanoid; Q04760; -.
DR KO; K01759; -.
DR OMA; WALSRKA; -.
DR OrthoDB; EOG4TQMB3; -.
DR PhylomeDB; Q04760; -.
DR BRENDA; 4.4.1.5; 2681.
DR SABIO-RK; Q04760; -.
DR UniPathway; UPA00619; UER00675.
DR BindingDB; Q04760; -.
DR ChEMBL; CHEMBL2424; -.
DR DrugBank; DB00143; Glutathione.
DR EvolutionaryTrace; Q04760; -.
DR GenomeRNAi; 2739; -.
DR NextBio; 10796; -.
DR Bgee; Q04760; -.
DR CleanEx; HS_GLO1; -.
DR Genevestigator; Q04760; -.
DR GermOnline; ENSG00000124767; Homo sapiens.
DR GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR GO; GO:0004462; F:lactoylglutathione lyase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:Compara.
DR GO; GO:0009438; P:methylglyoxal metabolic process; IEA:Compara.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:Compara.
DR InterPro; IPR004360; Glyas_Fos-R_dOase_dom.
DR InterPro; IPR004361; Glyoxalase_1.
DR InterPro; IPR018146; Glyoxalase_1_CS.
DR Pfam; PF00903; Glyoxalase; 1.
DR TIGRFAMs; TIGR00068; glyox_I; 1.
DR PROSITE; PS00934; GLYOXALASE_I_1; 1.
DR PROSITE; PS00935; GLYOXALASE_I_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Disulfide bond; Glutathionylation; Lyase;
KW Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Zinc.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 184 Lactoylglutathione lyase.
FT /FTId=PRO_0000168076.
FT METAL 34 34 Zinc.
FT METAL 100 100 Zinc.
FT METAL 127 127 Zinc.
FT METAL 173 173 Zinc.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 107 107 Phosphothreonine.
FT MOD_RES 139 139 S-glutathionyl cysteine.
FT MOD_RES 148 148 N6-acetyllysine.
FT DISULFID 19 20
FT DISULFID 61 139 Alternate.
FT VAR_SEQ 105 119 Missing (in isoform 2).
FT /FTId=VSP_041632.
FT VARIANT 19 19 C -> Y (in dbSNP:rs17855424).
FT /FTId=VAR_031078.
FT VARIANT 111 111 E -> A (in dbSNP:rs4746).
FT /FTId=VAR_013481.
FT MUTAGEN 19 19 C->A: No effect on NO-mediated
FT modification. Impaired NO-mediated
FT modification; when associated with A-20.
FT Loss of NO-mediated modification; when
FT associated with A-139.
FT MUTAGEN 20 20 C->A: No effect on NO-mediated
FT modification. Impaired NO-mediated
FT modification; when associated with A-19.
FT Loss of NO-mediated modification; when
FT associated with A-139.
FT MUTAGEN 45 45 S->A: No effect on phosphorylation.
FT MUTAGEN 61 61 C->A: No effect on NO-mediated
FT modification.
FT MUTAGEN 69 69 S->A: No effect on phosphorylation.
FT MUTAGEN 94 94 S->A: No effect on phosphorylation.
FT MUTAGEN 98 98 T->A: No effect on phosphorylation.
FT MUTAGEN 102 102 T->A: No effect on phosphorylation.
FT MUTAGEN 107 107 T->A: Loss of phosphorylation.
FT MUTAGEN 139 139 C->A: Impaired NO-mediated modification.
FT Loss of NO-mediated modification; when
FT associated with A-19 or A-20.
FT HELIX 13 18
FT HELIX 25 27
FT STRAND 31 38
FT HELIX 42 51
FT STRAND 56 63
FT TURN 64 67
FT STRAND 68 75
FT HELIX 78 80
FT HELIX 85 92
FT STRAND 96 104
FT HELIX 107 109
FT STRAND 118 122
FT STRAND 124 131
FT HELIX 135 144
FT STRAND 149 151
FT STRAND 155 158
FT STRAND 162 165
FT STRAND 171 175
FT HELIX 177 179
FT HELIX 181 183
SQ SEQUENCE 184 AA; 20778 MW; 46291B7878070028 CRC64;
MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK
CDFPIMKFSL YFLAYEDKND IPKEKDEKIA WALSRKATLE LTHNWGTEDD ETQSYHNGNS
DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKM
ATLM
//
