Full text data of GLRX
GLRX
(GRX)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Glutaredoxin-1 (Thioltransferase-1; TTase-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Glutaredoxin-1 (Thioltransferase-1; TTase-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00219025
IPI00219025 Glutaredoxin (thioltransferase) blood, Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. soluble 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 n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00219025 Glutaredoxin (thioltransferase) blood, Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. soluble 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 n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P35754
ID GLRX1_HUMAN Reviewed; 106 AA.
AC P35754; B2R4L2; Q3KQS1; Q6ICT1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 140.
DE RecName: Full=Glutaredoxin-1;
DE AltName: Full=Thioltransferase-1;
DE Short=TTase-1;
GN Name=GLRX; Synonyms=GRX;
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].
RC TISSUE=Brain;
RX PubMed=8018729; DOI=10.1016/0167-4781(94)90019-1;
RA Fernando M.R., Sumimoto H., Nanri H., Kawabata S., Iwanaga S.,
RA Minakami S., Fukumaki Y., Takeshige K.;
RT "Cloning and sequencing of the cDNA encoding human glutaredoxin.";
RL Biochim. Biophys. Acta 1218:229-231(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=7851394; DOI=10.1111/j.1432-1033.1995.tb20356.x;
RA Padilla C.A., Martinez-Galisteo E., Barcena J.A., Spyrou G.,
RA Holmgren A.;
RT "Purification from placenta, amino acid sequence, structure
RT comparisons and cDNA cloning of human glutaredoxin.";
RL Eur. J. Biochem. 227:27-34(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8645179;
RA Park J.B., Levine M.;
RT "Purification, cloning and expression of dehydroascorbic acid-reducing
RT activity from human neutrophils: identification as glutaredoxin.";
RL Biochem. J. 315:931-938(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9332366; DOI=10.1016/S0378-1119(97)00262-X;
RA Park J.B., Levine M.;
RT "The human glutaredoxin gene: determination of its organization,
RT transcription start point, and promoter analysis.";
RL Gene 197:189-193(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=11222536;
RA Qiao F., Xing K.Y., Liu A., Ehlers N., Raghavachari N., Lou M.F.;
RT "Human lens thioltransferase: cloning, purification, and function.";
RL Invest. Ophthalmol. Vis. Sci. 42:743-751(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, Skin, and Urinary bladder;
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 [13]
RP PROTEIN SEQUENCE OF 2-106.
RC TISSUE=Blood;
RX PubMed=8019414;
RA Papov V.V., Gravina S.A., Mieyal J.J., Biemann K.;
RT "The primary structure and properties of thioltransferase
RT (glutaredoxin) from human red blood cells.";
RL Protein Sci. 3:428-434(1994).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
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 [16]
RP STRUCTURE BY NMR.
RX PubMed=9677297; DOI=10.1006/jmbi.1998.1913;
RA Sun C., Berardi M.J., Bushweller J.H.;
RT "The NMR solution structure of human glutaredoxin in the fully reduced
RT form.";
RL J. Mol. Biol. 280:687-701(1998).
RN [17]
RP STRUCTURE BY NMR.
RX PubMed=9860827; DOI=10.1021/bi9806504;
RA Yang Y., Jao S.C., Nanduri S., Starke D.W., Mieyal J.J., Qin J.;
RT "Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S,
RT C78S, C82S mutant and NMR solution structure of its glutathionyl mixed
RT disulfide intermediate reflect catalytic specificity.";
RL Biochemistry 37:17145-17156(1998).
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in
CC the presence of NADPH and glutathione reductase. Reduces low
CC molecular weight disulfides and proteins.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glutaredoxin family.
CC -!- SIMILARITY: Contains 1 glutaredoxin domain.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/glrx/";
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DR EMBL; D21238; BAA04769.1; -; mRNA.
DR EMBL; X76648; CAA54094.1; -; mRNA.
DR EMBL; AF069668; AAC35798.1; -; mRNA.
DR EMBL; AF115105; AAC98318.1; -; Genomic_DNA.
DR EMBL; AF115104; AAC98318.1; JOINED; Genomic_DNA.
DR EMBL; AF162769; AAD43353.1; -; mRNA.
DR EMBL; BT006689; AAP35335.1; -; mRNA.
DR EMBL; CR450312; CAG29308.1; -; mRNA.
DR EMBL; CR542165; CAG46962.1; -; mRNA.
DR EMBL; AK311868; BAG34809.1; -; mRNA.
DR EMBL; DQ026062; AAY29058.1; -; Genomic_DNA.
DR EMBL; CH471084; EAW96056.1; -; Genomic_DNA.
DR EMBL; BC005304; AAH05304.1; -; mRNA.
DR EMBL; BC010965; AAH10965.1; -; mRNA.
DR EMBL; BC106075; AAI06076.1; -; mRNA.
DR PIR; S68701; S47472.
DR RefSeq; NP_001112362.1; NM_001118890.1.
DR RefSeq; NP_001230587.1; NM_001243658.1.
DR RefSeq; NP_001230588.1; NM_001243659.1.
DR RefSeq; NP_002055.1; NM_002064.2.
DR UniGene; Hs.28988; -.
DR PDB; 1B4Q; NMR; -; A=2-106.
DR PDB; 1JHB; NMR; -; A=1-106.
DR PDBsum; 1B4Q; -.
DR PDBsum; 1JHB; -.
DR ProteinModelPortal; P35754; -.
DR SMR; P35754; 2-106.
DR IntAct; P35754; 4.
DR MINT; MINT-4649604; -.
DR STRING; 9606.ENSP00000237858; -.
DR DrugBank; DB00143; Glutathione.
DR PhosphoSite; P35754; -.
DR DMDM; 1346143; -.
DR UCD-2DPAGE; P35754; -.
DR PaxDb; P35754; -.
DR PeptideAtlas; P35754; -.
DR PRIDE; P35754; -.
DR DNASU; 2745; -.
DR Ensembl; ENST00000237858; ENSP00000237858; ENSG00000173221.
DR Ensembl; ENST00000379979; ENSP00000369314; ENSG00000173221.
DR Ensembl; ENST00000505427; ENSP00000427353; ENSG00000173221.
DR Ensembl; ENST00000508780; ENSP00000422708; ENSG00000173221.
DR Ensembl; ENST00000512469; ENSP00000424636; ENSG00000173221.
DR GeneID; 2745; -.
DR KEGG; hsa:2745; -.
DR UCSC; uc003kln.4; human.
DR CTD; 2745; -.
DR GeneCards; GC05M095087; -.
DR HGNC; HGNC:4330; GLRX.
DR HPA; CAB008634; -.
DR MIM; 600443; gene.
DR neXtProt; NX_P35754; -.
DR PharmGKB; PA28731; -.
DR eggNOG; COG0695; -.
DR HOGENOM; HOG000095204; -.
DR HOVERGEN; HBG000283; -.
DR InParanoid; P35754; -.
DR KO; K03676; -.
DR OMA; YKFKPGH; -.
DR OrthoDB; EOG7QRQWZ; -.
DR PhylomeDB; P35754; -.
DR BioCyc; MetaCyc:HS04268-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P35754; -.
DR EvolutionaryTrace; P35754; -.
DR GeneWiki; GLRX; -.
DR GenomeRNAi; 2745; -.
DR NextBio; 10820; -.
DR PRO; PR:P35754; -.
DR Bgee; P35754; -.
DR CleanEx; HS_GLRX; -.
DR Genevestigator; P35754; -.
DR GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; TAS:ProtInc.
DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02180; GRX_euk; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Electron transport;
KW Polymorphism; Redox-active center; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 106 Glutaredoxin-1.
FT /FTId=PRO_0000141600.
FT DOMAIN 3 106 Glutaredoxin.
FT MOD_RES 2 2 N-acetylalanine.
FT DISULFID 23 26 Redox-active.
FT DISULFID 79 83
FT VARIANT 47 47 D -> Y (in dbSNP:rs4767).
FT /FTId=VAR_049189.
FT CONFLICT 96 96 L -> V (in Ref. 1; BAA04769).
FT HELIX 4 7
FT STRAND 15 19
FT HELIX 24 35
FT HELIX 40 42
FT STRAND 43 47
FT TURN 48 51
FT HELIX 54 64
FT STRAND 72 75
FT STRAND 78 82
FT HELIX 83 92
FT HELIX 94 102
SQ SEQUENCE 106 AA; 11776 MW; BB86FED55967EBE2 CRC64;
MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA TNHTNEIQDY
LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK QIGALQ
//
ID GLRX1_HUMAN Reviewed; 106 AA.
AC P35754; B2R4L2; Q3KQS1; Q6ICT1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 140.
DE RecName: Full=Glutaredoxin-1;
DE AltName: Full=Thioltransferase-1;
DE Short=TTase-1;
GN Name=GLRX; Synonyms=GRX;
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].
RC TISSUE=Brain;
RX PubMed=8018729; DOI=10.1016/0167-4781(94)90019-1;
RA Fernando M.R., Sumimoto H., Nanri H., Kawabata S., Iwanaga S.,
RA Minakami S., Fukumaki Y., Takeshige K.;
RT "Cloning and sequencing of the cDNA encoding human glutaredoxin.";
RL Biochim. Biophys. Acta 1218:229-231(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Spleen;
RX PubMed=7851394; DOI=10.1111/j.1432-1033.1995.tb20356.x;
RA Padilla C.A., Martinez-Galisteo E., Barcena J.A., Spyrou G.,
RA Holmgren A.;
RT "Purification from placenta, amino acid sequence, structure
RT comparisons and cDNA cloning of human glutaredoxin.";
RL Eur. J. Biochem. 227:27-34(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8645179;
RA Park J.B., Levine M.;
RT "Purification, cloning and expression of dehydroascorbic acid-reducing
RT activity from human neutrophils: identification as glutaredoxin.";
RL Biochem. J. 315:931-938(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9332366; DOI=10.1016/S0378-1119(97)00262-X;
RA Park J.B., Levine M.;
RT "The human glutaredoxin gene: determination of its organization,
RT transcription start point, and promoter analysis.";
RL Gene 197:189-193(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=11222536;
RA Qiao F., Xing K.Y., Liu A., Ehlers N., Raghavachari N., Lou M.F.;
RT "Human lens thioltransferase: cloning, purification, and function.";
RL Invest. Ophthalmol. Vis. Sci. 42:743-751(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA Korn B., Zuo D., Hu Y., LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, Skin, and Urinary bladder;
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 [13]
RP PROTEIN SEQUENCE OF 2-106.
RC TISSUE=Blood;
RX PubMed=8019414;
RA Papov V.V., Gravina S.A., Mieyal J.J., Biemann K.;
RT "The primary structure and properties of thioltransferase
RT (glutaredoxin) from human red blood cells.";
RL Protein Sci. 3:428-434(1994).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
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 [16]
RP STRUCTURE BY NMR.
RX PubMed=9677297; DOI=10.1006/jmbi.1998.1913;
RA Sun C., Berardi M.J., Bushweller J.H.;
RT "The NMR solution structure of human glutaredoxin in the fully reduced
RT form.";
RL J. Mol. Biol. 280:687-701(1998).
RN [17]
RP STRUCTURE BY NMR.
RX PubMed=9860827; DOI=10.1021/bi9806504;
RA Yang Y., Jao S.C., Nanduri S., Starke D.W., Mieyal J.J., Qin J.;
RT "Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S,
RT C78S, C82S mutant and NMR solution structure of its glutathionyl mixed
RT disulfide intermediate reflect catalytic specificity.";
RL Biochemistry 37:17145-17156(1998).
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in
CC the presence of NADPH and glutathione reductase. Reduces low
CC molecular weight disulfides and proteins.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glutaredoxin family.
CC -!- SIMILARITY: Contains 1 glutaredoxin domain.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/glrx/";
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DR EMBL; D21238; BAA04769.1; -; mRNA.
DR EMBL; X76648; CAA54094.1; -; mRNA.
DR EMBL; AF069668; AAC35798.1; -; mRNA.
DR EMBL; AF115105; AAC98318.1; -; Genomic_DNA.
DR EMBL; AF115104; AAC98318.1; JOINED; Genomic_DNA.
DR EMBL; AF162769; AAD43353.1; -; mRNA.
DR EMBL; BT006689; AAP35335.1; -; mRNA.
DR EMBL; CR450312; CAG29308.1; -; mRNA.
DR EMBL; CR542165; CAG46962.1; -; mRNA.
DR EMBL; AK311868; BAG34809.1; -; mRNA.
DR EMBL; DQ026062; AAY29058.1; -; Genomic_DNA.
DR EMBL; CH471084; EAW96056.1; -; Genomic_DNA.
DR EMBL; BC005304; AAH05304.1; -; mRNA.
DR EMBL; BC010965; AAH10965.1; -; mRNA.
DR EMBL; BC106075; AAI06076.1; -; mRNA.
DR PIR; S68701; S47472.
DR RefSeq; NP_001112362.1; NM_001118890.1.
DR RefSeq; NP_001230587.1; NM_001243658.1.
DR RefSeq; NP_001230588.1; NM_001243659.1.
DR RefSeq; NP_002055.1; NM_002064.2.
DR UniGene; Hs.28988; -.
DR PDB; 1B4Q; NMR; -; A=2-106.
DR PDB; 1JHB; NMR; -; A=1-106.
DR PDBsum; 1B4Q; -.
DR PDBsum; 1JHB; -.
DR ProteinModelPortal; P35754; -.
DR SMR; P35754; 2-106.
DR IntAct; P35754; 4.
DR MINT; MINT-4649604; -.
DR STRING; 9606.ENSP00000237858; -.
DR DrugBank; DB00143; Glutathione.
DR PhosphoSite; P35754; -.
DR DMDM; 1346143; -.
DR UCD-2DPAGE; P35754; -.
DR PaxDb; P35754; -.
DR PeptideAtlas; P35754; -.
DR PRIDE; P35754; -.
DR DNASU; 2745; -.
DR Ensembl; ENST00000237858; ENSP00000237858; ENSG00000173221.
DR Ensembl; ENST00000379979; ENSP00000369314; ENSG00000173221.
DR Ensembl; ENST00000505427; ENSP00000427353; ENSG00000173221.
DR Ensembl; ENST00000508780; ENSP00000422708; ENSG00000173221.
DR Ensembl; ENST00000512469; ENSP00000424636; ENSG00000173221.
DR GeneID; 2745; -.
DR KEGG; hsa:2745; -.
DR UCSC; uc003kln.4; human.
DR CTD; 2745; -.
DR GeneCards; GC05M095087; -.
DR HGNC; HGNC:4330; GLRX.
DR HPA; CAB008634; -.
DR MIM; 600443; gene.
DR neXtProt; NX_P35754; -.
DR PharmGKB; PA28731; -.
DR eggNOG; COG0695; -.
DR HOGENOM; HOG000095204; -.
DR HOVERGEN; HBG000283; -.
DR InParanoid; P35754; -.
DR KO; K03676; -.
DR OMA; YKFKPGH; -.
DR OrthoDB; EOG7QRQWZ; -.
DR PhylomeDB; P35754; -.
DR BioCyc; MetaCyc:HS04268-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR SABIO-RK; P35754; -.
DR EvolutionaryTrace; P35754; -.
DR GeneWiki; GLRX; -.
DR GenomeRNAi; 2745; -.
DR NextBio; 10820; -.
DR PRO; PR:P35754; -.
DR Bgee; P35754; -.
DR CleanEx; HS_GLRX; -.
DR Genevestigator; P35754; -.
DR GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; TAS:ProtInc.
DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; TAS:Reactome.
DR Gene3D; 3.40.30.10; -; 1.
DR InterPro; IPR011767; GLR_AS.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011899; Glutaredoxin_euk/vir.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR Pfam; PF00462; Glutaredoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; SSF52833; 1.
DR TIGRFAMs; TIGR02180; GRX_euk; 1.
DR PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; Electron transport;
KW Polymorphism; Redox-active center; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 106 Glutaredoxin-1.
FT /FTId=PRO_0000141600.
FT DOMAIN 3 106 Glutaredoxin.
FT MOD_RES 2 2 N-acetylalanine.
FT DISULFID 23 26 Redox-active.
FT DISULFID 79 83
FT VARIANT 47 47 D -> Y (in dbSNP:rs4767).
FT /FTId=VAR_049189.
FT CONFLICT 96 96 L -> V (in Ref. 1; BAA04769).
FT HELIX 4 7
FT STRAND 15 19
FT HELIX 24 35
FT HELIX 40 42
FT STRAND 43 47
FT TURN 48 51
FT HELIX 54 64
FT STRAND 72 75
FT STRAND 78 82
FT HELIX 83 92
FT HELIX 94 102
SQ SEQUENCE 106 AA; 11776 MW; BB86FED55967EBE2 CRC64;
MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA TNHTNEIQDY
LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK QIGALQ
//
MIM
600443
*RECORD*
*FIELD* NO
600443
*FIELD* TI
*600443 GLUTAREDOXIN; GLRX
;;GRX;;
THIOLTRANSFERASE
*FIELD* TX
CLONING
Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for
read moreribonucleotide reductase and also catalyzes glutathione-disulfide
oxidoreduction reactions in the presence of NADPH and glutathione
reductase. Padilla et al. (1995) purified a human placental glutaredoxin
to homogeneity and showed that its amino acid sequence was similar to
that of other known mammalian glutaredoxins (about 80% identity), with
some important differences. A cDNA that encodes the entire GRX open
reading frame (ORF) and flanking sequences was isolated from a human
spleen cDNA library. Glutaredoxin is a small protein of 12 kD.
MAPPING
Using a genomic clone for fluorescence in situ hybridization, Padilla et
al. (1996) mapped the GLRX gene to 5q14. This localization was in
agreement with that arrived at by somatic cell hybrid analysis.
GENE FUNCTION
Raghavachari et al. (2001) investigated how the expression of
thioltransferase (TTase), a critical thiol repair and dethiolating
enzyme, is regulated in human lens epithelial cells under oxidative
stress. They also examined whether depleting the primary cellular
antioxidant glutathione in these cells has any influence on TTase
expression under the same conditions. They found a transient increase in
TTase mRNA after 5 minutes of H(2)O(2) treatment. Upregulation reached a
maximum of 80% above normal by 10 minutes and gradually decreased as the
cells detoxified the oxidant. They found that manipulation of cellular
GSH resulted in minimal changes in TTase expression. When cells depleted
of GSH were subjected to oxidative stress, TTase expression was also
strongly upregulated. Raghavachari et al. (2001) concluded that the
upregulation of TTase expression in lens epithelial cells could be an
adaptive response of the cells to combat oxidative stress and restore
the vital functions of lens proteins and enzymes. They found that such
regulation was independent of cellular GSH concentration.
*FIELD* RF
1. Padilla, C. A.; Bajalica, S.; Lagercrantz, J.; Holmgren, A.: The
gene for human glutaredoxin (GLRX) is localized to human chromosome
5q14. Genomics 32: 455-457, 1996.
2. Padilla, C. A.; Martinez-Galisteo, E.; Barcena, J. A.; Spyrou,
G.; Holmgren, A.: Purification from placenta, amino acid sequence,
structure comparisons and cDNA cloning of human glutaredoxin. Europ.
J. Biochem. 227: 27-34, 1995.
3. Raghavachari, N.; Krysan, K.; Xing K.; Lou, M. F.: Regulation
of thioltransferase expression in human lens epithelial cells. Invest.
Ophthal. Vis. Sci. 42: 1002-1008, 2001.
*FIELD* CN
Jane Kelly - updated: 6/14/2001
*FIELD* CD
Victor A. McKusick: 3/7/1995
*FIELD* ED
carol: 09/24/2008
mcapotos: 6/19/2001
mcapotos: 6/14/2001
jamie: 2/5/1997
mark: 3/28/1996
terry: 3/27/1996
carol: 3/8/1995
carol: 3/7/1995
*RECORD*
*FIELD* NO
600443
*FIELD* TI
*600443 GLUTAREDOXIN; GLRX
;;GRX;;
THIOLTRANSFERASE
*FIELD* TX
CLONING
Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for
read moreribonucleotide reductase and also catalyzes glutathione-disulfide
oxidoreduction reactions in the presence of NADPH and glutathione
reductase. Padilla et al. (1995) purified a human placental glutaredoxin
to homogeneity and showed that its amino acid sequence was similar to
that of other known mammalian glutaredoxins (about 80% identity), with
some important differences. A cDNA that encodes the entire GRX open
reading frame (ORF) and flanking sequences was isolated from a human
spleen cDNA library. Glutaredoxin is a small protein of 12 kD.
MAPPING
Using a genomic clone for fluorescence in situ hybridization, Padilla et
al. (1996) mapped the GLRX gene to 5q14. This localization was in
agreement with that arrived at by somatic cell hybrid analysis.
GENE FUNCTION
Raghavachari et al. (2001) investigated how the expression of
thioltransferase (TTase), a critical thiol repair and dethiolating
enzyme, is regulated in human lens epithelial cells under oxidative
stress. They also examined whether depleting the primary cellular
antioxidant glutathione in these cells has any influence on TTase
expression under the same conditions. They found a transient increase in
TTase mRNA after 5 minutes of H(2)O(2) treatment. Upregulation reached a
maximum of 80% above normal by 10 minutes and gradually decreased as the
cells detoxified the oxidant. They found that manipulation of cellular
GSH resulted in minimal changes in TTase expression. When cells depleted
of GSH were subjected to oxidative stress, TTase expression was also
strongly upregulated. Raghavachari et al. (2001) concluded that the
upregulation of TTase expression in lens epithelial cells could be an
adaptive response of the cells to combat oxidative stress and restore
the vital functions of lens proteins and enzymes. They found that such
regulation was independent of cellular GSH concentration.
*FIELD* RF
1. Padilla, C. A.; Bajalica, S.; Lagercrantz, J.; Holmgren, A.: The
gene for human glutaredoxin (GLRX) is localized to human chromosome
5q14. Genomics 32: 455-457, 1996.
2. Padilla, C. A.; Martinez-Galisteo, E.; Barcena, J. A.; Spyrou,
G.; Holmgren, A.: Purification from placenta, amino acid sequence,
structure comparisons and cDNA cloning of human glutaredoxin. Europ.
J. Biochem. 227: 27-34, 1995.
3. Raghavachari, N.; Krysan, K.; Xing K.; Lou, M. F.: Regulation
of thioltransferase expression in human lens epithelial cells. Invest.
Ophthal. Vis. Sci. 42: 1002-1008, 2001.
*FIELD* CN
Jane Kelly - updated: 6/14/2001
*FIELD* CD
Victor A. McKusick: 3/7/1995
*FIELD* ED
carol: 09/24/2008
mcapotos: 6/19/2001
mcapotos: 6/14/2001
jamie: 2/5/1997
mark: 3/28/1996
terry: 3/27/1996
carol: 3/8/1995
carol: 3/7/1995