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Protein

Glutaredoxin-1

Gene

GLRX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.

GO - Molecular functioni

  1. electron carrier activity Source: InterPro
  2. glutathione disulfide oxidoreductase activity Source: ProtInc
  3. glutathione oxidoreductase activity Source: BHF-UCL
  4. protein N-terminus binding Source: UniProtKB

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. nucleobase-containing small molecule interconversion Source: Reactome
  3. nucleobase-containing small molecule metabolic process Source: Reactome
  4. positive regulation of membrane potential Source: BHF-UCL
  5. positive regulation of sodium ion transmembrane transporter activity Source: BHF-UCL
  6. protein deglutathionylation Source: BHF-UCL
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Electron transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:HS04268-MONOMER.
ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKP35754.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutaredoxin-1
Alternative name(s):
Thioltransferase-1
Short name:
TTase-1
Gene namesi
Name:GLRX
Synonyms:GRX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:4330. GLRX.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. mitochondrion Source: Ensembl
  4. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28731.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 106105Glutaredoxin-1PRO_0000141600Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei9 – 91N6-succinyllysineBy similarity
Disulfide bondi23 ↔ 26Redox-active
Disulfide bondi79 ↔ 83

Keywords - PTMi

Acetylation, Disulfide bond

Proteomic databases

MaxQBiP35754.
PaxDbiP35754.
PeptideAtlasiP35754.
PRIDEiP35754.

2D gel databases

UCD-2DPAGEP35754.

PTM databases

PhosphoSiteiP35754.

Expressioni

Gene expression databases

BgeeiP35754.
CleanExiHS_GLRX.
ExpressionAtlasiP35754. baseline and differential.
GenevestigatoriP35754.

Organism-specific databases

HPAiCAB008634.

Interactioni

Protein-protein interaction databases

BioGridi109007. 9 interactions.
IntActiP35754. 4 interactions.
MINTiMINT-4649604.
STRINGi9606.ENSP00000237858.

Structurei

Secondary structure

1
106
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 74Combined sources
Beta strandi15 – 195Combined sources
Helixi24 – 3512Combined sources
Helixi40 – 423Combined sources
Beta strandi43 – 475Combined sources
Turni48 – 514Combined sources
Helixi54 – 6411Combined sources
Beta strandi72 – 754Combined sources
Beta strandi78 – 825Combined sources
Helixi83 – 9210Combined sources
Helixi94 – 1029Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4QNMR-A2-106[»]
1JHBNMR-A1-106[»]
ProteinModelPortaliP35754.
SMRiP35754. Positions 2-106.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35754.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 106104GlutaredoxinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glutaredoxin family.Curated
Contains 1 glutaredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiCOG0695.
GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
HOVERGENiHBG000283.
InParanoidiP35754.
KOiK03676.
OMAiVFIGEEC.
OrthoDBiEOG7QRQWZ.
PhylomeDBiP35754.
TreeFamiTF326994.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35754-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA
60 70 80 90 100
TNHTNEIQDY LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK

QIGALQ
Length:106
Mass (Da):11,776
Last modified:January 23, 2007 - v2
Checksum:iBB86FED55967EBE2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti96 – 961L → V in BAA04769 (PubMed:8018729).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti47 – 471D → Y.
Corresponds to variant rs4767 [ dbSNP | Ensembl ].
VAR_049189

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21238 mRNA. Translation: BAA04769.1.
X76648 mRNA. Translation: CAA54094.1.
AF069668 mRNA. Translation: AAC35798.1.
AF115105, AF115104 Genomic DNA. Translation: AAC98318.1.
AF162769 mRNA. Translation: AAD43353.1.
BT006689 mRNA. Translation: AAP35335.1.
CR450312 mRNA. Translation: CAG29308.1.
CR542165 mRNA. Translation: CAG46962.1.
AK311868 mRNA. Translation: BAG34809.1.
DQ026062 Genomic DNA. Translation: AAY29058.1.
CH471084 Genomic DNA. Translation: EAW96056.1.
BC005304 mRNA. Translation: AAH05304.1.
BC010965 mRNA. Translation: AAH10965.1.
BC106075 mRNA. Translation: AAI06076.1.
CCDSiCCDS4078.1.
PIRiS68701. S47472.
RefSeqiNP_001112362.1. NM_001118890.1.
NP_001230587.1. NM_001243658.1.
NP_001230588.1. NM_001243659.1.
NP_002055.1. NM_002064.2.
UniGeneiHs.28988.

Genome annotation databases

EnsembliENST00000237858; ENSP00000237858; ENSG00000173221.
ENST00000379979; ENSP00000369314; ENSG00000173221.
ENST00000505427; ENSP00000427353; ENSG00000173221.
ENST00000508780; ENSP00000422708; ENSG00000173221.
ENST00000512469; ENSP00000424636; ENSG00000173221.
GeneIDi2745.
KEGGihsa:2745.
UCSCiuc003kln.4. human.

Polymorphism databases

DMDMi1346143.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21238 mRNA. Translation: BAA04769.1.
X76648 mRNA. Translation: CAA54094.1.
AF069668 mRNA. Translation: AAC35798.1.
AF115105, AF115104 Genomic DNA. Translation: AAC98318.1.
AF162769 mRNA. Translation: AAD43353.1.
BT006689 mRNA. Translation: AAP35335.1.
CR450312 mRNA. Translation: CAG29308.1.
CR542165 mRNA. Translation: CAG46962.1.
AK311868 mRNA. Translation: BAG34809.1.
DQ026062 Genomic DNA. Translation: AAY29058.1.
CH471084 Genomic DNA. Translation: EAW96056.1.
BC005304 mRNA. Translation: AAH05304.1.
BC010965 mRNA. Translation: AAH10965.1.
BC106075 mRNA. Translation: AAI06076.1.
CCDSiCCDS4078.1.
PIRiS68701. S47472.
RefSeqiNP_001112362.1. NM_001118890.1.
NP_001230587.1. NM_001243658.1.
NP_001230588.1. NM_001243659.1.
NP_002055.1. NM_002064.2.
UniGeneiHs.28988.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4QNMR-A2-106[»]
1JHBNMR-A1-106[»]
ProteinModelPortaliP35754.
SMRiP35754. Positions 2-106.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109007. 9 interactions.
IntActiP35754. 4 interactions.
MINTiMINT-4649604.
STRINGi9606.ENSP00000237858.

Chemistry

DrugBankiDB00143. Glutathione.

PTM databases

PhosphoSiteiP35754.

Polymorphism databases

DMDMi1346143.

2D gel databases

UCD-2DPAGEP35754.

Proteomic databases

MaxQBiP35754.
PaxDbiP35754.
PeptideAtlasiP35754.
PRIDEiP35754.

Protocols and materials databases

DNASUi2745.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000237858; ENSP00000237858; ENSG00000173221.
ENST00000379979; ENSP00000369314; ENSG00000173221.
ENST00000505427; ENSP00000427353; ENSG00000173221.
ENST00000508780; ENSP00000422708; ENSG00000173221.
ENST00000512469; ENSP00000424636; ENSG00000173221.
GeneIDi2745.
KEGGihsa:2745.
UCSCiuc003kln.4. human.

Organism-specific databases

CTDi2745.
GeneCardsiGC05M095087.
HGNCiHGNC:4330. GLRX.
HPAiCAB008634.
MIMi600443. gene.
neXtProtiNX_P35754.
PharmGKBiPA28731.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0695.
GeneTreeiENSGT00390000003677.
HOGENOMiHOG000095204.
HOVERGENiHBG000283.
InParanoidiP35754.
KOiK03676.
OMAiVFIGEEC.
OrthoDBiEOG7QRQWZ.
PhylomeDBiP35754.
TreeFamiTF326994.

Enzyme and pathway databases

BioCyciMetaCyc:HS04268-MONOMER.
ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
SABIO-RKP35754.

Miscellaneous databases

ChiTaRSiGLRX. human.
EvolutionaryTraceiP35754.
GeneWikiiGLRX.
GenomeRNAii2745.
NextBioi10820.
PROiP35754.
SOURCEiSearch...

Gene expression databases

BgeeiP35754.
CleanExiHS_GLRX.
ExpressionAtlasiP35754. baseline and differential.
GenevestigatoriP35754.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR011899. Glutaredoxin_euk/vir.
IPR014025. Glutaredoxin_subgr.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00462. Glutaredoxin. 1 hit.
[Graphical view]
PRINTSiPR00160. GLUTAREDOXIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
TIGRFAMsiTIGR02180. GRX_euk. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin."
    Padilla C.A., Martinez-Galisteo E., Barcena J.A., Spyrou G., Holmgren A.
    Eur. J. Biochem. 227:27-34(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Spleen.
  3. "Purification, cloning and expression of dehydroascorbic acid-reducing activity from human neutrophils: identification as glutaredoxin."
    Park J.B., Levine M.
    Biochem. J. 315:931-938(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  4. "The human glutaredoxin gene: determination of its organization, transcription start point, and promoter analysis."
    Park J.B., Levine M.
    Gene 197:189-193(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Human lens thioltransferase: cloning, purification, and function."
    Qiao F., Xing K.Y., Liu A., Ehlers N., Raghavachari N., Lou M.F.
    Invest. Ophthalmol. Vis. Sci. 42:743-751(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lens.
  6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  10. NIEHS SNPs program
    Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver, Skin and Urinary bladder.
  13. "The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells."
    Papov V.V., Gravina S.A., Mieyal J.J., Biemann K.
    Protein Sci. 3:428-434(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-106.
    Tissue: Blood.
  14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "The NMR solution structure of human glutaredoxin in the fully reduced form."
    Sun C., Berardi M.J., Bushweller J.H.
    J. Mol. Biol. 280:687-701(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  18. "Reactivity of the human thioltransferase (glutaredoxin) C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity."
    Yang Y., Jao S.C., Nanduri S., Starke D.W., Mieyal J.J., Qin J.
    Biochemistry 37:17145-17156(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiGLRX1_HUMAN
AccessioniPrimary (citable) accession number: P35754
Secondary accession number(s): B2R4L2, Q3KQS1, Q6ICT1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.