Glutaredoxin-1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P35754 (GLRX1_HUMAN)

Last modified July 7, 2009. Version 94. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Glutaredoxin-1
Alternative name(s):
    Thioltransferase-1
      Short name=TTase-1

Gene names

Name:	GLRX
Synonyms:	GRX

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	106 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function

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

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the glutaredoxin family.

Contains 1 glutaredoxin domain.

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Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Redox-active center
PTM	Acetylation Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Traceable author statement. Source: UniProtKB
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro glutathione disulfide oxidoreductase activity Ref.2 Traceable author statement. Source: ProtInc protein N-terminus binding Inferred from physical interaction. Source: UniProtKB protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.11

Chain

2 – 106

105

Glutaredoxin-1

PRO_0000141600

Regions

Domain

3 – 106

104

Glutaredoxin

Amino acid modifications

Modified residue

N-acetylalanine

Disulfide bond

23 ↔ 26

Redox-active

Disulfide bond

79 ↔ 83

Natural variations

Natural variant

D → Y: dbSNP rs4767.

VAR_049189

Experimental info

Sequence conflict

L → V in BAA04769. Ref.1

Secondary structure

106

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P35754-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: BB86FED55967EBE2
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FASTA

106

11,776

        10         20         30         40         50         60 
MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA TNHTNEIQDY 

        70         80         90        100 
LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK QIGALQ

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of the cDNA encoding human glutaredoxin." Fernando M.R., Sumimoto H., Nanri H., Kawabata S., Iwanaga S., Minakami S., Fukumaki Y., Takeshige K. Biochim. Biophys. Acta 1218:229-231(1994) [PubMed: 8018729] [Abstract] 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: 7851394] [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: 8645179] [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: 9332366] [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: 11222536] [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]	NIEHS SNPs program Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver, Skin and Urinary bladder.
[11]	"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: 8019414] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-106. Tissue: Blood.
[12]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	"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: 9677297] [Abstract] Cited for: STRUCTURE BY NMR.
[14]	"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: 9860827] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

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Web resources

NIEHS-SNPs

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Cross-references

Sequence databases

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.
DQ026062 Genomic DNA. Translation: AAY29058.1.
BC005304 mRNA. Translation: AAH05304.1.
BC010965 mRNA. Translation: AAH10965.1.
BC106075 mRNA. Translation: AAI06076.1.

IPI

IPI00219025.

PIR

S47472. S68701.

RefSeq

NP_001112362.1.
NP_002055.1.

UniGene

Hs.28988
Hs.712696

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B4Q	NMR	-	A	2-106	[»]
1JHB	NMR	-	A	1-106	[»]

ModBase

Search...

Proteomic databases

PeptideAtlas

P35754.

PRIDE

P35754.

Genome annotation databases

Ensembl

ENSG00000173221. Homo sapiens. [Contig view]

GeneID

2745.

KEGG

hsa:2745.

UCSC

uc003kln.2. human.

Organism-specific databases

GeneCards

GC05M095175.

H-InvDB

HIX0005047.

HGNC

HGNC:4330. GLRX.

HPA

CAB008634.

MIM

600443. gene.

PharmGKB

PA28731.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P35754.

HOVERGEN

P35754.

OMA

P35754. GGCSDLI.

Enzyme and pathway databases

Reactome

REACT_1698. Metablism of nucleotides.

Gene expression databases

ArrayExpress

P35754.

Bgee

P35754.

CleanEx

HS_GLRX.

GermOnline

ENSG00000173221. Homo sapiens.

Family and domain databases

InterPro

IPR011767. GLR_AS.
IPR002109. Glutaredoxin.
IPR014025. Glutaredoxin_sub.
IPR011899. GRX_euk.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

Pfam

PF00462. Glutaredoxin. 1 hit.
[Graphical view]

PRINTS

PR00160. GLUTAREDOXIN.

TIGRFAMs

TIGR02180. GRX_euk. 1 hit.

PROSITE

PS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00143. Glutathione.

NextBio

10820.

SOURCE

Search...

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Entry information

Entry name

GLRX1_HUMAN

Accession

Primary (citable) accession number: P35754
Secondary accession number(s): Q3KQS1, Q6ICT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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