Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glutathione peroxidase 6

Gene

GPX6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

BRENDAi1.11.1.9. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei3605. HsGPx06.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase 6 (EC:1.11.1.9)
Short name:
GPx-6
Short name:
GSHPx-6
Gene namesi
Name:GPX6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:4558. GPX6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28954.

Chemistry

DrugBankiDB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiGPX6.
DMDMi187692196.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence analysisAdd
BLAST
Chaini20 – 221202Glutathione peroxidase 6PRO_0000013081Add
BLAST

Proteomic databases

EPDiP59796.
PaxDbiP59796.
PeptideAtlasiP59796.
PRIDEiP59796.

Expressioni

Tissue specificityi

Expressed in olfactory epithelium and embryos.1 Publication

Gene expression databases

BgeeiP59796.
CleanExiHS_GPX6.
ExpressionAtlasiP59796. baseline and differential.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000354581.

Structurei

3D structure databases

ProteinModelPortaliP59796.
SMRiP59796. Positions 38-217.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP59796.
KOiK00432.
OMAiFQQYAGK.
OrthoDBiEOG7KQ23C.
PhylomeDBiP59796.
TreeFamiTF105318.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P59796-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFQQFQASCL VLFFLVGFAQ QTLKPQNRKV DCNKGVTGTI YEYGALTLNG
60 70 80 90 100
EEYIQFKQFA GKHVLFVNVA AYUGLAAQYP ELNALQEELK NFGVIVLAFP
110 120 130 140 150
CNQFGKQEPG TNSEILLGLK YVCPGSGFVP SFQLFEKGDV NGEKEQKVFT
160 170 180 190 200
FLKNSCPPTS DLLGSSSQLF WEPMKVHDIR WNFEKFLVGP DGVPVMHWFH
210 220
QAPVSTVKSD ILEYLKQFNT H
Length:221
Mass (Da):24,971
Last modified:February 26, 2008 - v2
Checksum:iE9B48AF5F17C3FDD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61Q → L.1 Publication
Corresponds to variant rs35510314 [ dbSNP | Ensembl ].
VAR_025249
Natural varianti13 – 131F → L.1 Publication
Corresponds to variant rs406113 [ dbSNP | Ensembl ].
VAR_025250
Natural varianti53 – 531Y → H.1 Publication
Corresponds to variant rs34825130 [ dbSNP | Ensembl ].
VAR_025251
Natural varianti58 – 581Q → H.1 Publication
Corresponds to variant rs6922986 [ dbSNP | Ensembl ].
VAR_025252
Natural varianti72 – 721Y → N.1 Publication
Corresponds to variant rs35062161 [ dbSNP | Ensembl ].
VAR_025253
Natural varianti136 – 1361E → D.1 Publication
Corresponds to variant rs35394555 [ dbSNP | Ensembl ].
VAR_025254
Natural varianti140 – 1401V → M.1 Publication
Corresponds to variant rs36055795 [ dbSNP | Ensembl ].
VAR_025255
Natural varianti157 – 1571P → S.1 Publication
Corresponds to variant rs35658392 [ dbSNP | Ensembl ].
VAR_025256
Natural varianti161 – 1611D → G.1 Publication
Corresponds to variant rs34955392 [ dbSNP | Ensembl ].
VAR_025257
Natural varianti188 – 1881V → A.1 Publication
Corresponds to variant rs35701070 [ dbSNP | Ensembl ].
VAR_025258

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei73 – 731Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY324826 mRNA. Translation: AAP85543.1.
DQ088982 Genomic DNA. Translation: AAY68223.1.
AL049543 Genomic DNA. No translation available.
Z98745 Genomic DNA. No translation available.
CCDSiCCDS43432.1.
RefSeqiNP_874360.1. NM_182701.1.
UniGeneiHs.448570.

Genome annotation databases

EnsembliENST00000361902; ENSP00000354581; ENSG00000198704.
GeneIDi257202.
KEGGihsa:257202.
UCSCiuc021yrx.1. human.

Keywords - Coding sequence diversityi

Polymorphism, Selenocysteine

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY324826 mRNA. Translation: AAP85543.1.
DQ088982 Genomic DNA. Translation: AAY68223.1.
AL049543 Genomic DNA. No translation available.
Z98745 Genomic DNA. No translation available.
CCDSiCCDS43432.1.
RefSeqiNP_874360.1. NM_182701.1.
UniGeneiHs.448570.

3D structure databases

ProteinModelPortaliP59796.
SMRiP59796. Positions 38-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000354581.

Chemistry

DrugBankiDB00143. Glutathione.

Protein family/group databases

PeroxiBasei3605. HsGPx06.

Polymorphism and mutation databases

BioMutaiGPX6.
DMDMi187692196.

Proteomic databases

EPDiP59796.
PaxDbiP59796.
PeptideAtlasiP59796.
PRIDEiP59796.

Protocols and materials databases

DNASUi257202.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361902; ENSP00000354581; ENSG00000198704.
GeneIDi257202.
KEGGihsa:257202.
UCSCiuc021yrx.1. human.

Organism-specific databases

CTDi257202.
GeneCardsiGPX6.
H-InvDBHIX0032860.
HGNCiHGNC:4558. GPX6.
MIMi607913. gene.
neXtProtiNX_P59796.
PharmGKBiPA28954.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1651. Eukaryota.
COG0386. LUCA.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP59796.
KOiK00432.
OMAiFQQYAGK.
OrthoDBiEOG7KQ23C.
PhylomeDBiP59796.
TreeFamiTF105318.

Enzyme and pathway databases

BRENDAi1.11.1.9. 2681.
ReactomeiR-HSA-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

GeneWikiiGPX6.
GenomeRNAii257202.
PROiP59796.
SOURCEiSearch...

Gene expression databases

BgeeiP59796.
CleanExiHS_GPX6.
ExpressionAtlasiP59796. baseline and differential.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR000889. Glutathione_peroxidase.
IPR029759. GPX_AS.
IPR029760. GPX_CS.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PANTHERiPTHR11592. PTHR11592. 1 hit.
PfamiPF00255. GSHPx. 1 hit.
[Graphical view]
PIRSFiPIRSF000303. Glutathion_perox. 1 hit.
PRINTSiPR01011. GLUTPROXDASE.
SUPFAMiSSF52833. SSF52833. 1 hit.
PROSITEiPS00460. GLUTATHIONE_PEROXID_1. 1 hit.
PS00763. GLUTATHIONE_PEROXID_2. 1 hit.
PS51355. GLUTATHIONE_PEROXID_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. NIEHS SNPs program
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-6; LEU-13; HIS-53; HIS-58; ASN-72; ASP-136; MET-140; SER-157; GLY-161 AND ALA-188.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiGPX6_HUMAN
AccessioniPrimary (citable) accession number: P59796
Secondary accession number(s): Q4PJ17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: February 26, 2008
Last modified: July 6, 2016
This is version 108 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.