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Protein

Glutathione peroxidase 1

Gene

GPX1

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

Functioni

Protects the hemoglobin in erythrocytes from oxidative breakdown.

Catalytic activityi

2 glutathione + H2O2 = glutathione disulfide + 2 H2O.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei49 – 491
Sitei49 – 491Subject to oxidation and hydroselenide loss to dehydroalanineBy similarity

GO - Molecular functioni

  • glutathione binding Source: Ensembl
  • glutathione peroxidase activity Source: BHF-UCL
  • phospholipid-hydroperoxide glutathione peroxidase activity Source: Ensembl
  • selenium binding Source: Ensembl
  • SH3 domain binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Enzyme and pathway databases

BioCyciMetaCyc:HS00019-MONOMER.
BRENDAi1.11.1.9. 2681.
ReactomeiREACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_150209. Synthesis of 5-eicosatetraenoic acids.
REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_2086. Purine catabolism.
REACT_264249. Detoxification of Reactive Oxygen Species.

Protein family/group databases

PeroxiBasei3600. HsGPx01-A.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione peroxidase 1 (EC:1.11.1.9)
Short name:
GPx-1
Short name:
GSHPx-1
Alternative name(s):
Cellular glutathione peroxidase
Gene namesi
Name:GPX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:4553. GPX1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: BHF-UCL
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • mitochondrial matrix Source: Reactome
  • mitochondrion Source: BHF-UCL
  • nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

MIMi138320. gene+phenotype.
PharmGKBiPA28949.

Chemistry

DrugBankiDB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiGPX1.
DMDMi311033481.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 203203Glutathione peroxidase 1PRO_0000066610Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881N6-acetyllysine; alternateBy similarity
Modified residuei88 – 881N6-succinyllysine; alternateBy similarity
Modified residuei114 – 1141N6-acetyllysine; alternateBy similarity
Modified residuei114 – 1141N6-succinyllysine; alternateBy similarity
Modified residuei148 – 1481N6-acetyllysine; alternateBy similarity
Modified residuei148 – 1481N6-succinyllysine; alternateBy similarity
Modified residuei201 – 2011Phosphoserine1 Publication

Post-translational modificationi

During periods of oxidative stress, Sec-49 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP07203.
PaxDbiP07203.
PRIDEiP07203.

2D gel databases

OGPiP07203.
SWISS-2DPAGEP07203.

PTM databases

PhosphoSiteiP07203.

Expressioni

Gene expression databases

BgeeiP07203.
CleanExiHS_GPX1.
ExpressionAtlasiP07203. baseline.
GenevisibleiP07203. HS.

Organism-specific databases

HPAiCAB011582.
HPA044758.

Interactioni

Subunit structurei

Homotetramer. Interacts with MIEN1.

Protein-protein interaction databases

BioGridi109134. 8 interactions.
IntActiP07203. 2 interactions.
STRINGi9606.ENSP00000407375.

Structurei

Secondary structure

1
203
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 183Combined sources
Helixi32 – 354Combined sources
Beta strandi38 – 458Combined sources
Beta strandi47 – 493Combined sources
Helixi52 – 6615Combined sources
Helixi67 – 693Combined sources
Beta strandi71 – 777Combined sources
Turni82 – 854Combined sources
Helixi89 – 913Combined sources
Helixi92 – 987Combined sources
Beta strandi108 – 1125Combined sources
Helixi124 – 1329Combined sources
Helixi147 – 1493Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi166 – 1694Combined sources
Beta strandi175 – 1795Combined sources
Helixi185 – 1884Combined sources
Helixi189 – 1968Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F8AX-ray1.50A/B14-198[»]
ProteinModelPortaliP07203.
SMRiP07203. Positions 14-197.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07203.

Family & Domainsi

Sequence similaritiesi

Belongs to the glutathione peroxidase family.Curated

Phylogenomic databases

eggNOGiCOG0386.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP07203.
KOiK00432.
OMAiCEVNGEK.
OrthoDBiEOG7KQ23C.
PhylomeDBiP07203.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P07203-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MCAARLAAAA AAAQSVYAFS ARPLAGGEPV SLGSLRGKVL LIENVASLUG
60 70 80 90 100
TTVRDYTQMN ELQRRLGPRG LVVLGFPCNQ FGHQENAKNE EILNSLKYVR
110 120 130 140 150
PGGGFEPNFM LFEKCEVNGA GAHPLFAFLR EALPAPSDDA TALMTDPKLI
160 170 180 190 200
TWSPVCRNDV AWNFEKFLVG PDGVPLRRYS RRFQTIDIEP DIEALLSQGP

SCA
Length:203
Mass (Da):22,088
Last modified:November 2, 2010 - v4
Checksum:i5DB11579C66FE8E5
GO
Isoform 2 (identifier: P07203-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     85-98: ENAKNEEILNSLKY → VRRAERGGAGADVQ
     99-203: Missing.

Note: Gene prediction based on EST data.
Show »
Length:98
Mass (Da):10,289
Checksum:i9AD713E53537E4A0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti93 – 931L → Q in CAA31992 (PubMed:2955287).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51R → P.1 Publication
Corresponds to variant rs8179169 [ dbSNP | Ensembl ].
VAR_020912
Natural varianti7 – 82Missing .5 Publications
VAR_020913
Natural varianti8 – 81Missing .3 Publications
VAR_020914
Natural varianti194 – 1941A → T.1 Publication
Corresponds to variant rs6446261 [ dbSNP | Ensembl ].
VAR_020915
Natural varianti200 – 2001P → L Frequent polymorphism. 4 Publications
Corresponds to variant rs1050450 [ dbSNP | Ensembl ].
VAR_007904

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei85 – 9814ENAKN…NSLKY → VRRAERGGAGADVQ in isoform 2. CuratedVSP_047369Add
BLAST
Alternative sequencei99 – 203105Missing in isoform 2. CuratedVSP_047370Add
BLAST

Non-standard residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-standard residuei49 – 491Selenocysteine

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00433 mRNA. Translation: CAA68491.1.
Y00483 Genomic DNA. Translation: CAB37833.1.
X13709 mRNA. Translation: CAA31992.1.
X13710 mRNA. Translation: CAA31993.1.
M21304 mRNA. Translation: AAA75389.2.
M83094 Genomic DNA. Translation: AAA67540.2.
AY327818 Genomic DNA. Translation: AAP80181.1.
AC121247 Genomic DNA. No translation available.
BC000742 mRNA. Translation: AAH00742.3.
CCDSiCCDS43091.1. [P07203-1]
CCDS54582.1. [P07203-2]
PIRiA42152. OPHUE.
RefSeqiNP_000572.2. NM_000581.2. [P07203-1]
NP_958799.1. NM_201397.1. [P07203-2]
UniGeneiHs.76686.

Genome annotation databases

EnsembliENST00000419349; ENSP00000391316; ENSG00000233276. [P07203-2]
ENST00000419783; ENSP00000407375; ENSG00000233276.
GeneIDi2876.
KEGGihsa:2876.
UCSCiuc021wxw.1. human. [P07203-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Selenocysteine

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

Glutathione peroxidase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00433 mRNA. Translation: CAA68491.1.
Y00483 Genomic DNA. Translation: CAB37833.1.
X13709 mRNA. Translation: CAA31992.1.
X13710 mRNA. Translation: CAA31993.1.
M21304 mRNA. Translation: AAA75389.2.
M83094 Genomic DNA. Translation: AAA67540.2.
AY327818 Genomic DNA. Translation: AAP80181.1.
AC121247 Genomic DNA. No translation available.
BC000742 mRNA. Translation: AAH00742.3.
CCDSiCCDS43091.1. [P07203-1]
CCDS54582.1. [P07203-2]
PIRiA42152. OPHUE.
RefSeqiNP_000572.2. NM_000581.2. [P07203-1]
NP_958799.1. NM_201397.1. [P07203-2]
UniGeneiHs.76686.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F8AX-ray1.50A/B14-198[»]
ProteinModelPortaliP07203.
SMRiP07203. Positions 14-197.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109134. 8 interactions.
IntActiP07203. 2 interactions.
STRINGi9606.ENSP00000407375.

Chemistry

ChEMBLiCHEMBL2163186.
DrugBankiDB00143. Glutathione.

Protein family/group databases

PeroxiBasei3600. HsGPx01-A.

PTM databases

PhosphoSiteiP07203.

Polymorphism and mutation databases

BioMutaiGPX1.
DMDMi311033481.

2D gel databases

OGPiP07203.
SWISS-2DPAGEP07203.

Proteomic databases

MaxQBiP07203.
PaxDbiP07203.
PRIDEiP07203.

Protocols and materials databases

DNASUi2876.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000419349; ENSP00000391316; ENSG00000233276. [P07203-2]
ENST00000419783; ENSP00000407375; ENSG00000233276.
GeneIDi2876.
KEGGihsa:2876.
UCSCiuc021wxw.1. human. [P07203-1]

Organism-specific databases

CTDi2876.
GeneCardsiGC03M049369.
H-InvDBHIX0003298.
HGNCiHGNC:4553. GPX1.
HPAiCAB011582.
HPA044758.
MIMi138320. gene+phenotype.
neXtProtiNX_P07203.
PharmGKBiPA28949.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0386.
GeneTreeiENSGT00760000119230.
HOGENOMiHOG000277055.
HOVERGENiHBG004333.
InParanoidiP07203.
KOiK00432.
OMAiCEVNGEK.
OrthoDBiEOG7KQ23C.
PhylomeDBiP07203.
TreeFamiTF105318.

Enzyme and pathway databases

BioCyciMetaCyc:HS00019-MONOMER.
BRENDAi1.11.1.9. 2681.
ReactomeiREACT_150201. Synthesis of 12-eicosatetraenoic acid derivatives.
REACT_150209. Synthesis of 5-eicosatetraenoic acids.
REACT_150422. Synthesis of 15-eicosatetraenoic acid derivatives.
REACT_2086. Purine catabolism.
REACT_264249. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiGPX1. human.
EvolutionaryTraceiP07203.
GeneWikiiGPX1.
GenomeRNAii2876.
NextBioi11353.
PROiP07203.
SOURCEiSearch...

Gene expression databases

BgeeiP07203.
CleanExiHS_GPX1.
ExpressionAtlasiP07203. baseline.
GenevisibleiP07203. HS.

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. "cDNA sequence coding for human glutathione peroxidase."
    Sukenaga Y., Ishida K., Takeda T., Takagi K.
    Nucleic Acids Res. 15:7178-7178(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 7-ALA-ALA-8 DEL.
  2. "Nucleotide sequence of a human gene for glutathione peroxidase."
    Ishida K., Morino T., Takagi K., Sukenaga Y.
    Nucleic Acids Res. 15:10051-10051(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT 7-ALA-ALA-8 DEL.
  3. "Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine."
    Mullenbach G.T., Tabrizi A., Irvine B.D., Bell G.I., Hallewell R.A.
    Nucleic Acids Res. 15:5484-5484(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 7-ALA-ALA-8 DEL.
    Tissue: Kidney.
  4. "Isolation and chromosomal localization of the human glutathione peroxidase gene."
    Chada S., le Beau M.M., Casey L., Newburger P.E.
    Genomics 6:268-271(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT 7-ALA-ALA-8 DEL.
  5. "Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1)."
    Moscow J.A., Morrow C.S., He R., Mullenbach G.T., Cowan K.H.
    J. Biol. Chem. 267:5949-5958(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT ALA-8 DEL.
  6. NIEHS SNPs program
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS PRO-5; THR-194 AND LEU-200.
  7. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Placenta.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Crystal structure of the selenocysteine to glycine mutant of human glutathione peroxidase 1."
    Structural genomics consortium (SGC)
    Submitted (FEB-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 14-198.
  12. "Low yield of polymorphisms from EST blast searching: analysis of genes related to oxidative stress and verification of the P197L polymorphism in GPX1."
    Forsberg L., de Faire U., Morgenstern R.
    Hum. Mutat. 13:294-300(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-200.
  13. "Association between the GCG polymorphism of the selenium dependent GPX1 gene and the risk of young onset prostate cancer."
    Kote-Jarai Z., Durocher F., Edwards S.M., Hamoudi R., Jackson R.A., Ardern-Jones A., Murkin A., Dearnaley D.P., Kirby R., Houlston R., Easton D.F., Eeles R.
    Prostate Cancer Prostatic Dis. 5:189-192(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ALA-8 DEL AND 7-ALA-ALA-8 DEL.
  14. "Functional variants in the glutathione peroxidase-1 (GPx-1) gene are associated with increased intima-media thickness of carotid arteries and risk of macrovascular diseases in Japanese type 2 diabetic patients."
    Hamanishi T., Furuta H., Kato H., Doi A., Tamai M., Shimomura H., Sakagashira S., Nishi M., Sasaki H., Sanke T., Nanjo K.
    Diabetes 53:2455-2460(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ALA-8 DEL AND LEU-200.
  15. "Increased risk of bladder cancer associated with a glutathione peroxidase 1 codon 198 variant."
    Ichimura Y., Habuchi T., Tsuchiya N., Wang L., Oyama C., Sato K., Nishiyama H., Ogawa O., Kato T.
    J. Urol. 172:728-732(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LEU-200.

Entry informationi

Entry nameiGPX1_HUMAN
AccessioniPrimary (citable) accession number: P07203
Secondary accession number(s): E9PAS1, Q7Z5H1, Q9BW12
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: November 2, 2010
Last modified: July 22, 2015
This is version 181 of the entry and version 4 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, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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.