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Protein

Glutathione S-transferase P

Gene

GSTP1

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

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration.1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei8Glutathione7 Publications1
Binding sitei14Glutathione7 Publications1
Binding sitei39Glutathione7 Publications1
Binding sitei45Glutathione7 Publications1

GO - Molecular functioni

  • dinitrosyl-iron complex binding Source: BHF-UCL
  • drug binding Source: Ensembl
  • glutathione binding Source: Ensembl
  • glutathione peroxidase activity Source: BHF-UCL
  • glutathione transferase activity Source: UniProtKB
  • JUN kinase binding Source: BHF-UCL
  • kinase regulator activity Source: BHF-UCL
  • nitric oxide binding Source: BHF-UCL
  • S-nitrosoglutathione binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

BioCyciZFISH:HS01468-MONOMER.
BRENDAi2.5.1.18. 2681.
ReactomeiR-HSA-156590. Glutathione conjugation.
R-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-6798695. Neutrophil degranulation.
SABIO-RKP09211.
SIGNORiP09211.

Chemistry databases

SwissLipidsiSLP:000001615.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase P (EC:2.5.1.18)
Alternative name(s):
GST class-pi
GSTP1-1
Gene namesi
Name:GSTP1
Synonyms:FAEES3, GST3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:4638. GSTP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • intracellular Source: BHF-UCL
  • mitochondrion Source: HPA
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: Ensembl
  • TRAF2-GSTP1 complex Source: BHF-UCL
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi8Y → F: Reduces catalytic activity about 50-fold. 2 Publications1
Mutagenesisi99D → A: Reduces affinity for glutathione. Slightly reduced catalytic activity. 1 Publication1

Organism-specific databases

DisGeNETi2950.
OpenTargetsiENSG00000084207.
PharmGKBiPA29028.

Chemistry databases

ChEMBLiCHEMBL3902.
DrugBankiDB01008. Busulfan.
DB04339. Carbocisteine.
DB00958. Carboplatin.
DB00291. Chlorambucil.
DB00515. Cisplatin.
DB01242. Clomipramine.
DB00773. Etoposide.
DB00143. Glutathione.
DB00526. Oxaliplatin.
DB00163. Vitamin E.

Polymorphism and mutation databases

BioMutaiGSTP1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources5 Publications
ChainiPRO_00001859002 – 210Glutathione S-transferase PAdd BLAST209

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4Phosphotyrosine; by EGFR1 Publication1
Modified residuei62PhosphothreonineCombined sources1
Modified residuei103N6-succinyllysineBy similarity1
Modified residuei116N6-succinyllysineBy similarity1
Modified residuei128N6-acetyllysineCombined sources1
Modified residuei199Phosphotyrosine; by EGFR1 Publication1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP09211.
PaxDbiP09211.
PeptideAtlasiP09211.
PRIDEiP09211.
TopDownProteomicsiP09211.

2D gel databases

DOSAC-COBS-2DPAGEP09211.
OGPiP09211.
REPRODUCTION-2DPAGEIPI00219757.
SWISS-2DPAGEP09211.
UCD-2DPAGEP09211.

PTM databases

iPTMnetiP09211.
PhosphoSitePlusiP09211.
SwissPalmiP09211.

Miscellaneous databases

PMAP-CutDBP09211.

Expressioni

Gene expression databases

BgeeiENSG00000084207.
CleanExiHS_GSTP1.
ExpressionAtlasiP09211. baseline and differential.
GenevisibleiP09211. HS.

Organism-specific databases

HPAiHPA019779.
HPA019869.

Interactioni

Subunit structurei

Homodimer. Interacts with CDK5.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPBP2Q926243EBI-353467,EBI-743771
KRT31Q153235EBI-353467,EBI-948001
KRTAP10-7P604093EBI-353467,EBI-10172290
KRTAP10-9P604113EBI-353467,EBI-10172052
NOTCH2NLQ7Z3S95EBI-353467,EBI-945833
PRDX6P300412EBI-353467,EBI-2255129
TRAF2Q129335EBI-353467,EBI-355744

GO - Molecular functioni

Protein-protein interaction databases

BioGridi109205. 44 interactors.
IntActiP09211. 48 interactors.
MINTiMINT-4998983.
STRINGi9606.ENSP00000381607.

Chemistry databases

BindingDBiP09211.

Structurei

Secondary structure

1210
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 8Combined sources6
Beta strandi10 – 12Combined sources3
Helixi13 – 15Combined sources3
Helixi16 – 24Combined sources9
Beta strandi29 – 33Combined sources5
Helixi36 – 41Combined sources6
Helixi43 – 47Combined sources5
Beta strandi48 – 51Combined sources4
Beta strandi55 – 58Combined sources4
Beta strandi61 – 64Combined sources4
Helixi66 – 76Combined sources11
Helixi84 – 110Combined sources27
Helixi112 – 135Combined sources24
Helixi138 – 140Combined sources3
Beta strandi144 – 148Combined sources5
Helixi151 – 166Combined sources16
Helixi170 – 173Combined sources4
Helixi175 – 185Combined sources11
Helixi188 – 195Combined sources8
Helixi197 – 200Combined sources4
Beta strandi204 – 208Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
10GSX-ray2.20A/B2-210[»]
11GSX-ray2.30A/B1-210[»]
12GSX-ray2.10A/B1-210[»]
13GSX-ray1.90A/B1-210[»]
14GSX-ray2.80A/B1-210[»]
16GSX-ray1.90A/B1-210[»]
17GSX-ray1.90A/B1-210[»]
18GSX-ray1.90A/B1-210[»]
19GSX-ray1.90A/B2-210[»]
1AQVX-ray1.94A/B2-210[»]
1AQWX-ray1.80A/B/C/D2-210[»]
1AQXX-ray2.00A/B/C/D2-210[»]
1EOGX-ray2.10A/B3-210[»]
1EOHX-ray2.50A/B/C/D/E/F/G/H2-210[»]
1GSSX-ray2.80A/B2-210[»]
1KBNX-ray2.00A/B2-210[»]
1LBKX-ray1.86A/B2-203[»]
1MD3X-ray2.03A/B2-210[»]
1MD4X-ray2.10A/B2-210[»]
1PGTX-ray1.80A/B1-210[»]
1PX6X-ray2.10A/B2-210[»]
1PX7X-ray2.03A/B2-210[»]
1ZGNX-ray2.10A/B2-210[»]
20GSX-ray2.45A/B2-210[»]
22GSX-ray1.90A/B1-210[»]
2A2RX-ray1.40A/B1-210[»]
2A2SX-ray1.70A/B1-210[»]
2GSSX-ray1.90A/B2-210[»]
2J9HX-ray2.40A/B2-210[»]
2PGTX-ray1.90A/B1-210[»]
3CSHX-ray1.55A/B2-210[»]
3CSIX-ray1.90A/B/C/D2-210[»]
3CSJX-ray1.90A/B2-210[»]
3DD3X-ray2.25A/B1-210[»]
3DGQX-ray1.60A/B1-210[»]
3GSSX-ray1.90A/B2-210[»]
3GUSX-ray1.53A/B2-210[»]
3HJMX-ray2.10A/B/C/D2-210[»]
3HJOX-ray1.95A/B2-210[»]
3HKRX-ray1.80A/B2-210[»]
3IE3X-ray1.80A/B2-210[»]
3KM6X-ray2.10A/B2-210[»]
3KMNX-ray1.80A/B2-210[»]
3KMOX-ray2.60A/B2-210[»]
3N9JX-ray1.85A/B1-210[»]
3PGTX-ray2.14A/B1-210[»]
4GSSX-ray2.50A/B2-210[»]
4PGTX-ray2.10A/B1-210[»]
5GSSX-ray1.95A/B2-210[»]
5JCWX-ray1.95A/B1-210[»]
6GSSX-ray1.90A/B2-210[»]
7GSSX-ray2.20A/B2-210[»]
8GSSX-ray1.90A/B/C2-210[»]
9GSSX-ray1.97A/B2-210[»]
ProteinModelPortaliP09211.
SMRiP09211.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09211.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 81GST N-terminalAdd BLAST80
Domaini83 – 204GST C-terminalAdd BLAST122

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni52 – 53Glutathione binding7 Publications2
Regioni65 – 66Glutathione binding7 Publications2

Sequence similaritiesi

Belongs to the GST superfamily. Pi family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiKOG1695. Eukaryota.
ENOG4111VAU. LUCA.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115733.
HOVERGENiHBG108324.
InParanoidiP09211.
KOiK00799.
OMAiLRCKYAT.
OrthoDBiEOG091G0K2E.
PhylomeDBiP09211.
TreeFamiTF105321.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01268. GSTRNSFRASEP.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09211-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPYTVVYFP VRGRCAALRM LLADQGQSWK EEVVTVETWQ EGSLKASCLY
60 70 80 90 100
GQLPKFQDGD LTLYQSNTIL RHLGRTLGLY GKDQQEAALV DMVNDGVEDL
110 120 130 140 150
RCKYISLIYT NYEAGKDDYV KALPGQLKPF ETLLSQNQGG KTFIVGDQIS
160 170 180 190 200
FADYNLLDLL LIHEVLAPGC LDAFPLLSAY VGRLSARPKL KAFLASPEYV
210
NLPINGNGKQ
Length:210
Mass (Da):23,356
Last modified:January 23, 2007 - v2
Checksum:i409E33FFAA338396
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti186A → P in CAA30894 (PubMed:3196325).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_014499105I → V in allele GSTP1*B and allele GSTP1*C. 3 PublicationsCorresponds to variant rs1695dbSNPEnsembl.1
Natural variantiVAR_014500114A → V in allele GSTP1*C. 2 PublicationsCorresponds to variant rs1138272dbSNPEnsembl.1
Natural variantiVAR_049493169G → D.Corresponds to variant rs41462048dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06547 mRNA. Translation: CAA29794.1.
M24485 Genomic DNA. Translation: AAA56823.1.
X08058 Genomic DNA. Translation: CAA30847.1.
X08094, X08095, X08096 Genomic DNA. Translation: CAA30894.1.
X15480 mRNA. Translation: CAA33508.1.
U12472 Genomic DNA. Translation: AAA64919.1.
U30897 mRNA. Translation: AAC51280.1.
U62589 mRNA. Translation: AAC51237.1.
U21689 Genomic DNA. Translation: AAC13869.1.
BT019949 mRNA. Translation: AAV38752.1.
BT019950 mRNA. Translation: AAV38753.1.
CR450361 mRNA. Translation: CAG29357.1.
AY324387 Genomic DNA. Translation: AAP72967.1.
BC010915 mRNA. Translation: AAH10915.1.
CCDSiCCDS41679.1.
PIRiA41177.
JS0153. A37378.
RefSeqiNP_000843.1. NM_000852.3.
UniGeneiHs.523836.

Genome annotation databases

EnsembliENST00000398606; ENSP00000381607; ENSG00000084207.
GeneIDi2950.
KEGGihsa:2950.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
SHMPD

The Singapore human mutation and polymorphism database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06547 mRNA. Translation: CAA29794.1.
M24485 Genomic DNA. Translation: AAA56823.1.
X08058 Genomic DNA. Translation: CAA30847.1.
X08094, X08095, X08096 Genomic DNA. Translation: CAA30894.1.
X15480 mRNA. Translation: CAA33508.1.
U12472 Genomic DNA. Translation: AAA64919.1.
U30897 mRNA. Translation: AAC51280.1.
U62589 mRNA. Translation: AAC51237.1.
U21689 Genomic DNA. Translation: AAC13869.1.
BT019949 mRNA. Translation: AAV38752.1.
BT019950 mRNA. Translation: AAV38753.1.
CR450361 mRNA. Translation: CAG29357.1.
AY324387 Genomic DNA. Translation: AAP72967.1.
BC010915 mRNA. Translation: AAH10915.1.
CCDSiCCDS41679.1.
PIRiA41177.
JS0153. A37378.
RefSeqiNP_000843.1. NM_000852.3.
UniGeneiHs.523836.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
10GSX-ray2.20A/B2-210[»]
11GSX-ray2.30A/B1-210[»]
12GSX-ray2.10A/B1-210[»]
13GSX-ray1.90A/B1-210[»]
14GSX-ray2.80A/B1-210[»]
16GSX-ray1.90A/B1-210[»]
17GSX-ray1.90A/B1-210[»]
18GSX-ray1.90A/B1-210[»]
19GSX-ray1.90A/B2-210[»]
1AQVX-ray1.94A/B2-210[»]
1AQWX-ray1.80A/B/C/D2-210[»]
1AQXX-ray2.00A/B/C/D2-210[»]
1EOGX-ray2.10A/B3-210[»]
1EOHX-ray2.50A/B/C/D/E/F/G/H2-210[»]
1GSSX-ray2.80A/B2-210[»]
1KBNX-ray2.00A/B2-210[»]
1LBKX-ray1.86A/B2-203[»]
1MD3X-ray2.03A/B2-210[»]
1MD4X-ray2.10A/B2-210[»]
1PGTX-ray1.80A/B1-210[»]
1PX6X-ray2.10A/B2-210[»]
1PX7X-ray2.03A/B2-210[»]
1ZGNX-ray2.10A/B2-210[»]
20GSX-ray2.45A/B2-210[»]
22GSX-ray1.90A/B1-210[»]
2A2RX-ray1.40A/B1-210[»]
2A2SX-ray1.70A/B1-210[»]
2GSSX-ray1.90A/B2-210[»]
2J9HX-ray2.40A/B2-210[»]
2PGTX-ray1.90A/B1-210[»]
3CSHX-ray1.55A/B2-210[»]
3CSIX-ray1.90A/B/C/D2-210[»]
3CSJX-ray1.90A/B2-210[»]
3DD3X-ray2.25A/B1-210[»]
3DGQX-ray1.60A/B1-210[»]
3GSSX-ray1.90A/B2-210[»]
3GUSX-ray1.53A/B2-210[»]
3HJMX-ray2.10A/B/C/D2-210[»]
3HJOX-ray1.95A/B2-210[»]
3HKRX-ray1.80A/B2-210[»]
3IE3X-ray1.80A/B2-210[»]
3KM6X-ray2.10A/B2-210[»]
3KMNX-ray1.80A/B2-210[»]
3KMOX-ray2.60A/B2-210[»]
3N9JX-ray1.85A/B1-210[»]
3PGTX-ray2.14A/B1-210[»]
4GSSX-ray2.50A/B2-210[»]
4PGTX-ray2.10A/B1-210[»]
5GSSX-ray1.95A/B2-210[»]
5JCWX-ray1.95A/B1-210[»]
6GSSX-ray1.90A/B2-210[»]
7GSSX-ray2.20A/B2-210[»]
8GSSX-ray1.90A/B/C2-210[»]
9GSSX-ray1.97A/B2-210[»]
ProteinModelPortaliP09211.
SMRiP09211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109205. 44 interactors.
IntActiP09211. 48 interactors.
MINTiMINT-4998983.
STRINGi9606.ENSP00000381607.

Chemistry databases

BindingDBiP09211.
ChEMBLiCHEMBL3902.
DrugBankiDB01008. Busulfan.
DB04339. Carbocisteine.
DB00958. Carboplatin.
DB00291. Chlorambucil.
DB00515. Cisplatin.
DB01242. Clomipramine.
DB00773. Etoposide.
DB00143. Glutathione.
DB00526. Oxaliplatin.
DB00163. Vitamin E.
SwissLipidsiSLP:000001615.

PTM databases

iPTMnetiP09211.
PhosphoSitePlusiP09211.
SwissPalmiP09211.

Polymorphism and mutation databases

BioMutaiGSTP1.

2D gel databases

DOSAC-COBS-2DPAGEP09211.
OGPiP09211.
REPRODUCTION-2DPAGEIPI00219757.
SWISS-2DPAGEP09211.
UCD-2DPAGEP09211.

Proteomic databases

EPDiP09211.
PaxDbiP09211.
PeptideAtlasiP09211.
PRIDEiP09211.
TopDownProteomicsiP09211.

Protocols and materials databases

DNASUi2950.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000398606; ENSP00000381607; ENSG00000084207.
GeneIDi2950.
KEGGihsa:2950.

Organism-specific databases

CTDi2950.
DisGeNETi2950.
GeneCardsiGSTP1.
HGNCiHGNC:4638. GSTP1.
HPAiHPA019779.
HPA019869.
MIMi134660. gene.
neXtProtiNX_P09211.
OpenTargetsiENSG00000084207.
PharmGKBiPA29028.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1695. Eukaryota.
ENOG4111VAU. LUCA.
GeneTreeiENSGT00550000074559.
HOGENOMiHOG000115733.
HOVERGENiHBG108324.
InParanoidiP09211.
KOiK00799.
OMAiLRCKYAT.
OrthoDBiEOG091G0K2E.
PhylomeDBiP09211.
TreeFamiTF105321.

Enzyme and pathway databases

BioCyciZFISH:HS01468-MONOMER.
BRENDAi2.5.1.18. 2681.
ReactomeiR-HSA-156590. Glutathione conjugation.
R-HSA-3299685. Detoxification of Reactive Oxygen Species.
R-HSA-6798695. Neutrophil degranulation.
SABIO-RKP09211.
SIGNORiP09211.

Miscellaneous databases

ChiTaRSiGSTP1. human.
EvolutionaryTraceiP09211.
GeneWikiiGSTP1.
GenomeRNAii2950.
PMAP-CutDBP09211.
PROiP09211.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000084207.
CleanExiHS_GSTP1.
ExpressionAtlasiP09211. baseline and differential.
GenevisibleiP09211. HS.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR003082. GST_pi.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01268. GSTRNSFRASEP.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGSTP1_HUMAN
AccessioniPrimary (citable) accession number: P09211
Secondary accession number(s): O00460, Q15690, Q5TZY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 202 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 11
    Human chromosome 11: 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

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.