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Protein

Target of rapamycin complex subunit LST8

Gene

MLST8

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

Functioni

Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, LST8 interacts directly with MTOR and enhances its kinase activity. In nutrient-poor conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR-mediated inhibition of MTOR activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'.2 Publications

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000167965-MONOMER.
ReactomeiR-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1632852. Macroautophagy.
R-HSA-165159. mTOR signalling.
R-HSA-166208. mTORC1-mediated signalling.
R-HSA-3371571. HSF1-dependent transactivation.
R-HSA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-HSA-389357. CD28 dependent PI3K/Akt signaling.
R-HSA-5218920. VEGFR2 mediated vascular permeability.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-5674400. Constitutive Signaling by AKT1 E17K in Cancer.
R-HSA-6804757. Regulation of TP53 Degradation.
SignaLinkiQ9BVC4.
SIGNORiQ9BVC4.

Names & Taxonomyi

Protein namesi
Recommended name:
Target of rapamycin complex subunit LST8
Short name:
TORC subunit LST8
Alternative name(s):
G protein beta subunit-like
Short name:
Gable
Short name:
Protein GbetaL
Mammalian lethal with SEC13 protein 8
Short name:
mLST8
Gene namesi
Name:MLST8
Synonyms:GBL, LST8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:24825. MLST8.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • TORC1 complex Source: UniProtKB
  • TORC2 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi72S → D: Impairs interaction with MTOR. 1 Publication1
Mutagenesisi192G → D: Abolishes interaction with MTOR. 1 Publication1
Mutagenesisi320F → S: Impairs interaction with MTOR. 1 Publication1

Organism-specific databases

DisGeNETi64223.
OpenTargetsiENSG00000167965.
PharmGKBiPA165450213.

Polymorphism and mutation databases

BioMutaiMLST8.
DMDMi74761285.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003264991 – 326Target of rapamycin complex subunit LST8Add BLAST326

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Isoform 3 (identifier: Q9BVC4-4)
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei7PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9BVC4.
MaxQBiQ9BVC4.
PaxDbiQ9BVC4.
PeptideAtlasiQ9BVC4.
PRIDEiQ9BVC4.

PTM databases

iPTMnetiQ9BVC4.
PhosphoSitePlusiQ9BVC4.

Expressioni

Tissue specificityi

Broadly expressed, with highest levels in skeletal muscle, heart and kidney.1 Publication

Gene expression databases

BgeeiENSG00000167965.
ExpressionAtlasiQ9BVC4. baseline and differential.
GenevisibleiQ9BVC4. HS.

Organism-specific databases

HPAiCAB019935.
HPA041841.

Interactioni

Subunit structurei

Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. mTORC1 binds to and is inhibited by FKBP12-rapamycin. Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Interacts directly with MTOR and RPTOR. Interacts with RHEB.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MTORP423454EBI-1387471,EBI-359260
RPTORQ8N1223EBI-1387471,EBI-1567928

Protein-protein interaction databases

BioGridi122113. 49 interactors.
DIPiDIP-39481N.
IntActiQ9BVC4. 26 interactors.
MINTiMINT-3046622.
STRINGi9606.ENSP00000380313.

Structurei

Secondary structure

1326
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 19Combined sources10
Beta strandi22 – 27Combined sources6
Turni29 – 31Combined sources3
Beta strandi34 – 39Combined sources6
Beta strandi47 – 50Combined sources4
Beta strandi54 – 60Combined sources7
Beta strandi65 – 72Combined sources8
Beta strandi78 – 81Combined sources4
Beta strandi86 – 93Combined sources8
Beta strandi97 – 104Combined sources8
Beta strandi107 – 113Combined sources7
Beta strandi122 – 126Combined sources5
Beta strandi131 – 136Combined sources6
Beta strandi140 – 147Combined sources8
Beta strandi152 – 156Combined sources5
Turni157 – 159Combined sources3
Beta strandi162 – 165Combined sources4
Beta strandi173 – 178Combined sources6
Beta strandi182 – 189Combined sources8
Beta strandi194 – 199Combined sources6
Helixi203 – 205Combined sources3
Beta strandi210 – 216Combined sources7
Beta strandi223 – 228Combined sources6
Beta strandi232 – 239Combined sources8
Beta strandi242 – 248Combined sources7
Turni249 – 251Combined sources3
Beta strandi254 – 259Combined sources6
Beta strandi263 – 265Combined sources3
Beta strandi273 – 278Combined sources6
Beta strandi282 – 289Combined sources8
Beta strandi292 – 298Combined sources7
Turni299 – 301Combined sources3
Beta strandi304 – 309Combined sources6
Beta strandi315 – 322Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4JSNX-ray3.20C/D1-326[»]
4JSPX-ray3.30C/D1-326[»]
4JSVX-ray3.50C/D1-326[»]
4JSXX-ray3.50C/D1-326[»]
4JT5X-ray3.45C/D1-323[»]
4JT6X-ray3.60C/D1-326[»]
5FLCelectron microscopy5.90D/H1-326[»]
ProteinModelPortaliQ9BVC4.
SMRiQ9BVC4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1 – 37WD 1PROSITE-ProRule annotation1 PublicationAdd BLAST37
Repeati40 – 80WD 2PROSITE-ProRule annotation1 PublicationAdd BLAST41
Repeati83 – 122WD 3PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati126 – 165WD 4PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati168 – 207WD 5PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati218 – 257WD 6PROSITE-ProRule annotation1 PublicationAdd BLAST40
Repeati268 – 309WD 7PROSITE-ProRule annotation1 PublicationAdd BLAST42

Sequence similaritiesi

Belongs to the WD repeat LST8 family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG0315. Eukaryota.
ENOG410XPVD. LUCA.
GeneTreeiENSGT00390000014795.
HOVERGENiHBG054763.
InParanoidiQ9BVC4.
KOiK08266.
OMAiRIWDLGE.
PhylomeDBiQ9BVC4.
TreeFamiTF318577.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BVC4-1) [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
MNTSPGTVGS DPVILATAGY DHTVRFWQAH SGICTRTVQH QDSQVNALEV
60 70 80 90 100
TPDRSMIAAA GYQHIRMYDL NSNNPNPIIS YDGVNKNIAS VGFHEDGRWM
110 120 130 140 150
YTGGEDCTAR IWDLRSRNLQ CQRIFQVNAP INCVCLHPNQ AELIVGDQSG
160 170 180 190 200
AIHIWDLKTD HNEQLIPEPE VSITSAHIDP DASYMAAVNS TGNCYVWNLT
210 220 230 240 250
GGIGDEVTQL IPKTKIPAHT RYALQCRFSP DSTLLATCSA DQTCKIWRTS
260 270 280 290 300
NFSLMTELSI KSGNPGESSR GWMWGCAFSG DSQYIVTASS DNLARLWCVE
310 320
TGEIKREYGG HQKAVVCLAF NDSVLG
Length:326
Mass (Da):35,876
Last modified:June 1, 2001 - v1
Checksum:i43A600D4EF2B6543
GO
Isoform 2 (identifier: Q9BVC4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Show »
Length:260
Mass (Da):28,728
Checksum:i92BC4236276B1274
GO
Isoform 3 (identifier: Q9BVC4-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEHAPWSPGASSRARAGHTM
     192-198: GNCYVWN → APRHLLG
     199-326: Missing.

Show »
Length:217
Mass (Da):23,850
Checksum:i3B611C65EAE88115
GO
Isoform 4 (identifier: Q9BVC4-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     44-44: Missing.

Show »
Length:325
Mass (Da):35,748
Checksum:iCF41EB9312C1788A
GO

Sequence cautioni

The sequence EAW85539 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti56M → V in BAB13990 (PubMed:14702039).Curated1
Sequence conflicti153H → Y in AAH88354 (PubMed:15489334).Curated1
Sequence conflicti248R → G in AAO73410 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0326651 – 66Missing in isoform 2. 2 PublicationsAdd BLAST66
Alternative sequenceiVSP_0326661M → MEHAPWSPGASSRARAGHTM in isoform 3. 1 Publication1
Alternative sequenceiVSP_04736844Missing in isoform 4. Curated1
Alternative sequenceiVSP_032667192 – 198GNCYVWN → APRHLLG in isoform 3. 1 Publication7
Alternative sequenceiVSP_032668199 – 326Missing in isoform 3. 1 PublicationAdd BLAST128

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY223837 mRNA. Translation: AAO73410.1.
AK021536 mRNA. Translation: BAG51036.1.
AK022227 mRNA. Translation: BAB13990.1.
AK302201 mRNA. Translation: BAG63562.1.
AC009065 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85538.1.
CH471112 Genomic DNA. Translation: EAW85539.1. Sequence problems.
CH471112 Genomic DNA. Translation: EAW85541.1.
CH471112 Genomic DNA. Translation: EAW85542.1.
BC001313 mRNA. Translation: AAH01313.1.
BC017119 mRNA. Translation: AAH17119.1.
BC052292 mRNA. Translation: AAH52292.1.
BC088354 mRNA. Translation: AAH88354.1.
AF195883 mRNA. Translation: AAF04308.1.
CCDSiCCDS10462.2. [Q9BVC4-1]
CCDS58409.1. [Q9BVC4-5]
RefSeqiNP_001186102.1. NM_001199173.1. [Q9BVC4-1]
NP_001186103.1. NM_001199174.1. [Q9BVC4-1]
NP_001186104.1. NM_001199175.1. [Q9BVC4-5]
NP_071767.3. NM_022372.4. [Q9BVC4-1]
XP_016879037.1. XM_017023548.1. [Q9BVC4-3]
XP_016879038.1. XM_017023549.1. [Q9BVC4-3]
UniGeneiHs.29203.

Genome annotation databases

EnsembliENST00000382450; ENSP00000371888; ENSG00000167965. [Q9BVC4-5]
ENST00000397124; ENSP00000380313; ENSG00000167965. [Q9BVC4-1]
ENST00000564088; ENSP00000457870; ENSG00000167965. [Q9BVC4-1]
ENST00000565250; ENSP00000455046; ENSG00000167965. [Q9BVC4-1]
ENST00000569417; ENSP00000456405; ENSG00000167965. [Q9BVC4-1]
GeneIDi64223.
KEGGihsa:64223.
UCSCiuc002coz.4. human. [Q9BVC4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY223837 mRNA. Translation: AAO73410.1.
AK021536 mRNA. Translation: BAG51036.1.
AK022227 mRNA. Translation: BAB13990.1.
AK302201 mRNA. Translation: BAG63562.1.
AC009065 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85538.1.
CH471112 Genomic DNA. Translation: EAW85539.1. Sequence problems.
CH471112 Genomic DNA. Translation: EAW85541.1.
CH471112 Genomic DNA. Translation: EAW85542.1.
BC001313 mRNA. Translation: AAH01313.1.
BC017119 mRNA. Translation: AAH17119.1.
BC052292 mRNA. Translation: AAH52292.1.
BC088354 mRNA. Translation: AAH88354.1.
AF195883 mRNA. Translation: AAF04308.1.
CCDSiCCDS10462.2. [Q9BVC4-1]
CCDS58409.1. [Q9BVC4-5]
RefSeqiNP_001186102.1. NM_001199173.1. [Q9BVC4-1]
NP_001186103.1. NM_001199174.1. [Q9BVC4-1]
NP_001186104.1. NM_001199175.1. [Q9BVC4-5]
NP_071767.3. NM_022372.4. [Q9BVC4-1]
XP_016879037.1. XM_017023548.1. [Q9BVC4-3]
XP_016879038.1. XM_017023549.1. [Q9BVC4-3]
UniGeneiHs.29203.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4JSNX-ray3.20C/D1-326[»]
4JSPX-ray3.30C/D1-326[»]
4JSVX-ray3.50C/D1-326[»]
4JSXX-ray3.50C/D1-326[»]
4JT5X-ray3.45C/D1-323[»]
4JT6X-ray3.60C/D1-326[»]
5FLCelectron microscopy5.90D/H1-326[»]
ProteinModelPortaliQ9BVC4.
SMRiQ9BVC4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122113. 49 interactors.
DIPiDIP-39481N.
IntActiQ9BVC4. 26 interactors.
MINTiMINT-3046622.
STRINGi9606.ENSP00000380313.

PTM databases

iPTMnetiQ9BVC4.
PhosphoSitePlusiQ9BVC4.

Polymorphism and mutation databases

BioMutaiMLST8.
DMDMi74761285.

Proteomic databases

EPDiQ9BVC4.
MaxQBiQ9BVC4.
PaxDbiQ9BVC4.
PeptideAtlasiQ9BVC4.
PRIDEiQ9BVC4.

Protocols and materials databases

DNASUi64223.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000382450; ENSP00000371888; ENSG00000167965. [Q9BVC4-5]
ENST00000397124; ENSP00000380313; ENSG00000167965. [Q9BVC4-1]
ENST00000564088; ENSP00000457870; ENSG00000167965. [Q9BVC4-1]
ENST00000565250; ENSP00000455046; ENSG00000167965. [Q9BVC4-1]
ENST00000569417; ENSP00000456405; ENSG00000167965. [Q9BVC4-1]
GeneIDi64223.
KEGGihsa:64223.
UCSCiuc002coz.4. human. [Q9BVC4-1]

Organism-specific databases

CTDi64223.
DisGeNETi64223.
GeneCardsiMLST8.
H-InvDBHIX0012725.
HGNCiHGNC:24825. MLST8.
HPAiCAB019935.
HPA041841.
MIMi612190. gene.
neXtProtiNX_Q9BVC4.
OpenTargetsiENSG00000167965.
PharmGKBiPA165450213.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0315. Eukaryota.
ENOG410XPVD. LUCA.
GeneTreeiENSGT00390000014795.
HOVERGENiHBG054763.
InParanoidiQ9BVC4.
KOiK08266.
OMAiRIWDLGE.
PhylomeDBiQ9BVC4.
TreeFamiTF318577.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000167965-MONOMER.
ReactomeiR-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1632852. Macroautophagy.
R-HSA-165159. mTOR signalling.
R-HSA-166208. mTORC1-mediated signalling.
R-HSA-3371571. HSF1-dependent transactivation.
R-HSA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-HSA-389357. CD28 dependent PI3K/Akt signaling.
R-HSA-5218920. VEGFR2 mediated vascular permeability.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-5674400. Constitutive Signaling by AKT1 E17K in Cancer.
R-HSA-6804757. Regulation of TP53 Degradation.
SignaLinkiQ9BVC4.
SIGNORiQ9BVC4.

Miscellaneous databases

ChiTaRSiMLST8. human.
GeneWikiiMLST8.
GenomeRNAii64223.
PROiQ9BVC4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000167965.
ExpressionAtlasiQ9BVC4. baseline and differential.
GenevisibleiQ9BVC4. HS.

Family and domain databases

Gene3Di2.130.10.10. 2 hits.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 5 hits.
[Graphical view]
PRINTSiPR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50998. SSF50998. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 3 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLST8_HUMAN
AccessioniPrimary (citable) accession number: Q9BVC4
Secondary accession number(s): B3KMM4
, B4DY00, D3DU88, Q5M800, Q86Y18, Q8WUI5, Q9HA66, Q9UJV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: June 1, 2001
Last modified: November 2, 2016
This is version 133 of the entry and version 1 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 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.