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Protein

Charged multivesicular body protein 3

Gene

CHMP3

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

Functioni

Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor. Isoform 2 prevents stress-mediated cell death and accumulation of reactive oxygen species when expressed in yeast cells.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei48Important for autoinhibitory function1
Binding sitei216STAMBP1

GO - Molecular functioni

  • phosphatidylcholine binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • ubiquitin-specific protease binding Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • autophagosome maturation Source: ParkinsonsUK-UCL
  • autophagy Source: ParkinsonsUK-UCL
  • cell cycle Source: UniProtKB-KW
  • cell separation after cytokinesis Source: UniProtKB
  • endosomal transport Source: Reactome
  • multivesicular body assembly Source: ParkinsonsUK-UCL
  • multivesicular body-lysosome fusion Source: ParkinsonsUK-UCL
  • multivesicular body sorting pathway Source: ParkinsonsUK-UCL
  • negative regulation of viral release from host cell Source: UniProtKB
  • positive regulation of viral release from host cell Source: UniProtKB
  • protein heterooligomerization Source: UniProtKB
  • protein polymerization Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of centrosome duplication Source: UniProtKB
  • regulation of early endosome to late endosome transport Source: ParkinsonsUK-UCL
  • regulation of viral process Source: UniProtKB
  • viral budding via host ESCRT complex Source: UniProtKB
  • viral life cycle Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Cell cycle, Cell division, Protein transport, Transport

Enzyme and pathway databases

BioCyciZFISH:MONOMER66-34376.
ReactomeiR-HSA-162588. Budding and maturation of HIV virion.
R-HSA-1632852. Macroautophagy.
R-HSA-917729. Endosomal Sorting Complex Required For Transport (ESCRT).
SignaLinkiQ9Y3E7.

Names & Taxonomyi

Protein namesi
Recommended name:
Charged multivesicular body protein 3
Alternative name(s):
Chromatin-modifying protein 3
Neuroendocrine differentiation factor
Vacuolar protein sorting-associated protein 24
Short name:
hVps24
Gene namesi
Name:CHMP3
Synonyms:CGI149, NEDF, VPS24
ORF Names:CGI-149
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:29865. CHMP3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB
  • cytosol Source: Reactome
  • ESCRT III complex Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • intracellular Source: ParkinsonsUK-UCL
  • late endosome Source: ParkinsonsUK-UCL
  • late endosome membrane Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi24 – 25RK → SA: Impairs HIV-1 release; when associated with S-28. 1 Publication2
Mutagenesisi28R → S: Impairs HIV-1 release; when associated with 24-S-A-25. 1 Publication1
Mutagenesisi48V → D: Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-64. Enhances inhibition of HIV-1 budding in vivo; when associated with D-168 and D-169. 1 Publication1
Mutagenesisi54K → S: Abolishes dimerization; when associated with N-56; E-59 and 62-D-E-63. 1 Publication1
Mutagenesisi56Q → N: Abolishes dimerization; when associated with S-54; E-59 and 62-D-E-63. 1 Publication1
Mutagenesisi59V → D: Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-62; D-168 and D-169. 2 Publications1
Mutagenesisi59V → E: Abolishes dimerization; when associated with S-54; N-56 and 62-D-E-63. 2 Publications1
Mutagenesisi62 – 63VL → DE: Abolishes dimerization; when associated with S-54; N-56 and E-59. 1 Publication2
Mutagenesisi62V → D: Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59; D-168 and D-169. 1 Publication1
Mutagenesisi64A → D: Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-48. 1 Publication1
Mutagenesisi78 – 79YA → AE: Abolishes dimerization. 1 Publication2
Mutagenesisi168 – 169IL → DD: Induces assembly with CHMP2A into helical tubes in vitro and slightly enhances inhibition of HIV-1 budding in vivo. Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59 and D-62. 1 Publication2
Mutagenesisi179 – 222Missing : Membrane association; releases autoinhibition. 1 PublicationAdd BLAST44
Mutagenesisi216 – 217RL → AA: Abolishes interaction with VPS4A and STAMBP. 1 Publication2
Mutagenesisi221 – 222Missing : Abolishes interaction with VPS4A and STAMBP. 1 Publication2
Mutagenesisi222Missing : Impairs interaction with VPS4A and STAMBP. 1 Publication1

Organism-specific databases

DisGeNETi51652.
OpenTargetsiENSG00000115561.
ENSG00000249884.
PharmGKBiPA134920495.

Polymorphism and mutation databases

BioMutaiCHMP3.
DMDMi73917763.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedSequence analysis
ChainiPRO_00002114792 – 222Charged multivesicular body protein 3Add BLAST221

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineSequence analysis1
Cross-linki179Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei200PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y3E7.
PaxDbiQ9Y3E7.
PeptideAtlasiQ9Y3E7.
PRIDEiQ9Y3E7.

PTM databases

iPTMnetiQ9Y3E7.
PhosphoSitePlusiQ9Y3E7.

Expressioni

Tissue specificityi

Widely expressed. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.1 Publication

Gene expression databases

BgeeiENSG00000115561.
CleanExiHS_VPS24.
GenevisibleiQ9Y3E7. HS.

Organism-specific databases

HPAiHPA015673.

Interactioni

Subunit structurei

Probable core component of the endosomal sorting required for transport complex III (ESCRT-III). ESCRT-III components are thought to multimerize to form a flat lattice on the perimeter membrane of the endosome. Several assembly forms of ESCRT-III may exist that interact and act sequentally. Forms a metastable monomer in solution; its core structure (without part of the putative autoinhibitory C-terminal acidic region) oligomerizes into a flat lattice via two different dimerization interfaces. In vitro, heteromerizes with CHMP2A (but not CHMP4) to form helical tubular structures that expose membrane-interacting sites on the outside whereas VPS4B can associate on the inside of the tubule. May interact with IGFBP7; the relevance of such interaction however remains unclear. Interacts with CHMP2A. Interacts with CHMP4A; the interaction requires the release of CHMP4A autoinhibition. Interacts with VPS4A. Interacts with STAMBP; the interaction appears to relieve the autoinhibition of CHMP3. Interacts with VTA1.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHMP2AO436333EBI-2118119,EBI-2692789
CHMP2BQ9UQN32EBI-2118119,EBI-718324
CHMP4BQ9H4445EBI-2118119,EBI-749627
STAMBPO9563019EBI-2118119,EBI-396676

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • ubiquitin-specific protease binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119660. 31 interactors.
1529307. 2 interactors.
DIPiDIP-48532N.
IntActiQ9Y3E7. 24 interactors.
MINTiMINT-1185988.
STRINGi9606.ENSP00000405575.

Structurei

Secondary structure

1222
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi15 – 53Combined sources39
Helixi57 – 100Combined sources44
Helixi109 – 112Combined sources4
Turni113 – 115Combined sources3
Beta strandi120 – 122Combined sources3
Helixi125 – 137Combined sources13
Helixi164 – 167Combined sources4
Beta strandi175 – 177Combined sources3
Helixi201 – 220Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GD5X-ray2.80A/B/C/D9-183[»]
2XZEX-ray1.75Q/R183-222[»]
3FRTX-ray4.00A/B8-222[»]
3FRVX-ray3.70A1-150[»]
ProteinModelPortaliQ9Y3E7.
SMRiQ9Y3E7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y3E7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 113Intramolecular interaction with C-terminusAdd BLAST112
Regioni59 – 64Important for autoinhibitory function6
Regioni151 – 222Interaction with VPS4AAdd BLAST72
Regioni151 – 220Intramolecular interaction with N-terminusAdd BLAST70
Regioni168 – 169Important for autoinhibitory function2
Regioni203 – 207Interaction with STAMBP5
Regioni221 – 222Interaction with STAMBP2

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili22 – 54Sequence analysisAdd BLAST33
Coiled coili141 – 222Sequence analysisAdd BLAST82

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi201 – 211MIT-interacting motifAdd BLAST11

Domaini

The acidic C-terminus and the basic N-termminus are thought to render the protein in a closed, soluble and inactive conformation through an autoinhibitory intramolecular interaction. The open and active conformation, which enables membrane binding and oligomerization, is achieved by interaction with other cellular binding partners, probably including other ESCRT components.

Sequence similaritiesi

Belongs to the SNF7 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
KOG3229. Eukaryota.
COG5491. LUCA.
GeneTreeiENSGT00550000074896.
HOGENOMiHOG000177219.
HOVERGENiHBG107031.
InParanoidiQ9Y3E7.
KOiK12193.
OMAiQKDVCVI.
OrthoDBiEOG091G0EZD.
PhylomeDBiQ9Y3E7.
TreeFamiTF105848.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

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

Isoform 1 (identifier: Q9Y3E7-1) [UniParc]FASTAAdd to basket
Also known as: Vps24alpha

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
MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD
60 70 80 90 100
AAKKGQKDVC IVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV
110 120 130 140 150
AGSLQKSTEV MKAMQSLVKI PEIQATMREL SKEMMKAGII EEMLEDTFES
160 170 180 190 200
MDDQEEMEEE AEMEIDRILF EITAGALGKA PSKVTDALPE PEPPGAMAAS
210 220
EDEEEEEEAL EAMQSRLATL RS
Length:222
Mass (Da):25,073
Last modified:January 23, 2007 - v3
Checksum:i7B1ACE5EA453E8C0
GO
Isoform 2 (identifier: Q9Y3E7-2) [UniParc]FASTAAdd to basket
Also known as: Vps24beta

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

Show »
Length:156
Mass (Da):17,326
Checksum:i7B10B4D1FB7E1B62
GO
Isoform 3 (identifier: Q9Y3E7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MGLFGKTQEKPPKEL → MEGELYSALKEEEASESVSSTNFSGEMHFYELVEDTKDGIWLVQ

Note: No experimental confirmation available.
Show »
Length:251
Mass (Da):28,386
Checksum:i0BA3A646BBC05B51
GO
Isoform 4 (identifier: Q9Y3E7-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     74-113: Missing.

Note: No experimental confirmation available.
Show »
Length:182
Mass (Da):20,770
Checksum:iE2951422F9E1A226
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti208E → D in AAF26737 (PubMed:11549700).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0410761 – 66Missing in isoform 2. 2 PublicationsAdd BLAST66
Alternative sequenceiVSP_0421241 – 15MGLFG…PPKEL → MEGELYSALKEEEASESVSS TNFSGEMHFYELVEDTKDGI WLVQ in isoform 3. 1 PublicationAdd BLAST15
Alternative sequenceiVSP_04212574 – 113Missing in isoform 4. CuratedAdd BLAST40

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF219226 mRNA. Translation: AAF26737.1.
AY364249 mRNA. Translation: AAQ76808.1.
AF151907 mRNA. Translation: AAD34144.1.
AK290725 mRNA. Translation: BAF83414.1.
AK294389 mRNA. Translation: BAG57645.1.
AK312353 mRNA. Translation: BAG35273.1.
AK315835 mRNA. Translation: BAF98726.1.
AC015971 Genomic DNA. Translation: AAX93078.1.
AC064848 Genomic DNA. No translation available.
AC068288 Genomic DNA. Translation: AAY24211.1.
CH471053 Genomic DNA. Translation: EAW99448.1.
CH471053 Genomic DNA. Translation: EAW99449.1.
CH471053 Genomic DNA. Translation: EAW99450.1.
CH471053 Genomic DNA. Translation: EAW99451.1.
BC004419 mRNA. Translation: AAH04419.1.
CCDSiCCDS33236.1. [Q9Y3E7-1]
CCDS42707.1. [Q9Y3E7-2]
CCDS54375.1. [Q9Y3E7-4]
RefSeqiNP_001005753.1. NM_001005753.2. [Q9Y3E7-2]
NP_001180446.1. NM_001193517.1. [Q9Y3E7-4]
NP_001185883.1. NM_001198954.1. [Q9Y3E7-3]
NP_057163.1. NM_016079.3. [Q9Y3E7-1]
UniGeneiHs.591582.

Genome annotation databases

EnsembliENST00000263856; ENSP00000263856; ENSG00000115561. [Q9Y3E7-1]
ENST00000409225; ENSP00000386590; ENSG00000115561. [Q9Y3E7-2]
ENST00000409727; ENSP00000387045; ENSG00000115561. [Q9Y3E7-4]
GeneIDi100526767.
51652.
KEGGihsa:100526767.
hsa:51652.
UCSCiuc002srj.4. human. [Q9Y3E7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF219226 mRNA. Translation: AAF26737.1.
AY364249 mRNA. Translation: AAQ76808.1.
AF151907 mRNA. Translation: AAD34144.1.
AK290725 mRNA. Translation: BAF83414.1.
AK294389 mRNA. Translation: BAG57645.1.
AK312353 mRNA. Translation: BAG35273.1.
AK315835 mRNA. Translation: BAF98726.1.
AC015971 Genomic DNA. Translation: AAX93078.1.
AC064848 Genomic DNA. No translation available.
AC068288 Genomic DNA. Translation: AAY24211.1.
CH471053 Genomic DNA. Translation: EAW99448.1.
CH471053 Genomic DNA. Translation: EAW99449.1.
CH471053 Genomic DNA. Translation: EAW99450.1.
CH471053 Genomic DNA. Translation: EAW99451.1.
BC004419 mRNA. Translation: AAH04419.1.
CCDSiCCDS33236.1. [Q9Y3E7-1]
CCDS42707.1. [Q9Y3E7-2]
CCDS54375.1. [Q9Y3E7-4]
RefSeqiNP_001005753.1. NM_001005753.2. [Q9Y3E7-2]
NP_001180446.1. NM_001193517.1. [Q9Y3E7-4]
NP_001185883.1. NM_001198954.1. [Q9Y3E7-3]
NP_057163.1. NM_016079.3. [Q9Y3E7-1]
UniGeneiHs.591582.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GD5X-ray2.80A/B/C/D9-183[»]
2XZEX-ray1.75Q/R183-222[»]
3FRTX-ray4.00A/B8-222[»]
3FRVX-ray3.70A1-150[»]
ProteinModelPortaliQ9Y3E7.
SMRiQ9Y3E7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119660. 31 interactors.
1529307. 2 interactors.
DIPiDIP-48532N.
IntActiQ9Y3E7. 24 interactors.
MINTiMINT-1185988.
STRINGi9606.ENSP00000405575.

PTM databases

iPTMnetiQ9Y3E7.
PhosphoSitePlusiQ9Y3E7.

Polymorphism and mutation databases

BioMutaiCHMP3.
DMDMi73917763.

Proteomic databases

EPDiQ9Y3E7.
PaxDbiQ9Y3E7.
PeptideAtlasiQ9Y3E7.
PRIDEiQ9Y3E7.

Protocols and materials databases

DNASUi51652.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263856; ENSP00000263856; ENSG00000115561. [Q9Y3E7-1]
ENST00000409225; ENSP00000386590; ENSG00000115561. [Q9Y3E7-2]
ENST00000409727; ENSP00000387045; ENSG00000115561. [Q9Y3E7-4]
GeneIDi100526767.
51652.
KEGGihsa:100526767.
hsa:51652.
UCSCiuc002srj.4. human. [Q9Y3E7-1]

Organism-specific databases

CTDi100526767.
51652.
DisGeNETi51652.
GeneCardsiCHMP3.
HGNCiHGNC:29865. CHMP3.
HPAiHPA015673.
MIMi610052. gene.
neXtProtiNX_Q9Y3E7.
OpenTargetsiENSG00000115561.
ENSG00000249884.
PharmGKBiPA134920495.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
KOG3229. Eukaryota.
COG5491. LUCA.
GeneTreeiENSGT00550000074896.
HOGENOMiHOG000177219.
HOVERGENiHBG107031.
InParanoidiQ9Y3E7.
KOiK12193.
OMAiQKDVCVI.
OrthoDBiEOG091G0EZD.
PhylomeDBiQ9Y3E7.
TreeFamiTF105848.

Enzyme and pathway databases

BioCyciZFISH:MONOMER66-34376.
ReactomeiR-HSA-162588. Budding and maturation of HIV virion.
R-HSA-1632852. Macroautophagy.
R-HSA-917729. Endosomal Sorting Complex Required For Transport (ESCRT).
SignaLinkiQ9Y3E7.

Miscellaneous databases

ChiTaRSiCHMP3. human.
EvolutionaryTraceiQ9Y3E7.
GeneWikiiVPS24.
PROiQ9Y3E7.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000115561.
CleanExiHS_VPS24.
GenevisibleiQ9Y3E7. HS.

Family and domain databases

InterProiIPR005024. Snf7_fam.
[Graphical view]
PfamiPF03357. Snf7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCHMP3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3E7
Secondary accession number(s): A8K3W0
, B4DG34, B8ZZM0, B8ZZX5, Q3ZTS9, Q53S71, Q53SU5, Q9NZ51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 140 of the entry and version 3 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

Miscellaneous

Its overexpression strongly inhibits HIV-1 release.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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.