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Protein

Set1/Ash2 histone methyltransferase complex subunit ASH2

Gene

ASH2L

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

Functioni

Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1 – 66PHD-type; atypicalAdd BLAST66
Zinc fingeri117 – 150C4-typeAdd BLAST34

GO - Molecular functioni

  • beta-catenin binding Source: BHF-UCL
  • DNA binding Source: UniProtKB
  • euchromatin binding Source: Ensembl
  • histone-lysine N-methyltransferase activity Source: Reactome
  • metal ion binding Source: UniProtKB-KW
  • transcription regulatory region DNA binding Source: UniProtKB

GO - Biological processi

  • beta-catenin-TCF complex assembly Source: Reactome
  • cellular response to DNA damage stimulus Source: MGI
  • hemopoiesis Source: UniProtKB
  • histone H3-K4 methylation Source: UniProtKB
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • regulation of transcription, DNA-templated Source: UniProtKB
  • response to estrogen Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB
  • transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000129691-MONOMER.
ReactomeiR-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SIGNORiQ9UBL3.

Names & Taxonomyi

Protein namesi
Recommended name:
Set1/Ash2 histone methyltransferase complex subunit ASH2
Alternative name(s):
ASH2-like protein
Gene namesi
Name:ASH2L
Synonyms:ASH2L1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:744. ASH2L.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • histone methyltransferase complex Source: UniProtKB
  • MLL1 complex Source: Ensembl
  • MLL3/4 complex Source: UniProtKB
  • nuclear euchromatin Source: Ensembl
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • Set1C/COMPASS complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi296R → K: Abolishes methylation. 1 Publication1
Mutagenesisi300R → K: Slightly decreased methylation. 1 Publication1

Organism-specific databases

DisGeNETi9070.
OpenTargetsiENSG00000129691.
PharmGKBiPA25044.

Chemistry databases

ChEMBLiCHEMBL3137282.

Polymorphism and mutation databases

BioMutaiASH2L.
DMDMi32141382.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000646971 – 628Set1/Ash2 histone methyltransferase complex subunit ASH2Add BLAST628

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei101PhosphoserineCombined sources1
Modified residuei296Asymmetric dimethylarginine; by PRMT1 and PRMT51 Publication1
Modified residuei316PhosphoserineCombined sources1
Isoform 2 (identifier: Q9UBL3-2)
Modified residuei1N-acetylmethionineCombined sources1
Isoform 3 (identifier: Q9UBL3-3)
Modified residuei1N-acetylmethionineCombined sources1

Post-translational modificationi

Both monomethylated and dimethylated on arginine residues in the C-terminus. Arg-296 is the major site. Methylation is not required for nuclear localization, nor for MLL complex integrity or maintenance of global histone H3K4me3 levels.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ9UBL3.
MaxQBiQ9UBL3.
PaxDbiQ9UBL3.
PeptideAtlasiQ9UBL3.
PRIDEiQ9UBL3.

PTM databases

iPTMnetiQ9UBL3.
PhosphoSitePlusiQ9UBL3.

Expressioni

Tissue specificityi

Ubiquitously expressed. Predominantly expressed in adult heart and testis and fetal lung and liver, with barely detectable expression in adult lung, liver, kidney, prostate, and peripheral leukocytes.1 Publication

Gene expression databases

BgeeiENSG00000129691.
CleanExiHS_ASH2L.
ExpressionAtlasiQ9UBL3. baseline and differential.
GenevisibleiQ9UBL3. HS.

Organism-specific databases

HPAiHPA042289.

Interactioni

Subunit structurei

Interacts with HCFC1. Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. Each complex is at least composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the facultative components PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin. Interacts with DPY30 and RBBP5; the interaction is direct. Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Interacts with SETD1A and SETD1B.10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHD8Q9HCK82EBI-540797,EBI-1169146
DPY30Q9C00516EBI-540797,EBI-744973
EP300Q094725EBI-540797,EBI-447295
HCFC1P516105EBI-540797,EBI-396176
NCOA6Q1468611EBI-540797,EBI-78670
PAXIP1Q6ZW4911EBI-540797,EBI-743225
RBBP5Q1529130EBI-540797,EBI-592823
TP53P046375EBI-540797,EBI-366083

GO - Molecular functioni

  • beta-catenin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi114528. 64 interactors.
DIPiDIP-29222N.
IntActiQ9UBL3. 55 interactors.
MINTiMINT-1194078.
STRINGi9606.ENSP00000340896.

Structurei

Secondary structure

1628
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi114 – 116Combined sources3
Turni118 – 120Combined sources3
Beta strandi123 – 125Combined sources3
Helixi126 – 129Combined sources4
Beta strandi142 – 146Combined sources5
Turni148 – 150Combined sources3
Beta strandi157 – 160Combined sources4
Helixi165 – 183Combined sources19
Turni193 – 196Combined sources4
Helixi197 – 203Combined sources7
Helixi205 – 207Combined sources3
Helixi219 – 221Combined sources3
Helixi223 – 228Combined sources6
Turni231 – 233Combined sources3
Beta strandi234 – 239Combined sources6
Helixi248 – 250Combined sources3
Beta strandi252 – 257Combined sources6
Helixi261 – 263Combined sources3
Helixi371 – 373Combined sources3
Beta strandi376 – 378Combined sources3
Beta strandi383 – 388Combined sources6
Beta strandi392 – 394Combined sources3
Beta strandi398 – 402Combined sources5
Beta strandi408 – 413Combined sources6
Beta strandi416 – 429Combined sources14
Beta strandi435 – 441Combined sources7
Beta strandi457 – 461Combined sources5
Turni462 – 465Combined sources4
Beta strandi467 – 469Combined sources3
Beta strandi472 – 474Combined sources3
Beta strandi485 – 492Combined sources8
Beta strandi540 – 545Combined sources6
Beta strandi548 – 556Combined sources9
Beta strandi562 – 571Combined sources10
Beta strandi573 – 577Combined sources5
Beta strandi579 – 581Combined sources3
Beta strandi587 – 589Combined sources3
Helixi594 – 597Combined sources4
Beta strandi599 – 602Combined sources4
Helixi603 – 615Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3RSNX-ray2.10A96-271[»]
3S32X-ray2.45A95-280[»]
3TOJX-ray2.07A/B370-496[»]
A/B539-617[»]
4RIQX-ray2.23C/F/I/L/O/R/U/X603-618[»]
4X8NX-ray2.10A380-495[»]
A539-598[»]
4X8PX-ray2.20A380-495[»]
A539-598[»]
5F6KX-ray2.41A/B380-496[»]
A/B539-598[»]
5F6LX-ray1.90B380-496[»]
B539-598[»]
ProteinModelPortaliQ9UBL3.
SMRiQ9UBL3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini360 – 583B30.2/SPRYPROSITE-ProRule annotationAdd BLAST224

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni67 – 177DNA-bindingAdd BLAST111

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1 – 66PHD-type; atypicalAdd BLAST66
Zinc fingeri117 – 150C4-typeAdd BLAST34

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2626. Eukaryota.
ENOG410Y5GC. LUCA.
GeneTreeiENSGT00390000010474.
HOGENOMiHOG000013137.
HOVERGENiHBG050592.
InParanoidiQ9UBL3.
KOiK14964.
OMAiCATCSRW.
OrthoDBiEOG091G069C.
PhylomeDBiQ9UBL3.
TreeFamiTF314785.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
PROSITEiPS50188. B302_SPRY. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UBL3-1) [UniParc]FASTAAdd to basket
Also known as: ASH2L1

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
MAAAGAGPGQ EAGAGPGPGA VANATGAEEG EMKPVAAGAA APPGEGISAA
60 70 80 90 100
PTVEPSSGEA EGGEANLVDV SGGLETESSN GKDTLEGAGD TSEVMDTQAG
110 120 130 140 150
SVDEENGRQL GEVELQCGIC TKWFTADTFG IDTSSCLPFM TNYSFHCNVC
160 170 180 190 200
HHSGNTYFLR KQANLKEMCL SALANLTWQS RTQDEHPKTM FSKDKDIIPF
210 220 230 240 250
IDKYWECMTT RQRPGKMTWP NNIVKTMSKE RDVFLVKEHP DPGSKDPEED
260 270 280 290 300
YPKFGLLDQD LSNIGPAYDN QKQSSAVSTS GNLNGGIAAG SSGKGRGAKR
310 320 330 340 350
KQQDGGTTGT TKKARSDPLF SAQRLPPHGY PLEHPFNKDG YRYILAEPDP
360 370 380 390 400
HAPDPEKLEL DCWAGKPIPG DLYRACLYER VLLALHDRAP QLKISDDRLT
410 420 430 440 450
VVGEKGYSMV RASHGVRKGA WYFEITVDEM PPDTAARLGW SQPLGNLQAP
460 470 480 490 500
LGYDKFSYSW RSKKGTKFHQ SIGKHYSSGY GQGDVLGFYI NLPEDTETAK
510 520 530 540 550
SLPDTYKDKA LIKFKSYLYF EEKDFVDKAE KSLKQTPHSE IIFYKNGVNQ
560 570 580 590 600
GVAYKDIFEG VYFPAISLYK SCTVSINFGP CFKYPPKDLT YRPMSDMGWG
610 620
AVVEHTLADV LYHVETEVDG RRSPPWEP
Length:628
Mass (Da):68,723
Last modified:May 1, 2000 - v1
Checksum:i8F5F007430D4B863
GO
Isoform 2 (identifier: Q9UBL3-2) [UniParc]FASTAAdd to basket
Also known as: ASH2L2

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: Missing.
     541-573: Missing.

Show »
Length:501
Mass (Da):56,477
Checksum:iBD76059C4DE39703
GO
Isoform 3 (identifier: Q9UBL3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-94: Missing.

Note: No experimental confirmation available.Combined sources
Show »
Length:534
Mass (Da):60,208
Checksum:i4317F1206E97C897
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti212Q → H in AAC13564 (PubMed:11466562).Curated1
Sequence conflicti217M → T in AAC13564 (PubMed:11466562).Curated1
Sequence conflicti292S → T in AAC13563 (PubMed:11466562).Curated1
Sequence conflicti351H → Q in AAC13564 (PubMed:11466562).Curated1
Sequence conflicti360L → I in AAC13564 (PubMed:11466562).Curated1
Sequence conflicti369P → S in AAC13564 (PubMed:11466562).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_050679478S → F.Corresponds to variant rs34167006dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0075771 – 94Missing in isoform 2 and isoform 3. 3 PublicationsAdd BLAST94
Alternative sequenceiVSP_007578541 – 573Missing in isoform 2. 1 PublicationAdd BLAST33

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF056718 mRNA. Translation: AAC13564.1.
AF056717 mRNA. Translation: AAC13563.1.
AB022785 Genomic DNA. Translation: BAA74520.1.
AB020982 mRNA. Translation: BAA35127.1.
AK291938 mRNA. Translation: BAF84627.1.
CH471080 Genomic DNA. Translation: EAW63337.1.
CH471080 Genomic DNA. Translation: EAW63336.1.
CH471080 Genomic DNA. Translation: EAW63340.1.
BC015936 mRNA. Translation: AAH15936.1.
CCDSiCCDS47840.1. [Q9UBL3-3]
CCDS59100.1. [Q9UBL3-2]
CCDS6101.1. [Q9UBL3-1]
RefSeqiNP_001098684.1. NM_001105214.2. [Q9UBL3-3]
NP_001248761.1. NM_001261832.1. [Q9UBL3-2]
NP_004665.2. NM_004674.4. [Q9UBL3-1]
UniGeneiHs.521530.

Genome annotation databases

EnsembliENST00000343823; ENSP00000340896; ENSG00000129691. [Q9UBL3-1]
ENST00000428278; ENSP00000395310; ENSG00000129691. [Q9UBL3-3]
ENST00000521652; ENSP00000430259; ENSG00000129691. [Q9UBL3-2]
GeneIDi9070.
KEGGihsa:9070.
UCSCiuc003xkt.6. human. [Q9UBL3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF056718 mRNA. Translation: AAC13564.1.
AF056717 mRNA. Translation: AAC13563.1.
AB022785 Genomic DNA. Translation: BAA74520.1.
AB020982 mRNA. Translation: BAA35127.1.
AK291938 mRNA. Translation: BAF84627.1.
CH471080 Genomic DNA. Translation: EAW63337.1.
CH471080 Genomic DNA. Translation: EAW63336.1.
CH471080 Genomic DNA. Translation: EAW63340.1.
BC015936 mRNA. Translation: AAH15936.1.
CCDSiCCDS47840.1. [Q9UBL3-3]
CCDS59100.1. [Q9UBL3-2]
CCDS6101.1. [Q9UBL3-1]
RefSeqiNP_001098684.1. NM_001105214.2. [Q9UBL3-3]
NP_001248761.1. NM_001261832.1. [Q9UBL3-2]
NP_004665.2. NM_004674.4. [Q9UBL3-1]
UniGeneiHs.521530.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3RSNX-ray2.10A96-271[»]
3S32X-ray2.45A95-280[»]
3TOJX-ray2.07A/B370-496[»]
A/B539-617[»]
4RIQX-ray2.23C/F/I/L/O/R/U/X603-618[»]
4X8NX-ray2.10A380-495[»]
A539-598[»]
4X8PX-ray2.20A380-495[»]
A539-598[»]
5F6KX-ray2.41A/B380-496[»]
A/B539-598[»]
5F6LX-ray1.90B380-496[»]
B539-598[»]
ProteinModelPortaliQ9UBL3.
SMRiQ9UBL3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114528. 64 interactors.
DIPiDIP-29222N.
IntActiQ9UBL3. 55 interactors.
MINTiMINT-1194078.
STRINGi9606.ENSP00000340896.

Chemistry databases

ChEMBLiCHEMBL3137282.

PTM databases

iPTMnetiQ9UBL3.
PhosphoSitePlusiQ9UBL3.

Polymorphism and mutation databases

BioMutaiASH2L.
DMDMi32141382.

Proteomic databases

EPDiQ9UBL3.
MaxQBiQ9UBL3.
PaxDbiQ9UBL3.
PeptideAtlasiQ9UBL3.
PRIDEiQ9UBL3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343823; ENSP00000340896; ENSG00000129691. [Q9UBL3-1]
ENST00000428278; ENSP00000395310; ENSG00000129691. [Q9UBL3-3]
ENST00000521652; ENSP00000430259; ENSG00000129691. [Q9UBL3-2]
GeneIDi9070.
KEGGihsa:9070.
UCSCiuc003xkt.6. human. [Q9UBL3-1]

Organism-specific databases

CTDi9070.
DisGeNETi9070.
GeneCardsiASH2L.
H-InvDBHIX0007454.
HGNCiHGNC:744. ASH2L.
HPAiHPA042289.
MIMi604782. gene.
neXtProtiNX_Q9UBL3.
OpenTargetsiENSG00000129691.
PharmGKBiPA25044.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2626. Eukaryota.
ENOG410Y5GC. LUCA.
GeneTreeiENSGT00390000010474.
HOGENOMiHOG000013137.
HOVERGENiHBG050592.
InParanoidiQ9UBL3.
KOiK14964.
OMAiCATCSRW.
OrthoDBiEOG091G069C.
PhylomeDBiQ9UBL3.
TreeFamiTF314785.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000129691-MONOMER.
ReactomeiR-HSA-201722. Formation of the beta-catenin:TCF transactivating complex.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SIGNORiQ9UBL3.

Miscellaneous databases

ChiTaRSiASH2L. human.
GeneWikiiASH2L.
GenomeRNAii9070.
PROiQ9UBL3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000129691.
CleanExiHS_ASH2L.
ExpressionAtlasiQ9UBL3. baseline and differential.
GenevisibleiQ9UBL3. HS.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
PROSITEiPS50188. B302_SPRY. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiASH2L_HUMAN
AccessioniPrimary (citable) accession number: Q9UBL3
Secondary accession number(s): A8K7C3
, D3DSW9, O60659, O60660, Q96B62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 153 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 8
    Human chromosome 8: 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.