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Protein

Histone-lysine N-methyltransferase EZH1

Gene

Ezh1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH1 complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Required for embryonic stem cell derivation and self-renewal, suggesting that it is involved in safeguarding embryonic stem cell identity. Compared to EZH2-containing complexes, it is less abundant in embryonic stem cells, has weak methyltransferase activity and plays a less critical role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 Publication

GO - Molecular functioni

  • histone methyltransferase activity (H3-K27 specific) Source: MGI

GO - Biological processi

  • hepatocyte homeostasis Source: MGI
  • histone H3-K27 trimethylation Source: MGI
  • liver regeneration Source: MGI
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • response to tetrachloromethane Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase EZH1 (EC:2.1.1.43)
Alternative name(s):
ENX-2
Enhancer of zeste homolog 1
Gene namesi
Name:Ezh1
Synonyms:Enx2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1097695. Ezh1.

Subcellular locationi

  • Nucleus By similarity

  • Note: Colocalizes with trimethylated 'Lys-27' of histone H3.By similarity

GO - Cellular componenti

  • ESC/E(Z) complex Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 747747Histone-lysine N-methyltransferase EZH1PRO_0000213991Add
BLAST

Proteomic databases

EPDiP70351.
MaxQBiP70351.
PaxDbiP70351.
PeptideAtlasiP70351.
PRIDEiP70351.

PTM databases

iPTMnetiP70351.
PhosphoSiteiP70351.

Expressioni

Tissue specificityi

Expressed at high levels in kidney, adrenal gland, testis and brain.1 Publication

Gene expression databases

BgeeiP70351.
CleanExiMM_EZH1.
GenevisibleiP70351. MM.

Interactioni

Subunit structurei

Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. The PRC2/EED-EZH1 is less abundant than the PRC2/EED-EZH2 complex, has weak methyltransferase activity and compacts chromatin in the absence of the methyltransferase cofactor S-adenosyl-L-methionine (SAM).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Jarid2Q623154EBI-2531737,EBI-493592
Mtf2Q023953EBI-2531737,EBI-2531578

Protein-protein interaction databases

BioGridi199563. 7 interactions.
DIPiDIP-56992N.
IntActiP70351. 7 interactions.
STRINGi10090.ENSMUSP00000102906.

Structurei

3D structure databases

ProteinModelPortaliP70351.
SMRiP70351. Positions 521-730.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini504 – 606103CXCPROSITE-ProRule annotationAdd
BLAST
Domaini613 – 728116SETPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi491 – 4966Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi524 – 60683Cys-richAdd
BLAST

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. EZ subfamily.PROSITE-ProRule annotation
Contains 1 CXC domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1079. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00760000119228.
HOVERGENiHBG002453.
InParanoidiP70351.
KOiK17451.
OrthoDBiEOG7VB2DR.
PhylomeDBiP70351.
TreeFamiTF314509.

Family and domain databases

InterProiIPR026489. CXC_dom.
IPR032926. EZH1.
IPR021654. EZH1/EZH2.
IPR001005. SANT/Myb.
IPR001214. SET_dom.
IPR033467. Tesmin/TSO1-like_CXC.
[Graphical view]
PANTHERiPTHR22884:SF333. PTHR22884:SF333. 1 hit.
PfamiPF11616. EZH2_WD-Binding. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM01114. CXC. 1 hit.
SM00717. SANT. 2 hits.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51633. CXC. 1 hit.
PS50280. SET. 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: P70351-1) [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
MDIASPPTSK CITYWKRKVK SEYMRLRQLK RLQANMGAKA LYVANFAKVQ
60 70 80 90 100
EKTQILNEEW KKLRVQPVQP MKPVSGHPFL KKCTIESIFP GFDSQDMLMR
110 120 130 140 150
SLNTVALVPI MYSWSPLQQN FMVEDETVLC NIPYMGDEVK EEDETFIEEL
160 170 180 190 200
INNYDGKVHG EEEMIPGSVL ISDAVFLELV DALNQYSDEE EDGHNDPSDG
210 220 230 240 250
KQDDSKEDLP VTRKRKRHAI EGNKKSSKKQ FPNDMIFSAI ASMFPENGVP
260 270 280 290 300
DDMKERYREL TEMSDPNALP PQCTPNIDGP NAKSVQREQS LHSFHTLFCR
310 320 330 340 350
RCFKYDCFLH PFHATPNVYK RKNKEIKIEP EPCGTDCFLL LEGAKEYAML
360 370 380 390 400
HNPRSKCSGR RRRRHPVVSA SCSNASASAM AETKEGDSDR DTGNDWASSS
410 420 430 440 450
SEANSRCQTP TKQKASPAPA QLCVVEAPSE PVEWTGAEES LFRVFHGTYF
460 470 480 490 500
NNFCSIARLL GTKTCKQVFQ FAVKESLILK LPTDELMNPA QKKKRKHRLW
510 520 530 540 550
AAHCRKIQLK KDNNSTQVYN YQPCDHPDRP CDSTCPCIMT QNFCEKFCQC
560 570 580 590 600
SPDCQNRFPG CRCKTQCNTK QCPCYLAVRE CDPDLCLTCG ASEHWDCKVV
610 620 630 640 650
SCKNCSIQRG LKKHLLLAPS DVAGWGTFIK ESVQKNEFIS EYCGELISQD
660 670 680 690 700
EADRRGKVYD KYMSSFLFNL NNDFVVDATR KGNKIRFANH SVNPNCYAKV
710 720 730 740
VMVNGDHRIG IFAKRAIQAG EELFFDYRYS QADALKYVGI ERETDVF
Length:747
Mass (Da):85,188
Last modified:February 1, 1997 - v1
Checksum:i43CECFBDF3E49192
GO
Isoform 2 (identifier: P70351-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     555-747: QNRFPGCRCK...VGIERETDVF → KSTLLSPSSTQVVGLGVPRLFSPAP

Show »
Length:579
Mass (Da):65,730
Checksum:iB42CCD4108D013EA
GO

Sequence cautioni

The sequence AAH07135.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAL90764.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAL90765.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA25018.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE23827.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE24446.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE32680.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE37674.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence EDL03899.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841T → A in BAE32680 (PubMed:16141072).Curated
Sequence conflicti446 – 4461H → Y in AAD54021 (PubMed:9473645).Curated
Sequence conflicti452 – 4521N → Y in AAD54021 (PubMed:9473645).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei555 – 747193QNRFP…ETDVF → KSTLLSPSSTQVVGLGVPRL FSPAP in isoform 2. 1 PublicationVSP_036388Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60453 mRNA. Translation: AAC53279.1.
AB004817 mRNA. Translation: BAA25018.1. Different initiation.
AF104360 Genomic DNA. Translation: AAD54021.1.
AF483490 mRNA. Translation: AAL90764.1. Different initiation.
AF483491 mRNA. Translation: AAL90765.1. Different initiation.
AK045374 mRNA. Translation: BAC32334.1.
AK138942 mRNA. Translation: BAE23827.1. Different initiation.
AK140694 mRNA. Translation: BAE24446.1. Different initiation.
AK154565 mRNA. Translation: BAE32680.1. Different initiation.
AK164192 mRNA. Translation: BAE37674.1. Different initiation.
AL590969 Genomic DNA. Translation: CAM19569.1.
AL590969 Genomic DNA. Translation: CAM19570.1.
CH466677 Genomic DNA. Translation: EDL03899.1. Different initiation.
BC007135 mRNA. Translation: AAH07135.1. Different initiation.
RefSeqiNP_031996.1. NM_007970.3.
XP_006532241.1. XM_006532178.2. [P70351-1]
UniGeneiMm.5027.

Genome annotation databases

EnsembliENSMUST00000100417; ENSMUSP00000097984; ENSMUSG00000006920. [P70351-2]
ENSMUST00000107284; ENSMUSP00000102905; ENSMUSG00000006920. [P70351-1]
GeneIDi14055.
KEGGimmu:14055.
UCSCiuc007lnw.3. mouse. [P70351-2]
uc011yfk.2. mouse. [P70351-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U60453 mRNA. Translation: AAC53279.1.
AB004817 mRNA. Translation: BAA25018.1. Different initiation.
AF104360 Genomic DNA. Translation: AAD54021.1.
AF483490 mRNA. Translation: AAL90764.1. Different initiation.
AF483491 mRNA. Translation: AAL90765.1. Different initiation.
AK045374 mRNA. Translation: BAC32334.1.
AK138942 mRNA. Translation: BAE23827.1. Different initiation.
AK140694 mRNA. Translation: BAE24446.1. Different initiation.
AK154565 mRNA. Translation: BAE32680.1. Different initiation.
AK164192 mRNA. Translation: BAE37674.1. Different initiation.
AL590969 Genomic DNA. Translation: CAM19569.1.
AL590969 Genomic DNA. Translation: CAM19570.1.
CH466677 Genomic DNA. Translation: EDL03899.1. Different initiation.
BC007135 mRNA. Translation: AAH07135.1. Different initiation.
RefSeqiNP_031996.1. NM_007970.3.
XP_006532241.1. XM_006532178.2. [P70351-1]
UniGeneiMm.5027.

3D structure databases

ProteinModelPortaliP70351.
SMRiP70351. Positions 521-730.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199563. 7 interactions.
DIPiDIP-56992N.
IntActiP70351. 7 interactions.
STRINGi10090.ENSMUSP00000102906.

PTM databases

iPTMnetiP70351.
PhosphoSiteiP70351.

Proteomic databases

EPDiP70351.
MaxQBiP70351.
PaxDbiP70351.
PeptideAtlasiP70351.
PRIDEiP70351.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000100417; ENSMUSP00000097984; ENSMUSG00000006920. [P70351-2]
ENSMUST00000107284; ENSMUSP00000102905; ENSMUSG00000006920. [P70351-1]
GeneIDi14055.
KEGGimmu:14055.
UCSCiuc007lnw.3. mouse. [P70351-2]
uc011yfk.2. mouse. [P70351-1]

Organism-specific databases

CTDi2145.
MGIiMGI:1097695. Ezh1.

Phylogenomic databases

eggNOGiKOG1079. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00760000119228.
HOVERGENiHBG002453.
InParanoidiP70351.
KOiK17451.
OrthoDBiEOG7VB2DR.
PhylomeDBiP70351.
TreeFamiTF314509.

Miscellaneous databases

PROiP70351.
SOURCEiSearch...

Gene expression databases

BgeeiP70351.
CleanExiMM_EZH1.
GenevisibleiP70351. MM.

Family and domain databases

InterProiIPR026489. CXC_dom.
IPR032926. EZH1.
IPR021654. EZH1/EZH2.
IPR001005. SANT/Myb.
IPR001214. SET_dom.
IPR033467. Tesmin/TSO1-like_CXC.
[Graphical view]
PANTHERiPTHR22884:SF333. PTHR22884:SF333. 1 hit.
PfamiPF11616. EZH2_WD-Binding. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM01114. CXC. 1 hit.
SM00717. SANT. 2 hits.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51633. CXC. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian homologues of the Polycomb-group gene Enhancer of zeste mediate gene silencing in Drosophila heterochromatin and at S. cerevisiae telomeres."
    Laible G., Wolf A., Dorn R., Reuter G., Nislow C., Lebersorger A., Popkin D., Pillus L., Jenuwein T.
    EMBO J. 16:3219-3232(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning and expression of a human/mouse Polycomb group gene, ENX-2/Enx-2."
    Ogawa M., Hiraoka Y., Taniguchi K., Aiso S.
    Biochim. Biophys. Acta 1395:151-158(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
  3. "The murine polycomb-group genes ezh1 and ezh2 map close to hox gene clusters on mouse chromosomes 11 and 6."
    Laible G., Haynes A.R., Lebersorger A., O'Carroll D., Mattei M.-G., Denny P., Brown S.D.M., Jenuwein T.
    Mamm. Genome 10:311-314(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  4. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
    Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
    Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: ILS and ISS.
  5. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Aorta, Cerebellum, Corpora quadrigemina, Hippocampus and Vein.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    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).
    Strain: FVB/N.
    Tissue: Mammary tumor.
  9. "EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency."
    Shen X., Liu Y., Hsu Y.-J., Fujiwara Y., Kim J., Mao X., Yuan G.-C., Orkin S.H.
    Mol. Cell 32:491-502(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
  10. "Polycomb-like 2 associates with PRC2 and regulates transcriptional networks during mouse embryonic stem cell self-renewal and differentiation."
    Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K., Torchia J., Krogan N.J., Reiter J.F., Stanford W.L.
    Cell Stem Cell 6:153-166(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PRC2 COMPLEX.

Entry informationi

Entry nameiEZH1_MOUSE
AccessioniPrimary (citable) accession number: P70351
Secondary accession number(s): A2A4K5
, Q3TPR1, Q3U3V5, Q3UU02, Q8BR85, Q922L1, Q9R089
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: July 6, 2016
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.