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Protein

E3 ubiquitin-protein ligase RING1

Gene

Ring1

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

Functioni

Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity (By similarity).By similarity3 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri48 – 8841RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • chromatin binding Source: MGI
  • ligase activity Source: UniProtKB-KW
  • ubiquitin-protein transferase activator activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

  • anterior/posterior pattern specification Source: MGI
  • camera-type eye morphogenesis Source: MGI
  • histone H2A monoubiquitination Source: MGI
  • histone ubiquitination Source: MGI
  • negative regulation of transcription, DNA-templated Source: MGI
  • regulation of catalytic activity Source: GOC
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-2559580. Oxidative Stress Induced Senescence.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-4570464. SUMOylation of RNA binding proteins.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RING1 (EC:6.3.2.-)
Alternative name(s):
Polycomb complex protein RING1
RING finger protein 1
Transcription repressor Ring1A
Gene namesi
Name:Ring1
Synonyms:Ring1A, Rnf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1101770. Ring1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nuclear body Source: MGI
  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • PcG protein complex Source: MGI
  • PRC1 complex Source: MGI
  • sex chromatin Source: MGI
  • ubiquitin ligase complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406E3 ubiquitin-protein ligase RING1PRO_0000056386Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphothreonineBy similarity
Modified residuei38 – 381PhosphoserineCombined sources
Modified residuei140 – 1401PhosphoserineBy similarity
Modified residuei187 – 1871PhosphoserineBy similarity
Modified residuei190 – 1901PhosphoserineBy similarity
Modified residuei215 – 2151PhosphothreonineBy similarity
Modified residuei229 – 2291PhosphoserineBy similarity
Modified residuei232 – 2321PhosphoserineBy similarity
Modified residuei248 – 2481PhosphoserineBy similarity
Modified residuei254 – 2541PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO35730.
MaxQBiO35730.
PaxDbiO35730.
PRIDEiO35730.

PTM databases

iPTMnetiO35730.
PhosphoSiteiO35730.

Expressioni

Developmental stagei

Expressed in cells of the central nervous system (CNS) from 8.5 to 11.5 dpc. Expressed in the hindbrain (in the rhombomere boundaries) at 10.5 dpc. Expressed in CNS (ventricular zone and spinal cord), peripheral nervous system (PNS, sensory cranial and spinal ganglia), olfactory and tongue epithelia at 13.5 dpc. Expressed in CNS, thymus, various epithelial cell types including the olfactory, tooth and tongue epithelia at 15.5 dpc.1 Publication

Gene expression databases

BgeeiO35730.
CleanExiMM_RING1.
GenevisibleiO35730. MM.

Interactioni

Subunit structurei

Component of chromatin-associated Polycomb (PcG) complexes. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2/RING2 MBLR, L3MBTL2 and YAF2. Interacts with CBX2 and PCGF6. Component of a PRC1-like complex. Component of repressive BCOR complex containing Polycomb group subcomplex at least composed of RYBP, PCGF1, BCOR and RNF2/RING2. Interacts with PHC2, PCGF2, RNF2; CBX6, CBX7 and CBX8. Interacts with BMI1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Bmi1P259164EBI-929310,EBI-927401
Cbx8Q9QXV12EBI-929310,EBI-1216641
Phc2Q9QWH12EBI-929310,EBI-642357
Rnf2Q9CQJ43EBI-929310,EBI-927321
RybpQ8CCI54EBI-929310,EBI-929290

Protein-protein interaction databases

BioGridi202894. 35 interactions.
IntActiO35730. 34 interactions.
MINTiMINT-158295.
STRINGi10090.ENSMUSP00000025183.

Structurei

3D structure databases

ProteinModelPortaliO35730.
SMRiO35730. Positions 12-111, 261-403.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 234205Necessary for transcriptional repressionAdd
BLAST
Regioni230 – 406177Necessary for interaction with CBX2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi201 – 2044Nuclear localization signalBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi171 – 344174Gly-richAdd
BLAST
Compositional biasi246 – 25813Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri48 – 8841RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0311. Eukaryota.
ENOG410XQ5G. LUCA.
GeneTreeiENSGT00390000016977.
HOGENOMiHOG000273917.
HOVERGENiHBG079942.
InParanoidiO35730.
KOiK10695.
OMAiQSASKTW.
OrthoDBiEOG7NGQC3.
PhylomeDBiO35730.
TreeFamiTF105501.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR032443. RAWUL.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF16207. RAWUL. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 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: O35730-1) [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
MTTPANAQNA SKTWELSLYE LHRTPQEAIM DGTEIAVSPR SLHSELMCPI
60 70 80 90 100
CLDMLKNTMT TKECLHRFCS DCIVTALRSG NKECPTCRKK LVSKRSLRPD
110 120 130 140 150
PNFDALISKI YPSREEYEAH QDRVLIRLSR LHNQQALSSS IEEGLRMQAM
160 170 180 190 200
HRAQRVRRPM PGSDQTATMS GGEGEPGEGE GDGEDVSSDS APDSAPGPAP
210 220 230 240 250
KRPRGAGAGA SSVGTGGGAA GGACGGAGSE DSGDRGGTLG GGTLGPPSPP
260 270 280 290 300
GAPSPPEPGG EIELVFRPHP LLVEKGEYCQ TRYVKTTGNA TVDHLSKYLA
310 320 330 340 350
LRIALERRQQ QETTEPGGPG GGASDTGGPD GGGGERGVAG GGEGPEEPAL
360 370 380 390 400
PSLEGVSEKQ YTIYIAPGGG AFTTLNGSLT LELVNEKFWK VSRPLELCYA

PTKDPK
Length:406
Mass (Da):42,631
Last modified:April 4, 2006 - v2
Checksum:i4F274E976974A2D8
GO
Isoform 2 (identifier: O35730-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Show »
Length:377
Mass (Da):39,347
Checksum:iD278DFD6834AF01A
GO
Isoform 3 (identifier: O35730-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     153-183: AQRVRRPMPGSDQTATMSGGEGEPGEGEGDG → CGEPETLLPMGLVWSTGLIVCIRAARWRPCS
     184-406: Missing.

Show »
Length:183
Mass (Da):20,800
Checksum:i1467B829756F2106
GO

Sequence cautioni

The sequence AAH09070.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541M → V in CAJ18427 (Ref. 4) Curated
Sequence conflicti68 – 681F → L in CAJ18427 (Ref. 4) Curated
Sequence conflicti68 – 681F → L in AAH09070 (PubMed:15489334).Curated
Sequence conflicti314 – 3141T → A in BAE33300 (PubMed:16141072).Curated
Sequence conflicti314 – 3141T → A (Ref. 4) Curated
Sequence conflicti314 – 3141T → A in AAH09070 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929Missing in isoform 2. 1 PublicationVSP_017695Add
BLAST
Alternative sequencei153 – 18331AQRVR…GEGDG → CGEPETLLPMGLVWSTGLIV CIRAARWRPCS in isoform 3. 2 PublicationsVSP_017696Add
BLAST
Alternative sequencei184 – 406223Missing in isoform 3. 2 PublicationsVSP_017697Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12881 mRNA. Translation: CAA73381.1.
AF100956 Genomic DNA. Translation: AAC69901.1.
AK154962 mRNA. Translation: BAE32956.1.
AK155509 mRNA. Translation: BAE33300.1.
CT010219 mRNA. Translation: CAJ18427.1.
BC009070 mRNA. Translation: AAH09070.1. Different initiation.
BC082771 mRNA. Translation: AAH82771.1.
CCDSiCCDS50070.1. [O35730-1]
RefSeqiNP_033092.3. NM_009066.3. [O35730-1]
UniGeneiMm.20343.

Genome annotation databases

EnsembliENSMUST00000025183; ENSMUSP00000025183; ENSMUSG00000024325. [O35730-1]
GeneIDi19763.
KEGGimmu:19763.
UCSCiuc008cas.2. mouse. [O35730-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12881 mRNA. Translation: CAA73381.1.
AF100956 Genomic DNA. Translation: AAC69901.1.
AK154962 mRNA. Translation: BAE32956.1.
AK155509 mRNA. Translation: BAE33300.1.
CT010219 mRNA. Translation: CAJ18427.1.
BC009070 mRNA. Translation: AAH09070.1. Different initiation.
BC082771 mRNA. Translation: AAH82771.1.
CCDSiCCDS50070.1. [O35730-1]
RefSeqiNP_033092.3. NM_009066.3. [O35730-1]
UniGeneiMm.20343.

3D structure databases

ProteinModelPortaliO35730.
SMRiO35730. Positions 12-111, 261-403.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202894. 35 interactions.
IntActiO35730. 34 interactions.
MINTiMINT-158295.
STRINGi10090.ENSMUSP00000025183.

PTM databases

iPTMnetiO35730.
PhosphoSiteiO35730.

Proteomic databases

EPDiO35730.
MaxQBiO35730.
PaxDbiO35730.
PRIDEiO35730.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025183; ENSMUSP00000025183; ENSMUSG00000024325. [O35730-1]
GeneIDi19763.
KEGGimmu:19763.
UCSCiuc008cas.2. mouse. [O35730-1]

Organism-specific databases

CTDi6015.
MGIiMGI:1101770. Ring1.

Phylogenomic databases

eggNOGiKOG0311. Eukaryota.
ENOG410XQ5G. LUCA.
GeneTreeiENSGT00390000016977.
HOGENOMiHOG000273917.
HOVERGENiHBG079942.
InParanoidiO35730.
KOiK10695.
OMAiQSASKTW.
OrthoDBiEOG7NGQC3.
PhylomeDBiO35730.
TreeFamiTF105501.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-2559580. Oxidative Stress Induced Senescence.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-4570464. SUMOylation of RNA binding proteins.

Miscellaneous databases

PROiO35730.
SOURCEiSearch...

Gene expression databases

BgeeiO35730.
CleanExiMM_RING1.
GenevisibleiO35730. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR032443. RAWUL.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF16207. RAWUL. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain."
    Schoorlemmer J., Marcos-Gutierrez C., Were F., Martinez R., Garcia E., Satijn D.P.E., Otte A.P., Vidal M.
    EMBO J. 16:5930-5942(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN TRANSCRIPTION REPRESSION, INTERACTION WITH CBX2, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
    Strain: Swiss Webster / NIH.
    Tissue: Embryo.
  2. "Sequence of the mouse major histocomaptibility locus class II region."
    Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J., Lasky S., Hood L.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 129/SvJ.
  3. "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 3).
    Strain: NOD.
  4. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  5. "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] (ISOFORMS 1 AND 3).
    Strain: Czech II.
    Tissue: Embryo and Mammary gland.
  6. "Polycomb group proteins Ring1A/B link ubiquitylation of histone H2A to heritable gene silencing and X inactivation."
    de Napoles M., Mermoud J.E., Wakao R., Tang Y.A., Endoh M., Appanah R., Nesterova T.B., Silva J., Otte A.P., Vidal M., Koseki H., Brockdorff N.
    Dev. Cell 7:663-676(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, FUNCTION.
  7. "Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing."
    Cao R., Tsukada Y., Zhang Y.
    Mol. Cell 20:845-854(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: RECONSTITUTION OF A PRC1-LIKE COMPLEX, INTERACTION WITH BMI1; CBX8 AND PHC2.
  8. "Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b."
    Buchwald G., van der Stoop P., Weichenrieder O., Perrakis A., van Lohuizen M., Sixma T.K.
    EMBO J. 25:2465-2474(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BMI1, SUBUNIT.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pancreas and Testis.

Entry informationi

Entry nameiRING1_MOUSE
AccessioniPrimary (citable) accession number: O35730
Secondary accession number(s): Q3U242
, Q3U333, Q4FK33, Q63ZX8, Q921Z8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2005
Last sequence update: April 4, 2006
Last modified: June 8, 2016
This is version 135 of the entry and version 2 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.