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Protein

Nuclear receptor coactivator 5

Gene

NCOA5

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

Functioni

Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2).1 Publication

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. glucose homeostasis Source: Ensembl
  2. negative regulation of insulin receptor signaling pathway Source: Ensembl
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor coactivator 5
Short name:
NCoA-5
Alternative name(s):
Coactivator independent of AF-2
Short name:
CIA
Gene namesi
Name:NCOA5
Synonyms:KIAA1637
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:15909. NCOA5.

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: HPA
  2. extracellular space Source: UniProtKB
  3. nucleoplasm Source: HPA
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi342 – 3421I → A: Abolishes E2-inducible strong interaction with ESR1, but not basal interaction. 1 Publication
Mutagenesisi348 – 3492LL → AA: Abolishes interaction with ESR1. 1 Publication

Organism-specific databases

PharmGKBiPA31474.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 579579Nuclear receptor coactivator 5PRO_0000094411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei3 – 31Phosphothreonine1 Publication
Modified residuei9 – 91Phosphoserine2 Publications
Modified residuei29 – 291Phosphoserine1 Publication
Modified residuei34 – 341Phosphoserine1 Publication
Modified residuei126 – 1261Phosphoserine1 Publication
Modified residuei151 – 1511Phosphoserine1 Publication
Modified residuei378 – 3781Phosphoserine1 Publication
Modified residuei381 – 3811Phosphoserine5 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9HCD5.
PaxDbiQ9HCD5.
PRIDEiQ9HCD5.

PTM databases

PhosphoSiteiQ9HCD5.

Miscellaneous databases

PMAP-CutDBQ9HCD5.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

BgeeiQ9HCD5.
CleanExiHS_NCOA5.
ExpressionAtlasiQ9HCD5. baseline and differential.
GenevestigatoriQ9HCD5.

Organism-specific databases

HPAiHPA050231.

Interactioni

Subunit structurei

Binds HTATIP2/TIP30. Interacts with YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and PPP1CA.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Nr1d2Q606742EBI-2863498,EBI-5326205From a different organism.

Protein-protein interaction databases

BioGridi121747. 26 interactions.
IntActiQ9HCD5. 7 interactions.
STRINGi9606.ENSP00000290231.

Structurei

Secondary structure

1
579
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi200 – 2078Combined sources
Helixi208 – 2103Combined sources
Helixi211 – 22111Combined sources
Turni222 – 2243Combined sources
Beta strandi227 – 2315Combined sources
Helixi238 – 24811Combined sources
Beta strandi251 – 2566Combined sources
Helixi258 – 2636Combined sources
Beta strandi265 – 2706Combined sources
Beta strandi272 – 2743Combined sources
Beta strandi277 – 2826Combined sources
Helixi283 – 30220Combined sources
Beta strandi304 – 3063Combined sources
Helixi345 – 3506Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V95NMR-A197-313[»]
2J7XX-ray2.10B338-354[»]
2J7YX-ray1.80B338-354[»]
ProteinModelPortaliQ9HCD5.
SMRiQ9HCD5. Positions 197-314.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HCD5.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 158158Transcription repressionAdd
BLAST
Regioni458 – 579122Transcription activationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi345 – 3495LXXLL motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi7 – 150144Arg/Asp-rich (mixed charge)Add
BLAST

Domaini

Contains one Leu-Xaa-Xaa-Leu-Leu (LxxLL) motif that is essential for the association with nuclear receptors.

Phylogenomic databases

eggNOGiNOG147049.
GeneTreeiENSGT00530000064134.
HOVERGENiHBG052585.
InParanoidiQ9HCD5.
OMAiGSARNMG.
OrthoDBiEOG7GTT6B.
PhylomeDBiQ9HCD5.
TreeFamiTF324704.

Family and domain databases

Gene3Di3.40.50.800. 1 hit.
InterProiIPR004154. Anticodon-bd.
[Graphical view]
SUPFAMiSSF52954. SSF52954. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HCD5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTAPSRPSP TRRDPYGFGD SRDSRRDRSP IRGSPRREPR DGRNGRDARD
60 70 80 90 100
SRDIRDPRDL RDHRHSRDLR DHRDSRSVRD VRDVRDLRDF RDLRDSRDFR
110 120 130 140 150
DQRDPMYDRY RDMRDSRDPM YRREGSYDRY LRMDDYCRRK DDSYFDRYRD
160 170 180 190 200
SFDGRGPPGP ESQSRAKERL KREERRREEL YRQYFEEIQR RFDAERPVDC
210 220 230 240 250
SVIVVNKQTK DYAESVGRKV RDLGMVVDLI FLNTEVSLSQ ALEDVSRGGS
260 270 280 290 300
PFAIVITQQH QIHRSCTVNI MFGTPQEHRN MPQADAMVLV ARNYERYKNE
310 320 330 340 350
CREKEREEIA RQAAKMADEA ILQERERGGP EEGVRGGHPP AIQSLINLLA
360 370 380 390 400
DNRYLTAEET DKIINYLRER KERLMRSSTD SLPGPISRQP LGATSGASLK
410 420 430 440 450
TQPSSQPLQS GQVLPSATPT PSAPPTSQQE LQAKILSLFN SGTVTANSSS
460 470 480 490 500
ASPSVAAGNT PNQNFSTAAN SQPQQRSQAS GNQPPSILGQ GGSAQNMGPR
510 520 530 540 550
PGAPSQGLFG QPSSRLAPAS NMTSQRPVSS TGINFDNPSV QKALDTLIQS
560 570
GPALSHLVSQ TTAQMGQPQA PMGSYQRHY
Length:579
Mass (Da):65,536
Last modified:February 12, 2003 - v2
Checksum:iD2ADCCEBEE566A91
GO

Sequence cautioni

The sequence AAG36793.1 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti326 – 3261E → G.
Corresponds to variant rs11549557 [ dbSNP | Ensembl ].
VAR_053530

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF230533 mRNA. Translation: AAG36793.1. Different initiation.
AF470686 mRNA. Translation: AAO33457.1.
AL035662, AL162458 Genomic DNA. Translation: CAI42972.1.
AL162458, AL035662 Genomic DNA. Translation: CAH74052.1.
CH471077 Genomic DNA. Translation: EAW75765.1.
CH471077 Genomic DNA. Translation: EAW75769.1.
BC140836 mRNA. Translation: AAI40837.1.
BC151133 mRNA. Translation: AAI51134.1.
AB046857 mRNA. Translation: BAB13463.1.
CCDSiCCDS13392.1.
RefSeqiNP_066018.1. NM_020967.2.
UniGeneiHs.654991.

Genome annotation databases

EnsembliENST00000290231; ENSP00000290231; ENSG00000124160.
GeneIDi57727.
KEGGihsa:57727.
UCSCiuc002xrd.3. human.

Polymorphism databases

DMDMi28380083.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF230533 mRNA. Translation: AAG36793.1. Different initiation.
AF470686 mRNA. Translation: AAO33457.1.
AL035662, AL162458 Genomic DNA. Translation: CAI42972.1.
AL162458, AL035662 Genomic DNA. Translation: CAH74052.1.
CH471077 Genomic DNA. Translation: EAW75765.1.
CH471077 Genomic DNA. Translation: EAW75769.1.
BC140836 mRNA. Translation: AAI40837.1.
BC151133 mRNA. Translation: AAI51134.1.
AB046857 mRNA. Translation: BAB13463.1.
CCDSiCCDS13392.1.
RefSeqiNP_066018.1. NM_020967.2.
UniGeneiHs.654991.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V95NMR-A197-313[»]
2J7XX-ray2.10B338-354[»]
2J7YX-ray1.80B338-354[»]
ProteinModelPortaliQ9HCD5.
SMRiQ9HCD5. Positions 197-314.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121747. 26 interactions.
IntActiQ9HCD5. 7 interactions.
STRINGi9606.ENSP00000290231.

PTM databases

PhosphoSiteiQ9HCD5.

Polymorphism databases

DMDMi28380083.

Proteomic databases

MaxQBiQ9HCD5.
PaxDbiQ9HCD5.
PRIDEiQ9HCD5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000290231; ENSP00000290231; ENSG00000124160.
GeneIDi57727.
KEGGihsa:57727.
UCSCiuc002xrd.3. human.

Organism-specific databases

CTDi57727.
GeneCardsiGC20M044690.
HGNCiHGNC:15909. NCOA5.
HPAiHPA050231.
neXtProtiNX_Q9HCD5.
PharmGKBiPA31474.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG147049.
GeneTreeiENSGT00530000064134.
HOVERGENiHBG052585.
InParanoidiQ9HCD5.
OMAiGSARNMG.
OrthoDBiEOG7GTT6B.
PhylomeDBiQ9HCD5.
TreeFamiTF324704.

Miscellaneous databases

ChiTaRSiNCOA5. human.
EvolutionaryTraceiQ9HCD5.
GeneWikiiNCOA5.
GenomeRNAii57727.
NextBioi64672.
PMAP-CutDBQ9HCD5.
PROiQ9HCD5.

Gene expression databases

BgeeiQ9HCD5.
CleanExiHS_NCOA5.
ExpressionAtlasiQ9HCD5. baseline and differential.
GenevestigatoriQ9HCD5.

Family and domain databases

Gene3Di3.40.50.800. 1 hit.
InterProiIPR004154. Anticodon-bd.
[Graphical view]
SUPFAMiSSF52954. SSF52954. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CIA, a novel estrogen receptor coactivator with a bifunctional nuclear receptor interacting determinant."
    Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F., Giguere V.
    Mol. Cell. Biol. 21:343-353(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH ESR1; ESR2 AND NR1D2, MUTAGENESIS OF ILE-342 AND 348-LEU-LEU-349.
    Tissue: Fetal kidney.
  2. "TIP30 interacts with an estrogen receptor alpha-interacting coactivator CIA and regulates c-myc transcription."
    Jiang C., Ito M., Piening V., Bruck K., Roeder R.G., Xiao H.
    J. Biol. Chem. 279:27781-27789(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 86-91 AND 280-292, FUNCTION, INTERACTION WITH HTATIP2.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Brain.
  6. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
    DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-579.
    Tissue: Brain.
  7. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G."
    Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.
    Biochim. Biophys. Acta 1774:1339-1350(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH ILF2; ILF3; YLPM1; KHDRBS1; RBMX AND PPP1CA, INTERACTION WITH YLPM1.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3; SER-9; SER-29; SER-34; SER-378 AND SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-126 AND SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "Solution structure of anticodon binding domain from nuclear receptor coactivator 5 (human KIAA1637 protein)."
    RIKEN structural genomics initiative (RSGI)
    Submitted (JUL-2004) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 197-313.

Entry informationi

Entry nameiNCOA5_HUMAN
AccessioniPrimary (citable) accession number: Q9HCD5
Secondary accession number(s): B2RTV9
, E1P5R0, Q6HA99, Q9H1F2, Q9H2T2, Q9H4Y9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: February 12, 2003
Last modified: March 4, 2015
This is version 116 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

External Data

Dasty 3

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 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.