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Protein

Doublecortin domain-containing protein 2

Gene

DCDC2

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

Functioni

Protein that plays a role in the inhibition of canonical Wnt signaling pathway. May be involved in neuronal migration during development of the cerebral neocortex. Involved in the control of ciliogenesis and ciliary length (PubMed:25601850).By similarity2 Publications

GO - Biological processi

  • cell projection organization Source: UniProtKB-KW
  • cellular defense response Source: ProtInc
  • intracellular signal transduction Source: InterPro
  • neuron migration Source: UniProtKB
  • positive regulation of smoothened signaling pathway Source: GO_Central
  • regulation of cilium assembly Source: UniProtKB
  • regulation of Wnt signaling pathway Source: UniProtKB
  • sensory perception of sound Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Neurogenesis

Names & Taxonomyi

Protein namesi
Recommended name:
Doublecortin domain-containing protein 2
Alternative name(s):
Protein RU2S
Gene namesi
Name:DCDC2
Synonyms:KIAA1154, RU2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:18141. DCDC2.

Subcellular locationi

GO - Cellular componenti

  • axoneme Source: UniProtKB
  • cytoplasm Source: GO_Central
  • cytoskeleton Source: UniProtKB-SubCell
  • kinocilium Source: UniProtKB
  • nucleus Source: HPA
  • primary cilium Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Dyslexia 2 (DYX2)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA relatively common, complex cognitive disorder characterized by an impairment of reading performance despite adequate motivational, educational and intellectual opportunities. It is a multifactorial trait, with evidence for familial clustering and heritability.
See also OMIM:600202
Nephronophthisis 19 (NPHP19)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of nephronophthisis, an autosomal recessive disorder characterized by chronic tubulointerstitial nephritis resulting in end-stage renal disease. NPHP19 patients also manifest hepatosplenomegaly, hepatic fibrosis, destruction of the bile ducts, focal bile ductal proliferation, ductal plate malformation, and cholestasis.
See also OMIM:616217
Deafness, autosomal recessive, 66 (DFNB66)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
See also OMIM:610212
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti424 – 4241Q → P in DFNB66; results in ciliary abnormalities including increased ciliary length. 1 Publication
VAR_074667

Keywords - Diseasei

Ciliopathy, Deafness, Disease mutation, Nephronophthisis, Non-syndromic deafness

Organism-specific databases

MalaCardsiDCDC2.
MIMi600202. phenotype.
610212. phenotype.
616217. phenotype.
PharmGKBiPA134978716.

Polymorphism and mutation databases

BioMutaiDCDC2.
DMDMi147744557.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 476476Doublecortin domain-containing protein 2PRO_0000079804Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei270 – 2701PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UHG0.
MaxQBiQ9UHG0.
PaxDbiQ9UHG0.
PRIDEiQ9UHG0.

PTM databases

iPTMnetiQ9UHG0.
PhosphoSiteiQ9UHG0.

Expressioni

Tissue specificityi

Ubiquitously expressed. In brain, highly expressed in the entorhinal cortex, inferior temporal cortex, medial temporal cortex, hypothalamus, amygdala and hippocampus.2 Publications

Gene expression databases

BgeeiQ9UHG0.
CleanExiHS_DCDC2.
ExpressionAtlasiQ9UHG0. baseline and differential.
GenevisibleiQ9UHG0. HS.

Organism-specific databases

HPAiHPA031582.
HPA031583.

Interactioni

Subunit structurei

Interacts with DVL1, DVL2 and DVL3.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MRFAP1Q9Y6053EBI-10303987,EBI-995714
NIF3L1Q9GZT83EBI-10303987,EBI-740897

Protein-protein interaction databases

BioGridi119558. 4 interactions.
IntActiQ9UHG0. 3 interactions.
STRINGi9606.ENSP00000367715.

Structurei

Secondary structure

1
476
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi139 – 1435Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi154 – 1585Combined sources
Helixi160 – 1634Combined sources
Helixi166 – 17611Combined sources
Beta strandi186 – 1894Combined sources
Beta strandi194 – 1974Combined sources
Beta strandi206 – 2105Combined sources
Helixi221 – 2244Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DNFNMR-A132-226[»]
ProteinModelPortaliQ9UHG0.
SMRiQ9UHG0. Positions 17-99, 132-226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UHG0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 10084Doublecortin 1PROSITE-ProRule annotationAdd
BLAST
Domaini139 – 22183Doublecortin 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 doublecortin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3757. Eukaryota.
ENOG410ZE6Q. LUCA.
GeneTreeiENSGT00510000046928.
HOGENOMiHOG000082435.
HOVERGENiHBG051319.
InParanoidiQ9UHG0.
OMAiKRPMEVV.
OrthoDBiEOG78D7K5.
PhylomeDBiQ9UHG0.
TreeFamiTF338406.

Family and domain databases

Gene3Di3.10.20.230. 2 hits.
InterProiIPR033036. DCDC2.
IPR003533. Doublecortin_dom.
[Graphical view]
PANTHERiPTHR23004:SF5. PTHR23004:SF5. 1 hit.
PfamiPF03607. DCX. 2 hits.
[Graphical view]
SMARTiSM00537. DCX. 2 hits.
[Graphical view]
PROSITEiPS50309. DC. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UHG0-1) [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
MSGSSARSSH LSQPVVKSVL VYRNGDPFYA GRRVVIHEKK VSSFEVFLKE
60 70 80 90 100
VTGGVQAPFG AVRNIYTPRT GHRIRKLDQI QSGGNYVAGG QEAFKKLNYL
110 120 130 140 150
DIGEIKKRPM EVVNTEVKPV IHSRINVSAR FRKPLQEPCT IFLIANGDLI
160 170 180 190 200
NPASRLLIPR KTLNQWDHVL QMVTEKITLR SGAVHRLYTL EGKLVESGAE
210 220 230 240 250
LENGQFYVAV GRDKFKKLPY SELLFDKSTM RRPFGQKASS LPPIVGSRKS
260 270 280 290 300
KGSGNDRHSK STVGSSDNSS PQPLKRKGKK EDVNSEKLTK LKQNVKLKNS
310 320 330 340 350
QETIPNSDEG IFKAGAERSE TRGAAEVQED EDTQVEVPVD QRPAEIVDEE
360 370 380 390 400
EDGEKANKDA EQKEDFSGMN GDLEEEGGRE ATDAPEQVEE ILDHSEQQAR
410 420 430 440 450
PARVNGGTDE ENGEELQQVN NELQLVLDKE RKSQGAGSGQ DEADVDPQRP
460 470
PRPEVKITSP EENENNQQNK DYAAVA
Length:476
Mass (Da):52,834
Last modified:May 15, 2007 - v2
Checksum:i50DD06EA2FB9BD53
GO
Isoform 2 (identifier: Q9UHG0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-247: Missing.
     248-307: RKSKGSGNDR...KNSQETIPNS → MKMWNNWGWC...FDFHCVFVSI

Note: No experimental confirmation available.
Show »
Length:229
Mass (Da):25,582
Checksum:iBAE1B1409AC4553E
GO

Sequence cautioni

The sequence CAB61371.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711G → D in AAH50704 (PubMed:15489334).Curated
Sequence conflicti370 – 3701N → K in CAB61371 (PubMed:17974005).Curated
Sequence conflicti424 – 4241Q → R in CAB61371 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti152 – 1521P → A.
Corresponds to variant rs33914824 [ dbSNP | Ensembl ].
VAR_050946
Natural varianti221 – 2211S → G.3 Publications
Corresponds to variant rs2274305 [ dbSNP | Ensembl ].
VAR_022890
Natural varianti424 – 4241Q → P in DFNB66; results in ciliary abnormalities including increased ciliary length. 1 Publication
VAR_074667
Natural varianti456 – 4561K → N.
Corresponds to variant rs9460973 [ dbSNP | Ensembl ].
VAR_050947

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 247247Missing in isoform 2. 1 PublicationVSP_014670Add
BLAST
Alternative sequencei248 – 30760RKSKG…TIPNS → MKMWNNWGWCGGRRRGCTKI LSTKKGIQMSIKNKHLIVIP AFSHTMSQLDFDFHCVFVSI in isoform 2. 1 PublicationVSP_014671Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF181720 Genomic DNA. Translation: AAF23610.1.
AF181721 mRNA. Translation: AAF23612.1.
AB032980 mRNA. Translation: BAA86468.2.
AL133043 mRNA. Translation: CAB61371.1. Different initiation.
AL359389 Genomic DNA. No translation available.
AL359713 Genomic DNA. No translation available.
FO393410 Genomic DNA. No translation available.
BC050704 mRNA. Translation: AAH50704.1.
CCDSiCCDS4550.1. [Q9UHG0-1]
PIRiT42643.
RefSeqiNP_001182539.1. NM_001195610.1. [Q9UHG0-1]
NP_057440.2. NM_016356.4. [Q9UHG0-1]
UniGeneiHs.61345.

Genome annotation databases

EnsembliENST00000378450; ENSP00000367711; ENSG00000146038. [Q9UHG0-2]
ENST00000378454; ENSP00000367715; ENSG00000146038. [Q9UHG0-1]
GeneIDi51473.
KEGGihsa:51473.
UCSCiuc003ndx.4. human. [Q9UHG0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF181720 Genomic DNA. Translation: AAF23610.1.
AF181721 mRNA. Translation: AAF23612.1.
AB032980 mRNA. Translation: BAA86468.2.
AL133043 mRNA. Translation: CAB61371.1. Different initiation.
AL359389 Genomic DNA. No translation available.
AL359713 Genomic DNA. No translation available.
FO393410 Genomic DNA. No translation available.
BC050704 mRNA. Translation: AAH50704.1.
CCDSiCCDS4550.1. [Q9UHG0-1]
PIRiT42643.
RefSeqiNP_001182539.1. NM_001195610.1. [Q9UHG0-1]
NP_057440.2. NM_016356.4. [Q9UHG0-1]
UniGeneiHs.61345.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DNFNMR-A132-226[»]
ProteinModelPortaliQ9UHG0.
SMRiQ9UHG0. Positions 17-99, 132-226.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119558. 4 interactions.
IntActiQ9UHG0. 3 interactions.
STRINGi9606.ENSP00000367715.

PTM databases

iPTMnetiQ9UHG0.
PhosphoSiteiQ9UHG0.

Polymorphism and mutation databases

BioMutaiDCDC2.
DMDMi147744557.

Proteomic databases

EPDiQ9UHG0.
MaxQBiQ9UHG0.
PaxDbiQ9UHG0.
PRIDEiQ9UHG0.

Protocols and materials databases

DNASUi51473.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378450; ENSP00000367711; ENSG00000146038. [Q9UHG0-2]
ENST00000378454; ENSP00000367715; ENSG00000146038. [Q9UHG0-1]
GeneIDi51473.
KEGGihsa:51473.
UCSCiuc003ndx.4. human. [Q9UHG0-1]

Organism-specific databases

CTDi51473.
GeneCardsiDCDC2.
HGNCiHGNC:18141. DCDC2.
HPAiHPA031582.
HPA031583.
MalaCardsiDCDC2.
MIMi600202. phenotype.
605755. gene.
610212. phenotype.
616217. phenotype.
neXtProtiNX_Q9UHG0.
PharmGKBiPA134978716.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3757. Eukaryota.
ENOG410ZE6Q. LUCA.
GeneTreeiENSGT00510000046928.
HOGENOMiHOG000082435.
HOVERGENiHBG051319.
InParanoidiQ9UHG0.
OMAiKRPMEVV.
OrthoDBiEOG78D7K5.
PhylomeDBiQ9UHG0.
TreeFamiTF338406.

Miscellaneous databases

ChiTaRSiDCDC2. human.
EvolutionaryTraceiQ9UHG0.
GeneWikiiDCDC2.
GenomeRNAii51473.
PROiQ9UHG0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UHG0.
CleanExiHS_DCDC2.
ExpressionAtlasiQ9UHG0. baseline and differential.
GenevisibleiQ9UHG0. HS.

Family and domain databases

Gene3Di3.10.20.230. 2 hits.
InterProiIPR033036. DCDC2.
IPR003533. Doublecortin_dom.
[Graphical view]
PANTHERiPTHR23004:SF5. PTHR23004:SF5. 1 hit.
PfamiPF03607. DCX. 2 hits.
[Graphical view]
SMARTiSM00537. DCX. 2 hits.
[Graphical view]
PROSITEiPS50309. DC. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A new antigen recognized by cytolytic T lymphocytes on a human kidney tumor results from reverse strand transcription."
    Van den Eynde B.J., Gaugler B., Probst-Kepper M., Michaux L., Devuyst O., Lorge F., Weynants P., Boon T.
    J. Exp. Med. 190:1793-1800(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT GLY-221.
  2. "Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain."
    Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.
    DNA Res. 6:329-336(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT GLY-221.
    Tissue: Brain.
  3. "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.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal brain.
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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), VARIANT GLY-221.
    Tissue: Colon.
  7. Cited for: INVOLVEMENT IN DYX2, TISSUE SPECIFICITY.
  8. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DVL1; DVL2 AND DVL3, INVOLVEMENT IN NPHP19.
  9. "A missense mutation in DCDC2 causes human recessive deafness DFNB66, likely by interfering with sensory hair cell and supporting cell cilia length regulation."
    Grati M., Chakchouk I., Ma Q., Bensaid M., Desmidt A., Turki N., Yan D., Baanannou A., Mittal R., Driss N., Blanton S., Farooq A., Lu Z., Liu X.Z., Masmoudi S.
    Hum. Mol. Genet. 24:2482-2491(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN DFNB66, VARIANT DFNB66 PRO-424, CHARACTERIZATION OF VARIANT DFNB66 PRO-424.
  10. "Solution structure of RSGI RUH-062, a DCX domain from human."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 132-226.

Entry informationi

Entry nameiDCDC2_HUMAN
AccessioniPrimary (citable) accession number: Q9UHG0
Secondary accession number(s): Q5VTR8
, Q5VTR9, Q86W35, Q9UFD1, Q9UHG1, Q9ULR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: May 15, 2007
Last modified: June 8, 2016
This is version 128 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, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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.