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Protein

Segment polarity protein dishevelled homolog DVL-2

Gene

DVL2

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

Functioni

Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Participates both in canonical and non-canonical Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling.By similarity1 Publication

GO - Molecular functioni

  • frizzled binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Wnt signaling pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000004975-MONOMER.
ReactomeiR-HSA-201681. TCF dependent signaling in response to WNT.
R-HSA-201688. WNT mediated activation of DVL.
R-HSA-2028269. Signaling by Hippo.
R-HSA-4086400. PCP/CE pathway.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641258. Degradation of DVL.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5099900. WNT5A-dependent internalization of FZD4.
R-HSA-5368598. Negative regulation of TCF-dependent signaling by DVL-interacting proteins.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiO14641.
SIGNORiO14641.

Names & Taxonomyi

Protein namesi
Recommended name:
Segment polarity protein dishevelled homolog DVL-2
Short name:
Dishevelled-2
Alternative name(s):
DSH homolog 2
Gene namesi
Name:DVL2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:3086. DVL2.

Subcellular locationi

  • Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Cytoplasmcytosol By similarity
  • Cytoplasmic vesicle By similarity
  • Nucleus 1 Publication

  • Note: Localizes at the cell membrane upon interaction with frizzled family members and promotes their internalization. Localizes to cytoplasmic puncta (By similarity). Interaction with FOXK1 and FOXK2 induces nuclear translocation (PubMed:25805136).By similarity1 Publication

GO - Cellular componenti

  • apical part of cell Source: Ensembl
  • clathrin-coated endocytic vesicle Source: Reactome
  • cytoplasm Source: BHF-UCL
  • cytoplasmic vesicle Source: MGI
  • cytosol Source: GO_Central
  • lateral plasma membrane Source: Ensembl
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi250 – 252TSS → AAA: Almost abolishes interaction with FOXK2. 1 Publication3
Mutagenesisi250T → A: No effect on interaction with FOXK2. 1 Publication1
Mutagenesisi251S → A: No effect on interaction with FOXK2. 1 Publication1
Mutagenesisi252S → A: Almost abolishes interaction with FOXK2. 1 Publication1
Mutagenesisi254 – 257SSVT → AAVA: Almost abolishes interaction with FOXK2. 1 Publication4
Mutagenesisi254S → A: Reduces interaction with FOXK2. 1 Publication1
Mutagenesisi255S → A: Almost abolishes interaction with FOXK2. 1 Publication1
Mutagenesisi257T → A: Almost abolishes interaction with FOXK2. 1 Publication1
Mutagenesisi259 – 262STMS → AAMA: Almost abolishes interaction with FOXK2. 1 Publication4
Mutagenesisi259S → A: Almost abolishes interaction with FOXK2. 1 Publication1
Mutagenesisi260T → A: No effect on interaction with FOXK2. 1 Publication1
Mutagenesisi262S → A: Almost abolishes interaction with FOXK2. 1 Publication1
Mutagenesisi267 – 269TVT → AVA: Almost abolishes interaction with FOXK2. 1 Publication3
Mutagenesisi267T → A: Almost abolishes interaction with FOXK2. 1 Publication1
Mutagenesisi269T → A: Almost abolishes interaction with FOXK2. 1 Publication1
Mutagenesisi275Y → F: No effect on interaction with FOXK2. 1 Publication1
Mutagenesisi281S → A: No effect on interaction with FOXK2. 1 Publication1
Mutagenesisi286S → A: No effect on interaction with FOXK2. 1 Publication1
Mutagenesisi295Y → F: No effect on interaction with FOXK2. 1 Publication1
Mutagenesisi298S → A: No effect on interaction with FOXK2. 1 Publication1
Mutagenesisi329S → A: No effect on interaction with FOXK2. 1 Publication1

Organism-specific databases

DisGeNETi1856.
OpenTargetsiENSG00000004975.
PharmGKBiPA27542.

Chemistry databases

ChEMBLiCHEMBL1255125.

Polymorphism and mutation databases

BioMutaiDVL2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001457461 – 736Segment polarity protein dishevelled homolog DVL-2Add BLAST736

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei37Omega-N-methylarginineBy similarity1
Modified residuei59PhosphoserineBy similarity1
Modified residuei143PhosphoserineBy similarity1
Modified residuei211PhosphoserineCombined sources1
Modified residuei231Omega-N-methylarginineBy similarity1
Modified residuei289Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei289Symmetric dimethylarginine; alternateBy similarity1
Modified residuei364PhosphothreonineBy similarity1
Modified residuei632Symmetric dimethylarginineBy similarity1
Modified residuei717PhosphoserineBy similarity1
Modified residuei718Dimethylated arginine; alternateBy similarity1
Modified residuei718Omega-N-methylarginine; alternateBy similarity1
Modified residuei720PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated by CSNK1D (PubMed:21422228, PubMed:9192851). WNT3A induces DVL2 phosphorylation by CSNK1E and MARK kinases (PubMed:25805136).3 Publications

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiO14641.
MaxQBiO14641.
PaxDbiO14641.
PeptideAtlasiO14641.
PRIDEiO14641.

PTM databases

iPTMnetiO14641.
PhosphoSitePlusiO14641.

Expressioni

Gene expression databases

BgeeiENSG00000004975.
CleanExiHS_DVL2.
ExpressionAtlasiO14641. baseline and differential.
GenevisibleiO14641. HS.

Organism-specific databases

HPAiCAB009312.
HPA021611.
HPA022914.
HPA064732.

Interactioni

Subunit structurei

Interacts through its PDZ domain with the C-terminal regions of VANGL1 and VANGL2. Interacts with Rac. Interacts with ARRB1; the interaction is enhanced by phosphorylation of DVL1 (By similarity). Can form large oligomers (via DIX domain). Interacts (via DIX domain) with DIXDC1 (via DIX domain). Interacts (via DEP domain) with AP2M1 and the AP-2 complex (By similarity). Interacts with DACT1 and FAM105B/otulin. Interacts with DCDC2. Interacts (when phosphorylated) with FOXK1 and FOXK2; the interaction induces DVL2 nuclear translocation (PubMed:25805136).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-740850,EBI-740850
APCP250542EBI-740850,EBI-727707
CK1EQ5R2U32EBI-740850,EBI-9106301
DACT1Q9NYF06EBI-740850,EBI-3951744
DIXDC1Q155Q32EBI-740850,EBI-1104700
LRRK2Q5S0073EBI-740850,EBI-5323863
Pard6aQ9Z1016EBI-740850,EBI-81732From a different organism.
Smurf2A2A5Z68EBI-740850,EBI-2348309From a different organism.
TIFAQ96CG33EBI-740850,EBI-740711
TP53P046374EBI-740850,EBI-366083
TRIM29Q141345EBI-740850,EBI-702370
WWTR1Q9GZV54EBI-740850,EBI-747743
ZNF165P499102EBI-740850,EBI-741694

GO - Molecular functioni

  • frizzled binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108189. 130 interactors.
DIPiDIP-34433N.
IntActiO14641. 141 interactors.
MINTiMINT-1435227.
STRINGi9606.ENSP00000005340.

Chemistry databases

BindingDBiO14641.

Structurei

Secondary structure

1736
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 20Combined sources7
Beta strandi27 – 33Combined sources7
Turni35 – 37Combined sources3
Helixi40 – 47Combined sources8
Beta strandi54 – 61Combined sources8
Turni62 – 64Combined sources3
Beta strandi65 – 71Combined sources7
Beta strandi84 – 90Combined sources7
Beta strandi265 – 270Combined sources6
Helixi272 – 275Combined sources4
Beta strandi280 – 285Combined sources6
Beta strandi293 – 299Combined sources7
Helixi304 – 308Combined sources5
Beta strandi316 – 320Combined sources5
Helixi330 – 341Combined sources12
Beta strandi343 – 345Combined sources3
Beta strandi347 – 352Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2REYX-ray1.55A261-355[»]
3CBXX-ray1.70A/B264-354[»]
3CBYX-ray1.50A/B264-354[»]
3CBZX-ray1.38A264-354[»]
3CC0X-ray1.75A/B/C264-354[»]
4WIPX-ray2.69A/B/C12-106[»]
5LNPX-ray1.99A/B/C/D416-510[»]
5SUYX-ray1.88A/B/C/D416-510[»]
5SUZX-ray1.84A/B416-509[»]
ProteinModelPortaliO14641.
SMRiO14641.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14641.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 93DIXPROSITE-ProRule annotationAdd BLAST83
Domaini267 – 339PDZPROSITE-ProRule annotationAdd BLAST73
Domaini433 – 507DEPPROSITE-ProRule annotationAdd BLAST75

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni250 – 355Required for interaction with FOXK21 PublicationAdd BLAST106

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi7 – 12Poly-Gly6
Compositional biasi235 – 240Poly-Arg6
Compositional biasi686 – 694Poly-Pro9

Domaini

The DIX domain mediates homooligomerization.By similarity

Sequence similaritiesi

Belongs to the DSH family.Curated
Contains 1 DEP domain.PROSITE-ProRule annotation
Contains 1 DIX domain.PROSITE-ProRule annotation
Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3571. Eukaryota.
ENOG410Y5G4. LUCA.
GeneTreeiENSGT00390000013552.
HOGENOMiHOG000017084.
HOVERGENiHBG005542.
InParanoidiO14641.
KOiK02353.
OMAiSFHLAMG.
OrthoDBiEOG091G041O.
PhylomeDBiO14641.
TreeFamiTF318198.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR024580. Dishevelled_C-dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR015506. Dsh/Dvl-rel.
IPR008341. DVL2.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF8. PTHR10878:SF8. 1 hit.
PfamiPF00610. DEP. 1 hit.
PF02377. Dishevelled. 1 hit.
PF00778. DIX. 1 hit.
PF12316. Dsh_C. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSiPR01760. DISHEVELLED.
PR01762. DISHEVELLED2.
SMARTiSM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14641-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGSSTGGGG VGETKVIYHL DEEETPYLVK IPVPAERITL GDFKSVLQRP
60 70 80 90 100
AGAKYFFKSM DQDFGVVKEE ISDDNARLPC FNGRVVSWLV SSDNPQPEMA
110 120 130 140 150
PPVHEPRAEL APPAPPLPPL PPERTSGIGD SRPPSFHPNV SSSHENLEPE
160 170 180 190 200
TETESVVSLR RERPRRRDSS EHGAGGHRTG GPSRLERHLA GYESSSTLMT
210 220 230 240 250
SELESTSLGD SDEEDTMSRF SSSTEQSSAS RLLKRHRRRR KQRPPRLERT
260 270 280 290 300
SSFSSVTDST MSLNIITVTL NMEKYNFLGI SIVGQSNERG DGGIYIGSIM
310 320 330 340 350
KGGAVAADGR IEPGDMLLQV NDMNFENMSN DDAVRVLRDI VHKPGPIVLT
360 370 380 390 400
VAKCWDPSPQ AYFTLPRNEP IQPIDPAAWV SHSAALTGTF PAYPGSSSMS
410 420 430 440 450
TITSGSSLPD GCEGRGLSVH TDMASVTKAM AAPESGLEVR DRMWLKITIP
460 470 480 490 500
NAFLGSDVVD WLYHHVEGFP ERREARKYAS GLLKAGLIRH TVNKITFSEQ
510 520 530 540 550
CYYVFGDLSG GCESYLVNLS LNDNDGSSGA SDQDTLAPLP GATPWPLLPT
560 570 580 590 600
FSYQYPAPHP YSPQPPPYHE LSSYTYGGGS ASSQHSEGSR SSGSTRSDGG
610 620 630 640 650
AGRTGRPEER APESKSGSGS ESEPSSRGGS LRRGGEASGT SDGGPPPSRG
660 670 680 690 700
STGGAPNLRA HPGLHPYGPP PGMALPYNPM MVVMMPPPPP PVPPAVQPPG
710 720 730
APPVRDLGSV PPELTASRQS FHMAMGNPSE FFVDVM
Length:736
Mass (Da):78,948
Last modified:January 1, 1998 - v1
Checksum:i4BAD95B6C3FE531B
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_064708282I → T Found in a renal cell carcinoma case; somatic mutation. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006012 mRNA. Translation: AAB65243.1.
BT009822 mRNA. Translation: AAP88824.1.
CH471108 Genomic DNA. Translation: EAW90244.1.
CH471108 Genomic DNA. Translation: EAW90245.1.
BC014844 mRNA. Translation: AAH14844.1.
CCDSiCCDS11091.1.
RefSeqiNP_004413.1. NM_004422.2.
UniGeneiHs.118640.

Genome annotation databases

EnsembliENST00000005340; ENSP00000005340; ENSG00000004975.
GeneIDi1856.
KEGGihsa:1856.
UCSCiuc002gez.2. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006012 mRNA. Translation: AAB65243.1.
BT009822 mRNA. Translation: AAP88824.1.
CH471108 Genomic DNA. Translation: EAW90244.1.
CH471108 Genomic DNA. Translation: EAW90245.1.
BC014844 mRNA. Translation: AAH14844.1.
CCDSiCCDS11091.1.
RefSeqiNP_004413.1. NM_004422.2.
UniGeneiHs.118640.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2REYX-ray1.55A261-355[»]
3CBXX-ray1.70A/B264-354[»]
3CBYX-ray1.50A/B264-354[»]
3CBZX-ray1.38A264-354[»]
3CC0X-ray1.75A/B/C264-354[»]
4WIPX-ray2.69A/B/C12-106[»]
5LNPX-ray1.99A/B/C/D416-510[»]
5SUYX-ray1.88A/B/C/D416-510[»]
5SUZX-ray1.84A/B416-509[»]
ProteinModelPortaliO14641.
SMRiO14641.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108189. 130 interactors.
DIPiDIP-34433N.
IntActiO14641. 141 interactors.
MINTiMINT-1435227.
STRINGi9606.ENSP00000005340.

Chemistry databases

BindingDBiO14641.
ChEMBLiCHEMBL1255125.

PTM databases

iPTMnetiO14641.
PhosphoSitePlusiO14641.

Polymorphism and mutation databases

BioMutaiDVL2.

Proteomic databases

EPDiO14641.
MaxQBiO14641.
PaxDbiO14641.
PeptideAtlasiO14641.
PRIDEiO14641.

Protocols and materials databases

DNASUi1856.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000005340; ENSP00000005340; ENSG00000004975.
GeneIDi1856.
KEGGihsa:1856.
UCSCiuc002gez.2. human.

Organism-specific databases

CTDi1856.
DisGeNETi1856.
GeneCardsiDVL2.
HGNCiHGNC:3086. DVL2.
HPAiCAB009312.
HPA021611.
HPA022914.
HPA064732.
MIMi602151. gene.
neXtProtiNX_O14641.
OpenTargetsiENSG00000004975.
PharmGKBiPA27542.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3571. Eukaryota.
ENOG410Y5G4. LUCA.
GeneTreeiENSGT00390000013552.
HOGENOMiHOG000017084.
HOVERGENiHBG005542.
InParanoidiO14641.
KOiK02353.
OMAiSFHLAMG.
OrthoDBiEOG091G041O.
PhylomeDBiO14641.
TreeFamiTF318198.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000004975-MONOMER.
ReactomeiR-HSA-201681. TCF dependent signaling in response to WNT.
R-HSA-201688. WNT mediated activation of DVL.
R-HSA-2028269. Signaling by Hippo.
R-HSA-4086400. PCP/CE pathway.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641258. Degradation of DVL.
R-HSA-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.
R-HSA-5099900. WNT5A-dependent internalization of FZD4.
R-HSA-5368598. Negative regulation of TCF-dependent signaling by DVL-interacting proteins.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
SignaLinkiO14641.
SIGNORiO14641.

Miscellaneous databases

ChiTaRSiDVL2. human.
EvolutionaryTraceiO14641.
GeneWikiiDVL2.
GenomeRNAii1856.
PROiO14641.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000004975.
CleanExiHS_DVL2.
ExpressionAtlasiO14641. baseline and differential.
GenevisibleiO14641. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.30.42.10. 1 hit.
InterProiIPR000591. DEP_dom.
IPR024580. Dishevelled_C-dom.
IPR008339. Dishevelled_fam.
IPR003351. Dishevelled_protein_dom.
IPR001158. DIX.
IPR015506. Dsh/Dvl-rel.
IPR008341. DVL2.
IPR001478. PDZ.
IPR029071. Ubiquitin-rel_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR10878. PTHR10878. 1 hit.
PTHR10878:SF8. PTHR10878:SF8. 1 hit.
PfamiPF00610. DEP. 1 hit.
PF02377. Dishevelled. 1 hit.
PF00778. DIX. 1 hit.
PF12316. Dsh_C. 1 hit.
PF00595. PDZ. 1 hit.
[Graphical view]
PRINTSiPR01760. DISHEVELLED.
PR01762. DISHEVELLED2.
SMARTiSM00021. DAX. 1 hit.
SM00049. DEP. 1 hit.
SM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF54236. SSF54236. 1 hit.
PROSITEiPS50186. DEP. 1 hit.
PS50841. DIX. 1 hit.
PS50106. PDZ. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDVL2_HUMAN
AccessioniPrimary (citable) accession number: O14641
Secondary accession number(s): D3DTN3, Q53XM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 30, 2016
This is version 172 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 17
    Human chromosome 17: 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.