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Protein

Formin-binding protein 1

Gene

FNBP1

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

Functioni

May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL.By similarity5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei166Mediates end-to-end attachment of dimers1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-HSA-8856828. Clathrin-mediated endocytosis.

Names & Taxonomyi

Protein namesi
Recommended name:
Formin-binding protein 1
Alternative name(s):
Formin-binding protein 17
Short name:
hFBP17
Gene namesi
Name:FNBP1
Synonyms:FBP17, KIAA0554
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:17069. FNBP1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Lysosome, Membrane

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with KMT2A/MLL1. The relatively low incidence of the KMT2A/MLL1-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7L → E: Impairs membrane tubulation but does not affect lipid-binding. 1 Publication1
Mutagenesisi33K → E: Abolishes membrane invagination. 2 Publications1
Mutagenesisi33K → Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-35. 2 Publications1
Mutagenesisi35R → Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-33. 1 Publication1
Mutagenesisi51 – 52KK → QQ: Impairs lipid-binding and induction of membrane tubulation. 1 Publication2
Mutagenesisi113 – 114RK → QQ: Impairs lipid-binding and induction of membrane tubulation. 1 Publication2
Mutagenesisi165T → A: Abolishes membrane invagination. 1 Publication1
Mutagenesisi166K → A: Abolishes membrane invagination. 1 Publication1
Mutagenesisi168D → A, N or R: No significant effect. 1 Publication1
Mutagenesisi210P → A: Disrupts helix kink and moderately increases diameter of the induced tubular membrane. 1 Publication1
Mutagenesisi515 – 520Missing : Abrogates interaction with TNKS. 1 Publication6
Mutagenesisi515R → A: Impairs interaction with TNKS. 1 Publication1
Mutagenesisi519D → A: Impairs interaction with TNKS; when associated with A-515. 1 Publication1
Mutagenesisi602P → L: Abrogates interaction with DNM1, DNM2 and DNM3. 1 Publication1

Organism-specific databases

DisGeNETi23048.
OpenTargetsiENSG00000187239.
PharmGKBiPA128394597.

Polymorphism and mutation databases

BioMutaiFNBP1.
DMDMi118572321.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002614301 – 617Formin-binding protein 1Add BLAST617

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei66N6-acetyllysineCombined sources1
Modified residuei110N6-acetyllysineCombined sources1
Modified residuei296PhosphoserineCombined sources1
Modified residuei299PhosphoserineCombined sources1
Modified residuei349PhosphoserineCombined sources1
Modified residuei359PhosphoserineCombined sources1
Modified residuei497PhosphoserineBy similarity1
Modified residuei500PhosphotyrosineBy similarity1
Modified residuei521PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ96RU3.
MaxQBiQ96RU3.
PaxDbiQ96RU3.
PeptideAtlasiQ96RU3.
PRIDEiQ96RU3.

PTM databases

iPTMnetiQ96RU3.
PhosphoSitePlusiQ96RU3.

Miscellaneous databases

PMAP-CutDBQ96RU3.

Expressioni

Tissue specificityi

Very highly expressed in the epithelial cells of the gastrointestinal tract, respiratory, reproductive and urinary systems. Also highly expressed in brown adipose tissue, cardiomyocytes, enteric ganglia and glucagon producing cells of the pancreas. Expressed in germ cells of the testis and all regions of the brain.2 Publications

Gene expression databases

BgeeiENSG00000187239.
ExpressionAtlasiQ96RU3. baseline and differential.
GenevisibleiQ96RU3. HS.

Organism-specific databases

HPAiHPA019691.
HPA022119.

Interactioni

Subunit structurei

Interacts specifically with GTP-bound RND2 and CDC42. Interacts with PDE6G and microtubules (By similarity). Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, DNM2, DNM3, FASLG/FASL, SNX2 and WASL/N-WASP. May interact with TNKS.By similarity11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1111248,EBI-1111248
DNM1Q051935EBI-1111248,EBI-713135
FASLGP480234EBI-1111248,EBI-495538
GABARAPO951662EBI-1111248,EBI-712001
SNX2O607494EBI-1111248,EBI-1046690
TNKSO952714EBI-1111248,EBI-1105254

Protein-protein interaction databases

BioGridi116686. 25 interactors.
DIPiDIP-35355N.
IntActiQ96RU3. 19 interactors.
MINTiMINT-238223.
STRINGi9606.ENSP00000413625.

Structurei

Secondary structure

1617
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 6Combined sources4
Turni7 – 9Combined sources3
Helixi11 – 52Combined sources42
Helixi68 – 160Combined sources93
Helixi166 – 206Combined sources41
Helixi208 – 238Combined sources31
Helixi241 – 257Combined sources17
Helixi261 – 272Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EFLX-ray2.61A1-300[»]
ProteinModelPortaliQ96RU3.
SMRiQ96RU3.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96RU3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 264F-BARPROSITE-ProRule annotationAdd BLAST264
Repeati416 – 491REMAdd BLAST76
Domaini550 – 611SH3PROSITE-ProRule annotationAdd BLAST62

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 335Interaction with microtubulesBy similarityAdd BLAST335
Regioni1 – 79Required for self-association and induction of membrane tubulationAdd BLAST79
Regioni251 – 617Required for self-association and induction of membrane tubulationAdd BLAST367
Regioni400 – 552Interaction with RND2By similarityAdd BLAST153
Regioni495 – 617Interaction with PDE6GBy similarityAdd BLAST123
Regioni514 – 617Required for interaction with TNKS1 PublicationAdd BLAST104
Regioni535 – 617Interaction with DNM1 and DNM31 PublicationAdd BLAST83
Regioni550 – 617Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH22 PublicationsAdd BLAST68
Regioni553 – 610Interaction with FASLGAdd BLAST58
Regioni553 – 609Interaction with DNM2 and WASLAdd BLAST57

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili67 – 2591 PublicationAdd BLAST193
Coiled coili398 – 490By similarityAdd BLAST93

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi340 – 345Poly-Pro6

Domaini

The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation.1 Publication

Sequence similaritiesi

Belongs to the FNBP1 family.Curated
Contains 1 F-BAR domain.PROSITE-ProRule annotation
Contains 1 REM (Hr1) repeat.Curated
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

eggNOGiENOG410INNY. Eukaryota.
ENOG410ZU0I. LUCA.
GeneTreeiENSGT00510000046403.
HOGENOMiHOG000231767.
HOVERGENiHBG002489.
InParanoidiQ96RU3.
KOiK20121.
OMAiNQEQHEY.
OrthoDBiEOG091G038P.
PhylomeDBiQ96RU3.
TreeFamiTF351162.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028532. FNBP1/FBP17.
IPR014729. Rossmann-like_a/b/a_fold.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10663:SF157. PTHR10663:SF157. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q96RU3-1) [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
MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS
60 70 80 90 100
KKYQPKKNSK EEEEYKYTSC KAFISNLNEM NDYAGQHEVI SENMASQIIV
110 120 130 140 150
DLARYVQELK QERKSNFHDG RKAQQHIETC WKQLESSKRR FERDCKEADR
160 170 180 190 200
AQQYFEKMDA DINVTKADVE KARQQAQIRH QMAEDSKADY SSILQKFNHE
210 220 230 240 250
QHEYYHTHIP NIFQKIQEME ERRIVRMGES MKTYAEVDRQ VIPIIGKCLD
260 270 280 290 300
GIVKAAESID QKNDSQLVIE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL
310 320 330 340 350
SNSRGEGKPD LKFGGKSKGK LWPFIKKNKL MSLLTSPHQP PPPPPASASP
360 370 380 390 400
SAVPNGPQSP KQQKEPLSHR FNEFMTSKPK IHCFRSLKRG LSLKLGATPE
410 420 430 440 450
DFSNLPPEQR RKKLQQKVDE LNKEIQKEMD QRDAITKMKD VYLKNPQMGD
460 470 480 490 500
PASLDHKLAE VSQNIEKLRV ETQKFEAWLA EVEGRLPARS EQARRQSGLY
510 520 530 540 550
DSQNPPTVNN CAQDRESPDG SYTEEQSQES EMKVLATDFD DEFDDEEPLP
560 570 580 590 600
AIGTCKALYT FEGQNEGTIS VVEGETLYVI EEDKGDGWTR IRRNEDEEGY
610
VPTSYVEVCL DKNAKDS
Length:617
Mass (Da):71,307
Last modified:November 28, 2006 - v2
Checksum:iF06E847C6E631EC3
GO
Isoform 2 (identifier: Q96RU3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     391-395: Missing.
     616-617: DS → GAKTYI

Show »
Length:616
Mass (Da):71,184
Checksum:iE82282A5164793B3
GO
Isoform 3 (identifier: Q96RU3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     330-358: Missing.
     616-617: DS → GAKTYI

Show »
Length:592
Mass (Da):68,883
Checksum:i0CB6B44D9E174667
GO
Isoform 4 (identifier: Q96RU3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-394: Missing.

Show »
Length:551
Mass (Da):64,056
Checksum:iBA7F73CA1A28A467
GO
Isoform 5 (identifier: Q96RU3-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     391-395: Missing.

Note: No experimental confirmation available.
Show »
Length:612
Mass (Da):70,752
Checksum:i9E2543B3EDF09004
GO

Sequence cautioni

The sequence AAH62463 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAK49824 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA25480 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA91451 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAI12149 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI12150 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI13910 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI13911 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti388K → E in BAA91451 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029388490S → N.1 PublicationCorresponds to variant rs1023000dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_021693329 – 394Missing in isoform 4. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_021694330 – 358Missing in isoform 3. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_021695391 – 395Missing in isoform 2 and isoform 5. 2 Publications5
Alternative sequenceiVSP_021696616 – 617DS → GAKTYI in isoform 2 and isoform 3. 1 Publication2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF265550 mRNA. Translation: AAK49824.1. Different initiation.
AB011126 mRNA. Translation: BAA25480.1. Different initiation.
AK000975 mRNA. Translation: BAA91451.1. Different initiation.
AK023681 mRNA. Translation: BAB14638.1.
AL136141, AL158207 Genomic DNA. Translation: CAI12149.1. Sequence problems.
AL136141, AL158207 Genomic DNA. Translation: CAI12150.1. Sequence problems.
AL158207, AL136141 Genomic DNA. Translation: CAI13910.1. Sequence problems.
AL158207, AL136141 Genomic DNA. Translation: CAI13911.1. Sequence problems.
BC062463 mRNA. Translation: AAH62463.1. Sequence problems.
BC101755 mRNA. Translation: AAI01756.1.
BC143513 mRNA. Translation: AAI43514.1.
CCDSiCCDS48040.1. [Q96RU3-1]
RefSeqiNP_055848.1. NM_015033.2. [Q96RU3-1]
XP_005251880.1. XM_005251823.2. [Q96RU3-2]
XP_005251881.1. XM_005251824.2. [Q96RU3-5]
XP_005251886.1. XM_005251829.2. [Q96RU3-3]
UniGeneiHs.189409.

Genome annotation databases

EnsembliENST00000355681; ENSP00000347907; ENSG00000187239. [Q96RU3-3]
ENST00000420781; ENSP00000407548; ENSG00000187239. [Q96RU3-5]
ENST00000446176; ENSP00000413625; ENSG00000187239. [Q96RU3-1]
GeneIDi23048.
KEGGihsa:23048.
UCSCiuc004byw.2. human. [Q96RU3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF265550 mRNA. Translation: AAK49824.1. Different initiation.
AB011126 mRNA. Translation: BAA25480.1. Different initiation.
AK000975 mRNA. Translation: BAA91451.1. Different initiation.
AK023681 mRNA. Translation: BAB14638.1.
AL136141, AL158207 Genomic DNA. Translation: CAI12149.1. Sequence problems.
AL136141, AL158207 Genomic DNA. Translation: CAI12150.1. Sequence problems.
AL158207, AL136141 Genomic DNA. Translation: CAI13910.1. Sequence problems.
AL158207, AL136141 Genomic DNA. Translation: CAI13911.1. Sequence problems.
BC062463 mRNA. Translation: AAH62463.1. Sequence problems.
BC101755 mRNA. Translation: AAI01756.1.
BC143513 mRNA. Translation: AAI43514.1.
CCDSiCCDS48040.1. [Q96RU3-1]
RefSeqiNP_055848.1. NM_015033.2. [Q96RU3-1]
XP_005251880.1. XM_005251823.2. [Q96RU3-2]
XP_005251881.1. XM_005251824.2. [Q96RU3-5]
XP_005251886.1. XM_005251829.2. [Q96RU3-3]
UniGeneiHs.189409.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EFLX-ray2.61A1-300[»]
ProteinModelPortaliQ96RU3.
SMRiQ96RU3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116686. 25 interactors.
DIPiDIP-35355N.
IntActiQ96RU3. 19 interactors.
MINTiMINT-238223.
STRINGi9606.ENSP00000413625.

PTM databases

iPTMnetiQ96RU3.
PhosphoSitePlusiQ96RU3.

Polymorphism and mutation databases

BioMutaiFNBP1.
DMDMi118572321.

Proteomic databases

EPDiQ96RU3.
MaxQBiQ96RU3.
PaxDbiQ96RU3.
PeptideAtlasiQ96RU3.
PRIDEiQ96RU3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355681; ENSP00000347907; ENSG00000187239. [Q96RU3-3]
ENST00000420781; ENSP00000407548; ENSG00000187239. [Q96RU3-5]
ENST00000446176; ENSP00000413625; ENSG00000187239. [Q96RU3-1]
GeneIDi23048.
KEGGihsa:23048.
UCSCiuc004byw.2. human. [Q96RU3-1]

Organism-specific databases

CTDi23048.
DisGeNETi23048.
GeneCardsiFNBP1.
HGNCiHGNC:17069. FNBP1.
HPAiHPA019691.
HPA022119.
MIMi606191. gene.
neXtProtiNX_Q96RU3.
OpenTargetsiENSG00000187239.
PharmGKBiPA128394597.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410INNY. Eukaryota.
ENOG410ZU0I. LUCA.
GeneTreeiENSGT00510000046403.
HOGENOMiHOG000231767.
HOVERGENiHBG002489.
InParanoidiQ96RU3.
KOiK20121.
OMAiNQEQHEY.
OrthoDBiEOG091G038P.
PhylomeDBiQ96RU3.
TreeFamiTF351162.

Enzyme and pathway databases

ReactomeiR-HSA-8856828. Clathrin-mediated endocytosis.

Miscellaneous databases

ChiTaRSiFNBP1. human.
EvolutionaryTraceiQ96RU3.
GeneWikiiFNBP1.
GenomeRNAii23048.
PMAP-CutDBQ96RU3.
PROiQ96RU3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000187239.
ExpressionAtlasiQ96RU3. baseline and differential.
GenevisibleiQ96RU3. HS.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR031160. F_BAR.
IPR001060. FCH_dom.
IPR028532. FNBP1/FBP17.
IPR014729. Rossmann-like_a/b/a_fold.
IPR001452. SH3_domain.
[Graphical view]
PANTHERiPTHR10663:SF157. PTHR10663:SF157. 1 hit.
PfamiPF00611. FCH. 1 hit.
PF14604. SH3_9. 1 hit.
[Graphical view]
SMARTiSM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51741. F_BAR. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFNBP1_HUMAN
AccessioniPrimary (citable) accession number: Q96RU3
Secondary accession number(s): B7ZL12
, E9PGQ4, O60301, Q3MIN8, Q5TC87, Q5TC88, Q6P658, Q7LGG2, Q9H8H8, Q9NWD1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 28, 2006
Last modified: November 2, 2016
This is version 129 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 9
    Human chromosome 9: 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.