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Protein

Alpha-(1,6)-fucosyltransferase

Gene

FUT8

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

Functioni

Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans.2 Publications

Catalytic activityi

GDP-beta-L-fucose + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl-beta-D-glucosaminyl)asparagine = GDP + N(4)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-(N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6))-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-(alpha-L-fucosyl-(1->6))-N-acetyl-beta-D-glucosaminyl)asparagine.1 Publication

Pathwayi: protein glycosylation

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

GO - Molecular functioni

  • glycoprotein 6-alpha-L-fucosyltransferase activity Source: UniProtKB

GO - Biological processi

  • cell migration Source: Ensembl
  • GDP-L-fucose metabolic process Source: UniProtKB
  • integrin-mediated signaling pathway Source: Ensembl
  • in utero embryonic development Source: UniProtKB
  • L-fucose catabolic process Source: UniProtKB
  • N-glycan processing Source: UniProtKB
  • oligosaccharide biosynthetic process Source: ProtInc
  • protein glycosylation in Golgi Source: InterPro
  • protein N-linked glycosylation Source: ProtInc
  • protein N-linked glycosylation via asparagine Source: UniProtKB
  • receptor metabolic process Source: Ensembl
  • regulation of cellular response to oxidative stress Source: Ensembl
  • regulation of gene expression Source: Ensembl
  • respiratory gaseous exchange Source: Ensembl
  • transforming growth factor beta receptor signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciZFISH:HS00491-MONOMER.
BRENDAi2.4.1.68. 2681.
ReactomeiR-HSA-975578. Reactions specific to the complex N-glycan synthesis pathway.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiGT23. Glycosyltransferase Family 23.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-(1,6)-fucosyltransferase (EC:2.4.1.68)
Short name:
Alpha1-6FucT
Alternative name(s):
Fucosyltransferase 8
GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase
GDP-fucose--glycoprotein fucosyltransferase
Glycoprotein 6-alpha-L-fucosyltransferase
Gene namesi
Name:FUT8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:4019. FUT8.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 9CytoplasmicSequence analysis9
Transmembranei10 – 30Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST21
Topological domaini31 – 575LumenalSequence analysisAdd BLAST545

GO - Cellular componenti

  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: UniProtKB
  • Golgi cisterna membrane Source: UniProtKB-SubCell
  • Golgi membrane Source: Reactome
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi365R → A or K: Complete loss of activity. 2 Publications1
Mutagenesisi366R → A or K: Decreases activity to 3%. 1 Publication1
Mutagenesisi368D → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi369K → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi373E → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi382Y → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi409D → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi410D → A: No effect on enzyme activity. 1 Publication1
Mutagenesisi453D → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi469S → A: Loss of enzyme activity. 1 Publication1

Organism-specific databases

DisGeNETi2530.
OpenTargetsiENSG00000033170.
PharmGKBiPA28435.

Chemistry databases

ChEMBLiCHEMBL3596087.

Polymorphism and mutation databases

BioMutaiFUT8.
DMDMi20138326.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000805261 – 575Alpha-(1,6)-fucosyltransferaseAdd BLAST575

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi204 ↔ 2661 Publication
Disulfide bondi212 ↔ 2301 Publication
Disulfide bondi218 ↔ 2221 Publication
Modified residuei278PhosphoserineBy similarity1
Disulfide bondi465 ↔ 4721 Publication

Post-translational modificationi

Tyrosine phosphorylated by PKDCC/VLK.1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

EPDiQ9BYC5.
MaxQBiQ9BYC5.
PaxDbiQ9BYC5.
PeptideAtlasiQ9BYC5.
PRIDEiQ9BYC5.

PTM databases

iPTMnetiQ9BYC5.
PhosphoSitePlusiQ9BYC5.

Expressioni

Gene expression databases

BgeeiENSG00000033170.
CleanExiHS_FUT8.
ExpressionAtlasiQ9BYC5. baseline and differential.
GenevisibleiQ9BYC5. HS.

Organism-specific databases

HPAiCAB017129.
HPA040863.
HPA043410.

Interactioni

Protein-protein interaction databases

BioGridi108806. 28 interactors.
IntActiQ9BYC5. 2 interactors.
STRINGi9606.ENSP00000353910.

Structurei

Secondary structure

1575
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi110 – 138Combined sources29
Helixi142 – 172Combined sources31
Turni173 – 175Combined sources3
Helixi176 – 199Combined sources24
Helixi204 – 206Combined sources3
Beta strandi209 – 213Combined sources5
Helixi220 – 236Combined sources17
Beta strandi240 – 244Combined sources5
Helixi255 – 257Combined sources3
Helixi282 – 285Combined sources4
Beta strandi287 – 291Combined sources5
Helixi294 – 296Combined sources3
Helixi310 – 312Combined sources3
Helixi313 – 319Combined sources7
Helixi323 – 335Combined sources13
Helixi340 – 353Combined sources14
Beta strandi357 – 364Combined sources8
Helixi379 – 394Combined sources16
Beta strandi403 – 409Combined sources7
Helixi411 – 420Combined sources10
Beta strandi424 – 427Combined sources4
Helixi437 – 441Combined sources5
Helixi446 – 459Combined sources14
Beta strandi460 – 465Combined sources6
Helixi470 – 479Combined sources10
Beta strandi482 – 484Combined sources3
Beta strandi490 – 494Combined sources5
Beta strandi506 – 509Combined sources4
Beta strandi528 – 534Combined sources7
Beta strandi536 – 544Combined sources9
Turni545 – 547Combined sources3
Beta strandi550 – 554Combined sources5
Helixi555 – 557Combined sources3
Beta strandi558 – 560Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DE0X-ray2.61X68-575[»]
ProteinModelPortaliQ9BYC5.
SMRiQ9BYC5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BYC5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini206 – 493GT23PROSITE-ProRule annotationAdd BLAST288
Domaini502 – 563SH3Add BLAST62

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni365 – 366Important for donor substrate binding2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi299 – 305SH3-bindingSequence analysis7

Sequence similaritiesi

Belongs to the glycosyltransferase 23 family.PROSITE-ProRule annotation
Contains 1 GT23 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.Curated

Keywords - Domaini

SH3 domain, SH3-binding, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3705. Eukaryota.
ENOG410YHM8. LUCA.
GeneTreeiENSGT00530000063737.
HOGENOMiHOG000204276.
HOVERGENiHBG028260.
InParanoidiQ9BYC5.
KOiK00717.
OMAiNARKLVC.
OrthoDBiEOG091G05GD.
PhylomeDBiQ9BYC5.
TreeFamiTF106108.

Family and domain databases

InterProiIPR015827. Alpha1_6FUT_euk.
IPR027350. GT23_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF14604. SH3_9. 1 hit.
[Graphical view]
PIRSFiPIRSF000472. Alpha1_6FUT_euk. 1 hit.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51659. GT23. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BYC5-1) [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
MRPWTGSWRW IMLILFAWGT LLFYIGGHLV RDNDHPDHSS RELSKILAKL
60 70 80 90 100
ERLKQQNEDL RRMAESLRIP EGPIDQGPAI GRVRVLEEQL VKAKEQIENY
110 120 130 140 150
KKQTRNGLGK DHEILRRRIE NGAKELWFFL QSELKKLKNL EGNELQRHAD
160 170 180 190 200
EFLLDLGHHE RSIMTDLYYL SQTDGAGDWR EKEAKDLTEL VQRRITYLQN
210 220 230 240 250
PKDCSKAKKL VCNINKGCGY GCQLHHVVYC FMIAYGTQRT LILESQNWRY
260 270 280 290 300
ATGGWETVFR PVSETCTDRS GISTGHWSGE VKDKNVQVVE LPIVDSLHPR
310 320 330 340 350
PPYLPLAVPE DLADRLVRVH GDPAVWWVSQ FVKYLIRPQP WLEKEIEEAT
360 370 380 390 400
KKLGFKHPVI GVHVRRTDKV GTEAAFHPIE EYMVHVEEHF QLLARRMQVD
410 420 430 440 450
KKRVYLATDD PSLLKEAKTK YPNYEFISDN SISWSAGLHN RYTENSLRGV
460 470 480 490 500
ILDIHFLSQA DFLVCTFSSQ VCRVAYEIMQ TLHPDASANF HSLDDIYYFG
510 520 530 540 550
GQNAHNQIAI YAHQPRTADE IPMEPGDIIG VAGNHWDGYS KGVNRKLGRT
560 570
GLYPSYKVRE KIETVKYPTY PEAEK
Length:575
Mass (Da):66,516
Last modified:March 5, 2002 - v2
Checksum:i5AE24A93881E18D0
GO
Isoform 2 (identifier: Q9BYC5-2) [UniParc]FASTAAdd to basket
Also known as: Retinal

The sequence of this isoform differs from the canonical sequence as follows:
     280-329: EVKDKNVQVV...HGDPAVWWVS → TPIMNLLVITLFPGQLDCTIDTQKIHFVE
     330-575: Missing.

Show »
Length:308
Mass (Da):35,795
Checksum:iFB52A33CFD91A366
GO
Isoform 3 (identifier: Q9BYC5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-163: Missing.

Show »
Length:412
Mass (Da):47,255
Checksum:i837F36AF48E7E4C3
GO
Isoform 4 (identifier: Q9BYC5-4) [UniParc]FASTAAdd to basket
Also known as: Retina-1, Retina-2

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MRPWTGSWRWIMLI → MHRQIWHLHWTLVR
     15-420: Missing.

Note: Seems to be only expressed in retina, inactive as a fucosyltransferase.
Show »
Length:169
Mass (Da):19,520
Checksum:i0ACD43AA0F56AB31
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti214I → T in BAG57538 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_054038101K → Q.Corresponds to variant rs2229678dbSNPEnsembl.1
Natural variantiVAR_033537267T → K.Corresponds to variant rs35949016dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0468371 – 163Missing in isoform 3. 1 PublicationAdd BLAST163
Alternative sequenceiVSP_0533611 – 14MRPWT…WIMLI → MHRQIWHLHWTLVR in isoform 4. 2 PublicationsAdd BLAST14
Alternative sequenceiVSP_05336215 – 420Missing in isoform 4. 2 PublicationsAdd BLAST406
Alternative sequenceiVSP_001807280 – 329EVKDK…VWWVS → TPIMNLLVITLFPGQLDCTI DTQKIHFVE in isoform 2. 1 PublicationAdd BLAST50
Alternative sequenceiVSP_001808330 – 575Missing in isoform 2. 1 PublicationAdd BLAST246

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89289 mRNA. Translation: BAA19764.1.
AH005745 Genomic DNA. Translation: AAB92372.2.
Y17979 mRNA. Translation: CAA76988.1.
Y17976 mRNA. Translation: CAA76985.1.
Y17977 mRNA. Translation: CAA76986.1.
Y17978 mRNA. Translation: CAA76987.1.
AB049828 Genomic DNA. Translation: BAB40975.1.
AB049740 mRNA. Translation: BAB40929.2.
AB032573 Genomic DNA. Translation: BAA92859.2.
AB032573 Genomic DNA. Translation: BAA92858.1.
AJ514324 mRNA. Translation: CAD55804.1.
AJ514325 mRNA. Translation: CAD55805.1.
AK294242 mRNA. Translation: BAG57538.1.
AL109847 Genomic DNA. No translation available.
AL161871 Genomic DNA. No translation available.
AL355840 Genomic DNA. No translation available.
AL359236 Genomic DNA. No translation available.
BC093889 mRNA. Translation: AAH93889.1.
BC101816 mRNA. Translation: AAI01817.1.
CCDSiCCDS9775.1. [Q9BYC5-1]
CCDS9776.2. [Q9BYC5-3]
PIRiJC5432.
RefSeqiNP_004471.4. NM_004480.4. [Q9BYC5-3]
NP_835368.1. NM_178155.2. [Q9BYC5-1]
NP_835369.1. NM_178156.2. [Q9BYC5-1]
UniGeneiHs.597649.
Hs.654961.

Genome annotation databases

EnsembliENST00000342677; ENSP00000345865; ENSG00000033170. [Q9BYC5-2]
ENST00000360689; ENSP00000353910; ENSG00000033170. [Q9BYC5-1]
ENST00000394586; ENSP00000378087; ENSG00000033170. [Q9BYC5-1]
ENST00000557164; ENSP00000452433; ENSG00000033170. [Q9BYC5-3]
GeneIDi2530.
KEGGihsa:2530.
UCSCiuc001xin.3. human. [Q9BYC5-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Fucosyltransferase 8

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D89289 mRNA. Translation: BAA19764.1.
AH005745 Genomic DNA. Translation: AAB92372.2.
Y17979 mRNA. Translation: CAA76988.1.
Y17976 mRNA. Translation: CAA76985.1.
Y17977 mRNA. Translation: CAA76986.1.
Y17978 mRNA. Translation: CAA76987.1.
AB049828 Genomic DNA. Translation: BAB40975.1.
AB049740 mRNA. Translation: BAB40929.2.
AB032573 Genomic DNA. Translation: BAA92859.2.
AB032573 Genomic DNA. Translation: BAA92858.1.
AJ514324 mRNA. Translation: CAD55804.1.
AJ514325 mRNA. Translation: CAD55805.1.
AK294242 mRNA. Translation: BAG57538.1.
AL109847 Genomic DNA. No translation available.
AL161871 Genomic DNA. No translation available.
AL355840 Genomic DNA. No translation available.
AL359236 Genomic DNA. No translation available.
BC093889 mRNA. Translation: AAH93889.1.
BC101816 mRNA. Translation: AAI01817.1.
CCDSiCCDS9775.1. [Q9BYC5-1]
CCDS9776.2. [Q9BYC5-3]
PIRiJC5432.
RefSeqiNP_004471.4. NM_004480.4. [Q9BYC5-3]
NP_835368.1. NM_178155.2. [Q9BYC5-1]
NP_835369.1. NM_178156.2. [Q9BYC5-1]
UniGeneiHs.597649.
Hs.654961.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DE0X-ray2.61X68-575[»]
ProteinModelPortaliQ9BYC5.
SMRiQ9BYC5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108806. 28 interactors.
IntActiQ9BYC5. 2 interactors.
STRINGi9606.ENSP00000353910.

Chemistry databases

ChEMBLiCHEMBL3596087.

Protein family/group databases

CAZyiGT23. Glycosyltransferase Family 23.

PTM databases

iPTMnetiQ9BYC5.
PhosphoSitePlusiQ9BYC5.

Polymorphism and mutation databases

BioMutaiFUT8.
DMDMi20138326.

Proteomic databases

EPDiQ9BYC5.
MaxQBiQ9BYC5.
PaxDbiQ9BYC5.
PeptideAtlasiQ9BYC5.
PRIDEiQ9BYC5.

Protocols and materials databases

DNASUi2530.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342677; ENSP00000345865; ENSG00000033170. [Q9BYC5-2]
ENST00000360689; ENSP00000353910; ENSG00000033170. [Q9BYC5-1]
ENST00000394586; ENSP00000378087; ENSG00000033170. [Q9BYC5-1]
ENST00000557164; ENSP00000452433; ENSG00000033170. [Q9BYC5-3]
GeneIDi2530.
KEGGihsa:2530.
UCSCiuc001xin.3. human. [Q9BYC5-1]

Organism-specific databases

CTDi2530.
DisGeNETi2530.
GeneCardsiFUT8.
HGNCiHGNC:4019. FUT8.
HPAiCAB017129.
HPA040863.
HPA043410.
MIMi602589. gene.
neXtProtiNX_Q9BYC5.
OpenTargetsiENSG00000033170.
PharmGKBiPA28435.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3705. Eukaryota.
ENOG410YHM8. LUCA.
GeneTreeiENSGT00530000063737.
HOGENOMiHOG000204276.
HOVERGENiHBG028260.
InParanoidiQ9BYC5.
KOiK00717.
OMAiNARKLVC.
OrthoDBiEOG091G05GD.
PhylomeDBiQ9BYC5.
TreeFamiTF106108.

Enzyme and pathway databases

UniPathwayiUPA00378.
BioCyciZFISH:HS00491-MONOMER.
BRENDAi2.4.1.68. 2681.
ReactomeiR-HSA-975578. Reactions specific to the complex N-glycan synthesis pathway.

Miscellaneous databases

ChiTaRSiFUT8. human.
EvolutionaryTraceiQ9BYC5.
GeneWikiiFUT8.
GenomeRNAii2530.
PROiQ9BYC5.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000033170.
CleanExiHS_FUT8.
ExpressionAtlasiQ9BYC5. baseline and differential.
GenevisibleiQ9BYC5. HS.

Family and domain databases

InterProiIPR015827. Alpha1_6FUT_euk.
IPR027350. GT23_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF14604. SH3_9. 1 hit.
[Graphical view]
PIRSFiPIRSF000472. Alpha1_6FUT_euk. 1 hit.
SMARTiSM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS51659. GT23. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFUT8_HUMAN
AccessioniPrimary (citable) accession number: Q9BYC5
Secondary accession number(s): B4DFS7
, G3V5N0, O00235, Q8IUA5, Q9BYC6, Q9P2U5, Q9P2U6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: November 30, 2016
This is version 158 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 14
    Human chromosome 14: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.