Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

ADP-ribosylation factor-like protein 2-binding protein

Gene

ARL2BP

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

Functioni

Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2.1 Publication

GO - Molecular functioni

  • GTPase regulator activity Source: ProtInc
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • maintenance of protein location in nucleus Source: UniProtKB
  • positive regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
  • regulation of insulin secretion Source: Reactome
  • signal transduction Source: ProtInc
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-422356. Regulation of insulin secretion.

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-ribosylation factor-like protein 2-binding protein
Short name:
ARF-like 2-binding protein
Short name:
ARL2-binding protein
Alternative name(s):
Binder of ARF2 protein 1
Gene namesi
Name:ARL2BP
Synonyms:BART, BART1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:17146. ARL2BP.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cilium Source: UniProtKB-KW
  • cytosol Source: Reactome
  • midbody Source: UniProtKB
  • mitochondrial intermembrane space Source: UniProtKB
  • mitochondrial matrix Source: Reactome
  • nucleus Source: UniProtKB-SubCell
  • spindle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Retinitis pigmentosa with or without situs inversus (RPSI)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by variable association of retinitis pigmentosa with situs inversus. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Situs inversus is a congenital abnormality in which organs in the thorax and the abdomen are opposite to their normal positions due to lateral transposition.
See also OMIM:615434
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451M → R in RPSI; drastic decrease ARL2-binding, diffuse cytoplasmic localization, no enrichement at cilia basal body. 1 Publication
Corresponds to variant rs398123053 [ dbSNP | Ensembl ].
VAR_070227

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi56 – 561E → A: Decreases interaction with ARL2. 1 Publication
Mutagenesisi57 – 571E → A: Decreases interaction with ARL2. 1 Publication
Mutagenesisi60 – 601L → A: Decreases interaction with ARL2.
Mutagenesisi74 – 741E → A: Decreases interaction with ARL2. 1 Publication
Mutagenesisi76 – 761Y → A: Decreases interaction with ARL2. 1 Publication
Mutagenesisi109 – 1091F → A: Decreases interaction with ARL2. 1 Publication
Mutagenesisi110 – 1101D → A: Decreases interaction with ARL2. 1 Publication
Mutagenesisi111 – 1111M → A: Does not decrease interaction with ARL2. 1 Publication
Mutagenesisi112 – 1121L → A: Decreases interaction with ARL2. 1 Publication
Mutagenesisi115 – 1151F → A: Decreases interaction with ARL2. 1 Publication

Keywords - Diseasei

Ciliopathy, Disease mutation

Organism-specific databases

MalaCardsiARL2BP.
MIMi615434. phenotype.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA134904608.

Polymorphism and mutation databases

BioMutaiARL2BP.
DMDMi74735245.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 163163ADP-ribosylation factor-like protein 2-binding proteinPRO_0000287113Add
BLAST

Proteomic databases

EPDiQ9Y2Y0.
MaxQBiQ9Y2Y0.
PaxDbiQ9Y2Y0.
PeptideAtlasiQ9Y2Y0.
PRIDEiQ9Y2Y0.
TopDownProteomicsiQ9Y2Y0-1. [Q9Y2Y0-1]

PTM databases

iPTMnetiQ9Y2Y0.
PhosphoSiteiQ9Y2Y0.

Expressioni

Tissue specificityi

Expressed in retina pigment epithelial cells (at protein level). Widely expressed.2 Publications

Gene expression databases

BgeeiQ9Y2Y0.
CleanExiHS_ARL2BP.
ExpressionAtlasiQ9Y2Y0. baseline and differential.
GenevisibleiQ9Y2Y0. HS.

Organism-specific databases

HPAiHPA043066.
HPA048440.

Interactioni

Subunit structurei

Found in a complex with ARL2BP, ARL2 and SLC25A6. Found in a complex with ARL2, ARL2BP and SLC25A4. Interacts with STAT2, STAT3 and STAT4. Interacts with GTP-bound ARL2 and ARL3; the complex ARL2-ARL2BP as well as ARL2BP alone, binds to ANT1. Interaction with ARL2 may be required for targeting to cilia basal body. Interacts with STAT3; interaction is enhanced with ARL2.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARL2P364045EBI-3449344,EBI-752365

Protein-protein interaction databases

BioGridi117110. 13 interactions.
DIPiDIP-48323N.
IntActiQ9Y2Y0. 4 interactions.
STRINGi9606.ENSP00000219204.

Structurei

Secondary structure

1
163
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 93Combined sources
Turni16 – 183Combined sources
Helixi20 – 3213Combined sources
Beta strandi33 – 353Combined sources
Helixi36 – 4813Combined sources
Helixi49 – 513Combined sources
Beta strandi54 – 585Combined sources
Helixi62 – 8423Combined sources
Helixi90 – 978Combined sources
Turni98 – 1003Combined sources
Turni101 – 1033Combined sources
Helixi109 – 1146Combined sources
Helixi118 – 13215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K9ANMR-A1-136[»]
3DOEX-ray2.25B1-163[»]
3DOFX-ray3.30B1-163[»]
ProteinModelPortaliQ9Y2Y0.
SMRiQ9Y2Y0. Positions 1-136.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y2Y0.

Family & Domainsi

Sequence similaritiesi

Belongs to the ARL2BP family.Curated

Phylogenomic databases

eggNOGiENOG410IKTQ. Eukaryota.
ENOG4111IGT. LUCA.
GeneTreeiENSGT00390000015052.
HOGENOMiHOG000024955.
HOVERGENiHBG105565.
InParanoidiQ9Y2Y0.
KOiK16742.
OMAiFMAFKEM.
OrthoDBiEOG7BCNDK.
PhylomeDBiQ9Y2Y0.
TreeFamiTF315143.

Family and domain databases

Gene3Di1.20.1520.10. 1 hit.
InterProiIPR023379. ARF-like_2-bdp_dom.
[Graphical view]
PfamiPF11527. ARL2_Bind_BART. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: Q9Y2Y0-1) [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
MDALEGESFA LSFSSASDAE FDAVVGYLED IIMDDEFQLL QRNFMDKYYL
60 70 80 90 100
EFEDTEENKL IYTPIFNEYI SLVEKYIEEQ LLQRIPEFNM AAFTTTLQHH
110 120 130 140 150
KDEVAGDIFD MLLTFTDFLA FKEMFLDYRA EKEGRGLDLS SGLVVTSLCK
160
SSSLPASQNN LRH
Length:163
Mass (Da):18,822
Last modified:November 1, 1999 - v1
Checksum:iE35EB5AC73FC1FEC
GO
Isoform 2 (identifier: Q9Y2Y0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-11: Missing.
     12-13: SF → MR

Note: No experimental confirmation available.
Show »
Length:152
Mass (Da):17,711
Checksum:i6CC6B4C0A11D35F4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271Y → C in AAH94878 (PubMed:15489334).Curated
Sequence conflicti50 – 501L → Q in AAH94878 (PubMed:15489334).Curated
Sequence conflicti61 – 611I → T in AAH94878 (PubMed:15489334).Curated
Sequence conflicti83 – 831Q → E in AAH94878 (PubMed:15489334).Curated
Sequence conflicti87 – 871E → G in AAH94878 (PubMed:15489334).Curated
Sequence conflicti154 – 1541L → T in AAH94878 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451M → R in RPSI; drastic decrease ARL2-binding, diffuse cytoplasmic localization, no enrichement at cilia basal body. 1 Publication
Corresponds to variant rs398123053 [ dbSNP | Ensembl ].
VAR_070227
Natural varianti87 – 871E → K.
Corresponds to variant rs7198865 [ dbSNP | Ensembl ].
VAR_053904

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1111Missing in isoform 2. 1 PublicationVSP_025317Add
BLAST
Alternative sequencei12 – 132SF → MR in isoform 2. 1 PublicationVSP_025318

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF126062 mRNA. Translation: AAD20633.1.
AK075050 mRNA. Translation: BAG52057.1.
CH471092 Genomic DNA. Translation: EAW82913.1.
BC003087 mRNA. Translation: AAH03087.1.
BC094878 mRNA. Translation: AAH94878.1.
CCDSiCCDS10776.1. [Q9Y2Y0-1]
RefSeqiNP_036238.1. NM_012106.3. [Q9Y2Y0-1]
UniGeneiHs.632873.
Hs.719024.

Genome annotation databases

EnsembliENST00000219204; ENSP00000219204; ENSG00000102931. [Q9Y2Y0-1]
GeneIDi23568.
KEGGihsa:23568.
UCSCiuc002elf.2. human. [Q9Y2Y0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF126062 mRNA. Translation: AAD20633.1.
AK075050 mRNA. Translation: BAG52057.1.
CH471092 Genomic DNA. Translation: EAW82913.1.
BC003087 mRNA. Translation: AAH03087.1.
BC094878 mRNA. Translation: AAH94878.1.
CCDSiCCDS10776.1. [Q9Y2Y0-1]
RefSeqiNP_036238.1. NM_012106.3. [Q9Y2Y0-1]
UniGeneiHs.632873.
Hs.719024.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K9ANMR-A1-136[»]
3DOEX-ray2.25B1-163[»]
3DOFX-ray3.30B1-163[»]
ProteinModelPortaliQ9Y2Y0.
SMRiQ9Y2Y0. Positions 1-136.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117110. 13 interactions.
DIPiDIP-48323N.
IntActiQ9Y2Y0. 4 interactions.
STRINGi9606.ENSP00000219204.

PTM databases

iPTMnetiQ9Y2Y0.
PhosphoSiteiQ9Y2Y0.

Polymorphism and mutation databases

BioMutaiARL2BP.
DMDMi74735245.

Proteomic databases

EPDiQ9Y2Y0.
MaxQBiQ9Y2Y0.
PaxDbiQ9Y2Y0.
PeptideAtlasiQ9Y2Y0.
PRIDEiQ9Y2Y0.
TopDownProteomicsiQ9Y2Y0-1. [Q9Y2Y0-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000219204; ENSP00000219204; ENSG00000102931. [Q9Y2Y0-1]
GeneIDi23568.
KEGGihsa:23568.
UCSCiuc002elf.2. human. [Q9Y2Y0-1]

Organism-specific databases

CTDi23568.
GeneCardsiARL2BP.
HGNCiHGNC:17146. ARL2BP.
HPAiHPA043066.
HPA048440.
MalaCardsiARL2BP.
MIMi615407. gene.
615434. phenotype.
neXtProtiNX_Q9Y2Y0.
Orphaneti791. Retinitis pigmentosa.
PharmGKBiPA134904608.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IKTQ. Eukaryota.
ENOG4111IGT. LUCA.
GeneTreeiENSGT00390000015052.
HOGENOMiHOG000024955.
HOVERGENiHBG105565.
InParanoidiQ9Y2Y0.
KOiK16742.
OMAiFMAFKEM.
OrthoDBiEOG7BCNDK.
PhylomeDBiQ9Y2Y0.
TreeFamiTF315143.

Enzyme and pathway databases

ReactomeiR-HSA-422356. Regulation of insulin secretion.

Miscellaneous databases

ChiTaRSiARL2BP. human.
EvolutionaryTraceiQ9Y2Y0.
GenomeRNAii23568.
PROiQ9Y2Y0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2Y0.
CleanExiHS_ARL2BP.
ExpressionAtlasiQ9Y2Y0. baseline and differential.
GenevisibleiQ9Y2Y0. HS.

Family and domain databases

Gene3Di1.20.1520.10. 1 hit.
InterProiIPR023379. ARF-like_2-bdp_dom.
[Graphical view]
PfamiPF11527. ARL2_Bind_BART. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning, and initial characterization."
    Sharer J.D., Kahn R.A.
    J. Biol. Chem. 274:27553-27561(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ARL2, TISSUE SPECIFICITY.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Ovary.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORMS 1 AND 2).
    Tissue: Brain and Mammary gland.
  5. "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: characterizing ARL1-binding proteins."
    Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.
    J. Biol. Chem. 276:22826-22837(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARL2 AND ARL3.
  6. "Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C."
    Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A., Cowan N.J.
    J. Biol. Chem. 277:14629-14634(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARL2 AND ARL3.
  7. "ARL2 and BART enter mitochondria and bind the adenine nucleotide transporter."
    Sharer J.D., Shern J.F., Van Valkenburgh H., Wallace D.C., Kahn R.A.
    Mol. Biol. Cell 13:71-83(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ANT1.
  8. "Arl2 and Arl3 regulate different microtubule-dependent processes."
    Zhou C., Cunningham L., Marcus A.I., Li Y., Kahn R.A.
    Mol. Biol. Cell 17:2476-2487(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. Cited for: FUNCTION, INTERACTION WITH STAT3 AND ARL2, SUBCELLULAR LOCATION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Erythroleukemia.
  12. "The structure of binder of Arl2 (BART) reveals a novel G protein binding domain: implications for function."
    Bailey L.K., Campbell L.J., Evetts K.A., Littlefield K., Rajendra E., Nietlispach D., Owen D., Mott H.R.
    J. Biol. Chem. 284:992-999(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-136, INTERACTION WITH ARL2.
  13. "Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition and binding mode of small GTPase with effector."
    Zhang T., Li S., Zhang Y., Zhong C., Lai Z., Ding J.
    Structure 17:602-610(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN A COMPLEX WITH ARL2; GTP AND MAGNESIUM IONS, INTERACTION WITH ARL2, MUTAGENESIS OF GLU-56; GLU-57; GLU-74; TYR-76; PHE-109; ASP-110; MET-111; LEU-112 AND PHE-115.
  14. Cited for: VARIANT RPSI ARG-45, INTERACTION WITH ARL2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiAR2BP_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2Y0
Secondary accession number(s): B3KQJ5, Q504R0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2007
Last sequence update: November 1, 1999
Last modified: July 6, 2016
This is version 117 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 16
    Human chromosome 16: 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.