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Protein

B- and T-lymphocyte attenuator

Gene

BTLA

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

Functioni

Lymphocyte inhibitory receptor which inhibits lymphocytes during immune response.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Adaptive immunity, Immunity

Enzyme and pathway databases

ReactomeiREACT_19344. Costimulation by the CD28 family.

Names & Taxonomyi

Protein namesi
Recommended name:
B- and T-lymphocyte attenuator
Alternative name(s):
B- and T-lymphocyte-associated protein
CD_antigen: CD272
Gene namesi
Name:BTLA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:21087. BTLA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 157127ExtracellularSequence AnalysisAdd
BLAST
Transmembranei158 – 17821HelicalSequence AnalysisAdd
BLAST
Topological domaini179 – 289111CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi226 – 2261Y → F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-257 and/or F-282. 2 Publications
Mutagenesisi257 – 2571Y → F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-226 and/or F-282. 2 Publications
Mutagenesisi282 – 2821Y → F: No change of phosphorylation implicated in interaction with PTPN6 and PTPN11. Severe reduction of phosphorylation; when associated with F-226 and/or F-257. 2 Publications

Organism-specific databases

PharmGKBiPA134968341.

Polymorphism and mutation databases

BioMutaiBTLA.
DMDMi296439425.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 289259B- and T-lymphocyte attenuatorPRO_0000014523Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 63PROSITE-ProRule annotation1 Publication
Disulfide bondi58 ↔ 115PROSITE-ProRule annotation1 Publication
Disulfide bondi72 ↔ 79PROSITE-ProRule annotation1 Publication
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi110 – 1101N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Phosphorylated on Tyr residues by TNFRSF14 and by antigen receptors cross-linking, both inducing association with PTPN6 and PTPN11.1 Publication
N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ7Z6A9.
PRIDEiQ7Z6A9.

PTM databases

PhosphoSiteiQ7Z6A9.

Expressioni

Gene expression databases

BgeeiQ7Z6A9.
CleanExiHS_BTLA.
GenevisibleiQ7Z6A9. HS.

Organism-specific databases

HPAiHPA047211.

Interactioni

Subunit structurei

Interacts with tyrosine phosphatases PTPN6/SHP-1 and PTPN11/SHP-2. Interacts with TNFRSF14/HVEM.4 Publications

Protein-protein interaction databases

BioGridi127411. 2 interactions.
DIPiDIP-48795N.
IntActiQ7Z6A9. 3 interactions.
MINTiMINT-8020099.
STRINGi9606.ENSP00000333919.

Structurei

Secondary structure

1
289
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi44 – 496Combined sources
Beta strandi54 – 618Combined sources
Beta strandi63 – 653Combined sources
Beta strandi68 – 747Combined sources
Beta strandi79 – 813Combined sources
Beta strandi87 – 915Combined sources
Beta strandi96 – 1049Combined sources
Helixi107 – 1093Combined sources
Beta strandi111 – 1199Combined sources
Beta strandi122 – 1254Combined sources
Beta strandi129 – 1346Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AW2X-ray2.80A/X26-137[»]
ProteinModelPortaliQ7Z6A9.
SMRiQ7Z6A9. Positions 34-137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7Z6A9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 132102Ig-like V-typeAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG42530.
GeneTreeiENSGT00390000017390.
HOGENOMiHOG000168895.
HOVERGENiHBG080937.
InParanoidiQ7Z6A9.
KOiK06707.
OMAiYAAICVR.
OrthoDBiEOG7F513T.
PhylomeDBiQ7Z6A9.
TreeFamiTF337694.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: Q7Z6A9-1) [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
MKTLPAMLGT GKLFWVFFLI PYLDIWNIHG KESCDVQLYI KRQSEHSILA
60 70 80 90 100
GDPFELECPV KYCANRPHVT WCKLNGTTCV KLEDRQTSWK EEKNISFFIL
110 120 130 140 150
HFEPVLPNDN GSYRCSANFQ SNLIESHSTT LYVTDVKSAS ERPSKDEMAS
160 170 180 190 200
RPWLLYRLLP LGGLPLLITT CFCLFCCLRR HQGKQNELSD TAGREINLVD
210 220 230 240 250
AHLKSEQTEA STRQNSQVLL SETGIYDNDP DLCFRMQEGS EVYSNPCLEE
260 270 280
NKPGIVYASL NHSVIGPNSR LARNVKEAPT EYASICVRS
Length:289
Mass (Da):32,834
Last modified:May 18, 2010 - v3
Checksum:iF4D1FF775D7D33F3
GO
Isoform 2 (identifier: Q7Z6A9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     135-182: Missing.

Show »
Length:241
Mass (Da):27,317
Checksum:i991AFF2495C3F612
GO

Sequence cautioni

The sequence BAD18396.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051V → M in AAP44003 (PubMed:12796776).Curated
Sequence conflicti138 – 1381S → G in AAP44003 (PubMed:12796776).Curated
Sequence conflicti148 – 1481M → V in AAP44003 (PubMed:12796776).Curated
Sequence conflicti171 – 1711C → W in AAP44003 (PubMed:12796776).Curated
Sequence conflicti219 – 2191L → P in BAD18396 (PubMed:14702039).Curated
Sequence conflicti223 – 2231T → A in AAP44003 (PubMed:12796776).Curated
Sequence conflicti243 – 2431Y → C in AAP44003 (PubMed:12796776).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti124 – 1241I → V.
Corresponds to variant rs16859633 [ dbSNP | Ensembl ].
VAR_056027
Natural varianti157 – 1571R → S.3 Publications
Corresponds to variant rs2931761 [ dbSNP | Ensembl ].
VAR_027607
Natural varianti267 – 2671P → L.5 Publications
Corresponds to variant rs9288952 [ dbSNP | Ensembl ].
VAR_027608

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei135 – 18248Missing in isoform 2. 3 PublicationsVSP_040305Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY293286 mRNA. Translation: AAP44003.1.
AY599411 mRNA. Translation: AAT44901.1.
DQ198368 mRNA. Translation: ABA54407.1.
AC092894 Genomic DNA. No translation available.
BC107091 mRNA. Translation: AAI07092.1.
BC107092 mRNA. Translation: AAI07093.1.
AK131204 mRNA. Translation: BAD18396.1. Different initiation.
CCDSiCCDS33819.1. [Q7Z6A9-1]
CCDS43130.1. [Q7Z6A9-2]
RefSeqiNP_001078826.1. NM_001085357.1. [Q7Z6A9-2]
NP_861445.3. NM_181780.3.
UniGeneiHs.445162.

Genome annotation databases

EnsembliENST00000334529; ENSP00000333919; ENSG00000186265. [Q7Z6A9-1]
ENST00000383680; ENSP00000373178; ENSG00000186265. [Q7Z6A9-2]
GeneIDi151888.
KEGGihsa:151888.
UCSCiuc003dza.4. human. [Q7Z6A9-1]
uc003dzb.4. human. [Q7Z6A9-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY293286 mRNA. Translation: AAP44003.1.
AY599411 mRNA. Translation: AAT44901.1.
DQ198368 mRNA. Translation: ABA54407.1.
AC092894 Genomic DNA. No translation available.
BC107091 mRNA. Translation: AAI07092.1.
BC107092 mRNA. Translation: AAI07093.1.
AK131204 mRNA. Translation: BAD18396.1. Different initiation.
CCDSiCCDS33819.1. [Q7Z6A9-1]
CCDS43130.1. [Q7Z6A9-2]
RefSeqiNP_001078826.1. NM_001085357.1. [Q7Z6A9-2]
NP_861445.3. NM_181780.3.
UniGeneiHs.445162.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AW2X-ray2.80A/X26-137[»]
ProteinModelPortaliQ7Z6A9.
SMRiQ7Z6A9. Positions 34-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127411. 2 interactions.
DIPiDIP-48795N.
IntActiQ7Z6A9. 3 interactions.
MINTiMINT-8020099.
STRINGi9606.ENSP00000333919.

PTM databases

PhosphoSiteiQ7Z6A9.

Polymorphism and mutation databases

BioMutaiBTLA.
DMDMi296439425.

Proteomic databases

PaxDbiQ7Z6A9.
PRIDEiQ7Z6A9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334529; ENSP00000333919; ENSG00000186265. [Q7Z6A9-1]
ENST00000383680; ENSP00000373178; ENSG00000186265. [Q7Z6A9-2]
GeneIDi151888.
KEGGihsa:151888.
UCSCiuc003dza.4. human. [Q7Z6A9-1]
uc003dzb.4. human. [Q7Z6A9-2]

Organism-specific databases

CTDi151888.
GeneCardsiGC03M112182.
HGNCiHGNC:21087. BTLA.
HPAiHPA047211.
MIMi607925. gene.
neXtProtiNX_Q7Z6A9.
PharmGKBiPA134968341.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42530.
GeneTreeiENSGT00390000017390.
HOGENOMiHOG000168895.
HOVERGENiHBG080937.
InParanoidiQ7Z6A9.
KOiK06707.
OMAiYAAICVR.
OrthoDBiEOG7F513T.
PhylomeDBiQ7Z6A9.
TreeFamiTF337694.

Enzyme and pathway databases

ReactomeiREACT_19344. Costimulation by the CD28 family.

Miscellaneous databases

EvolutionaryTraceiQ7Z6A9.
GeneWikiiBTLA.
GenomeRNAii151888.
NextBioi86817.
PROiQ7Z6A9.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z6A9.
CleanExiHS_BTLA.
GenevisibleiQ7Z6A9. HS.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
[Graphical view]
SMARTiSM00409. IG. 1 hit.
[Graphical view]
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF TYR-226; TYR-257 AND TYR-282, GLYCOSYLATION, FUNCTION, INTERACTION WITH PTPN6 AND PTPN11, VARIANTS SER-157 AND LEU-267.
  2. "Point mutations in the BTLA gene in multiple myeloma and other hematologic malignancies."
    Mao Y., Wang X., Wu H., Chen Y., Ge Y., Chen J., Zhang X.
    Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-267.
  3. "Human BTLA mRNA alternate splice transcript lacking transmembrane encoding region."
    Oaks M.K., Tector M.F., Mewissen G.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-267.
    Tissue: Peripheral blood.
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-289 (ISOFORM 1), VARIANTS SER-157 AND LEU-267.
  6. "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] OF 4-289 (ISOFORM 1), VARIANTS SER-157 AND LEU-267.
    Tissue: Trachea.
  7. "Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of B and T lymphocyte attenuator required for association with protein tyrosine phosphatases SHP-1 and SHP-2."
    Gavrieli M., Watanabe N., Loftin S.K., Murphy T.L., Murphy K.M.
    Biochem. Biophys. Res. Commun. 312:1236-1243(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-226; TYR-257 AND TYR-282, INTERACTION WITH PTPN6 AND PTPN11.
  8. "B and T lymphocyte attenuator regulates T cell activation through interaction with herpesvirus entry mediator."
    Sedy J.R., Gavrieli M., Potter K.G., Hurchla M.A., Lindsley R.C., Hildner K., Scheu S., Pfeffer K., Ware C.F., Murphy T.L., Murphy K.M.
    Nat. Immunol. 6:90-98(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TNFRSF14, PHOSPHORYLATION.
  9. "Attenuating lymphocyte activity: the crystal structure of the BTLA-HVEM complex."
    Compaan D.M., Gonzalez L.C., Tom I., Loyet K.M., Eaton D., Hymowitz S.G.
    J. Biol. Chem. 280:39553-39561(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 26-137 IN COMPLEX WITH TNFRSF14, DISULFIDE BONDS.

Entry informationi

Entry nameiBTLA_HUMAN
AccessioniPrimary (citable) accession number: Q7Z6A9
Secondary accession number(s): Q3B831, Q3HS85, Q6ZNH9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: May 18, 2010
Last modified: June 24, 2015
This is version 110 of the entry and version 3 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 cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.