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Protein

Guanylate-binding protein 2

Gene

GBP2

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

Functioni

Hydrolyzes GTP to GMP in 2 consecutive cleavage reactions, but the major reaction product is GDP (PubMed:8706832). Exhibits antiviral activity against influenza virus. Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes (By similarity).By similarity1 Publication

Catalytic activityi

GTP + H2O = GDP + phosphate.1 Publication

Kineticsi

  1. KM=313 µM for GTP1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi45 – 528GTPBy similarity
    Nucleotide bindingi67 – 693GTPBy similarity
    Nucleotide bindingi97 – 1015GTPBy similarity

    GO - Molecular functioni

    • GTPase activity Source: InterPro
    • GTP binding Source: ProtInc

    GO - Biological processi

    • immune response Source: ProtInc
    • interferon-gamma-mediated signaling pathway Source: Reactome
    • type I interferon signaling pathway Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiR-HSA-877300. Interferon gamma signaling.
    R-HSA-909733. Interferon alpha/beta signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanylate-binding protein 2 (EC:3.6.5.-1 Publication)
    Alternative name(s):
    GTP-binding protein 2
    Short name:
    GBP-2
    Short name:
    HuGBP-2
    Guanine nucleotide-binding protein 2
    Interferon-induced guanylate-binding protein 2
    Gene namesi
    Name:GBP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4183. GBP2.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi588 – 5914Missing : No effect on subcellular location by confocal microscopy, but loss of membrane-association by subcellular fractionation. 1 Publication

    Organism-specific databases

    PharmGKBiPA28597.

    Polymorphism and mutation databases

    BioMutaiGBP2.
    DMDMi226694187.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 588588Guanylate-binding protein 2PRO_0000190964Add
    BLAST
    Propeptidei589 – 5913Removed in mature formBy similarityPRO_0000370782

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei588 – 5881Cysteine methyl esterBy similarity
    Lipidationi588 – 5881S-geranylgeranyl cysteine1 Publication

    Post-translational modificationi

    Isoprenylation is required for proper subcellular location.1 Publication

    Keywords - PTMi

    Lipoprotein, Methylation, Prenylation

    Proteomic databases

    EPDiP32456.
    MaxQBiP32456.
    PaxDbiP32456.
    PeptideAtlasiP32456.
    PRIDEiP32456.

    PTM databases

    iPTMnetiP32456.
    PhosphoSiteiP32456.

    Expressioni

    Inductioni

    By IFNG/IFN-gamma during macrophage activation, and by TNF and IL1B.1 Publication

    Gene expression databases

    BgeeiP32456.
    CleanExiHS_GBP2.
    GenevisibleiP32456. HS.

    Organism-specific databases

    HPAiCAB045975.
    HPA042682.

    Interactioni

    Subunit structurei

    Homodimer; homodimerization occurs upon GTP-binding and is required for the association with membranous structures. Heterodimer with other family members, including GBP1, GBP3, GBP4 and GBP5.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q9WMX22EBI-714388,EBI-6863741From a different organism.

    Protein-protein interaction databases

    BioGridi108904. 43 interactions.
    IntActiP32456. 24 interactions.
    MINTiMINT-7004311.
    STRINGi9606.ENSP00000359497.

    Structurei

    3D structure databases

    ProteinModelPortaliP32456.
    SMRiP32456. Positions 7-580.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 276242GB1/RHD3-type GAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 309309GTPase domain (Globular)By similarityAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG2037. Eukaryota.
    ENOG410XR6Z. LUCA.
    GeneTreeiENSGT00550000074475.
    HOGENOMiHOG000266974.
    HOVERGENiHBG001979.
    InParanoidiP32456.
    OMAiFKDVDQT.
    OrthoDBiEOG7BW0J3.
    PhylomeDBiP32456.
    TreeFamiTF331602.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR030386. G_GB1_RHD3_dom.
    IPR003191. Guanylate-bd_C.
    IPR015894. Guanylate-bd_N.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF02263. GBP. 1 hit.
    PF02841. GBP_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48340. SSF48340. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS51715. G_GB1_RHD3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P32456-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAPEINLPGP MSLIDNTKGQ LVVNPEALKI LSAITQPVVV VAIVGLYRTG
    60 70 80 90 100
    KSYLMNKLAG KKNGFSLGST VKSHTKGIWM WCVPHPKKPE HTLVLLDTEG
    110 120 130 140 150
    LGDIEKGDNE NDSWIFALAI LLSSTFVYNS MGTINQQAMD QLHYVTELTD
    160 170 180 190 200
    RIKANSSPGN NSVDDSADFV SFFPAFVWTL RDFTLELEVD GEPITADDYL
    210 220 230 240 250
    ELSLKLRKGT DKKSKSFNDP RLCIRKFFPK RKCFVFDWPA PKKYLAHLEQ
    260 270 280 290 300
    LKEEELNPDF IEQVAEFCSY ILSHSNVKTL SGGIPVNGPR LESLVLTYVN
    310 320 330 340 350
    AISSGDLPCM ENAVLALAQI ENSAAVEKAI AHYEQQMGQK VQLPTETLQE
    360 370 380 390 400
    LLDLHRDSER EAIEVFMKNS FKDVDQMFQR KLGAQLEARR DDFCKQNSKA
    410 420 430 440 450
    SSDCCMALLQ DIFGPLEEDV KQGTFSKPGG YRLFTQKLQE LKNKYYQVPR
    460 470 480 490 500
    KGIQAKEVLK KYLESKEDVA DALLQTDQSL SEKEKAIEVE RIKAESAEAA
    510 520 530 540 550
    KKMLEEIQKK NEEMMEQKEK SYQEHVKQLT EKMERDRAQL MAEQEKTLAL
    560 570 580 590
    KLQEQERLLK EGFENESKRL QKDIWDIQMR SKSLEPICNI L
    Length:591
    Mass (Da):67,209
    Last modified:April 14, 2009 - v3
    Checksum:iB09B3C2F3C3E1EA2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti310 – 3101M → R in AAH73163 (PubMed:15489334).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti281 – 2811S → P.
    Corresponds to variant rs2230336 [ dbSNP | Ensembl ].
    VAR_054815
    Natural varianti285 – 2851P → A.5 Publications
    Corresponds to variant rs1803632 [ dbSNP | Ensembl ].
    VAR_054816
    Natural varianti303 – 3031S → G.4 Publications
    Corresponds to variant rs2230338 [ dbSNP | Ensembl ].
    VAR_054817

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M55543 mRNA. Translation: AAA67323.1.
    AL832451 mRNA. Translation: CAD89925.1.
    AK314325 mRNA. Translation: BAG36973.1.
    CR457062 mRNA. Translation: CAG33343.1.
    AC104459 Genomic DNA. No translation available.
    CH471097 Genomic DNA. Translation: EAW73146.1.
    BC073163 mRNA. Translation: AAH73163.1.
    CCDSiCCDS719.1.
    PIRiS70524.
    RefSeqiNP_004111.2. NM_004120.4.
    UniGeneiHs.386567.
    Hs.732899.
    Hs.734162.

    Genome annotation databases

    EnsembliENST00000370466; ENSP00000359497; ENSG00000162645.
    ENST00000464839; ENSP00000434282; ENSG00000162645.
    GeneIDi2634.
    KEGGihsa:2634.
    UCSCiuc001dmz.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M55543 mRNA. Translation: AAA67323.1.
    AL832451 mRNA. Translation: CAD89925.1.
    AK314325 mRNA. Translation: BAG36973.1.
    CR457062 mRNA. Translation: CAG33343.1.
    AC104459 Genomic DNA. No translation available.
    CH471097 Genomic DNA. Translation: EAW73146.1.
    BC073163 mRNA. Translation: AAH73163.1.
    CCDSiCCDS719.1.
    PIRiS70524.
    RefSeqiNP_004111.2. NM_004120.4.
    UniGeneiHs.386567.
    Hs.732899.
    Hs.734162.

    3D structure databases

    ProteinModelPortaliP32456.
    SMRiP32456. Positions 7-580.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108904. 43 interactions.
    IntActiP32456. 24 interactions.
    MINTiMINT-7004311.
    STRINGi9606.ENSP00000359497.

    PTM databases

    iPTMnetiP32456.
    PhosphoSiteiP32456.

    Polymorphism and mutation databases

    BioMutaiGBP2.
    DMDMi226694187.

    Proteomic databases

    EPDiP32456.
    MaxQBiP32456.
    PaxDbiP32456.
    PeptideAtlasiP32456.
    PRIDEiP32456.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000370466; ENSP00000359497; ENSG00000162645.
    ENST00000464839; ENSP00000434282; ENSG00000162645.
    GeneIDi2634.
    KEGGihsa:2634.
    UCSCiuc001dmz.3. human.

    Organism-specific databases

    CTDi2634.
    GeneCardsiGBP2.
    H-InvDBHIX0000764.
    HIX0077629.
    HGNCiHGNC:4183. GBP2.
    HPAiCAB045975.
    HPA042682.
    MIMi600412. gene.
    neXtProtiNX_P32456.
    PharmGKBiPA28597.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG2037. Eukaryota.
    ENOG410XR6Z. LUCA.
    GeneTreeiENSGT00550000074475.
    HOGENOMiHOG000266974.
    HOVERGENiHBG001979.
    InParanoidiP32456.
    OMAiFKDVDQT.
    OrthoDBiEOG7BW0J3.
    PhylomeDBiP32456.
    TreeFamiTF331602.

    Enzyme and pathway databases

    ReactomeiR-HSA-877300. Interferon gamma signaling.
    R-HSA-909733. Interferon alpha/beta signaling.

    Miscellaneous databases

    ChiTaRSiGBP2. human.
    GeneWikiiGBP2.
    GenomeRNAii2634.
    PROiP32456.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP32456.
    CleanExiHS_GBP2.
    GenevisibleiP32456. HS.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR030386. G_GB1_RHD3_dom.
    IPR003191. Guanylate-bd_C.
    IPR015894. Guanylate-bd_N.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF02263. GBP. 1 hit.
    PF02841. GBP_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48340. SSF48340. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS51715. G_GB1_RHD3. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP."
      Cheng Y.-S.E., Patterson C.E., Staeheli P.
      Mol. Cell. Biol. 11:4717-4725(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-285.
      Tissue: Keratinocyte.
    2. Schwemmle M.
      Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
      Tissue: Foreskin.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ALA-285 AND GLY-303.
      Tissue: Spinal cord.
    4. "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], VARIANTS ALA-285 AND GLY-303.
      Tissue: Thymus.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ALA-285 AND GLY-303.
    6. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS ALA-285 AND GLY-303.
    8. "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].
      Tissue: Skin.
    9. "GTPase properties of the interferon-induced human guanylate-binding protein 2."
      Neun R., Richter M.F., Staeheli P., Schwemmle M.
      FEBS Lett. 390:69-72(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    10. "Unique features of different members of the human guanylate-binding protein family."
      Tripal P., Bauer M., Naschberger E., Mortinger T., Hohenadl C., Cornali E., Thurau M., Sturzl M.
      J. Interferon Cytokine Res. 27:44-52(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INDUCTION.
    11. "Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner."
      Britzen-Laurent N., Bauer M., Berton V., Fischer N., Syguda A., Reipschlager S., Naschberger E., Herrmann C., Sturzl M.
      PLoS ONE 5:E14246-E14246(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-588, DIMERIZATION, MUTAGENESIS OF 588-CYS--LEU-591.

    Entry informationi

    Entry nameiGBP2_HUMAN
    AccessioniPrimary (citable) accession number: P32456
    Secondary accession number(s): Q6GPH0, Q6IAU2, Q86TB0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: April 14, 2009
    Last modified: July 6, 2016
    This is version 146 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. 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.