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Protein

Guanine nucleotide-binding protein-like 3-like protein

Gene

GNL3L

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

Functioni

Stabilizes TERF1 telomeric association by preventing TERF1 recruitment by PML. Stabilizes TERF1 protein by preventing its ubiquitination and hence proteasomal degradation. Does so by interfering with TERF1-binding to FBXO4 E3 ubiquitin-protein ligase. Required for cell proliferation. By stabilizing TRF1 protein during mitosis, promotes metaphase-to-anaphase transition. Stabilizes MDM2 protein by preventing its ubiquitination, and hence proteasomal degradation. By acting on MDM2, may affect TP53 activity. Required for normal processing of ribosomal pre-rRNA. Binds GTP.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi173 – 1764GTPSequence Analysis
Nucleotide bindingi259 – 2668GTPSequence Analysis
Nucleotide bindingi303 – 3064GTPSequence Analysis

GO - Molecular functioni

  1. GTPase activity Source: GO_Central
  2. GTP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. metabolic process Source: GOC
  2. ribosome biogenesis Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein-like 3-like protein
Gene namesi
Name:GNL3L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:25553. GNL3L.

Subcellular locationi

  1. Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. membrane Source: UniProtKB
  3. mitochondrion Source: HPA
  4. nucleolus Source: HPA
  5. nucleoplasm Source: HPA
  6. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 102KK → AA: Loss of nucleolar localization; when associated with 34-A-A-35. Loss of nuclear location; when associated with 19-A-A-20. 1 Publication
Mutagenesisi19 – 202KK → AA: Loss of nuclear location; when associated with 9-A-A-10. Loss of nuclear location; when associated with 34-A-A-35. 1 Publication
Mutagenesisi34 – 352KK → AA: Loss of nucleolar localization; when associated with 9-A-A-10. Loss of nuclear location; when associated with 19-A-A-20. 1 Publication
Mutagenesisi145 – 1473RDP → AAA: Loss of GTP binding. Loss of nucleolar localization. No effect on nuclear localization. 1 Publication
Mutagenesisi309 – 3102PG → AA: Loss of nucleolar localization. No effect on nuclear localization. 1 Publication

Organism-specific databases

PharmGKBiPA134922876.

Polymorphism and mutation databases

BioMutaiGNL3L.
DMDMi74752999.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 582582Guanine nucleotide-binding protein-like 3-like proteinPRO_0000284381Add
BLAST

Proteomic databases

MaxQBiQ9NVN8.
PaxDbiQ9NVN8.
PeptideAtlasiQ9NVN8.
PRIDEiQ9NVN8.

PTM databases

PhosphoSiteiQ9NVN8.

Expressioni

Developmental stagei

Up-regulated during mitosis and down-regulated in the G1 phase.1 Publication

Gene expression databases

BgeeiQ9NVN8.
CleanExiHS_GNL3L.
ExpressionAtlasiQ9NVN8. baseline and differential.
GenevestigatoriQ9NVN8.

Organism-specific databases

HPAiHPA036314.
HPA036315.

Interactioni

Subunit structurei

Interacts with MDM2; this interaction, which occurs in the nucleoplasm, stabilizes MDM2. Indirectly interacts with TP53, via MDM2-binding. Interacts with TERF1; this interaction probably occurs in the nucleoplasm and is increased during mitosis, when the nucleolus is disassembled. This binding may promote TERF1 homodimerization. Interacts with TERT.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ALAS1P131963EBI-746682,EBI-3905054
LZTS2Q9BRK43EBI-746682,EBI-741037
MDM2Q009878EBI-746682,EBI-389668
ROPN1Q9HAT03EBI-746682,EBI-1378139

Protein-protein interaction databases

BioGridi120037. 20 interactions.
IntActiQ9NVN8. 7 interactions.
MINTiMINT-1440315.
STRINGi9606.ENSP00000338573.

Structurei

3D structure databases

ProteinModelPortaliQ9NVN8.
SMRiQ9NVN8. Positions 126-402.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 310186CP-type GPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 3527Required for nucleolar localizationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili58 – 8831Sequence AnalysisAdd
BLAST

Domaini

In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.

Sequence similaritiesi

Belongs to the TRAFAC class YlqF/YawG GTPase family.PROSITE-ProRule annotation
Contains 1 CP-type G (guanine nucleotide-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG1161.
GeneTreeiENSGT00550000074731.
HOGENOMiHOG000207716.
HOVERGENiHBG051747.
InParanoidiQ9NVN8.
KOiK14538.
OMAiGITKFMQ.
OrthoDBiEOG7SXW2W.
PhylomeDBiQ9NVN8.
TreeFamiTF313085.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030378. G_CP_dom.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01926. MMR_HSR1. 1 hit.
[Graphical view]
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51721. G_CP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NVN8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKLRHKNKK PGEGSKGHKK ISWPYPQPAK QNGKKATSKV PSAPHFVHPN
60 70 80 90 100
DHANREAELK KKWVEEMREK QQAAREQERQ KRRTIESYCQ DVLRRQEEFE
110 120 130 140 150
HKEEVLQELN MFPQLDDEAT RKAYYKEFRK VVEYSDVILE VLDARDPLGC
160 170 180 190 200
RCFQMEEAVL RAQGNKKLVL VLNKIDLVPK EVVEKWLDYL RNELPTVAFK
210 220 230 240 250
ASTQHQVKNL NRCSVPVDQA SESLLKSKAC FGAENLMRVL GNYCRLGEVR
260 270 280 290 300
THIRVGVVGL PNVGKSSLIN SLKRSRACSV GAVPGITKFM QEVYLDKFIR
310 320 330 340 350
LLDAPGIVPG PNSEVGTILR NCVHVQKLAD PVTPVETILQ RCNLEEISNY
360 370 380 390 400
YGVSGFQTTE HFLTAVAHRL GKKKKGGLYS QEQAAKAVLA DWVSGKISFY
410 420 430 440 450
IPPPATHTLP THLSAEIVKE MTEVFDIEDT EQANEDTMEC LATGESDELL
460 470 480 490 500
GDTDPLEMEI KLLHSPMTKI ADAIENKTTV YKIGDLTGYC TNPNRHQMGW
510 520 530 540 550
AKRNVDHRPK SNSMVDVCSV DRRSVLQRIM ETDPLQQGQA LASALKNKKK
560 570 580
MQKRADKIAS KLSDSMMSAL DLSGNADDGV GD
Length:582
Mass (Da):65,573
Last modified:October 1, 2000 - v1
Checksum:iB65EE072424F54BC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti320 – 3201R → H.
Corresponds to variant rs2298284 [ dbSNP | Ensembl ].
VAR_049495

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001475 mRNA. Translation: BAA91712.1.
AL391139 Genomic DNA. Translation: CAI40396.1.
BC011720 mRNA. Translation: AAH11720.1.
CCDSiCCDS14360.1.
RefSeqiNP_001171748.1. NM_001184819.1.
NP_061940.1. NM_019067.5.
UniGeneiHs.654677.

Genome annotation databases

EnsembliENST00000336470; ENSP00000338573; ENSG00000130119.
ENST00000360845; ENSP00000354091; ENSG00000130119.
GeneIDi54552.
KEGGihsa:54552.
UCSCiuc004dth.2. human.

Polymorphism and mutation databases

BioMutaiGNL3L.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK001475 mRNA. Translation: BAA91712.1.
AL391139 Genomic DNA. Translation: CAI40396.1.
BC011720 mRNA. Translation: AAH11720.1.
CCDSiCCDS14360.1.
RefSeqiNP_001171748.1. NM_001184819.1.
NP_061940.1. NM_019067.5.
UniGeneiHs.654677.

3D structure databases

ProteinModelPortaliQ9NVN8.
SMRiQ9NVN8. Positions 126-402.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120037. 20 interactions.
IntActiQ9NVN8. 7 interactions.
MINTiMINT-1440315.
STRINGi9606.ENSP00000338573.

PTM databases

PhosphoSiteiQ9NVN8.

Polymorphism and mutation databases

BioMutaiGNL3L.
DMDMi74752999.

Proteomic databases

MaxQBiQ9NVN8.
PaxDbiQ9NVN8.
PeptideAtlasiQ9NVN8.
PRIDEiQ9NVN8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336470; ENSP00000338573; ENSG00000130119.
ENST00000360845; ENSP00000354091; ENSG00000130119.
GeneIDi54552.
KEGGihsa:54552.
UCSCiuc004dth.2. human.

Organism-specific databases

CTDi54552.
GeneCardsiGC0XP054573.
HGNCiHGNC:25553. GNL3L.
HPAiHPA036314.
HPA036315.
MIMi300873. gene.
neXtProtiNX_Q9NVN8.
PharmGKBiPA134922876.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1161.
GeneTreeiENSGT00550000074731.
HOGENOMiHOG000207716.
HOVERGENiHBG051747.
InParanoidiQ9NVN8.
KOiK14538.
OMAiGITKFMQ.
OrthoDBiEOG7SXW2W.
PhylomeDBiQ9NVN8.
TreeFamiTF313085.

Miscellaneous databases

ChiTaRSiGNL3L. human.
GenomeRNAii54552.
NextBioi57019.
PROiQ9NVN8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NVN8.
CleanExiHS_GNL3L.
ExpressionAtlasiQ9NVN8. baseline and differential.
GenevestigatoriQ9NVN8.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030378. G_CP_dom.
IPR006073. GTP_binding_domain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF01926. MMR_HSR1. 1 hit.
[Graphical view]
PRINTSiPR00326. GTP1OBG.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51721. G_CP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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: Lung.
  4. "The homologous putative GTPases Grn1p from fission yeast and the human GNL3L are required for growth and play a role in processing of nucleolar pre-rRNA."
    Du X., Rao M.R.K.S., Chen X.Q., Wu W., Mahalingam S., Balasundaram D.
    Mol. Biol. Cell 17:460-474(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "A novel lysine-rich domain and GTP binding motifs regulate the nucleolar retention of human guanine nucleotide binding protein, GNL3L."
    Rao M.R.K.S., Kumari G., Balasundaram D., Sankaranarayanan R., Mahalingam S.
    J. Mol. Biol. 364:637-654(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 9-LYS-LYS-10; 19-LYS-LYS-20; 34-LYS-LYS-35; 145-ARG--PRO-147 AND 309-PRO-GLY-310.
  6. "GNL3L stabilizes the TRF1 complex and promotes mitotic transition."
    Zhu Q., Meng L., Hsu J.K., Lin T., Teishima J., Tsai R.Y.
    J. Cell Biol. 185:827-839(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TERF1, DEVELOPMENTAL STAGE.
  7. "GNL3L depletion destabilizes MDM2 and induces p53-dependent G2/M arrest."
    Meng L., Hsu J.K., Tsai R.Y.
    Oncogene 30:1716-1726(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MDM2 AND TP53.

Entry informationi

Entry nameiGNL3L_HUMAN
AccessioniPrimary (citable) accession number: Q9NVN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 1, 2000
Last modified: April 29, 2015
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

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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

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.