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Protein

Ubiquitin-conjugating enzyme E2 B

Gene

UBE2B

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

Functioni

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. Associates to the E3 ligase RAD18 to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. May be involved in neurite outgrowth.5 Publications

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathway:iprotein ubiquitination

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei88 – 881Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • canonical Wnt signaling pathway Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • chiasma assembly Source: Ensembl
  • DNA damage response, detection of DNA damage Source: Reactome
  • DNA repair Source: UniProtKB
  • histone H2A ubiquitination Source: UniProtKB
  • histone lysine demethylation Source: Ensembl
  • in utero embryonic development Source: Ensembl
  • maintenance of chromatin silencing Source: Ensembl
  • negative regulation of apoptotic process Source: Ensembl
  • negative regulation of cAMP-mediated signaling Source: UniProtKB
  • negative regulation of histone phosphorylation Source: Ensembl
  • positive regulation of reciprocal meiotic recombination Source: Ensembl
  • postreplication repair Source: UniProtKB
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • protein autoubiquitination Source: UniProtKB
  • protein K11-linked ubiquitination Source: UniProtKB
  • protein K48-linked ubiquitination Source: UniProtKB
  • protein K63-linked ubiquitination Source: UniProtKB
  • protein monoubiquitination Source: UniProtKB
  • protein polyubiquitination Source: UniProtKB
  • protein stabilization Source: UniProtKB
  • protein ubiquitination Source: UniProtKB
  • response to drug Source: UniProtKB
  • response to UV Source: UniProtKB
  • spermatogenesis Source: UniProtKB
  • sperm axoneme assembly Source: Ensembl
  • synaptonemal complex organization Source: Ensembl
  • translesion synthesis Source: Reactome
  • ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.3.2.B6. 2681.
ReactomeiREACT_355480. Recognition of DNA damage by PCNA-containing replication complex.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP63146.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 B (EC:6.3.2.19)
Alternative name(s):
RAD6 homolog B
Short name:
HR6B
Short name:
hHR6B
Ubiquitin carrier protein B
Ubiquitin-conjugating enzyme E2-17 kDa
Ubiquitin-protein ligase B
Gene namesi
Name:UBE2B
Synonyms:RAD6B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:12473. UBE2B.

Subcellular locationi

  • Cell membrane By similarity
  • Nucleus By similarity

  • Note: In peripheral neurons, expressed both at the plasma membrane and in nuclei.By similarity

GO - Cellular componenti

  • chromatin Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • HULC complex Source: UniProtKB
  • nuclear chromatin Source: GO_Central
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
  • replication fork Source: UniProtKB
  • XY body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37123.

Polymorphism and mutation databases

BioMutaiUBE2B.
DMDMi52783814.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Ubiquitin-conjugating enzyme E2 BPRO_0000082447Add
BLAST

Proteomic databases

MaxQBiP63146.
PaxDbiP63146.
PRIDEiP63146.

Expressioni

Gene expression databases

BgeeiP63146.
CleanExiHS_UBE2B.
ExpressionAtlasiP63146. baseline and differential.
GenevisibleiP63146. HS.

Interactioni

Subunit structurei

Interacts with RAD18, UBR2 and WAC.2 Publications

Protein-protein interaction databases

BioGridi113168. 63 interactions.
DIPiDIP-29832N.
IntActiP63146. 16 interactions.
MINTiMINT-97455.
STRINGi9606.ENSP00000265339.

Structurei

Secondary structure

1
152
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815Combined sources
Beta strandi24 – 296Combined sources
Beta strandi32 – 4110Combined sources
Turni47 – 504Combined sources
Beta strandi52 – 587Combined sources
Turni61 – 655Combined sources
Beta strandi69 – 746Combined sources
Beta strandi85 – 873Combined sources
Helixi90 – 923Combined sources
Turni93 – 953Combined sources
Helixi102 – 11312Combined sources
Helixi124 – 1329Combined sources
Helixi134 – 14714Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JASNMR-A1-152[»]
1NXAmodel-A1-152[»]
2Y4WNMR-A1-152[»]
2YB6X-ray1.50A1-152[»]
2YBFX-ray2.00A1-152[»]
ProteinModelPortaliP63146.
SMRiP63146. Positions 3-152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63146.

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110565.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP63146.
KOiK10574.
OMAiEQSWVDS.
OrthoDBiEOG7M0NTH.
PhylomeDBiP63146.
TreeFamiTF101128.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63146-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTPARRRLM RDFKRLQEDP PVGVSGAPSE NNIMQWNAVI FGPEGTPFED
60 70 80 90 100
GTFKLVIEFS EEYPNKPPTV RFLSKMFHPN VYADGSICLD ILQNRWSPTY
110 120 130 140 150
DVSSILTSIQ SLLDEPNPNS PANSQAAQLY QENKREYEKR VSAIVEQSWN

DS
Length:152
Mass (Da):17,312
Last modified:September 27, 2004 - v1
Checksum:iCFDEEEE7E06840BE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 232VG → C (PubMed:1883845).Curated
Sequence conflicti41 – 411F → I (PubMed:1883845).Curated
Sequence conflicti54 – 541K → R (PubMed:1883845).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74525 mRNA. Translation: AAA35982.1.
X53251 mRNA. Translation: CAA37339.1.
BT007071 mRNA. Translation: AAP35734.1.
CR407634 mRNA. Translation: CAG28562.1.
DQ090910 Genomic DNA. Translation: AAY68224.1.
AK312012 mRNA. Translation: BAG34950.1.
CH471062 Genomic DNA. Translation: EAW62257.1.
CH471062 Genomic DNA. Translation: EAW62258.1.
BC005979 mRNA. Translation: AAH05979.1.
BC008404 mRNA. Translation: AAH08404.1.
BC008470 mRNA. Translation: AAH08470.1.
CCDSiCCDS4174.1.
PIRiB41222.
RefSeqiNP_003328.1. NM_003337.3.
UniGeneiHs.612096.
Hs.730071.

Genome annotation databases

EnsembliENST00000265339; ENSP00000265339; ENSG00000119048.
GeneIDi7320.
KEGGihsa:7320.
UCSCiuc003kzh.3. human.

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74525 mRNA. Translation: AAA35982.1.
X53251 mRNA. Translation: CAA37339.1.
BT007071 mRNA. Translation: AAP35734.1.
CR407634 mRNA. Translation: CAG28562.1.
DQ090910 Genomic DNA. Translation: AAY68224.1.
AK312012 mRNA. Translation: BAG34950.1.
CH471062 Genomic DNA. Translation: EAW62257.1.
CH471062 Genomic DNA. Translation: EAW62258.1.
BC005979 mRNA. Translation: AAH05979.1.
BC008404 mRNA. Translation: AAH08404.1.
BC008470 mRNA. Translation: AAH08470.1.
CCDSiCCDS4174.1.
PIRiB41222.
RefSeqiNP_003328.1. NM_003337.3.
UniGeneiHs.612096.
Hs.730071.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JASNMR-A1-152[»]
1NXAmodel-A1-152[»]
2Y4WNMR-A1-152[»]
2YB6X-ray1.50A1-152[»]
2YBFX-ray2.00A1-152[»]
ProteinModelPortaliP63146.
SMRiP63146. Positions 3-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113168. 63 interactions.
DIPiDIP-29832N.
IntActiP63146. 16 interactions.
MINTiMINT-97455.
STRINGi9606.ENSP00000265339.

Polymorphism and mutation databases

BioMutaiUBE2B.
DMDMi52783814.

Proteomic databases

MaxQBiP63146.
PaxDbiP63146.
PRIDEiP63146.

Protocols and materials databases

DNASUi7320.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265339; ENSP00000265339; ENSG00000119048.
GeneIDi7320.
KEGGihsa:7320.
UCSCiuc003kzh.3. human.

Organism-specific databases

CTDi7320.
GeneCardsiGC05P133706.
HGNCiHGNC:12473. UBE2B.
MIMi179095. gene.
neXtProtiNX_P63146.
PharmGKBiPA37123.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110565.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiP63146.
KOiK10574.
OMAiEQSWVDS.
OrthoDBiEOG7M0NTH.
PhylomeDBiP63146.
TreeFamiTF101128.

Enzyme and pathway databases

UniPathwayiUPA00143.
BRENDAi2.3.2.B6. 2681.
ReactomeiREACT_355480. Recognition of DNA damage by PCNA-containing replication complex.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP63146.

Miscellaneous databases

ChiTaRSiUBE2B. human.
EvolutionaryTraceiP63146.
GeneWikiiUBE2B.
GenomeRNAii7320.
NextBioi28622.
PROiP63146.
SOURCEiSearch...

Gene expression databases

BgeeiP63146.
CleanExiHS_UBE2B.
ExpressionAtlasiP63146. baseline and differential.
GenevisibleiP63146. HS.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human ubiquitin carrier protein E2(Mr = 17,000) is homologous to the yeast DNA repair gene RAD6."
    Schneider R., Eckerskorn C., Lottspeich F., Schweiger M.
    EMBO J. 9:1431-1435(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Tissue: Placenta.
  2. "Mammalian mRNAs encoding protein closely related to ubiquitin-conjugating enzyme encoded by yeast DNA repair gene RAD6."
    Woffendin C., Chen Z.Y., Staskus K., Retzel E.F., Plagemann P.G.
    Biochim. Biophys. Acta 1090:81-85(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "Structural and functional conservation of two human homologs of the yeast DNA repair gene RAD6."
    Koken M.H.M., Reynolds P., Jaspers-Dekker I., Prakash L., Prakash S., Bootsma D., Hoeijmakers J.H.J.
    Proc. Natl. Acad. Sci. U.S.A. 88:8865-8869(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
    Tissue: Brain.
  7. NIEHS SNPs program
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Bone marrow and Brain.
  10. "The human RAD18 gene product interacts with HHR6A and HHR6B."
    Xin H., Lin W., Sumanasekera W., Zhang Y., Wu X., Wang Z.
    Nucleic Acids Res. 28:2847-2854(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAD18.
  11. "The human homolog of yeast BRE1 functions as a transcriptional coactivator through direct activator interactions."
    Kim J., Hake S.B., Roeder R.G.
    Mol. Cell 20:759-770(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination."
    Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.
    J. Cell Biol. 175:703-708(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen."
    Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V., Hurwitz J., Prakash L., Prakash S., Haracska L.
    Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
    David Y., Ziv T., Admon A., Navon A.
    J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "WAC, a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcription."
    Zhang F., Yu X.
    Mol. Cell 41:384-397(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH WAC.
  16. "The NMR structure of the class I human ubiquitin-conjugating enzyme 2b."
    Miura T., Klaus W., Ross A., Guntert P., Senn H.
    J. Biomol. NMR 22:89-92(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiUBE2B_HUMAN
AccessioniPrimary (citable) accession number: P63146
Secondary accession number(s): B2R503
, D3DQA2, P23567, Q4PJ15, Q9D0J6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: July 22, 2015
This is version 121 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.