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Protein

Dual specificity tyrosine-phosphorylation-regulated kinase 2

Gene

DYRK2

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

Functioni

Serine/threonine-protein kinase involved in the regulation of the mitotic cell cycle, cell proliferation, apoptosis, organization of the cytoskeleton and neurite outgrowth. Functions in part via its role in ubiquitin-dependent proteasomal protein degradation. Functions downstream of ATM and phosphorylates p53/TP53 at 'Ser-46', and thereby contributes to the induction of apoptosis in response to DNA damage. Phosphorylates NFATC1, and thereby inhibits its accumulation in the nucleus and its transcription factor activity. Phosphorylates EIF2B5 at 'Ser-544', enabling its subsequent phosphorylation and inhibition by GSK3B. Likewise, phosphorylation of NFATC1, CRMP2/DPYSL2 and CRMP4/DPYSL3 promotes their subsequent phosphorylation by GSK3B. May play a general role in the priming of GSK3 substrates. Inactivates GYS1 by phosphorylation at 'Ser-641', and potentially also a second phosphorylation site, thus regulating glycogen synthesis. Mediates EDVP E3 ligase complex formation and is required for the phosphorylation and subsequent degradation of KATNA1. Phosphorylates TERT at 'Ser-457', promoting TERT ubiquitination by the EDVP complex. Phosphorylates SIAH2, and thereby increases its ubiquitin ligase activity. Promotes the proteasomal degradation of MYC and JUN, and thereby regulates progress through the mitotic cell cycle and cell proliferation. Promotes proteasomal degradation of GLI2 and GLI3, and thereby plays a role in smoothened and sonic hedgehog signaling. Plays a role in cytoskeleton organization and neurite outgrowth via its phosphorylation of DCX and DPYSL2. Phosphorylates CRMP2/DPYSL2, CRMP4/DPYSL3, DCX, EIF2B5, EIF4EBP1, GLI2, GLI3, GYS1, JUN, MDM2, MYC, NFATC1, p53/TP53, TAU/MAPT and KATNA1. Can phosphorylate histone H1, histone H3 and histone H2B (in vitro). Can phosphorylate CARHSP1 (in vitro).14 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Protein has several cofactor binding sites:

Enzyme regulationi

Activated by autophosphorylation on the second tyrosine residue in the Tyr-X-Tyr motif in the activation loop. Inhibited by acridine analogs, purvalanol, and barely by harmine. Inhibited by leucettine and leucettine derivatives.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei251ATPCurated1
Active sitei348Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi228 – 236ATPCurated9
Nucleotide bindingi301 – 304ATPCurated4

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • manganese ion binding Source: UniProtKB
  • protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
  • protein serine/threonine kinase activity Source: UniProtKB
  • protein tyrosine kinase activity Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: UniProtKB
  • negative regulation of NFAT protein import into nucleus Source: UniProtKB
  • positive regulation of glycogen biosynthetic process Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of signal transduction by p53 class mediator Source: Reactome
  • smoothened signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS05086-MONOMER.
BRENDAi2.7.12.1. 2681.
ReactomeiR-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
SignaLinkiQ92630.
SIGNORiQ92630.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity tyrosine-phosphorylation-regulated kinase 2 (EC:2.7.12.1)
Gene namesi
Name:DYRK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:3093. DYRK2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: Ensembl
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi106T → A: Impaired ATM-mediated phosphorylation, reduced affinity with MDM2 and altered MDM2-triggered ubiquitination. 1 Publication1
Mutagenesisi189 – 191KKR → NNN: Impaired nuclear translocation. 1 Publication3
Mutagenesisi251K → R: Abolishes protein serine/threonine kinase activity. 1 Publication1
Mutagenesisi442S → A: Impaired ATM-mediated phosphorylation, reduced affinity with MDM2 and altered MDM2-triggered ubiquitination. 1 Publication1

Organism-specific databases

DisGeNETi8445.
OpenTargetsiENSG00000127334.
PharmGKBiPA27550.

Chemistry databases

ChEMBLiCHEMBL4376.
GuidetoPHARMACOLOGYi2011.

Polymorphism and mutation databases

BioMutaiDYRK2.
DMDMi148887370.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000859361 – 601Dual specificity tyrosine-phosphorylation-regulated kinase 2Add BLAST601

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei30PhosphoserineCombined sources1
Modified residuei106Phosphothreonine; by ATM1 Publication1
Modified residuei381Phosphothreonine; by MAP3K101 Publication1
Modified residuei382Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei442Phosphoserine; by ATM1 Publication1
Modified residuei449Phosphoserine; by MAP3K101 Publication1

Post-translational modificationi

Autophosphorylates cotranslationally on the second tyrosine residue in the Tyr-X-Tyr motif in the activation loop, but once mature, does not have any protein tyrosine kinase activity. Phosphorylated at Thr-106 and Ser-442 by ATM in response to genotoxic stress.1 Publication
Under normal conditions, polyubiquitinated in the nucleus by MDM2, leading to its proteasomal degradation. Phosphorylation on Thr-106 and Ser-442 by ATM in response to genotoxic stress disrupts MDM2 binding and prevents MDM2-mediated ubiquitination and subsequent proteasomal degradation. Polyubiquitinated by SIAH2, leading to its proteasomal degradation. Polyubiquitinated by SIAH2 occurs under normal conditions, and is enhanced in response to hypoxia.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ92630.
MaxQBiQ92630.
PaxDbiQ92630.
PeptideAtlasiQ92630.
PRIDEiQ92630.

PTM databases

iPTMnetiQ92630.
PhosphoSitePlusiQ92630.

Expressioni

Tissue specificityi

Testis, after the onset of spermatogenesis.1 Publication

Inductioni

Accumulates in nucleus upon DNA damage. Induced in both esophageal and lung adenocarcinomas.2 Publications

Gene expression databases

BgeeiENSG00000127334.
CleanExiHS_DYRK2.
ExpressionAtlasiQ92630. baseline and differential.
GenevisibleiQ92630. HS.

Organism-specific databases

HPAiHPA027230.
HPA056902.

Interactioni

Subunit structurei

Component of an E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and VPRBP (EDVP complex). Interacts directly with EDD/UBR5, DDB1 and VPRBP. Interacts with SIAH2 and MDM2. Interacts with MAP3K10 and NFATC1. May also interact with CCNL2.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DYRK4Q9NR203EBI-749432,EBI-3914009
IKZF1Q134223EBI-749432,EBI-745305
KXD1Q9BQD33EBI-749432,EBI-739657
LZTS2Q9BRK43EBI-749432,EBI-741037
SP100P234973EBI-749432,EBI-751145
WDR62O433793EBI-749432,EBI-714790
ZBTB9Q96C003EBI-749432,EBI-395708

GO - Molecular functioni

  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114023. 51 interactors.
IntActiQ92630. 12 interactors.
MINTiMINT-1469581.
STRINGi9606.ENSP00000342105.

Chemistry databases

BindingDBiQ92630.

Structurei

Secondary structure

1601
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi149 – 152Combined sources4
Helixi156 – 163Combined sources8
Helixi164 – 166Combined sources3
Helixi169 – 174Combined sources6
Helixi175 – 177Combined sources3
Beta strandi179 – 181Combined sources3
Helixi198 – 201Combined sources4
Beta strandi206 – 208Combined sources3
Turni219 – 221Combined sources3
Beta strandi222 – 241Combined sources20
Turni242 – 245Combined sources4
Beta strandi246 – 253Combined sources8
Helixi257 – 274Combined sources18
Beta strandi287 – 293Combined sources7
Beta strandi296 – 301Combined sources6
Helixi308 – 314Combined sources7
Turni315 – 317Combined sources3
Helixi322 – 342Combined sources21
Helixi351 – 353Combined sources3
Beta strandi354 – 358Combined sources5
Beta strandi364 – 366Combined sources3
Helixi375 – 377Combined sources3
Helixi386 – 388Combined sources3
Helixi391 – 395Combined sources5
Helixi402 – 417Combined sources16
Helixi427 – 438Combined sources12
Helixi443 – 447Combined sources5
Helixi452 – 455Combined sources4
Beta strandi467 – 469Combined sources3
Beta strandi475 – 477Combined sources3
Helixi496 – 499Combined sources4
Turni500 – 502Combined sources3
Helixi506 – 515Combined sources10
Turni520 – 522Combined sources3
Helixi526 – 530Combined sources5
Turni533 – 535Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K2LX-ray2.36A146-552[»]
3KVWX-ray2.28A146-552[»]
4AZFX-ray2.55A146-540[»]
ProteinModelPortaliQ92630.
SMRiQ92630.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ92630.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini222 – 535Protein kinasePROSITE-ProRule annotationAdd BLAST314

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi189 – 191Nuclear localization signal1 Publication3

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0667. Eukaryota.
ENOG410XPET. LUCA.
GeneTreeiENSGT00760000119032.
HOGENOMiHOG000220863.
HOVERGENiHBG051426.
InParanoidiQ92630.
KOiK18669.
OMAiKLTTFEH.
OrthoDBiEOG091G0Q46.
PhylomeDBiQ92630.
TreeFamiTF314624.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 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: Q92630-1) [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
MLTRKPSAAA PAAYPTGRGG DSAVRQLQAS PGLGAGATRS GVGTGPPSPI
60 70 80 90 100
ALPPLRASNA AAAAHTIGGS KHTMNDHLHV GSHAHGQIQV QQLFEDNSNK
110 120 130 140 150
RTVLTTQPNG LTTVGKTGLP VVPERQLDSI HRRQGSSTSL KSMEGMGKVK
160 170 180 190 200
ATPMTPEQAM KQYMQKLTAF EHHEIFSYPE IYFLGLNAKK RQGMTGGPNN
210 220 230 240 250
GGYDDDQGSY VQVPHDHVAY RYEVLKVIGK GSFGQVVKAY DHKVHQHVAL
260 270 280 290 300
KMVRNEKRFH RQAAEEIRIL EHLRKQDKDN TMNVIHMLEN FTFRNHICMT
310 320 330 340 350
FELLSMNLYE LIKKNKFQGF SLPLVRKFAH SILQCLDALH KNRIIHCDLK
360 370 380 390 400
PENILLKQQG RSGIKVIDFG SSCYEHQRVY TYIQSRFYRA PEVILGARYG
410 420 430 440 450
MPIDMWSLGC ILAELLTGYP LLPGEDEGDQ LACMIELLGM PSQKLLDASK
460 470 480 490 500
RAKNFVSSKG YPRYCTVTTL SDGSVVLNGG RSRRGKLRGP PESREWGNAL
510 520 530 540 550
KGCDDPLFLD FLKQCLEWDP AVRMTPGQAL RHPWLRRRLP KPPTGEKTSV
560 570 580 590 600
KRITESTGAI TSISKLPPPS SSASKLRTNL AQMTDANGNI QQRTVLPKLV

S
Length:601
Mass (Da):66,652
Last modified:June 12, 2007 - v3
Checksum:iA7BEE25CDF944436
GO
Isoform 2 (identifier: Q92630-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: Missing.

Show »
Length:528
Mass (Da):59,715
Checksum:iAF2C6822ED9522D7
GO

Sequence cautioni

The sequence CAA73885 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti37A → P in CAA73885 (PubMed:9748265).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04045898S → G.1 PublicationCorresponds to variant rs35139851dbSNPEnsembl.1
Natural variantiVAR_040459198P → L in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_040460245H → N.1 PublicationCorresponds to variant rs34166200dbSNPEnsembl.1
Natural variantiVAR_040461295N → S.1 PublicationCorresponds to variant rs56293072dbSNPEnsembl.1
Natural variantiVAR_040462451R → Q.1 PublicationCorresponds to variant rs35688869dbSNPEnsembl.1
Natural variantiVAR_040463455F → Y.1 PublicationCorresponds to variant rs55774594dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0261151 – 73Missing in isoform 2. 1 PublicationAdd BLAST73

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13493 mRNA. Translation: CAA73885.1. Different initiation.
AK313937 mRNA. Translation: BAG36656.1.
CH471054 Genomic DNA. Translation: EAW97176.1.
BC005809 mRNA. Translation: AAH05809.1.
BC006375 mRNA. Translation: AAH06375.1.
Y09216 mRNA. Translation: CAA70418.1.
CCDSiCCDS8978.1. [Q92630-1]
CCDS8979.1. [Q92630-2]
RefSeqiNP_003574.1. NM_003583.3. [Q92630-2]
NP_006473.2. NM_006482.2. [Q92630-1]
XP_016875521.1. XM_017020032.1. [Q92630-2]
UniGeneiHs.173135.

Genome annotation databases

EnsembliENST00000344096; ENSP00000342105; ENSG00000127334. [Q92630-1]
ENST00000393555; ENSP00000377186; ENSG00000127334. [Q92630-2]
GeneIDi8445.
KEGGihsa:8445.
UCSCiuc001str.5. human. [Q92630-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13493 mRNA. Translation: CAA73885.1. Different initiation.
AK313937 mRNA. Translation: BAG36656.1.
CH471054 Genomic DNA. Translation: EAW97176.1.
BC005809 mRNA. Translation: AAH05809.1.
BC006375 mRNA. Translation: AAH06375.1.
Y09216 mRNA. Translation: CAA70418.1.
CCDSiCCDS8978.1. [Q92630-1]
CCDS8979.1. [Q92630-2]
RefSeqiNP_003574.1. NM_003583.3. [Q92630-2]
NP_006473.2. NM_006482.2. [Q92630-1]
XP_016875521.1. XM_017020032.1. [Q92630-2]
UniGeneiHs.173135.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3K2LX-ray2.36A146-552[»]
3KVWX-ray2.28A146-552[»]
4AZFX-ray2.55A146-540[»]
ProteinModelPortaliQ92630.
SMRiQ92630.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114023. 51 interactors.
IntActiQ92630. 12 interactors.
MINTiMINT-1469581.
STRINGi9606.ENSP00000342105.

Chemistry databases

BindingDBiQ92630.
ChEMBLiCHEMBL4376.
GuidetoPHARMACOLOGYi2011.

PTM databases

iPTMnetiQ92630.
PhosphoSitePlusiQ92630.

Polymorphism and mutation databases

BioMutaiDYRK2.
DMDMi148887370.

Proteomic databases

EPDiQ92630.
MaxQBiQ92630.
PaxDbiQ92630.
PeptideAtlasiQ92630.
PRIDEiQ92630.

Protocols and materials databases

DNASUi8445.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000344096; ENSP00000342105; ENSG00000127334. [Q92630-1]
ENST00000393555; ENSP00000377186; ENSG00000127334. [Q92630-2]
GeneIDi8445.
KEGGihsa:8445.
UCSCiuc001str.5. human. [Q92630-1]

Organism-specific databases

CTDi8445.
DisGeNETi8445.
GeneCardsiDYRK2.
HGNCiHGNC:3093. DYRK2.
HPAiHPA027230.
HPA056902.
MIMi603496. gene.
neXtProtiNX_Q92630.
OpenTargetsiENSG00000127334.
PharmGKBiPA27550.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0667. Eukaryota.
ENOG410XPET. LUCA.
GeneTreeiENSGT00760000119032.
HOGENOMiHOG000220863.
HOVERGENiHBG051426.
InParanoidiQ92630.
KOiK18669.
OMAiKLTTFEH.
OrthoDBiEOG091G0Q46.
PhylomeDBiQ92630.
TreeFamiTF314624.

Enzyme and pathway databases

BioCyciZFISH:HS05086-MONOMER.
BRENDAi2.7.12.1. 2681.
ReactomeiR-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
SignaLinkiQ92630.
SIGNORiQ92630.

Miscellaneous databases

ChiTaRSiDYRK2. human.
EvolutionaryTraceiQ92630.
GeneWikiiDYRK2.
GenomeRNAii8445.
PROiQ92630.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000127334.
CleanExiHS_DYRK2.
ExpressionAtlasiQ92630. baseline and differential.
GenevisibleiQ92630. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDYRK2_HUMAN
AccessioniPrimary (citable) accession number: Q92630
Secondary accession number(s): B2R9V9, Q9BRB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: June 12, 2007
Last modified: November 30, 2016
This is version 173 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 chromosome 12
    Human chromosome 12: 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. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. 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.