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Protein

E3 ubiquitin-protein ligase MIB1

Gene

MIB1

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

Functioni

E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors. Probably mediates ubiquitination and subsequent proteasomal degradation of DAPK1, thereby antagonizing anti-apoptotic effects of DAPK1 to promote TNF-induced apoptosis (By similarity). Involved in ubiquitination of centriolar satellite CEP131, CEP290 and PCM1 proteins and hence inhibits primary cilium formation in proliferating cells. Mediates 'Lys-63'-linked polyubiquitination of TBK1, which probably participates in kinase activation.By similarity1 Publication

Pathwayi: protein ubiquitination

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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri79 – 126ZZ-typePROSITE-ProRule annotationAdd BLAST48
Zinc fingeri819 – 854RING-type 1PROSITE-ProRule annotationAdd BLAST36
Zinc fingeri866 – 901RING-type 2PROSITE-ProRule annotationAdd BLAST36
Zinc fingeri963 – 996RING-type 3PROSITE-ProRule annotationAdd BLAST34

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Notch signaling pathway, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2691232. Constitutive Signaling by NOTCH1 HD Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
SignaLinkiQ86YT6.
SIGNORiQ86YT6.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase MIB1 (EC:6.3.2.-)
Alternative name(s):
DAPK-interacting protein 1
Short name:
DIP-1
Mind bomb homolog 1
Zinc finger ZZ type with ankyrin repeat domain protein 2
Gene namesi
Name:MIB1
Synonyms:DIP1, KIAA1323, ZZANK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:21086. MIB1.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasm Source: GO_Central
  • cytoplasmic vesicle Source: Ensembl
  • cytosol Source: Reactome
  • plasma membrane Source: UniProtKB-SubCell
  • postsynaptic density Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

Left ventricular non-compaction 7 (LVNC7)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease due to an arrest of myocardial morphogenesis. It is characterized by a hypertrophic left ventricle with deep trabeculations and with poor systolic function, with or without associated left ventricular dilation. In some cases, it is associated with other congenital heart anomalies.
See also OMIM:615092
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069620943V → F in LVNC7. 1 PublicationCorresponds to variant rs200035428dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi57534.
MalaCardsiMIB1.
MIMi615092. phenotype.
OpenTargetsiENSG00000101752.
Orphaneti54260. Left ventricular noncompaction.
PharmGKBiPA134862722.

Polymorphism and mutation databases

DMDMi68565512.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000559431 – 1006E3 ubiquitin-protein ligase MIB1Add BLAST1006

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei408PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated; possibly via autoubiquitination (By similarity). Ubiquitinated; this modification is inhibited in response to cellular stress, such as ultraviolet light (UV) radiation or heat shock.By similarity2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ86YT6.
MaxQBiQ86YT6.
PaxDbiQ86YT6.
PeptideAtlasiQ86YT6.
PRIDEiQ86YT6.

PTM databases

iPTMnetiQ86YT6.
PhosphoSitePlusiQ86YT6.

Expressioni

Tissue specificityi

Widely expressed at low level. Expressed at higher level in spinal cord, ovary, whole brain, and all specific brain regions examined.1 Publication

Gene expression databases

BgeeiENSG00000101752.
CleanExiHS_MIB1.
GenevisibleiQ86YT6. HS.

Organism-specific databases

HPAiCAB037044.
HPA019100.

Interactioni

Subunit structurei

Interacts with CEP131 and PCM1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Azi2Q9QYP62EBI-2129148,EBI-6115874From a different organism.
TBK1Q9UHD22EBI-2129148,EBI-356402

Protein-protein interaction databases

BioGridi121593. 73 interactors.
IntActiQ86YT6. 40 interactors.
MINTiMINT-2841371.
STRINGi9606.ENSP00000261537.

Structurei

Secondary structure

11006
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi17 – 20Combined sources4
Turni27 – 30Combined sources4
Beta strandi37 – 52Combined sources16
Beta strandi57 – 66Combined sources10
Beta strandi68 – 72Combined sources5
Helixi74 – 76Combined sources3
Turni86 – 88Combined sources3
Beta strandi91 – 105Combined sources15
Helixi110 – 114Combined sources5
Beta strandi124 – 127Combined sources4
Helixi140 – 142Combined sources3
Beta strandi145 – 152Combined sources8
Beta strandi156 – 159Combined sources4
Turni166 – 169Combined sources4
Beta strandi176 – 182Combined sources7
Beta strandi192 – 197Combined sources6
Beta strandi202 – 208Combined sources7
Helixi209 – 211Combined sources3
Beta strandi215 – 219Combined sources5
Beta strandi221 – 227Combined sources7
Helixi228 – 230Combined sources3
Beta strandi251 – 253Combined sources3
Helixi258 – 264Combined sources7
Turni265 – 269Combined sources5
Helixi273 – 276Combined sources4
Helixi277 – 280Combined sources4
Beta strandi283 – 288Combined sources6
Turni290 – 292Combined sources3
Beta strandi294 – 297Combined sources4
Beta strandi303 – 306Combined sources4
Helixi308 – 310Combined sources3
Beta strandi338 – 341Combined sources4
Helixi345 – 354Combined sources10
Helixi360 – 365Combined sources6
Beta strandi369 – 375Combined sources7
Beta strandi381 – 385Combined sources5
Beta strandi388 – 392Combined sources5
Helixi394 – 396Combined sources3
Beta strandi397 – 399Combined sources3
Beta strandi402 – 405Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4TSEX-ray2.06A/B239-409[»]
4XI6X-ray2.04A8-402[»]
4XI7X-ray2.05A8-402[»]
4XIBX-ray2.15A8-402[»]
ProteinModelPortaliQ86YT6.
SMRiQ86YT6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 74MIB/HERC2 1PROSITE-ProRule annotationAdd BLAST69
Domaini143 – 221MIB/HERC2 2PROSITE-ProRule annotationAdd BLAST79
Repeati430 – 460ANK 1Add BLAST31
Repeati463 – 492ANK 2Add BLAST30
Repeati496 – 525ANK 3Add BLAST30
Repeati529 – 558ANK 4Add BLAST30
Repeati562 – 591ANK 5Add BLAST30
Repeati595 – 627ANK 6Add BLAST33
Repeati631 – 661ANK 7Add BLAST31
Repeati665 – 694ANK 8Add BLAST30
Repeati698 – 729ANK 9Add BLAST32

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili935 – 962Sequence analysisAdd BLAST28

Sequence similaritiesi

Contains 9 ANK repeats.PROSITE-ProRule annotation
Contains 2 MIB/HERC2 domains.PROSITE-ProRule annotation
Contains 3 RING-type zinc fingers.PROSITE-ProRule annotation
Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri79 – 126ZZ-typePROSITE-ProRule annotationAdd BLAST48
Zinc fingeri819 – 854RING-type 1PROSITE-ProRule annotationAdd BLAST36
Zinc fingeri866 – 901RING-type 2PROSITE-ProRule annotationAdd BLAST36
Zinc fingeri963 – 996RING-type 3PROSITE-ProRule annotationAdd BLAST34

Keywords - Domaini

ANK repeat, Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4582. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00790000122981.
HOVERGENiHBG068386.
InParanoidiQ86YT6.
KOiK10645.
OMAiCYNERKT.
OrthoDBiEOG091G00Z0.
PhylomeDBiQ86YT6.
TreeFamiTF324147.

Family and domain databases

Gene3Di1.25.40.20. 4 hits.
3.30.40.10. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR010606. Mib_Herc2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF06701. MIB_HERC2. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 9 hits.
SM00184. RING. 3 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 6 hits.
PS51416. MIB_HERC2. 2 hits.
PS50089. ZF_RING_2. 3 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q86YT6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNSRNNRVM VEGVGARVVR GPDWKWGKQD GGEGHVGTVR SFESPEEVVV
60 70 80 90 100
VWDNGTAANY RCSGAYDLRI LDSAPTGIKH DGTMCDTCRQ QPIIGIRWKC
110 120 130 140 150
AECTNYDLCT VCYHGDKHHL RHRFYRITTP GSERVLLESR RKSKKITARG
160 170 180 190 200
IFAGARVVRG VDWQWEDQDG GNGRRGKVTE IQDWSASSPH SAAYVLWDNG
210 220 230 240 250
AKNLYRVGFE GMSDLKCVQD AKGGSFYRDH CPVLGEQNGN RNPGGLQIGD
260 270 280 290 300
LVNIDLDLEI VQSLQHGHGG WTDGMFETLT TTGTVCGIDE DHDIVVQYPS
310 320 330 340 350
GNRWTFNPAV LTKANIVRSG DAAQGAEGGT SQFQVGDLVQ VCYDLERIKL
360 370 380 390 400
LQRGHGEWAE AMLPTLGKVG RVQQIYSDSD LKVEVCGTSW TYNPAAVSKV
410 420 430 440 450
ASAGSAISNA SGERLSQLLK KLFETQESGD LNEELVKAAA NGDVAKVEDL
460 470 480 490 500
LKRPDVDVNG QCAGHTAMQA ASQNGHVDIL KLLLKQNVDV EAEDKDGDRA
510 520 530 540 550
VHHAAFGDEG AVIEVLHRGS ADLNARNKRR QTPLHIAVNK GHLQVVKTLL
560 570 580 590 600
DFGCHPSLQD SEGDTPLHDA ISKKRDDILA VLLEAGADVT ITNNNGFNAL
610 620 630 640 650
HHAALRGNPS AMRVLLSKLP RPWIVDEKKD DGYTALHLAA LNNHVEVAEL
660 670 680 690 700
LVHQGNANLD IQNVNQQTAL HLAVERQHTQ IVRLLVRAGA KLDIQDKDGD
710 720 730 740 750
TPLHEALRHH TLSQLRQLQD MQDVGKVDAA WEPSKNTLIM GLGTQGAEKK
760 770 780 790 800
SAASIACFLA ANGADLSIRN KKGQSPLDLC PDPNLCKALA KCHKEKVSGQ
810 820 830 840 850
VGSRSPSMIS NDSETLEECM VCSDMKRDTL FGPCGHIATC SLCSPRVKKC
860 870 880 890 900
LICKEQVQSR TKIEECVVCS DKKAAVLFQP CGHMCACENC ANLMKKCVQC
910 920 930 940 950
RAVVERRVPF IMCCGGKSSE DATDDISSGN IPVLQKDKDN TNVNADVQKL
960 970 980 990 1000
QQQLQDIKEQ TMCPVCLDRL KNMIFLCGHG TCQLCGDRMS ECPICRKAIE

RRILLY
Length:1,006
Mass (Da):110,136
Last modified:June 1, 2003 - v1
Checksum:i5D7D0D91AF98FF18
GO

Sequence cautioni

The sequence AAH22403 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAN18023 differs from that shown. Reason: Frameshift at position 3.Curated
The sequence BAC11439 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti327E → K in AAN18023 (Ref. 2) Curated1
Sequence conflicti398S → F in AAN18023 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_069385174R → H Found in a patient with severe mental retardation, psychomotor delay, no speech, sleep disturbances, feeding problems, abnormal breething, deep-set eyes and short philtrum. 1 PublicationCorresponds to variant rs755375969dbSNPEnsembl.1
Natural variantiVAR_069620943V → F in LVNC7. 1 PublicationCorresponds to variant rs200035428dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY149908 mRNA. Translation: AAN75493.1.
AY147849 mRNA. Translation: AAN18023.1. Frameshift.
EF444995 Genomic DNA. Translation: ACA06016.1.
BC022403 mRNA. Translation: AAH22403.1. Different initiation.
BC110581 mRNA. Translation: AAI10582.1.
BC110582 mRNA. Translation: AAI10583.1.
CR749635 mRNA. Translation: CAH18429.1.
AL713705 mRNA. Translation: CAD28502.1.
AB037744 mRNA. Translation: BAA92561.1.
AK075157 mRNA. Translation: BAC11439.1. Different initiation.
CCDSiCCDS11871.1.
RefSeqiNP_065825.1. NM_020774.3.
UniGeneiHs.140903.

Genome annotation databases

EnsembliENST00000261537; ENSP00000261537; ENSG00000101752.
GeneIDi57534.
KEGGihsa:57534.
UCSCiuc002ktq.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY149908 mRNA. Translation: AAN75493.1.
AY147849 mRNA. Translation: AAN18023.1. Frameshift.
EF444995 Genomic DNA. Translation: ACA06016.1.
BC022403 mRNA. Translation: AAH22403.1. Different initiation.
BC110581 mRNA. Translation: AAI10582.1.
BC110582 mRNA. Translation: AAI10583.1.
CR749635 mRNA. Translation: CAH18429.1.
AL713705 mRNA. Translation: CAD28502.1.
AB037744 mRNA. Translation: BAA92561.1.
AK075157 mRNA. Translation: BAC11439.1. Different initiation.
CCDSiCCDS11871.1.
RefSeqiNP_065825.1. NM_020774.3.
UniGeneiHs.140903.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4TSEX-ray2.06A/B239-409[»]
4XI6X-ray2.04A8-402[»]
4XI7X-ray2.05A8-402[»]
4XIBX-ray2.15A8-402[»]
ProteinModelPortaliQ86YT6.
SMRiQ86YT6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121593. 73 interactors.
IntActiQ86YT6. 40 interactors.
MINTiMINT-2841371.
STRINGi9606.ENSP00000261537.

PTM databases

iPTMnetiQ86YT6.
PhosphoSitePlusiQ86YT6.

Polymorphism and mutation databases

DMDMi68565512.

Proteomic databases

EPDiQ86YT6.
MaxQBiQ86YT6.
PaxDbiQ86YT6.
PeptideAtlasiQ86YT6.
PRIDEiQ86YT6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261537; ENSP00000261537; ENSG00000101752.
GeneIDi57534.
KEGGihsa:57534.
UCSCiuc002ktq.5. human.

Organism-specific databases

CTDi57534.
DisGeNETi57534.
GeneCardsiMIB1.
HGNCiHGNC:21086. MIB1.
HPAiCAB037044.
HPA019100.
MalaCardsiMIB1.
MIMi608677. gene.
615092. phenotype.
neXtProtiNX_Q86YT6.
OpenTargetsiENSG00000101752.
Orphaneti54260. Left ventricular noncompaction.
PharmGKBiPA134862722.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
KOG4582. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00790000122981.
HOVERGENiHBG068386.
InParanoidiQ86YT6.
KOiK10645.
OMAiCYNERKT.
OrthoDBiEOG091G00Z0.
PhylomeDBiQ86YT6.
TreeFamiTF324147.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2691232. Constitutive Signaling by NOTCH1 HD Domain Mutants.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
SignaLinkiQ86YT6.
SIGNORiQ86YT6.

Miscellaneous databases

ChiTaRSiMIB1. human.
GeneWikiiMIB1_(gene).
GenomeRNAii57534.
PROiQ86YT6.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101752.
CleanExiHS_MIB1.
GenevisibleiQ86YT6. HS.

Family and domain databases

Gene3Di1.25.40.20. 4 hits.
3.30.40.10. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR010606. Mib_Herc2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR000433. Znf_ZZ.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF06701. MIB_HERC2. 2 hits.
PF00569. ZZ. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 9 hits.
SM00184. RING. 3 hits.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 6 hits.
PS51416. MIB_HERC2. 2 hits.
PS50089. ZF_RING_2. 3 hits.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMIB1_HUMAN
AccessioniPrimary (citable) accession number: Q86YT6
Secondary accession number(s): B0YJ38
, Q2TB37, Q68D01, Q6YI51, Q8NBY0, Q8TCB5, Q8TCL7, Q9P2M3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: June 1, 2003
Last modified: November 30, 2016
This is version 139 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

Miscellaneous

In epilepsy brain tissue, levels of expression are increased in the cytoplasm and microsomal fractions (endoplasmic reticulum).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.