Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA replication licensing factor MCM2

Gene

MCM2

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

Functioni

Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri329 – 355C4-typeSequence analysisAdd BLAST27
Nucleotide bindingi523 – 530ATPSequence analysis8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: ProtInc
  • DNA helicase activity Source: InterPro
  • DNA replication origin binding Source: Ensembl
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cell cycle Source: ProtInc
  • cellular response to interleukin-4 Source: Ensembl
  • DNA replication Source: Reactome
  • DNA replication initiation Source: UniProtKB
  • DNA unwinding involved in DNA replication Source: Ensembl
  • G1/S transition of mitotic cell cycle Source: Reactome
  • nucleosome assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000073111-MONOMER.
ReactomeiR-HSA-176187. Activation of ATR in response to replication stress.
R-HSA-176974. Unwinding of DNA.
R-HSA-68867. Assembly of the pre-replicative complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-68962. Activation of the pre-replicative complex.
R-HSA-69052. Switching of origins to a post-replicative state.
R-HSA-69300. Removal of licensing factors from origins.
SIGNORiP49736.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor MCM2 (EC:3.6.4.12)
Alternative name(s):
Minichromosome maintenance protein 2 homolog
Nuclear protein BM28
Gene namesi
Name:MCM2
Synonyms:BM28, CCNL1, CDCL1, KIAA0030
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:6944. MCM2.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • chromatin Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • MCM complex Source: UniProtKB
  • microtubule cytoskeleton Source: HPA
  • nuclear chromosome, telomeric region Source: BHF-UCL
  • nuclear origin of replication recognition complex Source: Ensembl
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi27S → A: Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-41 and A-139. 1 Publication1
Mutagenesisi41S → A: Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-27 and A-139. 1 Publication1
Mutagenesisi108S → A: Reduces phosphorylation by ATR. 1 Publication1
Mutagenesisi139S → A: Impairs ATPase activity of the MCM-2-7 complex and reduces phosphorylation by the CDC7-DBF4 complex; when associated with A-27 and A-41. 1 Publication1

Organism-specific databases

DisGeNETi4171.
OpenTargetsiENSG00000073111.
PharmGKBiPA164742061.

Polymorphism and mutation databases

DMDMi41019490.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001940872 – 904DNA replication licensing factor MCM2Add BLAST903

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei12PhosphoserineBy similarity1
Modified residuei13PhosphoserineCombined sources1
Modified residuei25PhosphothreonineCombined sources1
Modified residuei26PhosphoserineCombined sources1
Modified residuei27PhosphoserineCombined sources1 Publication1
Modified residuei32PhosphoserineCombined sources1
Modified residuei39PhosphothreonineCombined sources1
Modified residuei40Phosphoserine; by CDC7Combined sources1 Publication1
Modified residuei41PhosphoserineCombined sources1 Publication1
Modified residuei53Phosphoserine; by CDC7Combined sources2 Publications1
Modified residuei59PhosphothreonineCombined sources1
Modified residuei108Phosphoserine; by ATRCombined sources2 Publications1
Modified residuei137PhosphotyrosineCombined sources1
Modified residuei139PhosphoserineCombined sources1 Publication1
Modified residuei216N6-acetyllysineCombined sources1
Modified residuei381PhosphoserineCombined sources1
Modified residuei484PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated on Ser-108 by ATR in proliferating cells. Ser-108 proliferation is increased by genotoxic agents. Ser-40 is mediated by the CDC7-DBF4 and CDC7-DBF4B complexes, while Ser-53 phosphorylation is only mediated by the CDC7-DBF4 complex. Phosphorylation by the CDC7-DBF4 complex during G1/S phase is required for the initiation of DNA replication.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP49736.
MaxQBiP49736.
PaxDbiP49736.
PeptideAtlasiP49736.
PRIDEiP49736.

PTM databases

iPTMnetiP49736.
PhosphoSitePlusiP49736.
SwissPalmiP49736.

Miscellaneous databases

PMAP-CutDBP49736.

Expressioni

Gene expression databases

BgeeiENSG00000073111.
CleanExiHS_CCNL1.
HS_MCM2.
ExpressionAtlasiP49736. baseline and differential.
GenevisibleiP49736. HS.

Organism-specific databases

HPAiCAB000303.
HPA031495.
HPA031496.

Interactioni

Subunit structurei

Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (Probable). Interacts with DBF4 (By similarity). Interacts with KAT7. May interact with MCM10.By similarityCurated5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKAP8O438237EBI-374819,EBI-1237481
HIST2H4BP628053EBI-374819,EBI-302023
MCM3P252055EBI-374819,EBI-355153
MCM5P339925EBI-374819,EBI-359410
MCM6Q1456613EBI-374819,EBI-374900
MCM7P3399321EBI-374819,EBI-355924
MCMBPQ9BTE34EBI-374819,EBI-749378
PLK1P533502EBI-374819,EBI-476768
SNF8Q96H208EBI-374819,EBI-747719
TERF2IPQ9NYB02EBI-374819,EBI-750109

Protein-protein interaction databases

BioGridi110339. 913 interactors.
DIPiDIP-31732N.
IntActiP49736. 57 interactors.
MINTiMINT-5004296.
STRINGi9606.ENSP00000265056.

Structurei

Secondary structure

1904
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi70 – 74Combined sources5
Helixi77 – 81Combined sources5
Helixi85 – 88Combined sources4
Beta strandi98 – 100Combined sources3
Helixi108 – 123Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UUZX-ray2.90C69-138[»]
5BNVX-ray2.79C/F61-130[»]
5BNXX-ray2.31C61-130[»]
5BO0X-ray2.91C61-130[»]
5C3IX-ray3.50D/H/L/P/T/X63-124[»]
5JA4X-ray2.42C61-130[»]
ProteinModelPortaliP49736.
SMRiP49736.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini473 – 679MCMAdd BLAST207

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 257Interaction with KAT7By similarityAdd BLAST256

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi655 – 658Arginine finger4

Sequence similaritiesi

Belongs to the MCM family.Curated
Contains 1 MCM domain.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri329 – 355C4-typeSequence analysisAdd BLAST27

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0477. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00850000132309.
HOVERGENiHBG106398.
InParanoidiP49736.
KOiK02540.
OMAiKYDRIAH.
OrthoDBiEOG091G026H.
PhylomeDBiP49736.
TreeFamiTF300772.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008045. MCM2.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR033762. MCM_OB.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11630:SF44. PTHR11630:SF44. 1 hit.
PfamiPF00493. MCM. 1 hit.
PF12619. MCM2_N. 1 hit.
PF14551. MCM_N. 1 hit.
PF17207. MCM_OB. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01658. MCMPROTEIN2.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P49736-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAESSESFTM ASSPAQRRRG NDPLTSSPGR SSRRTDALTS SPGRDLPPFE
60 70 80 90 100
DESEGLLGTE GPLEEEEDGE ELIGDGMERD YRAIPELDAY EAEGLALDDE
110 120 130 140 150
DVEELTASQR EAAERAMRQR DREAGRGLGR MRRGLLYDSD EEDEERPARK
160 170 180 190 200
RRQVERATED GEEDEEMIES IENLEDLKGH SVREWVSMAG PRLEIHHRFK
210 220 230 240 250
NFLRTHVDSH GHNVFKERIS DMCKENRESL VVNYEDLAAR EHVLAYFLPE
260 270 280 290 300
APAELLQIFD EAALEVVLAM YPKYDRITNH IHVRISHLPL VEELRSLRQL
310 320 330 340 350
HLNQLIRTSG VVTSCTGVLP QLSMVKYNCN KCNFVLGPFC QSQNQEVKPG
360 370 380 390 400
SCPECQSAGP FEVNMEETIY QNYQRIRIQE SPGKVAAGRL PRSKDAILLA
410 420 430 440 450
DLVDSCKPGD EIELTGIYHN NYDGSLNTAN GFPVFATVIL ANHVAKKDNK
460 470 480 490 500
VAVGELTDED VKMITSLSKD QQIGEKIFAS IAPSIYGHED IKRGLALALF
510 520 530 540 550
GGEPKNPGGK HKVRGDINVL LCGDPGTAKS QFLKYIEKVS SRAIFTTGQG
560 570 580 590 600
ASAVGLTAYV QRHPVSREWT LEAGALVLAD RGVCLIDEFD KMNDQDRTSI
610 620 630 640 650
HEAMEQQSIS ISKAGIVTSL QARCTVIAAA NPIGGRYDPS LTFSENVDLT
660 670 680 690 700
EPIISRFDIL CVVRDTVDPV QDEMLARFVV GSHVRHHPSN KEEEGLANGS
710 720 730 740 750
AAEPAMPNTY GVEPLPQEVL KKYIIYAKER VHPKLNQMDQ DKVAKMYSDL
760 770 780 790 800
RKESMATGSI PITVRHIESM IRMAEAHARI HLRDYVIEDD VNMAIRVMLE
810 820 830 840 850
SFIDTQKFSV MRSMRKTFAR YLSFRRDNNE LLLFILKQLV AEQVTYQRNR
860 870 880 890 900
FGAQQDTIEV PEKDLVDKAR QINIHNLSAF YDSELFRMNK FSHDLKRKMI

LQQF
Length:904
Mass (Da):101,896
Last modified:January 16, 2004 - v4
Checksum:i52C6DC61F128B404
GO

Sequence cautioni

The sequence BAA04642 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAA12177 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAA47749 differs from that shown. Reason: Frameshift at positions 115, 124, 127, 129, 154, 158, 773 and 811.Curated
The sequence CAA47749 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1M → S in CAA47749 (PubMed:8175912).Curated1
Sequence conflicti109Q → R in CAA47749 (PubMed:8175912).Curated1
Sequence conflicti388G → R in CAA47749 (PubMed:8175912).Curated1
Sequence conflicti407 – 408KP → NA in CAA47749 (PubMed:8175912).Curated2
Sequence conflicti407 – 408KP → NA in BAA12177 (Ref. 5) Curated2
Sequence conflicti495L → P in CAA47749 (PubMed:8175912).Curated1
Sequence conflicti555 – 556GL → AV in CAA47749 (PubMed:8175912).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02111168D → E.1 PublicationCorresponds to variant rs3087452dbSNPEnsembl.1
Natural variantiVAR_021112135L → F.1 PublicationCorresponds to variant rs2307314dbSNPEnsembl.1
Natural variantiVAR_033298166E → Q.1 PublicationCorresponds to variant rs1048225dbSNPEnsembl.1
Natural variantiVAR_016137396A → T.1 PublicationCorresponds to variant rs3087450dbSNPEnsembl.1
Natural variantiVAR_033299501G → R.1 PublicationCorresponds to variant rs13087457dbSNPEnsembl.1
Natural variantiVAR_016138667V → M.1 PublicationCorresponds to variant rs2307311dbSNPEnsembl.1
Natural variantiVAR_016139727A → T.2 PublicationsCorresponds to variant rs2307313dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67334 mRNA. Translation: CAA47749.1. Sequence problems.
D21063 mRNA. Translation: BAA04642.1. Different initiation.
AY675259 Genomic DNA. Translation: AAT70723.1.
BC006165 mRNA. Translation: AAH06165.3.
BC007670 mRNA. Translation: AAH07670.2.
BC007938 mRNA. Translation: AAH07938.2.
BC014272 mRNA. Translation: AAH14272.2.
BC017258 mRNA. Translation: AAH17258.2.
BC017490 mRNA. Translation: AAH17490.2.
BC030131 mRNA. Translation: AAH30131.2.
D83987 mRNA. Translation: BAA12177.1. Different initiation.
BT009734 mRNA. Translation: AAP88736.1.
CCDSiCCDS3043.1.
PIRiS42228.
RefSeqiNP_004517.2. NM_004526.3.
UniGeneiHs.477481.

Genome annotation databases

EnsembliENST00000265056; ENSP00000265056; ENSG00000073111.
GeneIDi4171.
KEGGihsa:4171.
UCSCiuc003ejp.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67334 mRNA. Translation: CAA47749.1. Sequence problems.
D21063 mRNA. Translation: BAA04642.1. Different initiation.
AY675259 Genomic DNA. Translation: AAT70723.1.
BC006165 mRNA. Translation: AAH06165.3.
BC007670 mRNA. Translation: AAH07670.2.
BC007938 mRNA. Translation: AAH07938.2.
BC014272 mRNA. Translation: AAH14272.2.
BC017258 mRNA. Translation: AAH17258.2.
BC017490 mRNA. Translation: AAH17490.2.
BC030131 mRNA. Translation: AAH30131.2.
D83987 mRNA. Translation: BAA12177.1. Different initiation.
BT009734 mRNA. Translation: AAP88736.1.
CCDSiCCDS3043.1.
PIRiS42228.
RefSeqiNP_004517.2. NM_004526.3.
UniGeneiHs.477481.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4UUZX-ray2.90C69-138[»]
5BNVX-ray2.79C/F61-130[»]
5BNXX-ray2.31C61-130[»]
5BO0X-ray2.91C61-130[»]
5C3IX-ray3.50D/H/L/P/T/X63-124[»]
5JA4X-ray2.42C61-130[»]
ProteinModelPortaliP49736.
SMRiP49736.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110339. 913 interactors.
DIPiDIP-31732N.
IntActiP49736. 57 interactors.
MINTiMINT-5004296.
STRINGi9606.ENSP00000265056.

PTM databases

iPTMnetiP49736.
PhosphoSitePlusiP49736.
SwissPalmiP49736.

Polymorphism and mutation databases

DMDMi41019490.

Proteomic databases

EPDiP49736.
MaxQBiP49736.
PaxDbiP49736.
PeptideAtlasiP49736.
PRIDEiP49736.

Protocols and materials databases

DNASUi4171.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265056; ENSP00000265056; ENSG00000073111.
GeneIDi4171.
KEGGihsa:4171.
UCSCiuc003ejp.5. human.

Organism-specific databases

CTDi4171.
DisGeNETi4171.
GeneCardsiMCM2.
HGNCiHGNC:6944. MCM2.
HPAiCAB000303.
HPA031495.
HPA031496.
MIMi116945. gene.
neXtProtiNX_P49736.
OpenTargetsiENSG00000073111.
PharmGKBiPA164742061.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0477. Eukaryota.
COG1241. LUCA.
GeneTreeiENSGT00850000132309.
HOVERGENiHBG106398.
InParanoidiP49736.
KOiK02540.
OMAiKYDRIAH.
OrthoDBiEOG091G026H.
PhylomeDBiP49736.
TreeFamiTF300772.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000073111-MONOMER.
ReactomeiR-HSA-176187. Activation of ATR in response to replication stress.
R-HSA-176974. Unwinding of DNA.
R-HSA-68867. Assembly of the pre-replicative complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-68962. Activation of the pre-replicative complex.
R-HSA-69052. Switching of origins to a post-replicative state.
R-HSA-69300. Removal of licensing factors from origins.
SIGNORiP49736.

Miscellaneous databases

ChiTaRSiMCM2. human.
GeneWikiiMCM2.
GenomeRNAii4171.
PMAP-CutDBP49736.
PROiP49736.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000073111.
CleanExiHS_CCNL1.
HS_MCM2.
ExpressionAtlasiP49736. baseline and differential.
GenevisibleiP49736. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008045. MCM2.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR033762. MCM_OB.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11630:SF44. PTHR11630:SF44. 1 hit.
PfamiPF00493. MCM. 1 hit.
PF12619. MCM2_N. 1 hit.
PF14551. MCM_N. 1 hit.
PF17207. MCM_OB. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01658. MCMPROTEIN2.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMCM2_HUMAN
AccessioniPrimary (citable) accession number: P49736
Secondary accession number(s): Q14577
, Q15023, Q8N2V1, Q969W7, Q96AE1, Q9BRM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 16, 2004
Last modified: November 30, 2016
This is version 185 of the entry and version 4 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

Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. Specifically a MCM467 subcomplex is shown to have in vitro helicase activity which is inhibited by the MCM2 subunit. The MCM2-7 hexamer is the proposed physiological active complex.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. 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.