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Protein

Proteasomal ubiquitin receptor ADRM1

Gene

ADRM1

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

Functioni

Functions as a proteasomal ubiquitin receptor. Recruits the deubiquitinating enzyme UCHL5 at the 26S proteasome and promotes its activity.5 Publications

GO - Molecular functioni

  • endopeptidase activator activity Source: UniProtKB
  • protease binding Source: UniProtKB
  • proteasome binding Source: UniProtKB

GO - Biological processi

  • positive regulation of endopeptidase activity Source: GOC
  • proteasome assembly Source: UniProtKB
  • transcription elongation from RNA polymerase II promoter Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasomal ubiquitin receptor ADRM1
Alternative name(s):
110 kDa cell membrane glycoprotein
Short name:
Gp110
Adhesion-regulating molecule 1
Short name:
ARM-1
Proteasome regulatory particle non-ATPase 13
Short name:
hRpn13
Rpn13 homolog
Gene namesi
Name:ADRM1
Synonyms:GP110
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15759. ADRM1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • integral component of plasma membrane Source: ProtInc
  • membrane Source: ProtInc
  • nucleoplasm Source: HPA
  • plasma membrane Source: HPA
  • proteasome complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24599.

Polymorphism and mutation databases

DMDMi20141265.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 407406Proteasomal ubiquitin receptor ADRM1PRO_0000020631Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine3 Publications
Cross-linki34 – 34Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei127 – 1271Phosphotyrosine1 Publication
Modified residuei140 – 1401Phosphoserine1 Publication
Modified residuei211 – 2111Phosphoserine1 Publication
Modified residuei217 – 2171Phosphothreonine2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ16186.
PaxDbiQ16186.
PRIDEiQ16186.

PTM databases

PhosphoSiteiQ16186.

Expressioni

Gene expression databases

BgeeiQ16186.
CleanExiHS_ADRM1.
ExpressionAtlasiQ16186. baseline and differential.
GenevisibleiQ16186. HS.

Organism-specific databases

HPAiHPA042266.

Interactioni

Subunit structurei

Interacts with PSMD1, ubiquitin and UCHL5.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DSK2P485104EBI-954387,EBI-6174From a different organism.
Psmd14O355932EBI-954387,EBI-772796From a different organism.
PSMD4P550364EBI-954387,EBI-359318
RAD23BP547272EBI-954387,EBI-954531
UBCP0CG4810EBI-954387,EBI-3390054
UBQLN1Q9UMX04EBI-954387,EBI-741480
UBQLN2Q9UHD94EBI-954387,EBI-947187
UCHL5Q9Y5K520EBI-954387,EBI-1051183

Protein-protein interaction databases

BioGridi116235. 54 interactions.
DIPiDIP-42668N.
IntActiQ16186. 49 interactions.
MINTiMINT-2869171.
STRINGi9606.ENSP00000253003.

Structurei

Secondary structure

1
407
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi23 – 264Combined sources
Beta strandi28 – 4013Combined sources
Beta strandi45 – 517Combined sources
Beta strandi57 – 6610Combined sources
Beta strandi69 – 757Combined sources
Beta strandi79 – 846Combined sources
Beta strandi89 – 913Combined sources
Beta strandi93 – 986Combined sources
Turni99 – 1013Combined sources
Beta strandi104 – 1096Combined sources
Helixi114 – 1163Combined sources
Helixi117 – 12913Combined sources
Turni191 – 1955Combined sources
Beta strandi202 – 2043Combined sources
Beta strandi249 – 2535Combined sources
Turni254 – 2563Combined sources
Helixi266 – 2738Combined sources
Beta strandi276 – 2783Combined sources
Beta strandi282 – 2843Combined sources
Helixi288 – 2914Combined sources
Helixi294 – 2974Combined sources
Helixi300 – 3023Combined sources
Helixi304 – 3107Combined sources
Helixi311 – 3133Combined sources
Helixi324 – 3263Combined sources
Helixi327 – 3326Combined sources
Helixi334 – 34815Combined sources
Turni349 – 3513Combined sources
Helixi353 – 3586Combined sources
Helixi363 – 3719Combined sources
Helixi374 – 38310Combined sources
Beta strandi386 – 3883Combined sources
Beta strandi395 – 3973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KQZNMR-A253-407[»]
2KR0NMR-A1-407[»]
2L5VNMR-A260-407[»]
2MKZNMR-A270-407[»]
4UELX-ray2.30C266-388[»]
4UEMX-ray2.82B266-388[»]
4WLQX-ray2.85B286-384[»]
4WLRX-ray2.00B285-386[»]
ProteinModelPortaliQ16186.
SMRiQ16186. Positions 1-407.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ16186.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 130109PHAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 132131Interaction with PSMD1Add
BLAST
Regioni362 – 40746Interaction with UCHL5Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi135 – 20268Gly-richAdd
BLAST
Compositional biasi193 – 25765Ser-richAdd
BLAST
Compositional biasi203 – 21311Poly-SerAdd
BLAST

Domaini

The PH domain mediates interactions with PSMD1 and ubiquitin. Preferential binding to the proximal subunit of K48-linked diubiquitin allows UCHL5 access to the distal subunit (By similarity).By similarity

Sequence similaritiesi

Belongs to the ADRM1 family.Curated
Contains 1 PH domain.Curated

Phylogenomic databases

eggNOGiNOG288027.
GeneTreeiENSGT00390000013839.
HOGENOMiHOG000005947.
HOVERGENiHBG073518.
InParanoidiQ16186.
OMAiMQNNAKP.
OrthoDBiEOG70KGQZ.
PhylomeDBiQ16186.
TreeFamiTF313410.

Family and domain databases

InterProiIPR006773. 26S_Psome_Ubiquitin-recp_Rpn13.
[Graphical view]
PANTHERiPTHR12225. PTHR12225. 1 hit.
PfamiPF04683. Proteasom_Rpn13. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q16186-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTSGALFPS LVPGSRGASN KYLVEFRAGK MSLKGTTVTP DKRKGLVYIQ
60 70 80 90 100
QTDDSLIHFC WKDRTSGNVE DDLIIFPDDC EFKRVPQCPS GRVYVLKFKA
110 120 130 140 150
GSKRLFFWMQ EPKTDQDEEH CRKVNEYLNN PPMPGALGAS GSSGHELSAL
160 170 180 190 200
GGEGGLQSLL GNMSHSQLMQ LIGPAGLGGL GGLGALTGPG LASLLGSSGP
210 220 230 240 250
PGSSSSSSSR SQSAAVTPSS TTSSTRATPA PSAPAAASAT SPSPAPSSGN
260 270 280 290 300
GASTAASPTQ PIQLSDLQSI LATMNVPAGP AGGQQVDLAS VLTPEIMAPI
310 320 330 340 350
LANADVQERL LPYLPSGESL PQTADEIQNT LTSPQFQQAL GMFSAALASG
360 370 380 390 400
QLGPLMCQFG LPAEAVEAAN KGDVEAFAKA MQNNAKPEQK EGDTKDKKDE

EEDMSLD
Length:407
Mass (Da):42,153
Last modified:January 23, 2002 - v2
Checksum:i2D38811DCA231864
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1421S → T in BAA11023 (PubMed:8033103).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64154 mRNA. Translation: BAA11023.1.
AL354836 Genomic DNA. Translation: CAC22308.1.
BR000321 mRNA. Translation: FAA00246.1.
BC010733 mRNA. Translation: AAH10733.1.
BC017245 mRNA. Translation: AAH17245.1.
CCDSiCCDS13496.1.
PIRiI52703.
RefSeqiNP_001268366.1. NM_001281437.1.
NP_001268367.1. NM_001281438.1.
NP_008933.2. NM_007002.3.
NP_783163.1. NM_175573.2.
XP_005260314.1. XM_005260257.1.
UniGeneiHs.90107.

Genome annotation databases

EnsembliENST00000253003; ENSP00000253003; ENSG00000130706.
ENST00000491935; ENSP00000478877; ENSG00000130706.
GeneIDi11047.
KEGGihsa:11047.
UCSCiuc002ycn.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64154 mRNA. Translation: BAA11023.1.
AL354836 Genomic DNA. Translation: CAC22308.1.
BR000321 mRNA. Translation: FAA00246.1.
BC010733 mRNA. Translation: AAH10733.1.
BC017245 mRNA. Translation: AAH17245.1.
CCDSiCCDS13496.1.
PIRiI52703.
RefSeqiNP_001268366.1. NM_001281437.1.
NP_001268367.1. NM_001281438.1.
NP_008933.2. NM_007002.3.
NP_783163.1. NM_175573.2.
XP_005260314.1. XM_005260257.1.
UniGeneiHs.90107.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KQZNMR-A253-407[»]
2KR0NMR-A1-407[»]
2L5VNMR-A260-407[»]
2MKZNMR-A270-407[»]
4UELX-ray2.30C266-388[»]
4UEMX-ray2.82B266-388[»]
4WLQX-ray2.85B286-384[»]
4WLRX-ray2.00B285-386[»]
ProteinModelPortaliQ16186.
SMRiQ16186. Positions 1-407.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116235. 54 interactions.
DIPiDIP-42668N.
IntActiQ16186. 49 interactions.
MINTiMINT-2869171.
STRINGi9606.ENSP00000253003.

PTM databases

PhosphoSiteiQ16186.

Polymorphism and mutation databases

DMDMi20141265.

Proteomic databases

MaxQBiQ16186.
PaxDbiQ16186.
PRIDEiQ16186.

Protocols and materials databases

DNASUi11047.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000253003; ENSP00000253003; ENSG00000130706.
ENST00000491935; ENSP00000478877; ENSG00000130706.
GeneIDi11047.
KEGGihsa:11047.
UCSCiuc002ycn.3. human.

Organism-specific databases

CTDi11047.
GeneCardsiGC20P060877.
HGNCiHGNC:15759. ADRM1.
HPAiHPA042266.
MIMi610650. gene.
neXtProtiNX_Q16186.
PharmGKBiPA24599.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG288027.
GeneTreeiENSGT00390000013839.
HOGENOMiHOG000005947.
HOVERGENiHBG073518.
InParanoidiQ16186.
OMAiMQNNAKP.
OrthoDBiEOG70KGQZ.
PhylomeDBiQ16186.
TreeFamiTF313410.

Miscellaneous databases

ChiTaRSiADRM1. human.
EvolutionaryTraceiQ16186.
GeneWikiiADRM1.
GenomeRNAii11047.
NextBioi41984.
PROiQ16186.
SOURCEiSearch...

Gene expression databases

BgeeiQ16186.
CleanExiHS_ADRM1.
ExpressionAtlasiQ16186. baseline and differential.
GenevisibleiQ16186. HS.

Family and domain databases

InterProiIPR006773. 26S_Psome_Ubiquitin-recp_Rpn13.
[Graphical view]
PANTHERiPTHR12225. PTHR12225. 1 hit.
PfamiPF04683. Proteasom_Rpn13. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of the complementary DNA of an M(r) 110,000 antigen expressed by human gastric carcinoma cells and upregulated by gamma-interferon."
    Shimada S., Ogawa M., Takahashi M., Schlom J., Greiner J.W.
    Cancer Res. 54:3831-3836(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A novel proteasome-interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes."
    Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K., Murata S.
    EMBO J. 25:4524-4536(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PSMD1 AND UCHL5, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Brain and Pancreas.
  5. "hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37."
    Qiu X.-B., Ouyang S.-Y., Li C.-J., Miao S., Wang L., Goldberg A.L.
    EMBO J. 25:5742-5753(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH UCHL5, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Adrm1, a putative cell adhesion regulating protein, is a novel proteasome-associated factor."
    Joergensen J.P., Lauridsen A.-M., Kristensen P., Dissing K., Johnsen A.H., Hendil K.B., Hartmann-Petersen R.
    J. Mol. Biol. 360:1043-1052(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH 26S PROTEASOME, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1."
    Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K., Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E.
    Nat. Cell Biol. 8:994-1002(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PSMD1 AND UCHL5, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
    Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
    Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. Cited for: FUNCTION, INTERACTION WITH UBIQUITIN.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND THR-217, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiADRM1_HUMAN
AccessioniPrimary (citable) accession number: Q16186
Secondary accession number(s): A0PKB1, Q96FJ7, Q9H1P2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2002
Last modified: June 24, 2015
This is version 133 of the entry and version 2 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

Caution

Although initially described as a cell membrane glycoprotein, ADRM1 is intracellular and non-glycosylated, and has probably no direct role in cell adhesion.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.