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Protein

Dipeptidyl peptidase 2

Gene

DPP7

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

Functioni

Plays an important role in the degradation of some oligopeptides.1 Publication

Catalytic activityi

Release of an N-terminal dipeptide, Xaa-Yaa-|-, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides.1 Publication

pH dependencei

Optimum pH is 5.5. Has low activity at pH 7 and is inactive at pH 8.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei162 – 1621Charge relay systemSequence Analysis
Active sitei418 – 4181Charge relay systemSequence Analysis
Active sitei443 – 4431Charge relay systemSequence Analysis

GO - Molecular functioni

  • dipeptidyl-peptidase activity Source: Ensembl
  • serine-type peptidase activity Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Enzyme and pathway databases

BRENDAi3.4.14.2. 2681.

Protein family/group databases

ESTHERihuman-DPP7. Prolylcarboxypeptidase.
MEROPSiS28.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Dipeptidyl peptidase 2 (EC:3.4.14.2)
Alternative name(s):
Dipeptidyl aminopeptidase II
Dipeptidyl peptidase 7
Dipeptidyl peptidase II
Short name:
DPP II
Quiescent cell proline dipeptidase
Gene namesi
Name:DPP7
Synonyms:DPP2, QPP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:14892. DPP7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  • cytosol Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: HPA
  • intracellular membrane-bounded organelle Source: HPA
  • lysosome Source: UniProtKB-SubCell
  • vesicle Source: CACAO
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Lysosome, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27469.

Polymorphism and mutation databases

BioMutaiDPP7.
DMDMi212276510.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 254Sequence AnalysisPRO_0000027314
Chaini26 – 492467Dipeptidyl peptidase 2PRO_0000027315Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi50 – 501N-linked (GlcNAc...)1 Publication
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi315 – 3151N-linked (GlcNAc...)1 Publication
Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi363 – 3631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ9UHL4.
PaxDbiQ9UHL4.
PRIDEiQ9UHL4.

PTM databases

PhosphoSiteiQ9UHL4.

Expressioni

Tissue specificityi

Detected in seminal plasma (at protein level).1 Publication

Gene expression databases

BgeeiQ9UHL4.
CleanExiHS_DPP7.
ExpressionAtlasiQ9UHL4. baseline and differential.
GenevisibleiQ9UHL4. HS.

Organism-specific databases

HPAiCAB025541.
HPA021282.
HPA059381.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi118989. 9 interactions.
IntActiQ9UHL4. 10 interactions.
STRINGi9606.ENSP00000360635.

Structurei

Secondary structure

1
492
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 409Combined sources
Turni47 – 504Combined sources
Beta strandi52 – 609Combined sources
Turni66 – 683Combined sources
Beta strandi71 – 755Combined sources
Helixi81 – 877Combined sources
Helixi89 – 9810Combined sources
Beta strandi101 – 1055Combined sources
Helixi117 – 1215Combined sources
Helixi131 – 14818Combined sources
Beta strandi156 – 1616Combined sources
Helixi163 – 17412Combined sources
Turni176 – 1783Combined sources
Beta strandi180 – 1856Combined sources
Helixi191 – 1933Combined sources
Helixi200 – 21011Combined sources
Helixi214 – 23320Combined sources
Helixi236 – 2438Combined sources
Beta strandi245 – 2473Combined sources
Helixi252 – 27120Combined sources
Beta strandi278 – 2847Combined sources
Helixi288 – 29710Combined sources
Helixi302 – 31413Combined sources
Beta strandi316 – 3183Combined sources
Beta strandi321 – 3233Combined sources
Helixi325 – 3284Combined sources
Helixi342 – 35110Combined sources
Turni352 – 3543Combined sources
Beta strandi363 – 3686Combined sources
Helixi375 – 38612Combined sources
Helixi394 – 3996Combined sources
Beta strandi409 – 4157Combined sources
Helixi421 – 4233Combined sources
Beta strandi430 – 4389Combined sources
Helixi445 – 4473Combined sources
Helixi456 – 47621Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JYHX-ray2.19A/B/C/D28-492[»]
3N0TX-ray2.45A/B/C/D28-492[»]
4EBBX-ray2.00A/B27-492[»]
ProteinModelPortaliQ9UHL4.
SMRiQ9UHL4. Positions 28-477.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UHL4.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S28 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG290141.
GeneTreeiENSGT00530000063027.
HOGENOMiHOG000238311.
HOVERGENiHBG005526.
InParanoidiQ9UHL4.
KOiK01276.
OMAiRWEFGTC.
OrthoDBiEOG78WKRN.
PhylomeDBiQ9UHL4.
TreeFamiTF314414.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR008758. Peptidase_S28.
[Graphical view]
PANTHERiPTHR11010. PTHR11010. 1 hit.
PfamiPF05577. Peptidase_S28. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9UHL4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSAPWAPVL LLALGLRGLQ AGARRAPDPG FQERFFQQRL DHFNFERFGN
60 70 80 90 100
KTFPQRFLVS DRFWVRGEGP IFFYTGNEGD VWAFANNSAF VAELAAERGA
110 120 130 140 150
LLVFAEHRYY GKSLPFGAQS TQRGHTELLT VEQALADFAE LLRALRRDLG
160 170 180 190 200
AQDAPAIAFG GSYGGMLSAY LRMKYPHLVA GALAASAPVL AVAGLGDSNQ
210 220 230 240 250
FFRDVTADFE GQSPKCTQGV REAFRQIKDL FLQGAYDTVR WEFGTCQPLS
260 270 280 290 300
DEKDLTQLFM FARNAFTVLA MMDYPYPTDF LGPLPANPVK VGCDRLLSEA
310 320 330 340 350
QRITGLRALA GLVYNASGSE HCYDIYRLYH SCADPTGCGT GPDARAWDYQ
360 370 380 390 400
ACTEINLTFA SNNVTDMFPD LPFTDELRQR YCLDTWGVWP RPDWLLTSFW
410 420 430 440 450
GGDLRAASNI IFSNGNLDPW AGGGIRRNLS ASVIAVTIQG GAHHLDLRAS
460 470 480 490
HPEDPASVVE ARKLEATIIG EWVKAARREQ QPALRGGPRL SL
Length:492
Mass (Da):54,341
Last modified:November 4, 2008 - v3
Checksum:i6C3EDECA90FA7583
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711I → T in AAF12747 (PubMed:10567372).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891A → G.2 Publications
Corresponds to variant rs10747049 [ dbSNP | Ensembl ].
VAR_047087

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF154502 mRNA. Translation: AAF12747.1.
AK292112 mRNA. Translation: BAF84801.1.
AL929554 Genomic DNA. Translation: CAH72872.1.
BC011907 mRNA. Translation: AAH11907.1.
BC016961 mRNA. Translation: AAH16961.1.
CCDSiCCDS7030.1.
PIRiS77568.
RefSeqiNP_037511.2. NM_013379.2.
UniGeneiHs.37916.

Genome annotation databases

EnsembliENST00000371579; ENSP00000360635; ENSG00000176978.
GeneIDi29952.
KEGGihsa:29952.
UCSCiuc004clh.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF154502 mRNA. Translation: AAF12747.1.
AK292112 mRNA. Translation: BAF84801.1.
AL929554 Genomic DNA. Translation: CAH72872.1.
BC011907 mRNA. Translation: AAH11907.1.
BC016961 mRNA. Translation: AAH16961.1.
CCDSiCCDS7030.1.
PIRiS77568.
RefSeqiNP_037511.2. NM_013379.2.
UniGeneiHs.37916.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JYHX-ray2.19A/B/C/D28-492[»]
3N0TX-ray2.45A/B/C/D28-492[»]
4EBBX-ray2.00A/B27-492[»]
ProteinModelPortaliQ9UHL4.
SMRiQ9UHL4. Positions 28-477.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118989. 9 interactions.
IntActiQ9UHL4. 10 interactions.
STRINGi9606.ENSP00000360635.

Chemistry

BindingDBiQ9UHL4.
ChEMBLiCHEMBL2111469.
GuidetoPHARMACOLOGYi1605.

Protein family/group databases

ESTHERihuman-DPP7. Prolylcarboxypeptidase.
MEROPSiS28.002.

PTM databases

PhosphoSiteiQ9UHL4.

Polymorphism and mutation databases

BioMutaiDPP7.
DMDMi212276510.

Proteomic databases

MaxQBiQ9UHL4.
PaxDbiQ9UHL4.
PRIDEiQ9UHL4.

Protocols and materials databases

DNASUi29952.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371579; ENSP00000360635; ENSG00000176978.
GeneIDi29952.
KEGGihsa:29952.
UCSCiuc004clh.3. human.

Organism-specific databases

CTDi29952.
GeneCardsiGC09M140004.
H-InvDBHIX0017204.
HIX0025819.
HGNCiHGNC:14892. DPP7.
HPAiCAB025541.
HPA021282.
HPA059381.
MIMi610537. gene.
neXtProtiNX_Q9UHL4.
PharmGKBiPA27469.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG290141.
GeneTreeiENSGT00530000063027.
HOGENOMiHOG000238311.
HOVERGENiHBG005526.
InParanoidiQ9UHL4.
KOiK01276.
OMAiRWEFGTC.
OrthoDBiEOG78WKRN.
PhylomeDBiQ9UHL4.
TreeFamiTF314414.

Enzyme and pathway databases

BRENDAi3.4.14.2. 2681.

Miscellaneous databases

ChiTaRSiDPP7. human.
EvolutionaryTraceiQ9UHL4.
GeneWikiiDPP7.
GenomeRNAii29952.
NextBioi52649.
PROiQ9UHL4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UHL4.
CleanExiHS_DPP7.
ExpressionAtlasiQ9UHL4. baseline and differential.
GenevisibleiQ9UHL4. HS.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR008758. Peptidase_S28.
[Graphical view]
PANTHERiPTHR11010. PTHR11010. 1 hit.
PfamiPF05577. Peptidase_S28. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence, purification, and cloning of an intracellular serine protease, quiescent cell proline dipeptidase."
    Underwood R., Chiravuri M., Lee H., Schmitz T., Kabcenell A.K., Yardley Y., Huber B.T.
    J. Biol. Chem. 274:34053-34058(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT GLY-89.
  2. "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: Synovial cell.
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [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], VARIANT GLY-89.
    Tissue: Brain.
  5. "Vesicular localization and characterization of a novel post-proline-cleaving aminodipeptidase, quiescent cell proline dipeptidase."
    Chiravuri M., Agarraberes F., Mathieu S.L., Lee H., Huber B.T.
    J. Immunol. 165:5695-5702(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50 AND ASN-315.
    Tissue: Liver.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "Kinetic investigation of human dipeptidyl peptidase II (DPPII)-mediated hydrolysis of dipeptide derivatives and its identification as quiescent cell proline dipeptidase (QPP)/dipeptidyl peptidase 7 (DPP7)."
    Maes M.B., Lambeir A.M., Gilany K., Senten K., Van der Veken P., Leiting B., Augustyns K., Scharpe S., De Meester I.
    Biochem. J. 386:315-324(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 28-492, PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiDPP2_HUMAN
AccessioniPrimary (citable) accession number: Q9UHL4
Secondary accession number(s): A8K7U7, Q5VSF1, Q969X4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 4, 2008
Last modified: July 22, 2015
This is version 138 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. Peptidase families
    Classification of peptidase families and list of entries
  7. 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.