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Protein

Peroxisomal trans-2-enoyl-CoA reductase

Gene

PECR

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

Functioni

Participates in chain elongation of fatty acids. Has no 2,4-dienoyl-CoA reductase activity.

Catalytic activityi

Acyl-CoA + NADP+ = trans-2,3-dehydroacyl-CoA + NADPH.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei179 – 1791Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi23 – 4725NADPBy similarityAdd
BLAST

GO - Molecular functioni

  1. receptor binding Source: UniProtKB
  2. trans-2-enoyl-CoA reductase (NADPH) activity Source: UniProtKB

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-UniPathway
  2. oxidation-reduction process Source: UniProtKB
  3. phytol metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS03889-MONOMER.
BRENDAi1.3.1.38. 2681.
UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal trans-2-enoyl-CoA reductase (EC:1.3.1.38)
Short name:
TERP
Alternative name(s):
2,4-dienoyl-CoA reductase-related protein
Short name:
DCR-RP
HPDHase
Short chain dehydrogenase/reductase family 29C member 1
pVI-ARL
Gene namesi
Name:PECR
Synonyms:SDR29C1
ORF Names:PRO1004
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:18281. PECR.

Subcellular locationi

Peroxisome 1 Publication

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: HPA
  2. mitochondrion Source: Ensembl
  3. peroxisomal membrane Source: UniProtKB
  4. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi303 – 3031Missing : Abolishes localization to peroxisomes. 1 Publication

Organism-specific databases

PharmGKBiPA134967510.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 303302Peroxisomal trans-2-enoyl-CoA reductasePRO_0000054740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321N6-succinyllysineBy similarity
Modified residuei49 – 491Phosphoserine1 Publication
Modified residuei179 – 1791Phosphotyrosine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BY49.
PaxDbiQ9BY49.
PRIDEiQ9BY49.

PTM databases

PhosphoSiteiQ9BY49.

Expressioni

Inductioni

Not induced by IR.1 Publication

Gene expression databases

BgeeiQ9BY49.
CleanExiHS_PECR.
ExpressionAtlasiQ9BY49. baseline and differential.
GenevestigatoriQ9BY49.

Organism-specific databases

HPAiHPA021593.
HPA022539.

Interactioni

Subunit structurei

Interacts with PEX5, probably required to target it into peroxisomes.2 Publications

Protein-protein interaction databases

BioGridi120932. 6 interactions.
IntActiQ9BY49. 1 interaction.
STRINGi9606.ENSP00000265322.

Structurei

Secondary structure

1
303
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni13 – 186Combined sources
Beta strandi20 – 245Combined sources
Turni25 – 273Combined sources
Helixi29 – 4012Combined sources
Beta strandi44 – 507Combined sources
Helixi52 – 6413Combined sources
Beta strandi74 – 785Combined sources
Helixi84 – 9815Combined sources
Beta strandi103 – 1064Combined sources
Helixi116 – 1183Combined sources
Helixi121 – 13111Combined sources
Helixi133 – 14513Combined sources
Helixi147 – 1504Combined sources
Beta strandi152 – 1576Combined sources
Helixi169 – 18820Combined sources
Helixi190 – 1923Combined sources
Beta strandi194 – 2018Combined sources
Helixi208 – 2103Combined sources
Helixi214 – 2218Combined sources
Helixi224 – 2274Combined sources
Helixi237 – 24711Combined sources
Helixi249 – 2513Combined sources
Beta strandi258 – 2625Combined sources
Helixi265 – 2673Combined sources
Helixi288 – 30215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YXMX-ray1.90A/B/C/D1-303[»]
ProteinModelPortaliQ9BY49.
SMRiQ9BY49. Positions 7-303.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BY49.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi301 – 3033Microbody targeting signal

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG105268.
InParanoidiQ9BY49.
KOiK07753.
OMAiCSGIRIN.
PhylomeDBiQ9BY49.
TreeFamiTF315256.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSiPR00081. GDHRDH.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BY49-1) [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
MASWAKGRSY LAPGLLQGQV AIVTGGATGI GKAIVKELLE LGSNVVIASR
60 70 80 90 100
KLERLKSAAD ELQANLPPTK QARVIPIQCN IRNEEEVNNL VKSTLDTFGK
110 120 130 140 150
INFLVNNGGG QFLSPAEHIS SKGWHAVLET NLTGTFYMCK AVYSSWMKEH
160 170 180 190 200
GGSIVNIIVP TKAGFPLAVH SGAARAGVYN LTKSLALEWA CSGIRINCVA
210 220 230 240 250
PGVIYSQTAV ENYGSWGQSF FEGSFQKIPA KRIGVPEEVS SVVCFLLSPA
260 270 280 290 300
ASFITGQSVD VDGGRSLYTH SYEVPDHDNW PKGAGDLSVV KKMKETFKEK

AKL
Length:303
Mass (Da):32,544
Last modified:March 29, 2005 - v2
Checksum:iBCCE6AB89F58382C
GO
Isoform 2 (identifier: Q9BY49-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-146: Missing.

Show »
Length:157
Mass (Da):16,834
Checksum:i8215EB7A51D81D48
GO

Sequence cautioni

The sequence AAF69798.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221I → F in CAB89810 (PubMed:11669066).Curated
Sequence conflicti129 – 1291E → R in CAB89810 (PubMed:11669066).Curated
Sequence conflicti135 – 1351T → S in CAB89810 (PubMed:11669066).Curated
Sequence conflicti248 – 2481S → P in CAG33426 (Ref. 5) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti149 – 1491E → K.
Corresponds to variant rs1429148 [ dbSNP | Ensembl ].
VAR_021535
Natural varianti297 – 2971F → L.
Corresponds to variant rs9288513 [ dbSNP | Ensembl ].
VAR_021536

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 146146Missing in isoform 2. 2 PublicationsVSP_013260Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF232009 mRNA. Translation: AAF69798.1. Different initiation.
AJ250303 mRNA. Translation: CAB89810.1.
AF212234 mRNA. Translation: AAK14920.1.
AF119841 mRNA. Translation: AAF69595.1.
CR457145 mRNA. Translation: CAG33426.1.
AK315795 mRNA. Translation: BAG38139.1.
AC010686 Genomic DNA. Translation: AAY14657.1.
BC002529 mRNA. Translation: AAH02529.1.
CCDSiCCDS33375.1. [Q9BY49-1]
RefSeqiNP_060911.2. NM_018441.5. [Q9BY49-1]
UniGeneiHs.281680.

Genome annotation databases

EnsembliENST00000265322; ENSP00000265322; ENSG00000115425. [Q9BY49-1]
GeneIDi55825.
KEGGihsa:55825.
UCSCiuc002vft.3. human. [Q9BY49-1]

Polymorphism databases

DMDMi62287123.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF232009 mRNA. Translation: AAF69798.1. Different initiation.
AJ250303 mRNA. Translation: CAB89810.1.
AF212234 mRNA. Translation: AAK14920.1.
AF119841 mRNA. Translation: AAF69595.1.
CR457145 mRNA. Translation: CAG33426.1.
AK315795 mRNA. Translation: BAG38139.1.
AC010686 Genomic DNA. Translation: AAY14657.1.
BC002529 mRNA. Translation: AAH02529.1.
CCDSiCCDS33375.1. [Q9BY49-1]
RefSeqiNP_060911.2. NM_018441.5. [Q9BY49-1]
UniGeneiHs.281680.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YXMX-ray1.90A/B/C/D1-303[»]
ProteinModelPortaliQ9BY49.
SMRiQ9BY49. Positions 7-303.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120932. 6 interactions.
IntActiQ9BY49. 1 interaction.
STRINGi9606.ENSP00000265322.

Chemistry

DrugBankiDB00173. Adenine.

PTM databases

PhosphoSiteiQ9BY49.

Polymorphism databases

DMDMi62287123.

Proteomic databases

MaxQBiQ9BY49.
PaxDbiQ9BY49.
PRIDEiQ9BY49.

Protocols and materials databases

DNASUi55825.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265322; ENSP00000265322; ENSG00000115425. [Q9BY49-1]
GeneIDi55825.
KEGGihsa:55825.
UCSCiuc002vft.3. human. [Q9BY49-1]

Organism-specific databases

CTDi55825.
GeneCardsiGC02M216867.
HGNCiHGNC:18281. PECR.
HPAiHPA021593.
HPA022539.
MIMi605843. gene.
neXtProtiNX_Q9BY49.
PharmGKBiPA134967510.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1028.
GeneTreeiENSGT00760000118868.
HOVERGENiHBG105268.
InParanoidiQ9BY49.
KOiK07753.
OMAiCSGIRIN.
PhylomeDBiQ9BY49.
TreeFamiTF315256.

Enzyme and pathway databases

UniPathwayiUPA00094.
BioCyciMetaCyc:HS03889-MONOMER.
BRENDAi1.3.1.38. 2681.

Miscellaneous databases

EvolutionaryTraceiQ9BY49.
GeneWikiiPECR.
GenomeRNAii55825.
NextBioi61022.
PROiQ9BY49.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BY49.
CleanExiHS_PECR.
ExpressionAtlasiQ9BY49. baseline and differential.
GenevestigatoriQ9BY49.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PRINTSiPR00081. GDHRDH.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and expression of mammalian peroxisomal trans-2-enoyl-coenzyme A reductase cDNAs."
    Das A.K., Uhler M.D., Hajra A.K.
    J. Biol. Chem. 275:24333-24340(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY.
  2. "Identification of a novel human peroxisomal 2,4-dienoyl-CoA reductase related protein using the M13 phage protein VI phage display technology."
    Amery L., Mannaerts G.P., Subramani S., Van Veldhoven P.P., Fransen M.
    Comb. Chem. High Throughput Screen. 4:545-552(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH PEX5, MUTAGENESIS OF LEU-303.
  3. "A novel gene expressed in human liver non-tumor tissues."
    Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.
    Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Liver.
  4. "Functional prediction of the coding sequences of 79 new genes deduced by analysis of cDNA clones from human fetal liver."
    Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal liver.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  6. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Colon.
  7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  9. "Ku86 autoantigen related protein-1 transcription initiates from a CpG island and is induced by p53 through a nearby p53 response element."
    Braastad C.D., Leguia M., Hendrickson E.A.
    Nucleic Acids Res. 30:1713-1724(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND TYR-179, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Crystal structure of peroxisomal trans 2-enoyl CoA reductase (PECRA)."
    Structural genomics consortium (SGC)
    Submitted (APR-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ADENINE AND PHOSPHATE.

Entry informationi

Entry nameiPECR_HUMAN
AccessioniPrimary (citable) accession number: Q9BY49
Secondary accession number(s): B2RE42
, Q53TC4, Q6IAK9, Q9NRD4, Q9NY60, Q9P1A4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: March 29, 2005
Last modified: April 1, 2015
This is version 125 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

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.