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Protein

Alpha-enolase

Gene

ENO1

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

Functioni

Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production.
MBP1 binds to the myc promoter and acts as a transcriptional repressor. May be a tumor suppressor.

Catalytic activityi

2-phospho-D-glycerate = phosphoenolpyruvate + H2O.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds two Mg2+ per subunit. Required for catalysis and for stabilizing the dimer.1 Publication

pH dependencei

Enolase activity is lost above pH 9.0. Immunoglobulin production stimulating activity is retained at pH 13.0.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi40 – 401Magnesium 1
Binding sitei158 – 1581SubstrateBy similarity
Binding sitei167 – 1671SubstrateBy similarity
Active sitei210 – 2101Proton donorBy similarity
Metal bindingi245 – 2451Magnesium 2
Metal bindingi293 – 2931Magnesium 2
Binding sitei293 – 2931SubstrateBy similarity
Metal bindingi318 – 3181Magnesium 2
Binding sitei318 – 3181SubstrateBy similarity
Active sitei343 – 3431Proton acceptorBy similarity
Binding sitei394 – 3941SubstrateBy similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. GTPase binding Source: UniProtKB
  3. magnesium ion binding Source: InterPro
  4. phosphopyruvate hydratase activity Source: ProtInc
  5. poly(A) RNA binding Source: UniProtKB
  6. sequence-specific DNA binding transcription factor activity Source: ProtInc
  7. transcription corepressor activity Source: ProtInc

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. gluconeogenesis Source: Reactome
  3. glucose metabolic process Source: Reactome
  4. glycolytic process Source: Reactome
  5. negative regulation of cell growth Source: UniProtKB
  6. negative regulation of transcription, DNA-templated Source: UniProtKB
  7. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
  8. pathogenesis Source: Reactome
  9. response to virus Source: UniProtKB
  10. small molecule metabolic process Source: Reactome
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Repressor

Keywords - Biological processi

Glycolysis, Plasminogen activation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000074800-MONOMER.
BRENDAi4.2.1.11. 2681.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RKP06733.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
C-myc promoter-binding protein
Enolase 1
MBP-1
MPB-1
Non-neural enolase
Short name:
NNE
Phosphopyruvate hydratase
Plasminogen-binding protein
Gene namesi
Name:ENO1
Synonyms:ENO1L1, MBPB1, MPB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3350. ENO1.

Subcellular locationi

  1. Cytoplasm 1 Publication
  2. Cell membrane 1 Publication
  3. CytoplasmmyofibrilsarcomereM line 1 Publication

  4. Note: Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form. ENO1 is localized to the M line.

GO - Cellular componenti

  1. cytoplasm Source: LIFEdb
  2. cytosol Source: Reactome
  3. extracellular space Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. M band Source: UniProtKB-SubCell
  6. membrane Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. phosphopyruvate hydratase complex Source: InterPro
  9. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi94 – 941M → I: MBP1 protein production. No MBP1 protein production; when associated with I-97. 1 Publication
Mutagenesisi97 – 971M → I: MBP1 protein production. No MBP1 protein production; when associated with I-94. 1 Publication
Mutagenesisi384 – 3841L → A: Loss of transcriptional repression and cell growth inhibition; when associated with A-388. 1 Publication
Mutagenesisi388 – 3881L → A: Loss of transcriptional repression and cell growth inhibition; when associated with A-384. 1 Publication

Organism-specific databases

PharmGKBiPA27786.

Polymorphism and mutation databases

BioMutaiENO1.
DMDMi119339.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 434433Alpha-enolasePRO_0000134097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei5 – 51N6-acetyllysine1 Publication
Modified residuei44 – 441Phosphotyrosine1 Publication
Modified residuei60 – 601N6-acetyllysine; alternateBy similarity
Modified residuei60 – 601N6-succinyllysine; alternateBy similarity
Modified residuei64 – 641N6-acetyllysine1 Publication
Modified residuei71 – 711N6-acetyllysine1 Publication
Modified residuei89 – 891N6-acetyllysine; alternate1 Publication
Modified residuei89 – 891N6-succinyllysine; alternateBy similarity
Modified residuei92 – 921N6-acetyllysineBy similarity
Modified residuei126 – 1261N6-acetyllysine1 Publication
Modified residuei193 – 1931N6-acetyllysine1 Publication
Modified residuei199 – 1991N6-acetyllysine1 Publication
Modified residuei202 – 2021N6-acetyllysineBy similarity
Modified residuei228 – 2281N6-acetyllysine; alternate1 Publication
Modified residuei228 – 2281N6-succinyllysine; alternateBy similarity
Modified residuei233 – 2331N6-acetyllysine; alternate1 Publication
Modified residuei233 – 2331N6-malonyllysine; alternate1 Publication
Modified residuei254 – 2541Phosphoserine1 Publication
Modified residuei256 – 2561N6-acetyllysine1 Publication
Modified residuei263 – 2631Phosphoserine2 Publications
Modified residuei272 – 2721Phosphoserine1 Publication
Modified residuei281 – 2811N6-acetyllysine1 Publication
Modified residuei285 – 2851N6-acetyllysine1 Publication
Modified residuei287 – 2871Phosphotyrosine1 Publication
Modified residuei291 – 2911Phosphoserine1 Publication
Modified residuei335 – 3351N6-acetyllysineBy similarity
Modified residuei343 – 3431N6-acetyllysineBy similarity
Modified residuei406 – 4061N6-acetyllysineBy similarity
Modified residuei420 – 4201N6-acetyllysine; alternate1 Publication
Modified residuei420 – 4201N6-malonyllysine; alternate1 Publication
Modified residuei420 – 4201N6-succinyllysine; alternateBy similarity

Post-translational modificationi

ISGylated.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP06733.
PaxDbiP06733.
PeptideAtlasiP06733.
PRIDEiP06733.

2D gel databases

DOSAC-COBS-2DPAGEP06733.
OGPiP06733.
REPRODUCTION-2DPAGEIPI00465248.
P06733.
SWISS-2DPAGEP06733.
UCD-2DPAGEP06733.

PTM databases

PhosphoSiteiP06733.

Miscellaneous databases

PMAP-CutDBP06733.

Expressioni

Tissue specificityi

The alpha/alpha homodimer is expressed in embryo and in most adult tissues. The alpha/beta heterodimer and the beta/beta homodimer are found in striated muscle, and the alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.

Developmental stagei

During ontogenesis, there is a transition from the alpha/alpha homodimer to the alpha/beta heterodimer in striated muscle cells, and to the alpha/gamma heterodimer in nerve cells.

Inductioni

Induced in diffuse large cell lymphoma (DLCL) after treatment with the natural biological agent, Bryo1. Up-regulated in response to enterovirus 71 (EV71) infection (at protein level).2 Publications

Gene expression databases

BgeeiP06733.
ExpressionAtlasiP06733. baseline and differential.
GenevestigatoriP06733.

Organism-specific databases

HPAiCAB018614.
CAB069394.
HPA068284.

Interactioni

Subunit structurei

Mammalian enolase is composed of 3 isozyme subunits, alpha, beta and gamma, which can form homodimers or heterodimers which are cell-type and development-specific. ENO1 interacts with PLG in the neuronal plasma membrane and promotes its activation. The C-terminal lysine is required for this binding (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ACHEP223032EBI-353877,EBI-1637793
Akt2Q608232EBI-353877,EBI-400263From a different organism.
PCNAP120043EBI-353877,EBI-358311
TTNQ8WZ423EBI-353877,EBI-681210
YWHAZP631042EBI-353877,EBI-347088

Protein-protein interaction databases

BioGridi108338. 226 interactions.
IntActiP06733. 62 interactions.
MINTiMINT-155303.

Structurei

Secondary structure

1
434
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128Combined sources
Beta strandi18 – 269Combined sources
Beta strandi29 – 346Combined sources
Helixi57 – 593Combined sources
Helixi63 – 719Combined sources
Helixi73 – 797Combined sources
Helixi87 – 9812Combined sources
Turni104 – 1063Combined sources
Helixi108 – 12518Combined sources
Helixi130 – 1389Combined sources
Beta strandi147 – 1548Combined sources
Helixi156 – 1583Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi167 – 1715Combined sources
Helixi178 – 20023Combined sources
Helixi202 – 2043Combined sources
Helixi220 – 23314Combined sources
Turni237 – 2393Combined sources
Beta strandi241 – 2455Combined sources
Helixi248 – 2503Combined sources
Turni259 – 2624Combined sources
Helixi267 – 2693Combined sources
Helixi273 – 28614Combined sources
Beta strandi289 – 2935Combined sources
Helixi301 – 31111Combined sources
Beta strandi313 – 3186Combined sources
Turni319 – 3235Combined sources
Helixi325 – 33410Combined sources
Beta strandi338 – 3425Combined sources
Helixi344 – 3474Combined sources
Helixi350 – 36213Combined sources
Beta strandi366 – 3705Combined sources
Helixi380 – 3878Combined sources
Beta strandi391 – 3944Combined sources
Helixi401 – 41717Combined sources
Helixi418 – 4203Combined sources
Helixi425 – 4273Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PSNX-ray2.20A/B/C/D1-434[»]
3B97X-ray2.20A/B/C/D2-434[»]
ProteinModelPortaliP06733.
SMRiP06733. Positions 2-434.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP06733.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni31 – 388Epitope recognized by CAR and healthy patient antibodies
Regioni56 – 638Epitope recognized by CAR antibodies
Regioni97 – 237141Required for repression of c-myc promoter activityAdd
BLAST
Regioni370 – 3734Substrate bindingBy similarity
Regioni405 – 43430Required for interaction with PLGBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiCOG0148.
GeneTreeiENSGT00550000074560.
HOVERGENiHBG000067.
InParanoidiP06733.
KOiK01689.
OMAiVSEKSCN.
OrthoDBiEOG776SQ1.
PhylomeDBiP06733.
TreeFamiTF300391.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]

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 initiation. AlignAdd to basket

Isoform alpha-enolase (identifier: P06733-1) [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
MSILKIHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DNDKTRYMGK GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN SEVILPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGAANFRE AMRIGAEVYH NLKNVIKEKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV VIGMDVAASE
260 270 280 290 300
FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD
310 320 330 340 350
WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVNEKSCNCL LLKVNQIGSV
360 370 380 390 400
TESLQACKLA QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR
410 420 430
SERLAKYNQL LRIEEELGSK AKFAGRNFRN PLAK
Length:434
Mass (Da):47,169
Last modified:January 23, 2007 - v2
Checksum:iA0ED663FCC15ADA5
GO
Isoform MBP-1 (identifier: P06733-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: Missing.

Note: It is uncertain whether the alternative initiation site is at Met-94 or at Met-97.

Show »
Length:341
Mass (Da):36,928
Checksum:i96D437CF21772928
GO

Sequence cautioni

The sequence AAA35698.1 differs from that shown.Sequencing errors.Curated
The sequence AAA35698.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551T → A in CAD97642 (PubMed:17974005).Curated
Sequence conflicti78 – 781V → A in BAD96237 (Ref. 7) Curated
Sequence conflicti187 – 1871E → G in CAD97642 (PubMed:17974005).Curated
Sequence conflicti199 – 1991K → R in BAD96912 (Ref. 7) Curated
Sequence conflicti252 – 2521F → S in CAA59331 (PubMed:8824716).Curated
Sequence conflicti310 – 3101S → I in CAD97642 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti177 – 1771N → K.1 Publication
Corresponds to variant rs11544513 [ dbSNP | Ensembl ].
VAR_025172
Natural varianti325 – 3251P → Q.
Corresponds to variant rs11544514 [ dbSNP | Ensembl ].
VAR_048936

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9393Missing in isoform MBP-1. 1 PublicationVSP_018725Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14328 mRNA. Translation: AAA52387.1.
X16288, X16289, X16290 Genomic DNA. Translation: CAA34360.1.
M55914 mRNA. Translation: AAA35698.1. Frameshift.
X84907 mRNA. Translation: CAA59331.1.
BT007163 mRNA. Translation: AAP35827.1.
AK315417 mRNA. Translation: BAG37806.1.
AL833741 mRNA. Translation: CAH56247.1.
BX537400 mRNA. Translation: CAD97642.1.
AK222517 mRNA. Translation: BAD96237.1.
AK223192 mRNA. Translation: BAD96912.1.
DQ056744 Genomic DNA. Translation: AAY43128.1.
AL139415 Genomic DNA. Translation: CAC42425.1.
CH471130 Genomic DNA. Translation: EAW71604.1.
BC001810 mRNA. Translation: AAH01810.1.
BC004325 mRNA. Translation: AAH04325.1.
BC004458 mRNA. Translation: AAH04458.1.
BC009218 mRNA. Translation: AAH09218.2.
BC009912 mRNA. Translation: AAH09912.1.
BC011130 mRNA. Translation: AAH11130.1.
BC015641 mRNA. Translation: AAH15641.1.
BC021166 mRNA. Translation: AAH21166.2.
BC022545 mRNA. Translation: AAH22545.1.
BC027725 mRNA. Translation: AAH27725.1.
BC050642 mRNA. Translation: AAH50642.1.
U88968 mRNA. Translation: AAC39935.1.
AF035286 mRNA. Translation: AAB88178.1.
CCDSiCCDS97.1. [P06733-1]
PIRiA39579.
S11696. A29170.
RefSeqiNP_001188412.1. NM_001201483.1. [P06733-2]
NP_001419.1. NM_001428.3. [P06733-1]
UniGeneiHs.517145.

Genome annotation databases

EnsembliENST00000234590; ENSP00000234590; ENSG00000074800. [P06733-1]
GeneIDi2023.
KEGGihsa:2023.
UCSCiuc001api.2. human. [P06733-1]

Polymorphism and mutation databases

BioMutaiENO1.

Keywords - Coding sequence diversityi

Alternative initiation, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M14328 mRNA. Translation: AAA52387.1.
X16288, X16289, X16290 Genomic DNA. Translation: CAA34360.1.
M55914 mRNA. Translation: AAA35698.1. Frameshift.
X84907 mRNA. Translation: CAA59331.1.
BT007163 mRNA. Translation: AAP35827.1.
AK315417 mRNA. Translation: BAG37806.1.
AL833741 mRNA. Translation: CAH56247.1.
BX537400 mRNA. Translation: CAD97642.1.
AK222517 mRNA. Translation: BAD96237.1.
AK223192 mRNA. Translation: BAD96912.1.
DQ056744 Genomic DNA. Translation: AAY43128.1.
AL139415 Genomic DNA. Translation: CAC42425.1.
CH471130 Genomic DNA. Translation: EAW71604.1.
BC001810 mRNA. Translation: AAH01810.1.
BC004325 mRNA. Translation: AAH04325.1.
BC004458 mRNA. Translation: AAH04458.1.
BC009218 mRNA. Translation: AAH09218.2.
BC009912 mRNA. Translation: AAH09912.1.
BC011130 mRNA. Translation: AAH11130.1.
BC015641 mRNA. Translation: AAH15641.1.
BC021166 mRNA. Translation: AAH21166.2.
BC022545 mRNA. Translation: AAH22545.1.
BC027725 mRNA. Translation: AAH27725.1.
BC050642 mRNA. Translation: AAH50642.1.
U88968 mRNA. Translation: AAC39935.1.
AF035286 mRNA. Translation: AAB88178.1.
CCDSiCCDS97.1. [P06733-1]
PIRiA39579.
S11696. A29170.
RefSeqiNP_001188412.1. NM_001201483.1. [P06733-2]
NP_001419.1. NM_001428.3. [P06733-1]
UniGeneiHs.517145.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2PSNX-ray2.20A/B/C/D1-434[»]
3B97X-ray2.20A/B/C/D2-434[»]
ProteinModelPortaliP06733.
SMRiP06733. Positions 2-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108338. 226 interactions.
IntActiP06733. 62 interactions.
MINTiMINT-155303.

PTM databases

PhosphoSiteiP06733.

Polymorphism and mutation databases

BioMutaiENO1.
DMDMi119339.

2D gel databases

DOSAC-COBS-2DPAGEP06733.
OGPiP06733.
REPRODUCTION-2DPAGEIPI00465248.
P06733.
SWISS-2DPAGEP06733.
UCD-2DPAGEP06733.

Proteomic databases

MaxQBiP06733.
PaxDbiP06733.
PeptideAtlasiP06733.
PRIDEiP06733.

Protocols and materials databases

DNASUi2023.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000234590; ENSP00000234590; ENSG00000074800. [P06733-1]
GeneIDi2023.
KEGGihsa:2023.
UCSCiuc001api.2. human. [P06733-1]

Organism-specific databases

CTDi2023.
GeneCardsiGC01M008921.
HGNCiHGNC:3350. ENO1.
HPAiCAB018614.
CAB069394.
HPA068284.
MIMi172430. gene.
neXtProtiNX_P06733.
PharmGKBiPA27786.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0148.
GeneTreeiENSGT00550000074560.
HOVERGENiHBG000067.
InParanoidiP06733.
KOiK01689.
OMAiVSEKSCN.
OrthoDBiEOG776SQ1.
PhylomeDBiP06733.
TreeFamiTF300391.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciMetaCyc:ENSG00000074800-MONOMER.
BRENDAi4.2.1.11. 2681.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RKP06733.

Miscellaneous databases

ChiTaRSiENO1. human.
EvolutionaryTraceiP06733.
GeneWikiiAlpha-enolase.
GenomeRNAii2023.
NextBioi8197.
PMAP-CutDBP06733.
PROiP06733.
SOURCEiSearch...

Gene expression databases

BgeeiP06733.
ExpressionAtlasiP06733. baseline and differential.
GenevestigatoriP06733.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_00318. Enolase.
InterProiIPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view]
PANTHERiPTHR11902. PTHR11902. 1 hit.
PfamiPF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF001400. Enolase. 1 hit.
PRINTSiPR00148. ENOLASE.
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsiTIGR01060. eno. 1 hit.
PROSITEiPS00164. ENOLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and nucleotide sequence of a full-length cDNA for human alpha enolase."
    Giallongo A., Feo S., Moore R., Croce C.M., Showe L.C.
    Proc. Natl. Acad. Sci. U.S.A. 83:6741-6745(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-ENOLASE).
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA-ENOLASE).
    Tissue: T-cell.
  3. "Cloning and characterization of a human c-myc promoter-binding protein."
    Ray R., Miller D.M.
    Mol. Cell. Biol. 11:2154-2161(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MBP-1), FUNCTION.
    Tissue: Cervix carcinoma.
  4. "Autoreactive epitopes within the human alpha-enolase and their recognition by sera from patients with endometriosis."
    Walter M., Berg H., Leidenberger F.A., Schweppe K.W., Northemann W.
    J. Autoimmun. 8:931-945(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-ENOLASE), MARKER FOR ENDOMETRIOSIS.
    Tissue: Endometrium.
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
    Tissue: Umbilical cord blood.
  7. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
    Tissue: Adipose tissue and Kidney proximal tubule.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-ENOLASE).
    Tissue: Retina and Stomach.
  9. NIEHS SNPs program
    Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-177.
  10. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "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] (ISOFORM ALPHA-ENOLASE).
    Tissue: Brain, Eye, Lung, Ovary, Placenta and Skin.
  13. "A two-dimensional gel database of human colon carcinoma proteins."
    Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.
    Electrophoresis 18:605-613(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-9 (ISOFORM ALPHA-ENOLASE).
    Tissue: Colon carcinoma.
  14. Bienvenut W.V., Lilla S., Zebisch A., Kolch W.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-28; 65-80; 121-162; 234-253; 270-281; 331-394 AND 407-420, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  15. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 16-28; 33-50; 93-103; 106-120; 163-179; 184-193; 203-221; 240-253; 257-262; 270-281; 286-326; 336-394 AND 407-412, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  16. "Molecular cloning and expression analysis of five novel genes in chromosome 1p36."
    Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.
    Genomics 50:187-198(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 166-434.
  17. "Large-scale concatenation cDNA sequencing."
    Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
    Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 171-434.
    Tissue: Brain.
  18. "Purification and characterization of immunoglobulin production stimulating factor-II beta derived from Namalwa cells."
    Sugahara T., Nakajima H., Shirahata S., Murakami H.
    Cytotechnology 10:137-146(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 203-228, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Tissue: Lymphoma.
  19. "Induced expression of alpha-enolase in differentiated diffuse large cell lymphoma."
    Mohamad R.M., Hamdan M.Y., Maki A., Al-Katib A.
    Enzyme Protein 48:37-44(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 270-281 AND 307-321, INDUCTION IN DIFFUSE LARGE CELL LYMPHOMA.
  20. "Functional domains of c-myc promoter binding protein 1 involved in transcriptional repression and cell growth regulation."
    Ghosh A.K., Steele R., Ray R.B.
    Mol. Cell. Biol. 19:2880-2886(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION OF MBP1, IDENTIFICATION OF REPRESSOR DOMAINS, MUTAGENESIS OF LEU-384 AND LEU-388.
  21. "ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1)."
    Feo S., Arcuri D., Piddini E., Passantino R., Giallongo A.
    FEBS Lett. 473:47-52(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A C-MYC TRANSCRIPTIONAL REPRESSOR, SUBCELLULAR LOCATION.
  22. "Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against alpha-enolase."
    Lopez-Alemany R., Longstaff C., Hawley S., Mirshahi M., Fabregas P., Jardi M., Merton E., Miles L.A., Felez J.
    Am. J. Hematol. 72:234-242(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PLASMINOGEN ACTIVATION.
  23. "Identification of an epitope of alpha-enolase (a candidate plasminogen receptor) by phage display."
    Arza B., Felez J., Lopez-Alemany R., Miles L.A., Munoz-Canoves P.
    Thromb. Haemost. 78:1097-1103(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLG.
  24. "Anti-enolase-alpha autoantibodies in cancer-associated retinopathy: epitope mapping and cytotoxicity on retinal cells."
    Adamus G., Amundson D., Seigel G.M., Machnicki M.
    J. Autoimmun. 11:671-677(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: EPITOPE MAPPING, ASSOCIATION WITH CAR.
  25. "Structural analysis of alpha-enolase. Mapping the functional domains involved in down-regulation of the c-myc protooncogene."
    Subramanian A., Miller D.M.
    J. Biol. Chem. 275:5958-5965(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF MBP1 AS AN ALPHA-ENOLASE ALTERNATIVE INITIATION PRODUCT, MUTAGENESIS OF MET-94 AND MET-97.
  26. "Multifunctional alpha-enolase: its role in diseases."
    Pancholi V.
    Cell. Mol. Life Sci. 58:902-920(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  27. "A novel 16-kilodalton cellular protein physically interacts with and antagonizes the functional activity of c-myc promoter-binding protein 1."
    Ghosh A.K., Majumder M., Steele R., White R.A., Ray R.B.
    Mol. Cell. Biol. 21:655-662(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION OF MBP1 WITH SEDL.
  28. "Proteomic analysis of human brain identifies alpha-enolase as a novel autoantigen in Hashimoto's encephalopathy."
    Ochi H., Horiuchi I., Araki N., Toda T., Araki T., Sato K., Murai H., Osoegawa M., Yamada T., Okamura K., Ogino T., Mizumoto K., Yamashita H., Saya H., Kira J.
    FEBS Lett. 528:197-202(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS AN AUTOANTIGEN IN HASHIMOTO ENCEPHALOPATHY.
  29. Cited for: ISGYLATION.
  30. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44 AND TYR-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
    Leong W.F., Chow V.T.
    Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  32. "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
    Wong J.J., Pung Y.F., Sze N.S., Chin K.C.
    Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ISGYLATION.
  33. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254 AND SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  34. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  35. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-5; LYS-64; LYS-71; LYS-89; LYS-126; LYS-193; LYS-199; LYS-228; LYS-233; LYS-256; LYS-281; LYS-285 AND LYS-420, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  36. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  37. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  38. Cited for: MALONYLATION AT LYS-233 AND LYS-420.
  39. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. "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 SER-263 AND SER-291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  41. "Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme."
    Kang H.J., Jung S.K., Kim S.J., Chung S.J.
    Acta Crystallogr. D 64:651-657(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-434, SUBUNIT, COFACTOR, METAL-BINDING SITES.

Entry informationi

Entry nameiENOA_HUMAN
AccessioniPrimary (citable) accession number: P06733
Secondary accession number(s): B2RD59
, P22712, Q16704, Q4TUS4, Q53FT9, Q53HR3, Q658M5, Q6GMP2, Q71V37, Q7Z3V6, Q8WU71, Q96GV1, Q9BT62, Q9UCH6, Q9UM55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 190 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

Miscellaneous

Used as a diagnostic marker for many tumors and, in the heterodimeric form, alpha/gamma, as a marker for hypoxic brain injury after cardiac arrest. Also marker for endometriosis. Antibodies against alpha-enolase are present in sera from patients with cancer-associated retinopathy syndrome (CAR), a progressive blinding disease which occurs in the presence of systemic tumor growth, primarily small-cell carcinoma of the lung and other malignancies. Is identified as an autoantigen in Hashimoto encephalopathy (HE) a rare autoimmune disease associated with Hashimoto thyroiditis (HT). HT is a disorder in which destructive processes overcome the potential capacity of thyroid replacement leading to hypothyroidism.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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.