ENO2

Protein identityUniProt · HPA

UniProt accession

P09104

Gene

ENO2

Ensembl

ENSG00000111674

Chromosome

12

Canonical length

434 aa

Protein class

Cancer-related genes, Candidate cardiovascular disease genes, Enzymes, Metabolic proteins, Plasma proteins, Predicted intracellular proteins

Subcellular location

Plasma membrane,Cytosol

Quaternary structure

Homodimer

OverviewNCBI Gene

This gene encodes one of the three enolase isoenzymes found in mammals. This isoenzyme, a homodimer, is found in mature neurons and cells of neuronal origin. A switch from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates. [provided by RefSeq, Jul 2008]

Canonical amino-acid sequenceUniProt

434 residues, UniProt reviewed canonical sequence.

>P09104|ENO2
     1  MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK
    61  GVLKAVDHIN STIAPALISS GLSVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK
   121  AGAAERELPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD
   181  AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKI
   241  VIGMDVAASE FYRDGKYDLD FKSPTDPSRY ITGDQLGALY QDFVRDYPVV SIEDPFDQDD
   301  WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA
   361  QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE
   421  ARFAGHNFRN PSVL

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against ENO2 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Cell surface

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.19

Highest tissue expression

1,573 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about ENO2.

Disease | ImmuneIEDB

Conditions an epitope on ENO2 was assayed in.

• multiple sclerosis B cell
• rheumatoid arthritis B cell

ReferencesPubMed · IEDB

Publications for ENO2 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.

Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. IEDB — curated epitope assays from the Immune Epitope Database (Vita et al., Nucleic Acids Research 2019). Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.47

gnomAD pLI

0.38

gnomAD missense Z

1.81

DepMap mean gene effect

-0.04

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• canonical glycolysis
• gluconeogenesis
• glycolytic process
• response to estradiol
• response to xenobiotic stimulus

Molecular functions

• enzyme binding
• identical protein binding
• magnesium ion binding
• phosphopyruvate hydratase activity
• protein-containing complex binding

Cellular components

• cell cortex
• cell surface
• cytosol
• extracellular exosome
• extracellular space
• growth cone
• membrane
• membrane raft
• perikaryon
• phosphopyruvate hydratase complex
• photoreceptor inner segment
• plasma membrane
• synaptic membrane

Protein domainsUniProt · Pfam · InterPro

• Enolase
• Enolase, conserved site
• Enolase, C-terminal TIM barrel domain
• Enolase, N-terminal
• Enolase-like, N-terminal
• Enolase-like, C-terminal domain superfamily
• Enolase, C-terminal TIM barrel domain
• Enolase, N-terminal domain

KeywordsUniProt

• Acetylation
• Cell membrane
• Cytoplasm
• Glycolysis
• Hydroxylation
• Isopeptide bond
• Lyase
• Magnesium
• Membrane
• Metal-binding
• Phosphoprotein
• Ubl conjugation

InteractionsUniProt · HPA

Protein binding partners of ENO2 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• ENO1