Protein detail

ENOB

Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)

Entry name ENOB	UniProt ID P13929	EVMP confidence score 0.53
Supporting publications (n) 2	Transmembrane count	Protein classification Candidate cardiovascular disease genesDisease related genesEnzymesHuman disease related genesMetabolic proteinsPlasma proteinsPotential drug targetsPredicted intracellular proteins

Basic Information

Protein Names

Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Enolase 3) (Muscle-specific enolase) (MSE) (Skeletal muscle enolase)

Protein Class (8)

Candidate cardiovascular disease genesDisease related genesEnzymesHuman disease related genesMetabolic proteinsPlasma proteinsPotential drug targetsPredicted intracellular proteins

Protein Function (7)

Human disease related genes:Congenital disorders of metabolism:Congenital disorders of carbohydrate metabolism
Predicted intracellular proteins
ENZYME proteins:Lyases
Potential drug targets
Candidate cardiovascular disease genes
Enzymes
Disease related genes

Ensembl

ENSG00000108515

Entrez Gene Symbol

ENO3

Gene Description

Enolase 3

Chromosome

Position

4948092-4957131

Supporting publications (n)

EVMP confidence score

0.53

Fluorescence & Localization

Tissue Specificheart muscleCell SpecificCardiomyocytes

Function & Pathway

Protein Function (7)

Human disease related genes:Congenital disorders of metabolism:Congenital disorders of carbohydrate metabolism
Predicted intracellular proteins
ENZYME proteins:Lyases
Potential drug targets
Candidate cardiovascular disease genes
Enzymes
Disease related genes

Cellular Component (6)

Molecular Function (3)

Biological Process (3)

KEGG (7)

Reactome (3)

Mediation Categories

Metabolism mediation

Relations & Evidence20

Ligand-Receptor Signaling (9)

9 records.

Category	Parent	Database	Transmitter
ecm	ecm	MatrixDB	Yes
ecm	ecm	OmniPath	Yes
extracellular	extracellular	LOCATE
extracellular	extracellular	OmniPath
intracellular	intracellular	LOCATE
intracellular	intracellular	ComPPI
intracellular	intracellular	GO_Intercell
intracellular	intracellular	UniProt_location
intracellular	intracellular	OmniPath

Protein Complex Composition (10)

10 records.

Component Gene Symbols	Component UniProt ID	Stoichiometry	Database	Database IDs
ENO3 GPI PGK1 PGK2	P00558 P06744 P07205 P13929	0:0:0:0	hu.MAP
ENO3 PGK1 PGK2 TSFM	P00558 P07205 P13929 P43897	0:0:0:0	hu.MAP
ENO3 GFUS PGK1 PGK2 TSFM	P00558 P07205 P13929 P43897 Q13630	0:0:0:0:0	hu.MAP
ENO3 GPI GSTO1 MPI PARK7 PGK2 PGM2 TKT	P06744 P07205 P13929 P29401 P34949 P78417 Q96G03 Q99497	0:0:0:0:0:0:0:0	hu.MAP
ENO3 GPI PDCD6IP PEF1 TMEM256	P06744 P13929 Q8N2U0 Q8WUM4 Q9UBV8	0:0:0:0:0	Havugimana2012	Havugimana2012:C_426
ENO3 IDH2 MTHFD1	P11586 P13929 P48735	0:0:0	hu.MAP2
ENO3	P13929	2	PDB	PDB:2xsx
CALR ENO3 RCN3	P13929 P27797 Q96D15	0:0:0	hu.MAP
CALR ENO3 WRAP53	P13929 P27797 Q9BUR4	0:0:0	hu.MAP
AKR1D1 ENO3 GSTO1	P13929 P51857 P78417	0:0:0	hu.MAP2

Isolation & Detection Technology (1)

1 record.

EV Isolation Method	Detection Method	Number of References	References
Differential Ultracentrifugation	Small R sequencing (Illumi HiSeq 2000 (Solexa)Mass spectrometry	1	37886648

Sequence, Structure & Domains

Sequences

Length

434

Mass

46,987

Sequence

MAMQKIFAREILDSRGNPTVEVDLHTAKGRFRAAVPSGASTGIYEALELRDGDKGRYLGKGVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKSKFGANAILGVSLAVCKAGAAEKGVPLYRHIADLAGNPDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFKEAMRIGAEVYHHLKGVIKAKYGKDATNVGDEGGFAPNILENNEALELLKTAIQAAGYPDKVVIGMDVAASEFYRNGKYDLDFKSPDDPARHITGEKLGELYKSFIKNYPVVSIEDPFDQDDWATWTSFLSGVNIQIVGDDLTVTNPKRIAQAVEKKACNCLLLKVNQIGSVTESIQACKLAQSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEALGDKAIFAGRKFRNPKAK

Alternative Products

Event=Alternative splicing; Named isoforms=3; Name=1; IsoId=P13929-1; Sequence=Displayed; Name=2; IsoId=P13929-2; Sequence=VSP_037753; Name=3; IsoId=P13929-3; Sequence=VSP_037752

Alternative Sequence

61..104; GVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKS -> A (in isoform 3); 150..177; Missing (in isoform 2)

3D Structural Models

Turn

104..106; 237..239; 259..262; 319..323

Helix

57..59; 63..71; 73..79; 87..98; 108..125; 130..138; 156..158; 178..200; 220..234; 248..251; 267..269; 273..286; 301..309; 325..334; 344..347; 350..362; 380..388; 401..417; 418..420; 425..427

Beta Strand

5..12; 18..26; 29..34; 43..45; 150..154; 159..162; 167..171; 241..245; 289..293; 313..318; 338..342; 366..370; 391..394

3D Structure

X-ray crystallography (1)

Domain & Motif Annotations

Protein Families

Enolase family

Sequence Similarities

Belongs to the enolase family.

Clinical Relevance

Disease Involvement (2)

Disease variantGlycogen storage disease

Related Diseases

Glycogen storage disease

Drugs (2)

SB203580 BARICITINIB

Antibody (3)

HPA000793 HPA068284 HPA068721

Interaction Protein

ENSG00000074800

Interaction Count

Interaction Dataset

intact_biogrid_opencell

Supporting Publications2

PMID	Title	Related sentences
37503071	A novel machine learning algorithm selects proteome signature to specifically identify cancer exosomes.	Employing datasets of exosome proteins from human cell lines, tissue, plasma, serum and urine samples from a variety of cancers, we identify Clathrin Heavy Chain (CLTC), Ezrin, (EZR), Talin-1 (TLN1), Adenylyl cyclase-associated protein 1 (CAP1) and Moesin (MSN) as highly abundant universal biomarkers for exosomes and define three panels of pan-cancer exosome proteins that distinguish cancer exosomes from other exosomes and aid in classifying cancer subtypes employing random forest models.
38529947	A novel machine learning algorithm selects proteome signature to specifically identify cancer exosomes.	Employing datasets of exosome proteins from human cell lines, tissue, plasma, serum, and urine samples from a variety of cancers, we identify Clathrin Heavy Chain (CLTC), Ezrin, (EZR), Talin-1 (TLN1), Adenylyl cyclase-associated protein 1 (CAP1), and Moesin (MSN) as highly abundant universal biomarkers for exosomes and define three panels of pan-cancer exosome proteins that distinguish cancer exosomes from other exosomes and aid in classifying cancer subtypes employing random forest models.