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Protein

Beta-enolase

Gene

ENO3

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

Functioni

Appears to have a function in striated muscle development and regeneration.

Catalytic activityi

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

Cofactori

Mg2+Note: Mg2+ is required for catalysis and for stabilizing the dimer.

Pathway:iglycolysis

This protein is involved in step 4 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase, Glyceraldehyde-3-phosphate dehydrogenase (HEL-S-162eP), Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (GAPDHS)
  2. Phosphoglycerate kinase 2 (PGK2), Phosphoglycerate kinase 1 (PGK1)
  3. no protein annotated in this organism
  4. Alpha-enolase (ENO1), Beta-enolase (ENO3), Enolase, Enolase, Enolase (ENO3), Enolase (ENO2), Enolase (ENO3), Enolase (ENO2), Enolase (ENO1), Enolase (ENO3), Enolase (ENO1), Enolase, Enolase, Enolase (ENO3), Gamma-enolase (ENO2)
  5. Pyruvate kinase, Pyruvate kinase PKM (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase (PKM2), Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase (PKM), Pyruvate kinase, Pyruvate kinase PKLR (PKLR), Pyruvate kinase, Pyruvate kinase (PKM2), Pyruvate kinase (HEL-S-30), Pyruvate kinase (PKM), Pyruvate kinase (PKM2)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

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

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • phosphopyruvate hydratase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000108515-MONOMER.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RKP13929.
UniPathwayiUPA00109; UER00187.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-enolase (EC:4.2.1.11)
Alternative name(s):
2-phospho-D-glycerate hydro-lyase
Enolase 3
Muscle-specific enolase
Short name:
MSE
Skeletal muscle enolase
Gene namesi
Name:ENO3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:3354. ENO3.

Subcellular locationi

  • Cytoplasm

  • Note: Localized to the Z line. Some colocalization with CKM at M-band (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • phosphopyruvate hydratase complex Source: InterPro
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Glycogen storage disease 13 (GSD13)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA metabolic disorder that results in exercise-induced myalgias, generalized muscle weakness and fatigability. It is characterized by increased serum creatine kinase and decreased enolase 3 activity. Dramatically reduced protein levels with focal sarcoplasmic accumulation of glycogen-beta particles are detected on ultrastructural analysis.

See also OMIM:612932
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti156 – 1561G → D in GSD13; when associated with E-374. 1 Publication
Corresponds to variant rs121918403 [ dbSNP | Ensembl ].
VAR_020620
Natural varianti374 – 3741G → E in GSD13; when associated with D-156. 1 Publication
VAR_020621

Keywords - Diseasei

Disease mutation, Glycogen storage disease

Organism-specific databases

MIMi612932. phenotype.
Orphaneti99849. Glycogen storage disease due to muscle beta-enolase deficiency.
PharmGKBiPA27789.

Polymorphism and mutation databases

BioMutaiENO3.
DMDMi425906077.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 434433Beta-enolasePRO_0000134107Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei5 – 51N6-acetyllysineBy similarity
Modified residuei26 – 261PhosphothreonineBy similarity
Modified residuei44 – 441PhosphotyrosineBy similarity
Modified residuei60 – 601N6-acetyllysine; alternateBy similarity
Modified residuei60 – 601N6-succinyllysine; alternateBy similarity
Modified residuei64 – 641N6-acetyllysineBy similarity
Modified residuei89 – 891N6-acetyllysine; alternateBy similarity
Modified residuei89 – 891N6-succinyllysine; alternateBy similarity
Modified residuei92 – 921N6-acetyllysineBy similarity
Modified residuei126 – 1261N6-acetyllysineBy similarity
Modified residuei176 – 1761Phosphoserine1 Publication
Modified residuei193 – 1931N6-acetyllysineBy similarity
Modified residuei197 – 1971N6-acetyllysineBy similarity
Modified residuei199 – 1991N6-acetyllysineBy similarity
Modified residuei202 – 2021N6-acetyllysineBy similarity
Modified residuei228 – 2281N6-acetyllysine; alternateBy similarity
Modified residuei228 – 2281N6-succinyllysine; alternateBy similarity
Modified residuei256 – 2561N6-acetyllysineBy similarity
Modified residuei263 – 2631Phosphoserine1 Publication
Modified residuei281 – 2811N6-acetyllysineBy similarity
Modified residuei285 – 2851N6-acetyllysineBy similarity
Modified residuei287 – 2871PhosphotyrosineBy similarity
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei335 – 3351N6-acetyllysineBy similarity
Modified residuei343 – 3431N6-acetyllysineBy similarity
Modified residuei406 – 4061N6-acetyllysineBy similarity
Modified residuei420 – 4201N6-acetyllysine; alternateBy similarity
Modified residuei420 – 4201N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP13929.
PaxDbiP13929.
PRIDEiP13929.

2D gel databases

UCD-2DPAGEP13929.

PTM databases

PhosphoSiteiP13929.

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.

Gene expression databases

BgeeiP13929.
CleanExiHS_ENO3.
ExpressionAtlasiP13929. baseline and differential.
GenevisibleiP13929. HS.

Organism-specific databases

HPAiHPA000793.
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. Interacts with PNKD.1 Publication

Protein-protein interaction databases

BioGridi108341. 9 interactions.
IntActiP13929. 18 interactions.
STRINGi9606.ENSP00000324105.

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
Beta strandi43 – 453Combined sources
Helixi57 – 593Combined sources
Helixi63 – 719Combined sources
Helixi73 – 797Combined sources
Helixi87 – 9812Combined sources
Turni104 – 1063Combined sources
Helixi108 – 12518Combined sources
Helixi130 – 1389Combined sources
Beta strandi150 – 1545Combined sources
Helixi156 – 1583Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi167 – 1715Combined sources
Helixi178 – 20023Combined sources
Helixi220 – 23415Combined sources
Turni237 – 2393Combined sources
Beta strandi241 – 2455Combined sources
Helixi248 – 2514Combined sources
Turni259 – 2624Combined sources
Helixi267 – 2693Combined sources
Helixi273 – 28614Combined sources
Beta strandi289 – 2935Combined sources
Helixi301 – 3099Combined 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 – 3889Combined 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
2XSXX-ray1.70A/B1-434[»]
ProteinModelPortaliP13929.
SMRiP13929. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni370 – 3734Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the enolase family.Curated

Phylogenomic databases

eggNOGiCOG0148.
GeneTreeiENSGT00550000074560.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP13929.
KOiK01689.
OMAiFRHPKIN.
PhylomeDBiP13929.
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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P13929-1) [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
MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR
60 70 80 90 100
DGDKGRYLGK GVLKAVENIN NTLGPALLQK KLSVVDQEKV DKFMIELDGT
110 120 130 140 150
ENKSKFGANA ILGVSLAVCK AGAAEKGVPL YRHIADLAGN PDLILPVPAF
160 170 180 190 200
NVINGGSHAG NKLAMQEFMI LPVGASSFKE AMRIGAEVYH HLKGVIKAKY
210 220 230 240 250
GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV VIGMDVAASE
260 270 280 290 300
FYRNGKYDLD FKSPDDPARH ITGEKLGELY KSFIKNYPVV SIEDPFDQDD
310 320 330 340 350
WATWTSFLSG VNIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV
360 370 380 390 400
TESIQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR
410 420 430
SERLAKYNQL MRIEEALGDK AIFAGRKFRN PKAK
Length:434
Mass (Da):46,987
Last modified:November 28, 2012 - v5
Checksum:i4D9D8DCF32CF153F
GO
Isoform 2 (identifier: P13929-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     150-177: Missing.

Note: No experimental confirmation available.
Show »
Length:406
Mass (Da):44,115
Checksum:iE0D4621669448D46
GO
Isoform 3 (identifier: P13929-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     61-104: GVLKAVENINNTLGPALLQKKLSVVDQEKVDKFMIELDGTENKS → A

Note: No experimental confirmation available.
Show »
Length:391
Mass (Da):42,248
Checksum:i0B6DB38924087E00
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711N → S.3 Publications
Corresponds to variant rs238238 [ dbSNP | Ensembl ].
VAR_020618
Natural varianti85 – 851V → A.4 Publications
Corresponds to variant rs238239 [ dbSNP | Ensembl ].
VAR_020619
Natural varianti156 – 1561G → D in GSD13; when associated with E-374. 1 Publication
Corresponds to variant rs121918403 [ dbSNP | Ensembl ].
VAR_020620
Natural varianti374 – 3741G → E in GSD13; when associated with D-156. 1 Publication
VAR_020621

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei61 – 10444GVLKA…TENKS → A in isoform 3. 1 PublicationVSP_037752Add
BLAST
Alternative sequencei150 – 17728Missing in isoform 2. 1 PublicationVSP_037753Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16504 mRNA. Translation: CAA34513.1.
X51957 mRNA. Translation: CAA36216.1.
X55976 Genomic DNA. Translation: CAA39446.1.
X56832 Genomic DNA. Translation: CAA40163.1.
AK300662 mRNA. Translation: BAG62348.1.
AK300709 mRNA. Translation: BAG62388.1.
AC004771 Genomic DNA. No translation available.
AC109333 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90375.1.
CH471108 Genomic DNA. Translation: EAW90379.1.
CH471108 Genomic DNA. Translation: EAW90380.1.
BC017249 mRNA. Translation: AAH17249.1.
CCDSiCCDS11062.1. [P13929-1]
CCDS54070.1. [P13929-3]
PIRiS06756.
RefSeqiNP_001180432.1. NM_001193503.1. [P13929-3]
NP_001967.3. NM_001976.4. [P13929-1]
NP_443739.3. NM_053013.3. [P13929-1]
XP_011522031.1. XM_011523729.1. [P13929-1]
UniGeneiHs.224171.

Genome annotation databases

EnsembliENST00000323997; ENSP00000324105; ENSG00000108515.
ENST00000518175; ENSP00000431087; ENSG00000108515.
ENST00000519584; ENSP00000430636; ENSG00000108515. [P13929-3]
GeneIDi2027.
KEGGihsa:2027.
UCSCiuc002gab.4. human. [P13929-1]
uc010vss.2. human. [P13929-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16504 mRNA. Translation: CAA34513.1.
X51957 mRNA. Translation: CAA36216.1.
X55976 Genomic DNA. Translation: CAA39446.1.
X56832 Genomic DNA. Translation: CAA40163.1.
AK300662 mRNA. Translation: BAG62348.1.
AK300709 mRNA. Translation: BAG62388.1.
AC004771 Genomic DNA. No translation available.
AC109333 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90375.1.
CH471108 Genomic DNA. Translation: EAW90379.1.
CH471108 Genomic DNA. Translation: EAW90380.1.
BC017249 mRNA. Translation: AAH17249.1.
CCDSiCCDS11062.1. [P13929-1]
CCDS54070.1. [P13929-3]
PIRiS06756.
RefSeqiNP_001180432.1. NM_001193503.1. [P13929-3]
NP_001967.3. NM_001976.4. [P13929-1]
NP_443739.3. NM_053013.3. [P13929-1]
XP_011522031.1. XM_011523729.1. [P13929-1]
UniGeneiHs.224171.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XSXX-ray1.70A/B1-434[»]
ProteinModelPortaliP13929.
SMRiP13929. Positions 1-434.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108341. 9 interactions.
IntActiP13929. 18 interactions.
STRINGi9606.ENSP00000324105.

PTM databases

PhosphoSiteiP13929.

Polymorphism and mutation databases

BioMutaiENO3.
DMDMi425906077.

2D gel databases

UCD-2DPAGEP13929.

Proteomic databases

MaxQBiP13929.
PaxDbiP13929.
PRIDEiP13929.

Protocols and materials databases

DNASUi2027.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323997; ENSP00000324105; ENSG00000108515.
ENST00000518175; ENSP00000431087; ENSG00000108515.
ENST00000519584; ENSP00000430636; ENSG00000108515. [P13929-3]
GeneIDi2027.
KEGGihsa:2027.
UCSCiuc002gab.4. human. [P13929-1]
uc010vss.2. human. [P13929-3]

Organism-specific databases

CTDi2027.
GeneCardsiGC17P004851.
H-InvDBHIX0013457.
HGNCiHGNC:3354. ENO3.
HPAiHPA000793.
HPA068284.
MIMi131370. gene.
612932. phenotype.
neXtProtiNX_P13929.
Orphaneti99849. Glycogen storage disease due to muscle beta-enolase deficiency.
PharmGKBiPA27789.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0148.
GeneTreeiENSGT00550000074560.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP13929.
KOiK01689.
OMAiFRHPKIN.
PhylomeDBiP13929.
TreeFamiTF300391.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00187.
BioCyciMetaCyc:ENSG00000108515-MONOMER.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RKP13929.

Miscellaneous databases

ChiTaRSiENO3. human.
GeneWikiiENO3.
GenomeRNAii2027.
NextBioi8207.
PROiP13929.
SOURCEiSearch...

Gene expression databases

BgeeiP13929.
CleanExiHS_ENO3.
ExpressionAtlasiP13929. baseline and differential.
GenevisibleiP13929. HS.

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. "Structure of human muscle (beta) enolase mRNA and protein deduced from a genomic clone."
    Peshavaria M., Hinks L.J., Day I.N.M.
    Nucleic Acids Res. 17:8862-8862(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Nucleotide sequence of a cDNA encoding the human muscle-specific enolase (MSE)."
    Cali L., Feo S., Oliva D., Giallongo A.
    Nucleic Acids Res. 18:1893-1893(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ALA-85.
  3. "Molecular structure of the human muscle-specific enolase gene (ENO3)."
    Peshavaria M., Day I.N.M.
    Biochem. J. 275:427-433(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  4. "Structural features of the human gene for muscle-specific enolase. Differential splicing in the 5'-untranslated sequence generates two forms of mRNA."
    Giallongo A., Venturella S., Oliva D., Barbieri G., Rubino P., Feo S.
    Eur. J. Biochem. 214:367-374(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS SER-71 AND ALA-85.
  5. "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] (ISOFORMS 2 AND 3), VARIANTS SER-71 AND ALA-85.
    Tissue: Skeletal muscle.
  6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS SER-71 AND ALA-85.
    Tissue: Muscle.
  9. "Characterization of MR-1, a novel myofibrillogenesis regulator in human muscle."
    Li T.-B., Liu X.-H., Feng S., Hu Y., Yang W.-X., Han Y., Wang Y.-G., Gong L.-M.
    Acta Biochim. Biophys. Sin. 36:412-418(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PNKD.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  12. "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-176 AND SER-263, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: VARIANTS GSD13 ASP-156 AND GLU-374.

Entry informationi

Entry nameiENOB_HUMAN
AccessioniPrimary (citable) accession number: P13929
Secondary accession number(s): B4DUI6
, B4DUM6, D3DTL2, E7ENK8, Q96AE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 28, 2012
Last modified: July 22, 2015
This is version 167 of the entry and version 5 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 17
    Human chromosome 17: 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.