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P13929

- ENOB_HUMAN

UniProt

P13929 - ENOB_HUMAN

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Protein
Beta-enolase
Gene
ENO3
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Cofactori

Magnesium. Required for catalysis and for stabilizing the dimer.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei158 – 1581Substrate By similarity
Binding sitei167 – 1671Substrate By similarity
Active sitei210 – 2101Proton donor By similarity
Metal bindingi245 – 2451Magnesium By similarity
Metal bindingi293 – 2931Magnesium By similarity
Binding sitei293 – 2931Substrate By similarity
Metal bindingi318 – 3181Magnesium By similarity
Binding sitei318 – 3181Substrate By similarity
Active sitei343 – 3431Proton acceptor By similarity
Binding sitei394 – 3941Substrate By similarity

GO - Molecular functioni

  1. magnesium ion binding Source: InterPro
  2. phosphopyruvate hydratase activity Source: ProtInc

GO - Biological processi

  1. aging Source: Ensembl
  2. carbohydrate metabolic process Source: Reactome
  3. gluconeogenesis Source: Reactome
  4. glucose metabolic process Source: Reactome
  5. glycolytic process Source: Reactome
  6. response to drug Source: Ensembl
  7. skeletal muscle tissue regeneration Source: Ensembl
  8. small molecule metabolic process Source: Reactome
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: 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.UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. extracellular space Source: UniProt
  4. phosphopyruvate hydratase complex Source: InterPro
  5. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Glycogen storage disease 13 (GSD13) [MIM:612932]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 434433Beta-enolaseUniRule annotation
PRO_0000134107Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

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.UniRule annotation

Gene expression databases

ArrayExpressiP13929.
BgeeiP13929.
CleanExiHS_ENO3.
GenevestigatoriP13929.

Organism-specific databases

HPAiHPA000793.

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. 10 interactions.
IntActiP13929. 17 interactions.
STRINGi9606.ENSP00000324105.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 128
Beta strandi18 – 269
Beta strandi29 – 346
Beta strandi43 – 453
Helixi57 – 593
Helixi63 – 719
Helixi73 – 797
Helixi87 – 9812
Turni104 – 1063
Helixi108 – 12518
Helixi130 – 1389
Beta strandi150 – 1545
Helixi156 – 1583
Beta strandi159 – 1624
Beta strandi167 – 1715
Helixi178 – 20023
Helixi220 – 23415
Turni237 – 2393
Beta strandi241 – 2455
Helixi248 – 2514
Turni259 – 2624
Helixi267 – 2693
Helixi273 – 28614
Beta strandi289 – 2935
Helixi301 – 3099
Beta strandi313 – 3186
Turni319 – 3235
Helixi325 – 33410
Beta strandi338 – 3425
Helixi344 – 3474
Helixi350 – 36213
Beta strandi366 – 3705
Helixi380 – 3889
Beta strandi391 – 3944
Helixi401 – 41717
Helixi418 – 4203
Helixi425 – 4273

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XSXX-ray1.70A/B1-434[»]
ProteinModelPortaliP13929.
SMRiP13929. Positions 1-434.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the enolase family.

Phylogenomic databases

eggNOGiCOG0148.
HOGENOMiHOG000072174.
HOVERGENiHBG000067.
InParanoidiP13929.
KOiK01689.
OMAiGELYKNF.
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. Align

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

MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR    50
DGDKGRYLGK GVLKAVENIN NTLGPALLQK KLSVVDQEKV DKFMIELDGT 100
ENKSKFGANA ILGVSLAVCK AGAAEKGVPL YRHIADLAGN PDLILPVPAF 150
NVINGGSHAG NKLAMQEFMI LPVGASSFKE AMRIGAEVYH HLKGVIKAKY 200
GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV VIGMDVAASE 250
FYRNGKYDLD FKSPDDPARH ITGEKLGELY KSFIKNYPVV SIEDPFDQDD 300
WATWTSFLSG VNIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV 350
TESIQACKLA QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR 400
SERLAKYNQL MRIEEALGDK AIFAGRKFRN PKAK 434
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.
VSP_037752Add
BLAST
Alternative sequencei150 – 17728Missing in isoform 2.
VSP_037753Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
UniGeneiHs.224171.

Genome annotation databases

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

Polymorphism databases

DMDMi425906077.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS11062.1. [P13929-1 ]
CCDS54070.1. [P13929-3 ]
PIRi S06756.
RefSeqi NP_001180432.1. NM_001193503.1. [P13929-3 ]
NP_001967.3. NM_001976.4. [P13929-1 ]
NP_443739.3. NM_053013.3. [P13929-1 ]
UniGenei Hs.224171.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XSX X-ray 1.70 A/B 1-434 [» ]
ProteinModelPortali P13929.
SMRi P13929. Positions 1-434.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108341. 10 interactions.
IntActi P13929. 17 interactions.
STRINGi 9606.ENSP00000324105.

PTM databases

PhosphoSitei P13929.

Polymorphism databases

DMDMi 425906077.

2D gel databases

UCD-2DPAGE P13929.

Proteomic databases

MaxQBi P13929.
PaxDbi P13929.
PRIDEi P13929.

Protocols and materials databases

DNASUi 2027.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000323997 ; ENSP00000324105 ; ENSG00000108515 . [P13929-1 ]
ENST00000518175 ; ENSP00000431087 ; ENSG00000108515 . [P13929-1 ]
ENST00000519584 ; ENSP00000430636 ; ENSG00000108515 . [P13929-3 ]
GeneIDi 2027.
KEGGi hsa:2027.
UCSCi uc002gab.4. human. [P13929-1 ]
uc010vss.2. human. [P13929-3 ]

Organism-specific databases

CTDi 2027.
GeneCardsi GC17P004851.
H-InvDB HIX0013457.
HGNCi HGNC:3354. ENO3.
HPAi HPA000793.
MIMi 131370. gene.
612932. phenotype.
neXtProti NX_P13929.
Orphaneti 99849. Glycogen storage disease due to muscle beta-enolase deficiency.
PharmGKBi PA27789.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0148.
HOGENOMi HOG000072174.
HOVERGENi HBG000067.
InParanoidi P13929.
KOi K01689.
OMAi GELYKNF.
PhylomeDBi P13929.
TreeFami TF300391.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00187 .
BioCyci MetaCyc:ENSG00000108515-MONOMER.
Reactomei REACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RK P13929.

Miscellaneous databases

GeneWikii ENO3.
GenomeRNAii 2027.
NextBioi 8207.
PROi P13929.
SOURCEi Search...

Gene expression databases

ArrayExpressi P13929.
Bgeei P13929.
CleanExi HS_ENO3.
Genevestigatori P13929.

Family and domain databases

Gene3Di 3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPi MF_00318. Enolase.
InterProi IPR000941. Enolase.
IPR020810. Enolase_C.
IPR029065. Enolase_C-like.
IPR020809. Enolase_CS.
IPR020811. Enolase_N.
IPR029017. Enolase_N_like.
[Graphical view ]
PANTHERi PTHR11902. PTHR11902. 1 hit.
Pfami PF00113. Enolase_C. 1 hit.
PF03952. Enolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF001400. Enolase. 1 hit.
PRINTSi PR00148. ENOLASE.
SUPFAMi SSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
TIGRFAMsi TIGR01060. eno. 1 hit.
PROSITEi PS00164. ENOLASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. 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: September 3, 2014
This is version 157 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

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