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P38117

- ETFB_HUMAN

UniProt

P38117 - ETFB_HUMAN

Protein

Electron transfer flavoprotein subunit beta

Gene

ETFB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    The electron transfer flavoprotein serves as a specific electron acceptor for several dehydrogenases, including five acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase).

    Cofactori

    Binds 1 FAD per dimer.
    Binds 1 AMP per subunit.

    GO - Molecular functioni

    1. electron carrier activity Source: ProtInc

    GO - Biological processi

    1. cellular metabolic process Source: Reactome
    2. respiratory electron transport chain Source: Reactome
    3. small molecule metabolic process Source: Reactome

    Keywords - Biological processi

    Electron transport, Transport

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_22393. Respiratory electron transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Electron transfer flavoprotein subunit beta
    Short name:
    Beta-ETF
    Gene namesi
    Name:ETFB
    ORF Names:FP585
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3482. ETFB.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. intracellular membrane-bounded organelle Source: HPA
    3. mitochondrial matrix Source: Reactome
    4. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Glutaric aciduria 2B (GA2B) [MIM:231680]: An autosomal recessively inherited disorder of fatty acid, amino acid, and choline metabolism. It is characterized by multiple acyl-CoA dehydrogenase deficiencies resulting in large excretion not only of glutaric acid, but also of lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti128 – 1281D → N in GA2B. 1 Publication
    VAR_025804
    Natural varianti164 – 1641R → Q in GA2B. 1 Publication
    Corresponds to variant rs104894677 [ dbSNP | Ensembl ].
    VAR_002369

    Keywords - Diseasei

    Disease mutation, Glutaricaciduria

    Organism-specific databases

    MIMi231680. phenotype.
    Orphaneti394532. Multiple acyl-CoA dehydrogenation deficiency, mild type.
    394529. Multiple acyl-CoA dehydrogenation deficiency, severe neonatal type.
    PharmGKBiPA27898.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 255254Electron transfer flavoprotein subunit betaPRO_0000167870Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei19 – 191N6-acetyllysine; alternateBy similarity
    Modified residuei19 – 191N6-succinyllysine; alternateBy similarity
    Modified residuei35 – 351N6-acetyllysine; alternateBy similarity
    Modified residuei35 – 351N6-succinyllysine; alternateBy similarity
    Modified residuei56 – 561N6-acetyllysineBy similarity
    Modified residuei59 – 591N6-acetyllysine; alternateBy similarity
    Modified residuei59 – 591N6-succinyllysine; alternateBy similarity
    Modified residuei110 – 1101N6-acetyllysine; alternateBy similarity
    Modified residuei110 – 1101N6-succinyllysine; alternateBy similarity
    Modified residuei114 – 1141N6-acetyllysineBy similarity
    Modified residuei116 – 1161N6-acetyllysine; alternateBy similarity
    Modified residuei116 – 1161N6-succinyllysine; alternateBy similarity
    Modified residuei200 – 2001N6-acetyllysineBy similarity
    Modified residuei210 – 2101N6-acetyllysine; alternateBy similarity
    Modified residuei210 – 2101N6-succinyllysine; alternateBy similarity
    Modified residuei238 – 2381N6-acetyllysineBy similarity
    Modified residuei248 – 2481N6-acetyllysine; alternateBy similarity
    Modified residuei248 – 2481N6-succinyllysine; alternateBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP38117.
    PaxDbiP38117.
    PeptideAtlasiP38117.
    PRIDEiP38117.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00004902.
    UCD-2DPAGEP38117.

    PTM databases

    PhosphoSiteiP38117.

    Expressioni

    Tissue specificityi

    Abundant in liver, heart and skeletal muscle. A weak expression is seen in the brain, placenta, lung, kidney and pancreas.

    Gene expression databases

    ArrayExpressiP38117.
    BgeeiP38117.
    CleanExiHS_ETFB.
    GenevestigatoriP38117.

    Organism-specific databases

    HPAiHPA018910.
    HPA018921.
    HPA018923.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit.

    Protein-protein interaction databases

    BioGridi108410. 9 interactions.
    DIPiDIP-6162N.
    IntActiP38117. 3 interactions.
    MINTiMINT-1520912.
    STRINGi9606.ENSP00000346173.

    Structurei

    Secondary structure

    1
    255
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 95
    Beta strandi12 – 143
    Beta strandi16 – 183
    Beta strandi26 – 294
    Beta strandi36 – 383
    Helixi40 – 5415
    Beta strandi59 – 6810
    Helixi71 – 8111
    Beta strandi84 – 907
    Helixi93 – 964
    Helixi101 – 11515
    Beta strandi118 – 1247
    Turni127 – 1293
    Helixi134 – 1429
    Beta strandi146 – 15611
    Beta strandi159 – 1668
    Beta strandi169 – 18315
    Helixi185 – 1873
    Helixi195 – 2006
    Turni201 – 2033
    Beta strandi206 – 2094
    Helixi211 – 2144
    Beta strandi221 – 2288
    Helixi242 – 25110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EFVX-ray2.10B1-255[»]
    1T9GX-ray2.90S1-255[»]
    2A1TX-ray2.80S1-255[»]
    2A1UX-ray2.11B1-255[»]
    ProteinModelPortaliP38117.
    SMRiP38117. Positions 4-255.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP38117.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ETF beta-subunit/FixA family.Curated

    Phylogenomic databases

    eggNOGiCOG2086.
    HOGENOMiHOG000247877.
    HOVERGENiHBG005614.
    KOiK03521.
    OMAiIDFAIKP.
    OrthoDBiEOG7X3QS5.
    PhylomeDBiP38117.
    TreeFamiTF314039.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    InterProiIPR000049. ET-Flavoprotein_bsu_CS.
    IPR014730. ETF_a/b_N.
    IPR012255. ETF_b.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR21294. PTHR21294. 1 hit.
    PfamiPF01012. ETF. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000090. Beta-ETF. 1 hit.
    SMARTiSM00893. ETF. 1 hit.
    [Graphical view]
    PROSITEiPS01065. ETF_BETA. 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 splicing. Align

    Isoform 1 (identifier: P38117-1) [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

    MAELRVLVAV KRVIDYAVKI RVKPDRTGVV TDGVKHSMNP FCEIAVEEAV    50
    RLKEKKLVKE VIAVSCGPAQ CQETIRTALA MGADRGIHVE VPPAEAERLG 100
    PLQVARVLAK LAEKEKVDLV LLGKQAIDDD CNQTGQMTAG FLDWPQGTFA 150
    SQVTLEGDKL KVEREIDGGL ETLRLKLPAV VTADLRLNEP RYATLPNIMK 200
    AKKKKIEVIK PGDLGVDLTS KLSVISVEDP PQRTAGVKVE TTEDLVAKLK 250
    EIGRI 255
    Length:255
    Mass (Da):27,844
    Last modified:January 23, 2007 - v3
    Checksum:i47E6EAEF50EB2C80
    GO
    Isoform 2 (identifier: P38117-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-19: AELRVLVAVKRVIDYAVK → MYLSLWVTIN...DPTPSPPAGQ

    Show »
    Length:347
    Mass (Da):37,566
    Checksum:i87FD84ABA5129BD4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti198 – 1981I → S in CAB37832. (PubMed:7912128)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti128 – 1281D → N in GA2B. 1 Publication
    VAR_025804
    Natural varianti154 – 1541T → M.2 Publications
    Corresponds to variant rs1130426 [ dbSNP | Ensembl ].
    VAR_008548
    Natural varianti164 – 1641R → Q in GA2B. 1 Publication
    Corresponds to variant rs104894677 [ dbSNP | Ensembl ].
    VAR_002369

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 1918AELRV…DYAVK → MYLSLWVTINTVNLRNTLSG LRGAVTTVGMIKSDVPGTQE WLDERRRQGDLPLPTNSNPV LSLELCDPGQGPAPFQAVVV LIQPGRGLALRPPPSCLFPP DPTPSPPAGQ in isoform 2. 2 PublicationsVSP_017850Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71129 mRNA. Translation: CAA50441.1.
    AF436663
    , AF436658, AF436659, AF436660, AF436661, AF436662 Genomic DNA. Translation: AAN03713.1.
    AF370381 mRNA. Translation: AAQ15217.1.
    CR456827 mRNA. Translation: CAG33108.1.
    AK055285 mRNA. Translation: BAG51494.1.
    BC093961 mRNA. Translation: AAH93961.1.
    BC093963 mRNA. Translation: AAH93963.1.
    X76067 Genomic DNA. Translation: CAB37832.1.
    CCDSiCCDS12828.1. [P38117-1]
    PIRiS32482.
    RefSeqiNP_001014763.1. NM_001014763.1.
    NP_001976.1. NM_001985.2. [P38117-1]
    UniGeneiHs.348531.

    Genome annotation databases

    EnsembliENST00000309244; ENSP00000311930; ENSG00000105379. [P38117-1]
    ENST00000354232; ENSP00000346173; ENSG00000105379. [P38117-2]
    GeneIDi2109.
    KEGGihsa:2109.
    UCSCiuc002pwg.3. human. [P38117-2]
    uc002pwh.3. human. [P38117-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71129 mRNA. Translation: CAA50441.1 .
    AF436663
    , AF436658 , AF436659 , AF436660 , AF436661 , AF436662 Genomic DNA. Translation: AAN03713.1 .
    AF370381 mRNA. Translation: AAQ15217.1 .
    CR456827 mRNA. Translation: CAG33108.1 .
    AK055285 mRNA. Translation: BAG51494.1 .
    BC093961 mRNA. Translation: AAH93961.1 .
    BC093963 mRNA. Translation: AAH93963.1 .
    X76067 Genomic DNA. Translation: CAB37832.1 .
    CCDSi CCDS12828.1. [P38117-1 ]
    PIRi S32482.
    RefSeqi NP_001014763.1. NM_001014763.1.
    NP_001976.1. NM_001985.2. [P38117-1 ]
    UniGenei Hs.348531.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EFV X-ray 2.10 B 1-255 [» ]
    1T9G X-ray 2.90 S 1-255 [» ]
    2A1T X-ray 2.80 S 1-255 [» ]
    2A1U X-ray 2.11 B 1-255 [» ]
    ProteinModelPortali P38117.
    SMRi P38117. Positions 4-255.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108410. 9 interactions.
    DIPi DIP-6162N.
    IntActi P38117. 3 interactions.
    MINTi MINT-1520912.
    STRINGi 9606.ENSP00000346173.

    PTM databases

    PhosphoSitei P38117.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00004902.
    UCD-2DPAGE P38117.

    Proteomic databases

    MaxQBi P38117.
    PaxDbi P38117.
    PeptideAtlasi P38117.
    PRIDEi P38117.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309244 ; ENSP00000311930 ; ENSG00000105379 . [P38117-1 ]
    ENST00000354232 ; ENSP00000346173 ; ENSG00000105379 . [P38117-2 ]
    GeneIDi 2109.
    KEGGi hsa:2109.
    UCSCi uc002pwg.3. human. [P38117-2 ]
    uc002pwh.3. human. [P38117-1 ]

    Organism-specific databases

    CTDi 2109.
    GeneCardsi GC19M051848.
    HGNCi HGNC:3482. ETFB.
    HPAi HPA018910.
    HPA018921.
    HPA018923.
    MIMi 130410. gene.
    231680. phenotype.
    neXtProti NX_P38117.
    Orphaneti 394532. Multiple acyl-CoA dehydrogenation deficiency, mild type.
    394529. Multiple acyl-CoA dehydrogenation deficiency, severe neonatal type.
    PharmGKBi PA27898.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2086.
    HOGENOMi HOG000247877.
    HOVERGENi HBG005614.
    KOi K03521.
    OMAi IDFAIKP.
    OrthoDBi EOG7X3QS5.
    PhylomeDBi P38117.
    TreeFami TF314039.

    Enzyme and pathway databases

    Reactomei REACT_22393. Respiratory electron transport.

    Miscellaneous databases

    EvolutionaryTracei P38117.
    GeneWikii ETFB.
    GenomeRNAii 2109.
    NextBioi 8527.
    PROi P38117.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P38117.
    Bgeei P38117.
    CleanExi HS_ETFB.
    Genevestigatori P38117.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    InterProi IPR000049. ET-Flavoprotein_bsu_CS.
    IPR014730. ETF_a/b_N.
    IPR012255. ETF_b.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    PANTHERi PTHR21294. PTHR21294. 1 hit.
    Pfami PF01012. ETF. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000090. Beta-ETF. 1 hit.
    SMARTi SM00893. ETF. 1 hit.
    [Graphical view ]
    PROSITEi PS01065. ETF_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and mitochondrial import of the beta-subunit of the human electron-transfer flavoprotein."
      Finocchiaro G., Colombo I., Garavaglia B., Gellera C., Valdameri G., Garbuglio N., Didonato S.
      Eur. J. Biochem. 213:1003-1008(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal liver.
    2. "Clear relationship between ETF/ETFDH genotype and phenotype in patients with multiple acyl-CoA dehydrogenation deficiency."
      Olsen R.K.J., Andresen B.S., Christensen E., Bross P., Skovby F., Gregersen N.
      Hum. Mutat. 22:12-23(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GA2B ASN-128.
    3. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT MET-154.
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    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] (ISOFORM 2).
      Tissue: Brain.
    6. "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).
      Tissue: Cerebellum.
    7. "Mutations and polymorphisms of the gene encoding the beta-subunit of the electron transfer flavoprotein in three patients with glutaric acidemia type II."
      Colombo I., Finocchiaro G., Garavaglia B., Garbuglio N., Yamaguchi S., Frerman F., Berra B., Didonato S.
      Hum. Mol. Genet. 3:429-435(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-199, VARIANT GA2B GLN-164.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Three-dimensional structure of human electron transfer flavoprotein to 2.1-A resolution."
      Roberts D.L., Frerman F.E., Kim J.-J.P.
      Proc. Natl. Acad. Sci. U.S.A. 93:14355-14360(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
    10. "A polymorphic variant in the human electron transfer flavoprotein alpha-chain (alpha-T171) displays decreased thermal stability and is overrepresented in very-long-chain acyl-CoA dehydrogenase-deficient patients with mild childhood presentation."
      Bross P., Pedersen P., Winter V., Nyholm M., Johansen B.N., Olsen R.K., Corydon M.J., Andresen B.S., Eiberg H., Kolvraa S., Gregersen N.
      Mol. Genet. Metab. 67:138-147(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MET-154.

    Entry informationi

    Entry nameiETFB_HUMAN
    AccessioniPrimary (citable) accession number: P38117
    Secondary accession number(s): B3KNY2
    , Q6IBH7, Q71RF6, Q9Y3S7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 153 of the entry and version 3 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 19
      Human chromosome 19: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3