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P13804

- ETFA_HUMAN

UniProt

P13804 - ETFA_HUMAN

Protein

Electron transfer flavoprotein subunit alpha, mitochondrial

Gene

ETFA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi274 – 30229FADSequence AnalysisAdd
    BLAST

    GO - Molecular functioni

    1. electron carrier activity Source: UniProtKB
    2. flavin adenine dinucleotide binding Source: UniProtKB
    3. oxidoreductase activity Source: UniProtKB

    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 alpha, mitochondrial
    Short name:
    Alpha-ETF
    Gene namesi
    Name:ETFA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:3481. ETFA.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial matrix Source: Reactome
    3. mitochondrion Source: UniProt

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Glutaric aciduria 2A (GA2A) [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 varianti116 – 1161G → R in GA2A. 1 Publication
    VAR_002366
    Natural varianti157 – 1571V → G in GA2A. 1 Publication
    VAR_002367
    Natural varianti266 – 2661T → M in GA2A. 1 Publication
    VAR_002368

    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.
    PharmGKBiPA27897.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 333Electron transfer flavoprotein subunit alpha, mitochondrialPRO_0000008650
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei59 – 591N6-acetyllysine; alternateBy similarity
    Modified residuei59 – 591N6-succinyllysine; alternateBy similarity
    Modified residuei62 – 621N6-acetyllysineBy similarity
    Modified residuei69 – 691N6-acetyllysine; alternateBy similarity
    Modified residuei69 – 691N6-succinyllysine; alternateBy similarity
    Modified residuei75 – 751N6-acetyllysineBy similarity
    Modified residuei85 – 851N6-acetyllysine; alternateBy similarity
    Modified residuei85 – 851N6-succinyllysine; alternateBy similarity
    Modified residuei101 – 1011N6-acetyllysineBy similarity
    Modified residuei139 – 1391N6-acetyllysineBy similarity
    Modified residuei158 – 1581N6-acetyllysine; alternateBy similarity
    Modified residuei158 – 1581N6-succinyllysine; alternateBy similarity
    Modified residuei164 – 1641N6-acetyllysineBy similarity
    Modified residuei187 – 1871N6-succinyllysineBy similarity
    Modified residuei203 – 2031N6-acetyllysine; alternateBy similarity
    Modified residuei203 – 2031N6-succinyllysine; alternateBy similarity
    Modified residuei216 – 2161N6-succinyllysineBy similarity
    Modified residuei226 – 2261N6-acetyllysine; alternateBy similarity
    Modified residuei226 – 2261N6-succinyllysine; alternateBy similarity
    Modified residuei232 – 2321N6-acetyllysine; alternateBy similarity
    Modified residuei232 – 2321N6-succinyllysine; alternateBy similarity
    Modified residuei301 – 3011N6-succinyllysineBy similarity

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP13804.
    PaxDbiP13804.
    PeptideAtlasiP13804.
    PRIDEiP13804.

    2D gel databases

    UCD-2DPAGEP13804.

    PTM databases

    PhosphoSiteiP13804.

    Expressioni

    Gene expression databases

    ArrayExpressiP13804.
    BgeeiP13804.
    CleanExiHS_ETFA.
    GenevestigatoriP13804.

    Organism-specific databases

    HPAiHPA018990.
    HPA018993.
    HPA018996.
    HPA024089.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit.

    Protein-protein interaction databases

    BioGridi108409. 16 interactions.
    DIPiDIP-6161N.
    IntActiP13804. 7 interactions.
    MINTiMINT-5002447.
    STRINGi9606.ENSP00000267950.

    Structurei

    Secondary structure

    1
    333
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi21 – 255
    Beta strandi28 – 314
    Helixi36 – 4510
    Beta strandi49 – 5810
    Helixi61 – 699
    Beta strandi75 – 806
    Helixi82 – 843
    Helixi89 – 10315
    Beta strandi106 – 1138
    Helixi114 – 12714
    Beta strandi132 – 1354
    Beta strandi137 – 1404
    Beta strandi143 – 1486
    Turni149 – 1524
    Beta strandi153 – 1597
    Beta strandi162 – 1687
    Helixi170 – 1723
    Beta strandi178 – 1803
    Beta strandi184 – 1874
    Beta strandi196 – 2049
    Helixi212 – 2143
    Beta strandi216 – 2216
    Helixi223 – 2253
    Helixi229 – 2313
    Helixi232 – 24110
    Beta strandi244 – 2474
    Helixi249 – 2535
    Helixi259 – 2613
    Beta strandi262 – 2643
    Beta strandi273 – 2797
    Helixi284 – 2874
    Turni288 – 2925
    Beta strandi294 – 3018
    Helixi306 – 3094
    Beta strandi312 – 3176
    Helixi319 – 32911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EFVX-ray2.10A20-333[»]
    1T9GX-ray2.90R1-333[»]
    2A1TX-ray2.80R1-333[»]
    2A1UX-ray2.11A1-333[»]
    ProteinModelPortaliP13804.
    SMRiP13804. Positions 20-331.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP13804.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ETF alpha-subunit/FixB family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG2025.
    HOGENOMiHOG000247865.
    HOVERGENiHBG002317.
    InParanoidiP13804.
    KOiK03522.
    OMAiTITAAKH.
    OrthoDBiEOG76MK8R.
    PhylomeDBiP13804.
    TreeFamiTF105763.

    Family and domain databases

    Gene3Di3.40.50.1220. 1 hit.
    3.40.50.620. 1 hit.
    InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR001308. ETF_a.
    IPR014730. ETF_a/b_N.
    IPR014731. ETF_asu_C.
    IPR018206. ETF_asu_C_CS.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF01012. ETF. 1 hit.
    PF00766. ETF_alpha. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000089. Electra_flavoP_a. 1 hit.
    SMARTiSM00893. ETF. 1 hit.
    [Graphical view]
    SUPFAMiSSF52467. SSF52467. 1 hit.
    PROSITEiPS00696. ETF_ALPHA. 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: P13804-1) [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

    MFRAAAPGQL RRAASLLRFQ STLVIAEHAN DSLAPITLNT ITAATRLGGE    50
    VSCLVAGTKC DKVAQDLCKV AGIAKVLVAQ HDVYKGLLPE ELTPLILATQ 100
    KQFNYTHICA GASAFGKNLL PRVAAKLEVA PISDIIAIKS PDTFVRTIYA 150
    GNALCTVKCD EKVKVFSVRG TSFDAAATSG GSASSEKASS TSPVEISEWL 200
    DQKLTKSDRP ELTGAKVVVS GGRGLKSGEN FKLLYDLADQ LHAAVGASRA 250
    AVDAGFVPND MQVGQTGKIV APELYIAVGI SGAIQHLAGM KDSKTIVAIN 300
    KDPEAPIFQV ADYGIVADLF KVVPEMTEIL KKK 333
    Length:333
    Mass (Da):35,080
    Last modified:January 1, 1990 - v1
    Checksum:i2EC6D1ADE68CBDB5
    GO
    Isoform 2 (identifier: P13804-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         14-62: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:284
    Mass (Da):30,026
    Checksum:i3AC6D1AA1BE79C6D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti116 – 1161G → R in GA2A. 1 Publication
    VAR_002366
    Natural varianti157 – 1571V → G in GA2A. 1 Publication
    VAR_002367
    Natural varianti171 – 1711T → I.1 Publication
    Corresponds to variant rs1801591 [ dbSNP | Ensembl ].
    VAR_008547
    Natural varianti266 – 2661T → M in GA2A. 1 Publication
    VAR_002368

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei14 – 6249Missing in isoform 2. 1 PublicationVSP_043246Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04058 mRNA. Translation: AAA52406.1.
    S55815 mRNA. No translation available.
    S55816 mRNA. No translation available.
    AJ224002 Genomic DNA. Translation: CAA11802.1.
    AF436657
    , AF436646, AF436647, AF436648, AF436649, AF436650, AF436651, AF436652, AF436653, AF436654, AF436655, AF436656 Genomic DNA. Translation: AAN03712.1.
    BT009796 mRNA. Translation: AAP88798.1.
    AK292979 mRNA. Translation: BAF85668.1.
    AK300044 mRNA. Translation: BAG61855.1.
    AC027243 Genomic DNA. No translation available.
    AC091100 Genomic DNA. No translation available.
    CH471136 Genomic DNA. Translation: EAW99221.1.
    BC015526 mRNA. Translation: AAH15526.1.
    BC095457 mRNA. Translation: AAH95457.1.
    CCDSiCCDS32299.1. [P13804-1]
    CCDS45311.1. [P13804-2]
    PIRiA31998.
    RefSeqiNP_000117.1. NM_000126.3. [P13804-1]
    NP_001121188.1. NM_001127716.1. [P13804-2]
    UniGeneiHs.39925.

    Genome annotation databases

    EnsembliENST00000433983; ENSP00000399273; ENSG00000140374. [P13804-2]
    ENST00000557943; ENSP00000452762; ENSG00000140374. [P13804-1]
    GeneIDi2108.
    KEGGihsa:2108.
    UCSCiuc002bbt.2. human. [P13804-1]
    uc010bkq.1. human. [P13804-2]

    Polymorphism databases

    DMDMi119636.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04058 mRNA. Translation: AAA52406.1 .
    S55815 mRNA. No translation available.
    S55816 mRNA. No translation available.
    AJ224002 Genomic DNA. Translation: CAA11802.1 .
    AF436657
    , AF436646 , AF436647 , AF436648 , AF436649 , AF436650 , AF436651 , AF436652 , AF436653 , AF436654 , AF436655 , AF436656 Genomic DNA. Translation: AAN03712.1 .
    BT009796 mRNA. Translation: AAP88798.1 .
    AK292979 mRNA. Translation: BAF85668.1 .
    AK300044 mRNA. Translation: BAG61855.1 .
    AC027243 Genomic DNA. No translation available.
    AC091100 Genomic DNA. No translation available.
    CH471136 Genomic DNA. Translation: EAW99221.1 .
    BC015526 mRNA. Translation: AAH15526.1 .
    BC095457 mRNA. Translation: AAH95457.1 .
    CCDSi CCDS32299.1. [P13804-1 ]
    CCDS45311.1. [P13804-2 ]
    PIRi A31998.
    RefSeqi NP_000117.1. NM_000126.3. [P13804-1 ]
    NP_001121188.1. NM_001127716.1. [P13804-2 ]
    UniGenei Hs.39925.

    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 A 20-333 [» ]
    1T9G X-ray 2.90 R 1-333 [» ]
    2A1T X-ray 2.80 R 1-333 [» ]
    2A1U X-ray 2.11 A 1-333 [» ]
    ProteinModelPortali P13804.
    SMRi P13804. Positions 20-331.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108409. 16 interactions.
    DIPi DIP-6161N.
    IntActi P13804. 7 interactions.
    MINTi MINT-5002447.
    STRINGi 9606.ENSP00000267950.

    PTM databases

    PhosphoSitei P13804.

    Polymorphism databases

    DMDMi 119636.

    2D gel databases

    UCD-2DPAGE P13804.

    Proteomic databases

    MaxQBi P13804.
    PaxDbi P13804.
    PeptideAtlasi P13804.
    PRIDEi P13804.

    Protocols and materials databases

    DNASUi 2108.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000433983 ; ENSP00000399273 ; ENSG00000140374 . [P13804-2 ]
    ENST00000557943 ; ENSP00000452762 ; ENSG00000140374 . [P13804-1 ]
    GeneIDi 2108.
    KEGGi hsa:2108.
    UCSCi uc002bbt.2. human. [P13804-1 ]
    uc010bkq.1. human. [P13804-2 ]

    Organism-specific databases

    CTDi 2108.
    GeneCardsi GC15M076508.
    HGNCi HGNC:3481. ETFA.
    HPAi HPA018990.
    HPA018993.
    HPA018996.
    HPA024089.
    MIMi 231680. phenotype.
    608053. gene.
    neXtProti NX_P13804.
    Orphaneti 394532. Multiple acyl-CoA dehydrogenation deficiency, mild type.
    394529. Multiple acyl-CoA dehydrogenation deficiency, severe neonatal type.
    PharmGKBi PA27897.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2025.
    HOGENOMi HOG000247865.
    HOVERGENi HBG002317.
    InParanoidi P13804.
    KOi K03522.
    OMAi TITAAKH.
    OrthoDBi EOG76MK8R.
    PhylomeDBi P13804.
    TreeFami TF105763.

    Enzyme and pathway databases

    Reactomei REACT_22393. Respiratory electron transport.

    Miscellaneous databases

    EvolutionaryTracei P13804.
    GeneWikii ETFA.
    GenomeRNAii 2108.
    NextBioi 8523.
    PROi P13804.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13804.
    Bgeei P13804.
    CleanExi HS_ETFA.
    Genevestigatori P13804.

    Family and domain databases

    Gene3Di 3.40.50.1220. 1 hit.
    3.40.50.620. 1 hit.
    InterProi IPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR001308. ETF_a.
    IPR014730. ETF_a/b_N.
    IPR014731. ETF_asu_C.
    IPR018206. ETF_asu_C_CS.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF01012. ETF. 1 hit.
    PF00766. ETF_alpha. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000089. Electra_flavoP_a. 1 hit.
    SMARTi SM00893. ETF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52467. SSF52467. 1 hit.
    PROSITEi PS00696. ETF_ALPHA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and nucleotide sequence of cDNAs encoding the alpha-subunit of human electron transfer flavoprotein."
      Finocchiaro G., Ito M., Ikeda Y., Tanaka K.
      J. Biol. Chem. 263:15773-15780(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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].
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "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 1 AND 2).
      Tissue: Trachea.
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Chondrosarcoma and Colon.
    8. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 86-101 AND 170-203, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "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).
    11. "Molecular characterization of variant alpha-subunit of electron transfer flavoprotein in three patients with glutaric acidemia type II -- and identification of glycine substitution for valine-157 in the sequence of the precursor, producing an unstable mature protein in a patient."
      Indo Y., Glassberg R., Yokota I., Tanaka K.
      Am. J. Hum. Genet. 49:575-580(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GA2A GLY-157.
    12. "Glutaric acidemia type II. Heterogeneity in beta-oxidation flux, polypeptide synthesis, and complementary DNA mutations in the alpha subunit of electron transfer flavoprotein in eight patients."
      Freneaux E., Sheffield V.C., Molin L., Shires A., Rhead W.
      J. Clin. Invest. 90:1679-1686(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GA2A ARG-116 AND MET-266.
    13. "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 ILE-171.

    Entry informationi

    Entry nameiETFA_HUMAN
    AccessioniPrimary (citable) accession number: P13804
    Secondary accession number(s): B4DT43, Q53XN3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: January 1, 1990
    Last modified: October 1, 2014
    This is version 164 of the entry and version 1 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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