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P13804

- ETFA_HUMAN

UniProt

P13804 - ETFA_HUMAN

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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

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 – 30229FADAdd
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
Complete GO annotation...

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

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
Complete GO annotation...

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 – ?Mitochondrion

Amino acid modifications

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

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.

Miscellaneous databases

EvolutionaryTraceiP13804.

Family & Domainsi

Sequence similaritiesi

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

« Hide 'large scale' publications
  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

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