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P38117

- ETFB_HUMAN

UniProt

P38117 - ETFB_HUMAN

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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

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

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei16 – 161FAD1 Publication

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
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 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
Complete GO annotation...

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi165 – 1651E → A or Q: Drastically increases interprotein electron transfer rates. 1 Publication
Mutagenesisi195 – 1951L → A: Severely impaired in complex formation with ACADM. 1 Publication

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,N6,N6-trimethyllysine; by METTL20; alternate1 Publication
Modified residuei200 – 2001N6-acetyllysine; alternateBy similarity
Modified residuei203 – 2031N6,N6,N6-trimethyllysine; by METTL201 Publication
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, Methylation

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

BgeeiP38117.
CleanExiHS_ETFB.
ExpressionAtlasiP38117. baseline and differential.
GenevestigatoriP38117.

Organism-specific databases

HPAiHPA018910.
HPA018921.
HPA018923.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit.1 Publication

Protein-protein interaction databases

BioGridi108410. 10 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 – 95Combined sources
Beta strandi12 – 143Combined sources
Beta strandi16 – 183Combined sources
Beta strandi26 – 294Combined sources
Beta strandi36 – 383Combined sources
Helixi40 – 5415Combined sources
Beta strandi59 – 6810Combined sources
Helixi71 – 8111Combined sources
Beta strandi84 – 907Combined sources
Helixi93 – 964Combined sources
Helixi101 – 11515Combined sources
Beta strandi118 – 1247Combined sources
Turni127 – 1293Combined sources
Helixi134 – 1429Combined sources
Beta strandi146 – 15611Combined sources
Beta strandi159 – 1668Combined sources
Beta strandi169 – 18315Combined sources
Helixi185 – 1873Combined sources
Helixi195 – 2006Combined sources
Turni201 – 2033Combined sources
Beta strandi206 – 2094Combined sources
Helixi211 – 2144Combined sources
Beta strandi221 – 2288Combined sources
Helixi242 – 25110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni183 – 20523Recognition loop2 PublicationsAdd
BLAST

Domaini

The recognition loop recognizes a hydrophobic patch at the surface of interacting dehydrogenases and acts as a static anchor at the interface.1 Publication

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG2086.
GeneTreeiENSGT00390000009936.
HOGENOMiHOG000247877.
HOVERGENiHBG005614.
InParanoidiP38117.
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

        10         20         30         40         50
MAELRVLVAV KRVIDYAVKI RVKPDRTGVV TDGVKHSMNP FCEIAVEEAV
60 70 80 90 100
RLKEKKLVKE VIAVSCGPAQ CQETIRTALA MGADRGIHVE VPPAEAERLG
110 120 130 140 150
PLQVARVLAK LAEKEKVDLV LLGKQAIDDD CNQTGQMTAG FLDWPQGTFA
160 170 180 190 200
SQVTLEGDKL KVEREIDGGL ETLRLKLPAV VTADLRLNEP RYATLPNIMK
210 220 230 240 250
AKKKKIEVIK PGDLGVDLTS KLSVISVEDP PQRTAGVKVE TTEDLVAKLK

EIGRI
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:
     1-19: MAELRVLVAVKRVIDYAVK → MYLSLWVTIN...DPTPSPPAGQ

Show »
Length:346
Mass (Da):37,434
Checksum:i29C992C07350130A
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 sequencei1 – 1919MAELR…DYAVK → MYLSLWVTINTVNLRNTLSG LRGAVTTVGMIKSDVPGTQE WLDERRRQGDLPLPTNSNPV LSLELCDPGQGPAPFQAVVV LIQPGRGLALRPPPSCLFPP DPTPSPPAGQ in isoform 2. 2 PublicationsVSP_017850Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
AK291881 mRNA. Translation: BAF84570.1.
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.
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:
EMBLi
GenBanki
DDBJi
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 .
AK291881 mRNA. Translation: BAF84570.1 .
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:
PDBei
RCSB PDBi
PDBji
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. 10 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 .
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.
GeneTreei ENSGT00390000009936.
HOGENOMi HOG000247877.
HOVERGENi HBG005614.
InParanoidi P38117.
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

Bgeei P38117.
CleanExi HS_ETFB.
ExpressionAtlasi P38117. baseline and differential.
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

« Hide 'large scale' publications
  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] (ISOFORMS 1 AND 2), VARIANT MET-154.
    Tissue: Brain and Skeletal muscle.
  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. "Human METTL20 methylates lysine residues adjacent to the recognition loop of the electron transfer flavoprotein in mitochondria."
    Rhein V.F., Carroll J., He J., Ding S., Fearnley I.M., Walker J.E.
    J. Biol. Chem. 289:24640-24651(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-200 AND LYS-203.
  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) IN COMPLEX WITH ETFA, COFACTORS, SUBUNIT, FAD BINDING SITES.
  11. "Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain acyl-CoA dehydrogenase complex."
    Toogood H.S., van Thiel A., Basran J., Sutcliffe M.J., Scrutton N.S., Leys D.
    J. Biol. Chem. 279:32904-32912(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH ETFA AND ACADM, MUTAGENESIS OF LEU-195.
  12. "Stabilization of non-productive conformations underpins rapid electron transfer to electron-transferring flavoprotein."
    Toogood H.S., van Thiel A., Scrutton N.S., Leys D.
    J. Biol. Chem. 280:30361-30366(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF MUTANT ALA-165 IN COMPLEX WITH ETFA AND ACADM, MUTAGENESIS OF GLU-165.
  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 MET-154.

Entry informationi

Entry nameiETFB_HUMAN
AccessioniPrimary (citable) accession number: P38117
Secondary accession number(s): A8K766
, B3KNY2, Q6IBH7, Q71RF6, Q9Y3S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 155 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