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P38117 (ETFB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Electron transfer flavoprotein subunit beta

Short name=Beta-ETF
Gene names
Name:ETFB
ORF Names:FP585
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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).

Cofactor

Binds 1 FAD per dimer.

Binds 1 AMP per subunit.

Subunit structure

Heterodimer of an alpha and a beta subunit.

Subcellular location

Mitochondrion matrix.

Tissue specificity

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.7

Sequence similarities

Belongs to the ETF beta-subunit/FixA family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P38117-1)

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.
Isoform 2 (identifier: P38117-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 255254Electron transfer flavoprotein subunit beta
PRO_0000167870

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue191N6-acetyllysine; alternate By similarity
Modified residue191N6-succinyllysine; alternate By similarity
Modified residue351N6-acetyllysine; alternate By similarity
Modified residue351N6-succinyllysine; alternate By similarity
Modified residue561N6-acetyllysine By similarity
Modified residue591N6-acetyllysine; alternate By similarity
Modified residue591N6-succinyllysine; alternate By similarity
Modified residue1101N6-acetyllysine; alternate By similarity
Modified residue1101N6-succinyllysine; alternate By similarity
Modified residue1141N6-acetyllysine By similarity
Modified residue1161N6-acetyllysine; alternate By similarity
Modified residue1161N6-succinyllysine; alternate By similarity
Modified residue2001N6-acetyllysine By similarity
Modified residue2101N6-acetyllysine; alternate By similarity
Modified residue2101N6-succinyllysine; alternate By similarity
Modified residue2381N6-acetyllysine By similarity
Modified residue2481N6-acetyllysine; alternate By similarity
Modified residue2481N6-succinyllysine; alternate By similarity

Natural variations

Alternative sequence2 – 1918AELRV…DYAVK → MYLSLWVTINTVNLRNTLSG LRGAVTTVGMIKSDVPGTQE WLDERRRQGDLPLPTNSNPV LSLELCDPGQGPAPFQAVVV LIQPGRGLALRPPPSCLFPP DPTPSPPAGQ in isoform 2.
VSP_017850
Natural variant1281D → N in GA2B. Ref.2
VAR_025804
Natural variant1541T → M. Ref.3 Ref.10
Corresponds to variant rs1130426 [ dbSNP | Ensembl ].
VAR_008548
Natural variant1641R → Q in GA2B. Ref.7
Corresponds to variant rs104894677 [ dbSNP | Ensembl ].
VAR_002369

Experimental info

Sequence conflict1981I → S in CAB37832. Ref.7

Secondary structure

................................................ 255
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 47E6EAEF50EB2C80

FASTA25527,844
        10         20         30         40         50         60 
MAELRVLVAV KRVIDYAVKI RVKPDRTGVV TDGVKHSMNP FCEIAVEEAV RLKEKKLVKE 

        70         80         90        100        110        120 
VIAVSCGPAQ CQETIRTALA MGADRGIHVE VPPAEAERLG PLQVARVLAK LAEKEKVDLV 

       130        140        150        160        170        180 
LLGKQAIDDD CNQTGQMTAG FLDWPQGTFA SQVTLEGDKL KVEREIDGGL ETLRLKLPAV 

       190        200        210        220        230        240 
VTADLRLNEP RYATLPNIMK AKKKKIEVIK PGDLGVDLTS KLSVISVEDP PQRTAGVKVE 

       250 
TTEDLVAKLK EIGRI 

« Hide

Isoform 2 [UniParc].

Checksum: 87FD84ABA5129BD4
Show »

FASTA34737,566

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X71129 mRNA. Translation: CAA50441.1.
AF436663 expand/collapse EMBL AC list , 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.
PIRS32482.
RefSeqNP_001014763.1. NM_001014763.1.
NP_001976.1. NM_001985.2.
UniGeneHs.348531.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EFVX-ray2.10B1-255[»]
1T9GX-ray2.90S1-255[»]
2A1TX-ray2.80S1-255[»]
2A1UX-ray2.11B1-255[»]
ProteinModelPortalP38117.
SMRP38117. Positions 4-255.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108410. 8 interactions.
DIPDIP-6162N.
IntActP38117. 3 interactions.
MINTMINT-1520912.
STRING9606.ENSP00000346173.

PTM databases

PhosphoSiteP38117.

2D gel databases

REPRODUCTION-2DPAGEIPI00004902.
UCD-2DPAGEP38117.

Proteomic databases

PaxDbP38117.
PeptideAtlasP38117.
PRIDEP38117.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309244; ENSP00000311930; ENSG00000105379. [P38117-1]
ENST00000354232; ENSP00000346173; ENSG00000105379. [P38117-2]
GeneID2109.
KEGGhsa:2109.
UCSCuc002pwg.3. human. [P38117-2]
uc002pwh.3. human. [P38117-1]

Organism-specific databases

CTD2109.
GeneCardsGC19M051848.
HGNCHGNC:3482. ETFB.
HPAHPA018910.
HPA018921.
HPA018923.
MIM130410. gene.
231680. phenotype.
neXtProtNX_P38117.
Orphanet26791. Glutaric acidemia type 2.
PharmGKBPA27898.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2086.
HOGENOMHOG000247877.
HOVERGENHBG005614.
KOK03521.
OMAEDPPVRQ.
OrthoDBEOG7X3QS5.
PhylomeDBP38117.
TreeFamTF314039.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP38117.
BgeeP38117.
CleanExHS_ETFB.
GenevestigatorP38117.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
InterProIPR000049. ET-Flavoprotein_bsu_CS.
IPR014730. ETF_a/b_N.
IPR012255. ETF_b.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR21294. PTHR21294. 1 hit.
PfamPF01012. ETF. 1 hit.
[Graphical view]
PIRSFPIRSF000090. Beta-ETF. 1 hit.
SMARTSM00893. ETF. 1 hit.
[Graphical view]
PROSITEPS01065. ETF_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP38117.
GeneWikiETFB.
GenomeRNAi2109.
NextBio8527.
PROP38117.
SOURCESearch...

Entry information

Entry nameETFB_HUMAN
AccessionPrimary (citable) accession number: P38117
Secondary accession number(s): B3KNY2 expand/collapse secondary AC list , Q6IBH7, Q71RF6, Q9Y3S7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM