ETFB_HUMAN
ID ETFB_HUMAN Reviewed; 255 AA.
AC P38117; A8K766; B3KNY2; Q6IBH7; Q71RF6; Q9Y3S7;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Electron transfer flavoprotein subunit beta {ECO:0000305};
DE Short=Beta-ETF {ECO:0000303|PubMed:8504797};
GN Name=ETFB {ECO:0000312|HGNC:HGNC:3482}; ORFNames=FP585;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal liver;
RX PubMed=8504797; DOI=10.1111/j.1432-1033.1993.tb17847.x;
RA Finocchiaro G., Colombo I., Garavaglia B., Gellera C., Valdameri G.,
RA Garbuglio N., Didonato S.;
RT "cDNA cloning and mitochondrial import of the beta-subunit of the human
RT electron-transfer flavoprotein.";
RL Eur. J. Biochem. 213:1003-1008(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GA2B ASN-128, CHARACTERIZATION
RP OF VARIANT GA2B ASN-128, AND FUNCTION.
RX PubMed=12815589; DOI=10.1002/humu.10226;
RA Olsen R.K.J., Andresen B.S., Christensen E., Bross P., Skovby F.,
RA Gregersen N.;
RT "Clear relationship between ETF/ETFDH genotype and phenotype in patients
RT with multiple acyl-CoA dehydrogenation deficiency.";
RL Hum. Mutat. 22:12-23(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT MET-154.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP MET-154.
RC TISSUE=Brain, and Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-199, VARIANT GA2B GLN-164,
RP CHARACTERIZATION OF VARIANT GA2B GLN-164, AND FUNCTION.
RX PubMed=7912128; DOI=10.1093/hmg/3.3.429;
RA Colombo I., Finocchiaro G., Garavaglia B., Garbuglio N., Yamaguchi S.,
RA Frerman F., Berra B., Didonato S.;
RT "Mutations and polymorphisms of the gene encoding the beta-subunit of the
RT electron transfer flavoprotein in three patients with glutaric acidemia
RT type II.";
RL Hum. Mol. Genet. 3:429-435(1994).
RN [8]
RP REVIEW.
RX PubMed=17941859; DOI=10.1111/j.1742-4658.2007.06107.x;
RA Toogood H.S., Leys D., Scrutton N.S.;
RT "Dynamics driving function: new insights from electron transferring
RT flavoproteins and partner complexes.";
RL FEBS J. 274:5481-5504(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP SUBCELLULAR LOCATION, SUBUNIT, AND METHYLATION AT LYS-200 AND LYS-203.
RX PubMed=25023281; DOI=10.1074/jbc.m114.580464;
RA Rhein V.F., Carroll J., He J., Ding S., Fearnley I.M., Walker J.E.;
RT "Human METTL20 methylates lysine residues adjacent to the recognition loop
RT of the electron transfer flavoprotein in mitochondria.";
RL J. Biol. Chem. 289:24640-24651(2014).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND SER-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-200, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP FUNCTION, SUBUNIT, METHYLATION AT LYS-200 AND LYS-203, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND MUTAGENESIS OF 200-LYS--LYS-202; 200-LYS--LYS-203;
RP LYS-200 AND LYS-203.
RX PubMed=25416781; DOI=10.1074/jbc.m114.614115;
RA Malecki J., Ho A.Y., Moen A., Dahl H.A., Falnes P.O.;
RT "Human METTL20 is a mitochondrial lysine methyltransferase that targets the
RT beta subunit of electron transfer flavoprotein (ETFbeta) and modulates its
RT activity.";
RL J. Biol. Chem. 290:423-434(2015).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [15]
RP INTERACTION WITH ETFRF1, AND IDENTIFICATION IN A COMPLEX WITH ETFA AND
RP ETFRF1.
RX PubMed=27499296; DOI=10.1016/j.molcel.2016.06.033;
RA Floyd B.J., Wilkerson E.M., Veling M.T., Minogue C.E., Xia C., Beebe E.T.,
RA Wrobel R.L., Cho H., Kremer L.S., Alston C.L., Gromek K.A., Dolan B.K.,
RA Ulbrich A., Stefely J.A., Bohl S.L., Werner K.M., Jochem A.,
RA Westphall M.S., Rensvold J.W., Taylor R.W., Prokisch H., Kim J.J.,
RA Coon J.J., Pagliarini D.J.;
RT "Mitochondrial protein interaction mapping identifies regulators of
RT respiratory chain function.";
RL Mol. Cell 63:621-632(2016).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH ETFA AND AMP,
RP FUNCTION, AND SUBUNIT.
RX PubMed=8962055; DOI=10.1073/pnas.93.25.14355;
RA Roberts D.L., Frerman F.E., Kim J.-J.P.;
RT "Three-dimensional structure of human electron transfer flavoprotein to
RT 2.1-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:14355-14360(1996).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH AMP; ETFA AND ACADM,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF LEU-195.
RX PubMed=15159392; DOI=10.1074/jbc.m404884200;
RA Toogood H.S., van Thiel A., Basran J., Sutcliffe M.J., Scrutton N.S.,
RA Leys D.;
RT "Extensive domain motion and electron transfer in the human electron
RT transferring flavoprotein.medium chain acyl-CoA dehydrogenase complex.";
RL J. Biol. Chem. 279:32904-32912(2004).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF MUTANT ALA-165 IN COMPLEX WITH
RP AMP; ETFA AND ACADM, FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLU-165.
RX PubMed=15975918; DOI=10.1074/jbc.m505562200;
RA Toogood H.S., van Thiel A., Scrutton N.S., Leys D.;
RT "Stabilization of non-productive conformations underpins rapid electron
RT transfer to electron-transferring flavoprotein.";
RL J. Biol. Chem. 280:30361-30366(2005).
RN [19]
RP VARIANT MET-154.
RX PubMed=10356313; DOI=10.1006/mgme.1999.2856;
RA Bross P., Pedersen P., Winter V., Nyholm M., Johansen B.N., Olsen R.K.,
RA Corydon M.J., Andresen B.S., Eiberg H., Kolvraa S., Gregersen N.;
RT "A polymorphic variant in the human electron transfer flavoprotein alpha-
RT chain (alpha-T171) displays decreased thermal stability and is
RT overrepresented in very-long-chain acyl-CoA dehydrogenase-deficient
RT patients with mild childhood presentation.";
RL Mol. Genet. Metab. 67:138-147(1999).
CC -!- FUNCTION: Heterodimeric electron transfer flavoprotein that accepts
CC electrons from several mitochondrial dehydrogenases, including acyl-CoA
CC dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase
CC (PubMed:25416781, PubMed:15159392, PubMed:15975918). It transfers the
CC electrons to the main mitochondrial respiratory chain via ETF-
CC ubiquinone oxidoreductase (Probable). Required for normal mitochondrial
CC fatty acid oxidation and normal amino acid metabolism (PubMed:12815589,
CC PubMed:7912128). ETFB binds an AMP molecule that probably has a purely
CC structural role (PubMed:8962055, PubMed:15159392, PubMed:15975918).
CC {ECO:0000269|PubMed:12815589, ECO:0000269|PubMed:15159392,
CC ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:25416781,
CC ECO:0000269|PubMed:7912128, ECO:0000269|PubMed:8962055,
CC ECO:0000303|PubMed:17941859, ECO:0000305}.
CC -!- SUBUNIT: Heterodimer composed of ETFA and ETFB (PubMed:25023281,
CC PubMed:25416781, PubMed:8962055, PubMed:15159392, PubMed:15975918).
CC Identified in a complex that contains ETFA, ETFB and ETFRF1
CC (PubMed:27499296). Interacts with ACADM (PubMed:15159392,
CC PubMed:15975918). {ECO:0000269|PubMed:15159392,
CC ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:25023281,
CC ECO:0000269|PubMed:25416781, ECO:0000269|PubMed:27499296,
CC ECO:0000269|PubMed:8962055}.
CC -!- INTERACTION:
CC P38117; P13804: ETFA; NbExp=2; IntAct=EBI-1056543, EBI-1052886;
CC P38117; Q6IPR1: ETFRF1; NbExp=7; IntAct=EBI-1056543, EBI-12292149;
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000305|PubMed:25023281, ECO:0000305|PubMed:8504797}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P38117-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P38117-2; Sequence=VSP_017850;
CC -!- TISSUE SPECIFICITY: Abundant in liver, heart and skeletal muscle. A
CC weak expression is seen in the brain, placenta, lung, kidney and
CC pancreas. {ECO:0000269|PubMed:8504797}.
CC -!- DOMAIN: The recognition loop recognizes a hydrophobic patch at the
CC surface of interacting dehydrogenases and acts as a static anchor at
CC the interface. {ECO:0000269|PubMed:15159392}.
CC -!- PTM: Methylated. Trimethylation at Lys-200 and Lys-203 may negatively
CC regulate the activity in electron transfer from acyl-CoA
CC dehydrogenases. {ECO:0000269|PubMed:25023281,
CC ECO:0000269|PubMed:25416781}.
CC -!- DISEASE: Glutaric aciduria 2B (GA2B) [MIM:231680]: An autosomal
CC recessively inherited disorder of fatty acid, amino acid, and choline
CC metabolism. It is characterized by multiple acyl-CoA dehydrogenase
CC deficiencies resulting in large excretion not only of glutaric acid,
CC but also of lactic, ethylmalonic, butyric, isobutyric, 2-methyl-
CC butyric, and isovaleric acids. {ECO:0000269|PubMed:12815589,
CC ECO:0000269|PubMed:7912128}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the ETF beta-subunit/FixA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X71129; CAA50441.1; -; mRNA.
DR EMBL; AF436663; AAN03713.1; -; Genomic_DNA.
DR EMBL; AF436658; AAN03713.1; JOINED; Genomic_DNA.
DR EMBL; AF436659; AAN03713.1; JOINED; Genomic_DNA.
DR EMBL; AF436660; AAN03713.1; JOINED; Genomic_DNA.
DR EMBL; AF436661; AAN03713.1; JOINED; Genomic_DNA.
DR EMBL; AF436662; AAN03713.1; JOINED; Genomic_DNA.
DR EMBL; AF370381; AAQ15217.1; -; mRNA.
DR EMBL; CR456827; CAG33108.1; -; mRNA.
DR EMBL; AK055285; BAG51494.1; -; mRNA.
DR EMBL; AK291881; BAF84570.1; -; mRNA.
DR EMBL; BC093961; AAH93961.1; -; mRNA.
DR EMBL; BC093963; AAH93963.1; -; mRNA.
DR EMBL; X76067; CAB37832.1; -; Genomic_DNA.
DR CCDS; CCDS12828.1; -. [P38117-1]
DR CCDS; CCDS33085.1; -. [P38117-2]
DR PIR; S32482; S32482.
DR RefSeq; NP_001014763.1; NM_001014763.1. [P38117-2]
DR RefSeq; NP_001976.1; NM_001985.2. [P38117-1]
DR PDB; 1EFV; X-ray; 2.10 A; B=1-255.
DR PDB; 1T9G; X-ray; 2.90 A; S=1-255.
DR PDB; 2A1T; X-ray; 2.80 A; S=1-255.
DR PDB; 2A1U; X-ray; 2.11 A; B=1-255.
DR PDBsum; 1EFV; -.
DR PDBsum; 1T9G; -.
DR PDBsum; 2A1T; -.
DR PDBsum; 2A1U; -.
DR AlphaFoldDB; P38117; -.
DR SMR; P38117; -.
DR BioGRID; 108410; 139.
DR ComplexPortal; CPX-2731; Mitochondrial electron transfer flavoprotein complex.
DR DIP; DIP-6162N; -.
DR IntAct; P38117; 59.
DR MINT; P38117; -.
DR STRING; 9606.ENSP00000346173; -.
DR ChEMBL; CHEMBL4105744; -.
DR iPTMnet; P38117; -.
DR PhosphoSitePlus; P38117; -.
DR SwissPalm; P38117; -.
DR BioMuta; ETFB; -.
DR REPRODUCTION-2DPAGE; IPI00004902; -.
DR UCD-2DPAGE; P38117; -.
DR CPTAC; CPTAC-504; -.
DR CPTAC; CPTAC-505; -.
DR EPD; P38117; -.
DR jPOST; P38117; -.
DR MassIVE; P38117; -.
DR MaxQB; P38117; -.
DR PaxDb; P38117; -.
DR PeptideAtlas; P38117; -.
DR PRIDE; P38117; -.
DR ProteomicsDB; 55282; -. [P38117-1]
DR ProteomicsDB; 55283; -. [P38117-2]
DR TopDownProteomics; P38117-1; -. [P38117-1]
DR TopDownProteomics; P38117-2; -. [P38117-2]
DR Antibodypedia; 19013; 252 antibodies from 35 providers.
DR DNASU; 2109; -.
DR Ensembl; ENST00000309244.9; ENSP00000311930.3; ENSG00000105379.10. [P38117-1]
DR Ensembl; ENST00000354232.8; ENSP00000346173.3; ENSG00000105379.10. [P38117-2]
DR GeneID; 2109; -.
DR KEGG; hsa:2109; -.
DR MANE-Select; ENST00000309244.9; ENSP00000311930.3; NM_001985.3; NP_001976.1.
DR UCSC; uc002pwg.4; human. [P38117-1]
DR CTD; 2109; -.
DR DisGeNET; 2109; -.
DR GeneCards; ETFB; -.
DR GeneReviews; ETFB; -.
DR HGNC; HGNC:3482; ETFB.
DR HPA; ENSG00000105379; Tissue enhanced (liver).
DR MalaCards; ETFB; -.
DR MIM; 130410; gene.
DR MIM; 231680; phenotype.
DR neXtProt; NX_P38117; -.
DR OpenTargets; ENSG00000105379; -.
DR Orphanet; 394532; Multiple acyl-CoA dehydrogenase deficiency, mild type.
DR Orphanet; 394529; Multiple acyl-CoA dehydrogenase deficiency, severe neonatal type.
DR PharmGKB; PA27898; -.
DR VEuPathDB; HostDB:ENSG00000105379; -.
DR eggNOG; KOG3180; Eukaryota.
DR GeneTree; ENSGT00390000009936; -.
DR HOGENOM; CLU_060196_0_0_1; -.
DR InParanoid; P38117; -.
DR OMA; YNGGMVP; -.
DR OrthoDB; 1092876at2759; -.
DR PhylomeDB; P38117; -.
DR TreeFam; TF314039; -.
DR PathwayCommons; P38117; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-8876725; Protein methylation.
DR SignaLink; P38117; -.
DR BioGRID-ORCS; 2109; 206 hits in 1073 CRISPR screens.
DR ChiTaRS; ETFB; human.
DR EvolutionaryTrace; P38117; -.
DR GeneWiki; ETFB; -.
DR GenomeRNAi; 2109; -.
DR Pharos; P38117; Tchem.
DR PRO; PR:P38117; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P38117; protein.
DR Bgee; ENSG00000105379; Expressed in apex of heart and 203 other tissues.
DR ExpressionAtlas; P38117; baseline and differential.
DR Genevisible; P38117; HS.
DR GO; GO:0045251; C:electron transfer flavoprotein complex; IPI:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0009055; F:electron transfer activity; IDA:UniProtKB.
DR GO; GO:0009063; P:cellular amino acid catabolic process; IDA:ComplexPortal.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IDA:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:ComplexPortal.
DR CDD; cd01714; ETF_beta; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR000049; ET-Flavoprotein_bsu_CS.
DR InterPro; IPR014730; ETF_a/b_N.
DR InterPro; IPR012255; ETF_b.
DR InterPro; IPR033948; ETF_beta_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR21294; PTHR21294; 1.
DR Pfam; PF01012; ETF; 1.
DR PIRSF; PIRSF000090; Beta-ETF; 1.
DR SMART; SM00893; ETF; 1.
DR PROSITE; PS01065; ETF_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Disease variant;
KW Electron transport; Glutaricaciduria; Methylation; Mitochondrion;
KW Phosphoprotein; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..255
FT /note="Electron transfer flavoprotein subunit beta"
FT /id="PRO_0000167870"
FT REGION 183..205
FT /note="Recognition loop"
FT /evidence="ECO:0000269|PubMed:15159392,
FT ECO:0000269|PubMed:25023281"
FT BINDING 9
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:15159392,
FT ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8962055,
FT ECO:0007744|PDB:1EFV, ECO:0007744|PDB:1T9G,
FT ECO:0007744|PDB:2A1T"
FT BINDING 39..42
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:15159392,
FT ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8962055,
FT ECO:0007744|PDB:1EFV, ECO:0007744|PDB:1T9G,
FT ECO:0007744|PDB:2A1T"
FT BINDING 66
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:15159392,
FT ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8962055,
FT ECO:0007744|PDB:1EFV, ECO:0007744|PDB:1T9G,
FT ECO:0007744|PDB:2A1T"
FT BINDING 123..134
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:15159392,
FT ECO:0000269|PubMed:15975918, ECO:0000269|PubMed:8962055,
FT ECO:0007744|PDB:1EFV, ECO:0007744|PDB:1T9G,
FT ECO:0007744|PDB:2A1T"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 200
FT /note="N6,N6,N6-trimethyllysine; by ETFBKMT; alternate"
FT /evidence="ECO:0000269|PubMed:25023281,
FT ECO:0000269|PubMed:25416781"
FT MOD_RES 200
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCW4"
FT MOD_RES 200
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 203
FT /note="N6,N6,N6-trimethyllysine; by ETFBKMT"
FT /evidence="ECO:0000269|PubMed:25023281,
FT ECO:0000269|PubMed:25416781"
FT MOD_RES 210
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCW4"
FT MOD_RES 210
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCW4"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 238
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCW4"
FT MOD_RES 248
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCW4"
FT MOD_RES 248
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCW4"
FT VAR_SEQ 1..19
FT /note="MAELRVLVAVKRVIDYAVK -> MYLSLWVTINTVNLRNTLSGLRGAVTTVG
FT MIKSDVPGTQEWLDERRRQGDLPLPTNSNPVLSLELCDPGQGPAPFQAVVVLIQPGRGL
FT ALRPPPSCLFPPDPTPSPPAGQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15498874"
FT /id="VSP_017850"
FT VARIANT 128
FT /note="D -> N (in GA2B; decreased protein stability;
FT dbSNP:rs104894678)"
FT /evidence="ECO:0000269|PubMed:12815589"
FT /id="VAR_025804"
FT VARIANT 154
FT /note="T -> M (in dbSNP:rs1130426)"
FT /evidence="ECO:0000269|PubMed:10356313,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15498874"
FT /id="VAR_008548"
FT VARIANT 164
FT /note="R -> Q (in GA2B; reduced electron transfer activity;
FT dbSNP:rs104894677)"
FT /evidence="ECO:0000269|PubMed:7912128"
FT /id="VAR_002369"
FT MUTAGEN 165
FT /note="E->A,Q: Drastically increases interprotein electron
FT transfer rates."
FT /evidence="ECO:0000269|PubMed:15975918"
FT MUTAGEN 195
FT /note="L->A: Severely impaired in complex formation with
FT ACADM."
FT /evidence="ECO:0000269|PubMed:15159392"
FT MUTAGEN 200..203
FT /note="KAKK->RAKR: Does not abolish electron transfer
FT activity. Abolishes sensitivity to inhibition by lysine
FT methyltransferase ETFBKMT."
FT /evidence="ECO:0000269|PubMed:25416781"
FT MUTAGEN 200..202
FT /note="KAK->RAR: Does not abolish methylation by ETFBKMT."
FT /evidence="ECO:0000269|PubMed:25416781"
FT MUTAGEN 200
FT /note="K->R: Does not abolish electron transfer activity.
FT Decreases sensitivity to inhibition by lysine
FT methyltransferase ETFBKMT."
FT /evidence="ECO:0000269|PubMed:25416781"
FT MUTAGEN 203
FT /note="K->R: Does not abolish electron transfer activity.
FT Decreases sensitivity to inhibition by lysine
FT methyltransferase ETFBKMT."
FT /evidence="ECO:0000269|PubMed:25416781"
FT CONFLICT 198
FT /note="I -> S (in Ref. 7; CAB37832)"
FT /evidence="ECO:0000305"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1EFV"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1EFV"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:1T9G"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1EFV"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1EFV"
FT HELIX 40..54
FT /evidence="ECO:0007829|PDB:1EFV"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:1EFV"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:1EFV"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1EFV"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:1EFV"
FT HELIX 101..115
FT /evidence="ECO:0007829|PDB:1EFV"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1EFV"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:1EFV"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:1EFV"
FT STRAND 146..156
FT /evidence="ECO:0007829|PDB:1EFV"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:1EFV"
FT STRAND 169..183
FT /evidence="ECO:0007829|PDB:1EFV"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:1EFV"
FT HELIX 195..200
FT /evidence="ECO:0007829|PDB:1EFV"
FT TURN 201..203
FT /evidence="ECO:0007829|PDB:1EFV"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:1EFV"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:1EFV"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:1EFV"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:1EFV"
SQ SEQUENCE 255 AA; 27844 MW; 47E6EAEF50EB2C80 CRC64;
MAELRVLVAV KRVIDYAVKI RVKPDRTGVV TDGVKHSMNP FCEIAVEEAV RLKEKKLVKE
VIAVSCGPAQ CQETIRTALA MGADRGIHVE VPPAEAERLG PLQVARVLAK LAEKEKVDLV
LLGKQAIDDD CNQTGQMTAG FLDWPQGTFA SQVTLEGDKL KVEREIDGGL ETLRLKLPAV
VTADLRLNEP RYATLPNIMK AKKKKIEVIK PGDLGVDLTS KLSVISVEDP PQRTAGVKVE
TTEDLVAKLK EIGRI
