ETFA

Protein sy'n cael ei godio yn y corff dynol gan y genyn ETFA yw ETFA a elwir hefyd yn Electron transfer flavoprotein subunit alpha, mitochondrial ac Electron transfer flavoprotein alpha subunit (Saesneg). Segment o DNA yw'r genyn, sy'n amgodio ffwythiant arbennig. Mae'r genyn yma wedi ei leoli ar yr edefyn ôl o gromosom dynol 15, band 15q24.2-q24.3.

ETFA
Strwythurau PDB Human UniProt search: PDBe RCSB Rhestr o ddynodwyr PDB 1EFV, 1T9G, 2A1T, 2A1U
Dynodwyr
Cyfenwau	ETFA, EMA, GA2, MADD, electron transfer flavoprotein alpha subunit, electron transfer flavoprotein subunit alpha
Dynodwyr allanol	OMIM: 608053 HomoloGene: 100 GeneCards: ETFA
Patrwm RNA pattern Rhagor o gyfeiriadau
Ontoleg y genyn Gweithrediad moleciwlaidd • electron transfer activity • oxidoreductase activity • flavin adenine dinucleotide binding • GO:0001948, GO:0016582 protein binding Cydrannau o'r gell • mitochondrial matrix • extracellular exosome • mitocondria Prosesau biolegol • respiratory electron transport chain • fatty acid beta-oxidation using acyl-CoA dehydrogenase • electron transport chain Sources:Amigo / QuickGO
Orthologau
Species	Bod dynol	Llygoden
Entrez	2108	n/a
Ensembl	ENSG00000140374	n/a
UniProt	P13804	n/a
RefSeq (mRNA)	NM_000126 NM_001127716	n/a
RefSeq (protein)	NP_000117 NP_001121188	n/a
Lleoliad (UCSC)	n/a	n/a
PubMed search		n/a
Wicidata
Gweld/Golygu Bod dynol

Cyfystyron

Yn aml mae gan enynnau lawer o gyfystyron. Mae hyn oherwydd eu bod yn aml yn cael eu darganfod gan nifer o bobl mewn cyd-destunau gwahanol heb wybod mai'r un genynnau oeddyn nhw. Hefyd mae gan wahanol gymunedau gwyddonol safonau gwahanol ar gyfer enwi genynnau. Dyma restr o gyfystyron ar gyfer y genyn ETFA.

• EMA
• GA2
• MADD

Llyfryddiaeth

• "Exploring the effects of tert-butylhydroperoxide induced liver injury using proteomic approach. ". Toxicology. 2014. PMID 24394546.
• "Electron transfer flavoprotein domain II orientation monitored using double electron-electron resonance between an enzymatically reduced, native FAD cofactor, and spin labels. ". Protein Sci. 2011. PMID 21308847.
• "A polymorphic position in electron transfer flavoprotein modulates kinetic stability as evidenced by thermal stress. ". FEBS Lett. 2011. PMID 21219902.
• "Transient multiple acyl-CoA dehydrogenation deficiency in a newborn female caused by maternal riboflavin deficiency. ". Mol Genet Metab. 2007. PMID 17689999.
• "Electron transfer and conformational change in complexes of trimethylamine dehydrogenase and electron transferring flavoprotein.". J Biol Chem. 2002. PMID 11756429.