CPLM-001622

Genbank Nucleotide ID

Persulfide dioxygenase ETHE1, mitochondrial

Protein Synonyms/Alias

Ethylmalonic encephalopathy protein 1; Hepatoma subtracted clone one protein; Sulfur dioxygenase ETHE1

Homo sapiens (Human)

Position	Peptide	Type	References
66	PRDAQLIKELGLRLL	acetylation	[1]
66	PRDAQLIKELGLRLL	ubiquitination	[2, 3, 4, 5]
172	DFQQGCAKTLYHSVH	acetylation	[1]

[1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]

Functional Description

Sulfur dioxygenase that plays an essential role in hydrogen sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide (H(2)S) is first oxidized by SQRDL, giving rise to cysteine persulfide residues. ETHE1 consumes molecular oxygen to catalyze the oxidation of the persulfide, once it has been transferred to a thiophilic acceptor, such as glutathione (R-SSH). Plays an important role in metabolic homeostasis in mitochondria by metabolizing hydrogen sulfide and preventing the accumulation of supraphysiological H(2)S levels that have toxic effects, due to the inhibition of cytochrome c oxidase. First described as a protein that can shuttle between the nucleus and the cytoplasm and suppress p53-induced apoptosis by sequestering the transcription factor RELA/NFKB3 in the cytoplasm and preventing its accumulation in the nucleus (PubMed:12398897).

METAL 79 79 Iron; catalytic (Probable).
METAL 135 135 Iron; catalytic (Probable).
METAL 154 154 Iron; catalytic (Probable).
MOD_RES 14 14 Phosphoserine (By similarity).
MOD_RES 66 66 N6-acetyllysine.

Acetylation; Complete proteome; Cytoplasm; Dioxygenase; Disease mutation; Metal-binding; Mitochondrion; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO:0005634; C:nucleus; IDA:HPA.
GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO:0005506; F:iron ion binding; IDA:UniProtKB.
GO:0050313; F:sulfur dioxygenase activity; IDA:UniProtKB.
GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
GO:0070813; P:hydrogen sulfide metabolic process; IDA:UniProtKB.
GO:0070221; P:sulfide oxidation, using sulfide:quinone oxidoreductase; TAS:Reactome.
GO:0000098; P:sulfur amino acid catabolic process; TAS:Reactome.

IPR001279; Beta-lactamas-like.

PF00753; Lactamase_B

SM00849; Lactamase_B