dbPTM

ETHE1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ETHE1_HUMAN
UniProt AC	O95571
Protein Name	Persulfide dioxygenase ETHE1, mitochondrial
Gene Name	ETHE1
Organism	Homo sapiens (Human).
Sequence Length	254
Subcellular Localization	Cytoplasm . Nucleus . Mitochondrion matrix .
Protein 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]
Protein Sequence	MAEAVLRVARRQLSQRGGSGAPILLRQMFEPVSCTFTYLLGDRESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYHSVHEKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIDFAVPANMRCGVQTPTA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	RVARRQLSQRGGSGA HHHHHHHHHCCCCCC	14.97	28464451
19	Phosphorylation	QLSQRGGSGAPILLR HHHHCCCCCCCCHHH	34.31	30266825
38	Phosphorylation	PVSCTFTYLLGDRES CEEEEEEEEECCHHH	8.85	24719451
66	Ubiquitination	PRDAQLIKELGLRLL CCHHHHHHHHHHHHH	56.32	21890473
66	Acetylation	PRDAQLIKELGLRLL CCHHHHHHHHHHHHH	56.32	19608861
66	2-Hydroxyisobutyrylation	PRDAQLIKELGLRLL CCHHHHHHHHHHHHH	56.32	-
66	Succinylation	PRDAQLIKELGLRLL CCHHHHHHHHHHHHH	56.32	23954790
74	Phosphorylation	ELGLRLLYAVNTHCH HHHHHHHHHHHCCCC	17.07	-
170	S-nitrosylation	RTDFQQGCAKTLYHS CCHHHHHHHHHHHHH	2.81	2212679
172	Acetylation	DFQQGCAKTLYHSVH HHHHHHHHHHHHHHH	43.04	23954790
172	Succinylation	DFQQGCAKTLYHSVH HHHHHHHHHHHHHHH	43.04	-
172	Malonylation	DFQQGCAKTLYHSVH HHHHHHHHHHHHHHH	43.04	26320211
172	Succinylation	DFQQGCAKTLYHSVH HHHHHHHHHHHHHHH	43.04	23954790
173	Phosphorylation	FQQGCAKTLYHSVHE HHHHHHHHHHHHHHH	17.64	28152594
175	Phosphorylation	QGCAKTLYHSVHEKI HHHHHHHHHHHHHHH	9.40	28152594
177	Phosphorylation	CAKTLYHSVHEKIFT HHHHHHHHHHHHHHC	16.18	28152594
218	Phosphorylation	LNPRLTLSCEEFVKI CCCCCEEEHHHHHHH	17.78	27251275
245	Sulfoxidation	DFAVPANMRCGVQTP EEECCCCCCCCCCCC	3.99	21406390

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of ETHE1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ETHE1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of ETHE1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IGS21_HUMAN	IGSF21	physical	16169070
LRIF1_HUMAN	LRIF1	physical	16169070
TF65_HUMAN	RELA	physical	12398897
P53_HUMAN	TP53	physical	17353187
HDAC1_HUMAN	HDAC1	physical	17353187
A4_HUMAN	APP	physical	21832049
IDHC_HUMAN	IDH1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
602473	Ethylmalonic encephalopathy (EE)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ETHE1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66 AND LYS-172, AND MASSSPECTROMETRY.	19608861 [Abstract]