ATP5E_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATP5E_HUMAN
• UniProt AC: P56381
• Protein Name: ATP synthase subunit epsilon, mitochondrial {ECO:0000305}
• Gene Name: ATP5F1E {ECO:0000312|HGNC:HGNC:838}
• Organism: Homo sapiens (Human).
• Sequence Length: 51
• Subcellular Localization: Mitochondrion. Mitochondrion inner membrane.
• Protein Description: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity)..
• Protein Sequence: MVAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAEKTSGSNVKIVKVKKE

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	YWRQAGLSYIRYSQI HHHHCCCCHHHHHHH	20.00	28152594
12	Phosphorylation	WRQAGLSYIRYSQIC HHHCCCCHHHHHHHH	8.41	28152594
15	Phosphorylation	AGLSYIRYSQICAKA CCCCHHHHHHHHHHH	8.72	28152594
16	Phosphorylation	GLSYIRYSQICAKAV CCCHHHHHHHHHHHH	11.83	28152594
21	Succinylation	RYSQICAKAVRDALK HHHHHHHHHHHHHHH	42.90	-
21	Succinylation	RYSQICAKAVRDALK HHHHHHHHHHHHHHH	42.90	-
21	Malonylation	RYSQICAKAVRDALK HHHHHHHHHHHHHHH	42.90	26320211
21	Ubiquitination	RYSQICAKAVRDALK HHHHHHHHHHHHHHH	42.90	22817900
21	Acetylation	RYSQICAKAVRDALK HHHHHHHHHHHHHHH	42.90	19608861
28	Ubiquitination	KAVRDALKTEFKANA HHHHHHHHHHHHHHH	47.96	29967540
28	Acetylation	KAVRDALKTEFKANA HHHHHHHHHHHHHHH	47.96	25953088
28	Succinylation	KAVRDALKTEFKANA HHHHHHHHHHHHHHH	47.96	23954790
29	Phosphorylation	AVRDALKTEFKANAE HHHHHHHHHHHHHHH	47.72	20833797
32	Succinylation	DALKTEFKANAEKTS HHHHHHHHHHHHCCC	34.20	-
32	Acetylation	DALKTEFKANAEKTS HHHHHHHHHHHHCCC	34.20	25953088
32	Succinylation	DALKTEFKANAEKTS HHHHHHHHHHHHCCC	34.20	27452117
37	Succinylation	EFKANAEKTSGSNVK HHHHHHHCCCCCCCE	45.65	-
37	Acetylation	EFKANAEKTSGSNVK HHHHHHHCCCCCCCE	45.65	25953088
37	Succinylation	EFKANAEKTSGSNVK HHHHHHHCCCCCCCE	45.65	-
44	Acetylation	KTSGSNVKIVKVKKE CCCCCCCEEEEEECC	46.13	23749302
44	Ubiquitination	KTSGSNVKIVKVKKE CCCCCCCEEEEEECC	46.13	29967540
44	Succinylation	KTSGSNVKIVKVKKE CCCCCCCEEEEEECC	46.13	23954790

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

Oops, there are no upstream regulatory protein records of ATP5E_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATP5E_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ATP5E_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CP17A_HUMAN	CYP17A1	physical	21988832
ATPD_HUMAN	ATP5D	physical	26344197
ATP5I_HUMAN	ATP5I	physical	26344197
ATP5J_HUMAN	ATP5J	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 614053: Mitochondrial complex V deficiency, nuclear 3 (MC5DN3)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"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-21, AND MASS SPECTROMETRY.
PubMed: 19608861