ATP8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATP8_HUMAN
• UniProt AC: P03928
• Protein Name: ATP synthase protein 8
• Gene Name: MT-ATP8
• Organism: Homo sapiens (Human).
• Sequence Length: 68
• Subcellular Localization: Mitochondrion membrane; Single-pass membrane protein.
• 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(0) domain. Minor subunit located with subunit a in the membrane (By similarity)..
• Protein Sequence: MPQLNTTVWPTMITPMLLTLFLITQLKMLNTNYHLPPSPKPMKMKNYNKPWEPKWTKICSLHSLPPQS

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
31	Phosphorylation	TQLKMLNTNYHLPPS HHHHHHCCCCCCCCC	32.94	28122231
33	Phosphorylation	LKMLNTNYHLPPSPK HHHHCCCCCCCCCCC	11.60	28122231
38	Phosphorylation	TNYHLPPSPKPMKMK CCCCCCCCCCCCCCC	43.55	25159151
40	Ubiquitination	YHLPPSPKPMKMKNY CCCCCCCCCCCCCCC	63.18	21890473
40	Acetylation	YHLPPSPKPMKMKNY CCCCCCCCCCCCCCC	63.18	26210075
47	Phosphorylation	KPMKMKNYNKPWEPK CCCCCCCCCCCCCCC	21.03	28152594
49	Acetylation	MKMKNYNKPWEPKWT CCCCCCCCCCCCCCC	40.94	23236377
49	Malonylation	MKMKNYNKPWEPKWT CCCCCCCCCCCCCCC	40.94	26320211
54	Acetylation	YNKPWEPKWTKICSL CCCCCCCCCCEECCC	56.85	23236377
54	Succinylation	YNKPWEPKWTKICSL CCCCCCCCCCEECCC	56.85	-
54	Ubiquitination	YNKPWEPKWTKICSL CCCCCCCCCCEECCC	56.85	21890473
54	Succinylation	YNKPWEPKWTKICSL CCCCCCCCCCEECCC	56.85	21890473
57	Acetylation	PWEPKWTKICSLHSL CCCCCCCEECCCCCC	40.37	-
57	Ubiquitination	PWEPKWTKICSLHSL CCCCCCCEECCCCCC	40.37	21890473

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

Oops, there are no upstream regulatory protein records of ATP8_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATP8_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 ATP8_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of ATP8_HUMAN !!

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 516070: Mitochondrial complex V deficiency, mitochondrial 2 (MC5DM2)
• 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-49, AND MASS SPECTROMETRY.
PubMed: 19608861