ATP5L_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATP5L_MOUSE
• UniProt AC: Q9CPQ8
• Protein Name: ATP synthase subunit g, mitochondrial
• Gene Name: Atp5l
• Organism: Mus musculus (Mouse).
• Sequence Length: 103
• 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(0) domain. Minor subunit located with subunit a in the membrane..
• Protein Sequence: MAKFIRNFAEKAPSMVAAAVTYSKPRLATFWHYAKVELVPPTPAEIPTAIQSVKKIIQSAKTGSFKHLTVKEAVLNGLVATEVWMWFYIGEIIGKRGIVGYDV

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
2	Acetylation	------MAKFIRNFA ------CHHHHHHHH	18.57	-
11	Acetylation	FIRNFAEKAPSMVAA HHHHHHHHCHHHHHH	63.27	23576753
11	Succinylation	FIRNFAEKAPSMVAA HHHHHHHHCHHHHHH	63.27	24315375
14	Phosphorylation	NFAEKAPSMVAAAVT HHHHHCHHHHHHHHH	30.65	-
23	O-linked_Glycosylation	VAAAVTYSKPRLATF HHHHHHCCCCCEEEH	27.15	55411085
24	Acetylation	AAAVTYSKPRLATFW HHHHHCCCCCEEEHH	24.60	23864654
24	Ubiquitination	AAAVTYSKPRLATFW HHHHHCCCCCEEEHH	24.60	-
24	Succinylation	AAAVTYSKPRLATFW HHHHHCCCCCEEEHH	24.60	23954790
33	Phosphorylation	RLATFWHYAKVELVP CEEEHHEEEEEEECC	9.94	25195567
35	Succinylation	ATFWHYAKVELVPPT EEHHEEEEEEECCCC	29.13	24315375
35	Acetylation	ATFWHYAKVELVPPT EEHHEEEEEEECCCC	29.13	23576753
42	Phosphorylation	KVELVPPTPAEIPTA EEEECCCCCCCCCHH	29.12	-
54	Succinylation	PTAIQSVKKIIQSAK CHHHHHHHHHHHHCC	43.43	23806337
54	Ubiquitination	PTAIQSVKKIIQSAK CHHHHHHHHHHHHCC	43.43	-
54	Acetylation	PTAIQSVKKIIQSAK CHHHHHHHHHHHHCC	43.43	23576753
55	Succinylation	TAIQSVKKIIQSAKT HHHHHHHHHHHHCCC	42.77	26388266
55	Acetylation	TAIQSVKKIIQSAKT HHHHHHHHHHHHCCC	42.77	24062335
55	Malonylation	TAIQSVKKIIQSAKT HHHHHHHHHHHHCCC	42.77	26320211
61	Succinylation	KKIIQSAKTGSFKHL HHHHHHCCCCCCCCE	59.68	23806337
61	Ubiquitination	KKIIQSAKTGSFKHL HHHHHHCCCCCCCCE	59.68	27667366
61	Malonylation	KKIIQSAKTGSFKHL HHHHHHCCCCCCCCE	59.68	26320211
61	Acetylation	KKIIQSAKTGSFKHL HHHHHHCCCCCCCCE	59.68	23806337
66	Acetylation	SAKTGSFKHLTVKEA HCCCCCCCCEEHHHH	39.13	23864654
66	Succinylation	SAKTGSFKHLTVKEA HCCCCCCCCEEHHHH	39.13	23806337

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

Oops, there are no upstream regulatory protein records of ATP5L_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATP5L_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of ATP5L_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ATP5L_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54 AND LYS-66, AND MASSSPECTROMETRY.
PubMed: 16916647