ATP5H_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATP5H_MOUSE
• UniProt AC: Q9DCX2
• Protein Name: ATP synthase subunit d, mitochondrial
• Gene Name: Atp5h
• Organism: Mus musculus (Mouse).
• Sequence Length: 161
• 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 and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements..
• Protein Sequence: MAGRKLALKTIDWVSFVEVMPQNQKAIGNALKSWNETFHARLASLSEKPPAIDWAYYRANVAKPGLVDDFEKKYNALKIPVPEDKYTALVDQEEKEDVKSCAEFVSGSQLRIQEYEKQLEKMRNIIPFDQMTIDDLNEIFPETKLDKKKYPYWPHQPIENL

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	------MAGRKLALK ------CCCCHHHHH	26.88	-
9	Acetylation	AGRKLALKTIDWVSF CCCHHHHHHCCEEEE	37.52	23954790
15	Phosphorylation	LKTIDWVSFVEVMPQ HHHCCEEEEEEECCC	21.22	29899451
25	Acetylation	EVMPQNQKAIGNALK EECCCCHHHHHHHHH	49.90	23954790
25	Succinylation	EVMPQNQKAIGNALK EECCCCHHHHHHHHH	49.90	26388266
32	Acetylation	KAIGNALKSWNETFH HHHHHHHHHHHHHHH	51.52	23864654
32	Ubiquitination	KAIGNALKSWNETFH HHHHHHHHHHHHHHH	51.52	-
32	Succinylation	KAIGNALKSWNETFH HHHHHHHHHHHHHHH	51.52	23806337
44	Phosphorylation	TFHARLASLSEKPPA HHHHHHHHHCCCCCC	36.70	23737553
48	Acetylation	RLASLSEKPPAIDWA HHHHHCCCCCCCCHH	53.58	23864654
48	Ubiquitination	RLASLSEKPPAIDWA HHHHHCCCCCCCCHH	53.58	27667366
48	Succinylation	RLASLSEKPPAIDWA HHHHHCCCCCCCCHH	53.58	26388266
56	Phosphorylation	PPAIDWAYYRANVAK CCCCCHHHHHCCCCC	6.82	26032504
57	Phosphorylation	PAIDWAYYRANVAKP CCCCHHHHHCCCCCC	8.76	25195567
63	Acetylation	YYRANVAKPGLVDDF HHHCCCCCCCCCHHH	35.02	23864654
63	Ubiquitination	YYRANVAKPGLVDDF HHHCCCCCCCCCHHH	35.02	-
63	Succinylation	YYRANVAKPGLVDDF HHHCCCCCCCCCHHH	35.02	26388266
72	Malonylation	GLVDDFEKKYNALKI CCCHHHHHHHCCCCC	61.63	26320211
72	Acetylation	GLVDDFEKKYNALKI CCCHHHHHHHCCCCC	61.63	23864654
72	Succinylation	GLVDDFEKKYNALKI CCCHHHHHHHCCCCC	61.63	23806337
73	Succinylation	LVDDFEKKYNALKIP CCHHHHHHHCCCCCC	36.22	24315375
73	Acetylation	LVDDFEKKYNALKIP CCHHHHHHHCCCCCC	36.22	24062335
78	Malonylation	EKKYNALKIPVPEDK HHHHCCCCCCCCCHH	42.42	26320211
78	Ubiquitination	EKKYNALKIPVPEDK HHHHCCCCCCCCCHH	42.42	27667366
78	Succinylation	EKKYNALKIPVPEDK HHHHCCCCCCCCCHH	42.42	23806337
78	Acetylation	EKKYNALKIPVPEDK HHHHCCCCCCCCCHH	42.42	23864654
78	Glutarylation	EKKYNALKIPVPEDK HHHHCCCCCCCCCHH	42.42	24703693
85	Ubiquitination	KIPVPEDKYTALVDQ CCCCCCHHHEEECCH	42.72	-
85	Succinylation	KIPVPEDKYTALVDQ CCCCCCHHHEEECCH	42.72	23806337
85	Acetylation	KIPVPEDKYTALVDQ CCCCCCHHHEEECCH	42.72	23864654
86	Phosphorylation	IPVPEDKYTALVDQE CCCCCHHHEEECCHH	15.01	25195567
95	Succinylation	ALVDQEEKEDVKSCA EECCHHHHHCHHHHH	59.47	23806337
95	Malonylation	ALVDQEEKEDVKSCA EECCHHHHHCHHHHH	59.47	26320211
95	Ubiquitination	ALVDQEEKEDVKSCA EECCHHHHHCHHHHH	59.47	-
95	Acetylation	ALVDQEEKEDVKSCA EECCHHHHHCHHHHH	59.47	23864654
99	Succinylation	QEEKEDVKSCAEFVS HHHHHCHHHHHHHHC	52.73	26388266
99	Acetylation	QEEKEDVKSCAEFVS HHHHHCHHHHHHHHC	52.73	23864654
100	Phosphorylation	EEKEDVKSCAEFVSG HHHHCHHHHHHHHCH	20.57	25521595
101	Glutathionylation	EKEDVKSCAEFVSGS HHHCHHHHHHHHCHH	3.31	24333276
101	S-nitrosylation	EKEDVKSCAEFVSGS HHHCHHHHHHHHCHH	3.31	24895380
101	S-palmitoylation	EKEDVKSCAEFVSGS HHHCHHHHHHHHCHH	3.31	28526873
101	S-nitrosocysteine	EKEDVKSCAEFVSGS HHHCHHHHHHHHCHH	3.31	-
106	Phosphorylation	KSCAEFVSGSQLRIQ HHHHHHHCHHHHHHH	37.74	28464351
117	Malonylation	LRIQEYEKQLEKMRN HHHHHHHHHHHHHHC	60.32	26320211
117	Acetylation	LRIQEYEKQLEKMRN HHHHHHHHHHHHHHC	60.32	23864654
117	Ubiquitination	LRIQEYEKQLEKMRN HHHHHHHHHHHHHHC	60.32	-
121	Acetylation	EYEKQLEKMRNIIPF HHHHHHHHHHCCCCC	52.32	23864654
132	Phosphorylation	IIPFDQMTIDDLNEI CCCCCCCCHHHHHHH	18.67	23140645
144	Succinylation	NEIFPETKLDKKKYP HHHCCCCCCCCCCCC	53.69	23806337
144	Acetylation	NEIFPETKLDKKKYP HHHCCCCCCCCCCCC	53.69	24062335
147	Acetylation	FPETKLDKKKYPYWP CCCCCCCCCCCCCCC	62.70	24062335
147	Succinylation	FPETKLDKKKYPYWP CCCCCCCCCCCCCCC	62.70	26388266
148	Acetylation	PETKLDKKKYPYWPH CCCCCCCCCCCCCCC	58.15	2392013
148	Succinylation	PETKLDKKKYPYWPH CCCCCCCCCCCCCCC	58.15	24315375
149	Acetylation	ETKLDKKKYPYWPHQ CCCCCCCCCCCCCCC	58.14	24062335
149	Succinylation	ETKLDKKKYPYWPHQ CCCCCCCCCCCCCCC	58.14	23806337
149	Malonylation	ETKLDKKKYPYWPHQ CCCCCCCCCCCCCCC	58.14	26320211
150	Phosphorylation	TKLDKKKYPYWPHQP CCCCCCCCCCCCCCC	15.50	-
152	Phosphorylation	LDKKKYPYWPHQPIE CCCCCCCCCCCCCCC	28.60	25195567

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

Oops, there are no upstream regulatory protein records of ATP5H_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATP5H_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 ATP5H_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ATP5H_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-63; LYS-78; LYS-85; LYS-99;LYS-117 AND LYS-149, AND MASS SPECTROMETRY.
PubMed: 16916647