dbPTM

ATPO_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATPO_HUMAN
UniProt AC	P48047
Protein Name	ATP synthase subunit O, mitochondrial
Gene Name	ATP5O
Organism	Homo sapiens (Human).
Sequence Length	213
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	MAAPAVSGLSRQVRCFSTSVVRPFAKLVRPPVQVYGIEGRYATALYSAASKQNKLEQVEKELLRVAQILKEPKVAASVLNPYVKRSIKVKSLNDITAKERFSPLTTNLINLLAENGRLSNTQGVVSAFSTMMSVHRGEVPCTVTSASPLEEATLSELKTVLKSFLSQGQVLKLEAKTDPSILGGMIVRIGEKYVDMSVKTKIQKLGRAMREIV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MAAPAVSGLSRQVR -CCCCCCCCCCCCHH	35.80	23532336
10	Phosphorylation	APAVSGLSRQVRCFS CCCCCCCCCCHHHCC	24.96	25367160
29	Methylation	RPFAKLVRPPVQVYG HCHHHHHCCCEEEEE	40.00	-
35	Phosphorylation	VRPPVQVYGIEGRYA HCCCEEEEEECHHHH	8.69	28152594
41	Phosphorylation	VYGIEGRYATALYSA EEEECHHHHHHHHHH	21.11	28152594
43	Phosphorylation	GIEGRYATALYSAAS EECHHHHHHHHHHHH	14.30	24850871
46	Phosphorylation	GRYATALYSAASKQN HHHHHHHHHHHHHCC	8.19	28152594
47	Phosphorylation	RYATALYSAASKQNK HHHHHHHHHHHHCCH	20.43	28152594
50	Phosphorylation	TALYSAASKQNKLEQ HHHHHHHHHCCHHHH	34.19	28152594
51	Ubiquitination	ALYSAASKQNKLEQV HHHHHHHHCCHHHHH	53.84	22817900
51	2-Hydroxyisobutyrylation	ALYSAASKQNKLEQV HHHHHHHHCCHHHHH	53.84	-
54	Malonylation	SAASKQNKLEQVEKE HHHHHCCHHHHHHHH	51.40	26320211
54	2-Hydroxyisobutyrylation	SAASKQNKLEQVEKE HHHHHCCHHHHHHHH	51.40	-
54	Ubiquitination	SAASKQNKLEQVEKE HHHHHCCHHHHHHHH	51.40	23000965
54	Acetylation	SAASKQNKLEQVEKE HHHHHCCHHHHHHHH	51.40	23954790
60	Ubiquitination	NKLEQVEKELLRVAQ CHHHHHHHHHHHHHH	55.60	23000965
60	Acetylation	NKLEQVEKELLRVAQ CHHHHHHHHHHHHHH	55.60	25825284
60	2-Hydroxyisobutyrylation	NKLEQVEKELLRVAQ CHHHHHHHHHHHHHH	55.60	-
60	Malonylation	NKLEQVEKELLRVAQ CHHHHHHHHHHHHHH	55.60	26320211
64	Methylation	QVEKELLRVAQILKE HHHHHHHHHHHHHCC	34.06	-
70	2-Hydroxyisobutyrylation	LRVAQILKEPKVAAS HHHHHHHCCCCHHHH	73.86	-
70	Malonylation	LRVAQILKEPKVAAS HHHHHHHCCCCHHHH	73.86	26320211
70	Acetylation	LRVAQILKEPKVAAS HHHHHHHCCCCHHHH	73.86	23954790
70	Ubiquitination	LRVAQILKEPKVAAS HHHHHHHCCCCHHHH	73.86	21890473
73	Acetylation	AQILKEPKVAASVLN HHHHCCCCHHHHHCC	45.67	-
73	Malonylation	AQILKEPKVAASVLN HHHHCCCCHHHHHCC	45.67	26320211
73	2-Hydroxyisobutyrylation	AQILKEPKVAASVLN HHHHCCCCHHHHHCC	45.67	-
73	Ubiquitination	AQILKEPKVAASVLN HHHHCCCCHHHHHCC	45.67	23000965
77	Phosphorylation	KEPKVAASVLNPYVK CCCCHHHHHCCHHHH	19.87	28152594
82	Phosphorylation	AASVLNPYVKRSIKV HHHHCCHHHHHHCEE	19.96	28152594
84	Acetylation	SVLNPYVKRSIKVKS HHCCHHHHHHCEECC	34.29	25953088
84	2-Hydroxyisobutyrylation	SVLNPYVKRSIKVKS HHCCHHHHHHCEECC	34.29	-
84	Ubiquitination	SVLNPYVKRSIKVKS HHCCHHHHHHCEECC	34.29	22817900
84	Malonylation	SVLNPYVKRSIKVKS HHCCHHHHHHCEECC	34.29	26320211
86	Phosphorylation	LNPYVKRSIKVKSLN CCHHHHHHCEECCHH	22.50	20068231
88	Ubiquitination	PYVKRSIKVKSLNDI HHHHHHCEECCHHCC	44.87	21906983
90	Malonylation	VKRSIKVKSLNDITA HHHHCEECCHHCCCC	44.20	26320211
90	Acetylation	VKRSIKVKSLNDITA HHHHCEECCHHCCCC	44.20	27452117
90	Succinylation	VKRSIKVKSLNDITA HHHHCEECCHHCCCC	44.20	-
90	2-Hydroxyisobutyrylation	VKRSIKVKSLNDITA HHHHCEECCHHCCCC	44.20	-
90	Ubiquitination	VKRSIKVKSLNDITA HHHHCEECCHHCCCC	44.20	22817900
90	Succinylation	VKRSIKVKSLNDITA HHHHCEECCHHCCCC	44.20	-
91	Phosphorylation	KRSIKVKSLNDITAK HHHCEECCHHCCCCH	35.08	20068231
96	Phosphorylation	VKSLNDITAKERFSP ECCHHCCCCHHHCCH	34.24	21406692
98	Ubiquitination	SLNDITAKERFSPLT CHHCCCCHHHCCHHH	40.55	22817900
98	Acetylation	SLNDITAKERFSPLT CHHCCCCHHHCCHHH	40.55	25953088
98	Malonylation	SLNDITAKERFSPLT CHHCCCCHHHCCHHH	40.55	26320211
141	Glutathionylation	VHRGEVPCTVTSASP CCCCCCCCEEECCCH	6.04	22555962
153	Phosphorylation	ASPLEEATLSELKTV CCHHHHHCHHHHHHH	33.81	24641631
155	Phosphorylation	PLEEATLSELKTVLK HHHHHCHHHHHHHHH	36.21	21712546
158	Succinylation	EATLSELKTVLKSFL HHCHHHHHHHHHHHH	32.32	21890473
158	Acetylation	EATLSELKTVLKSFL HHCHHHHHHHHHHHH	32.32	23954790
158	Succinylation	EATLSELKTVLKSFL HHCHHHHHHHHHHHH	32.32	-
158	Ubiquitination	EATLSELKTVLKSFL HHCHHHHHHHHHHHH	32.32	23000965
162	Succinylation	SELKTVLKSFLSQGQ HHHHHHHHHHHHCCC	34.52	27452117
162	Acetylation	SELKTVLKSFLSQGQ HHHHHHHHHHHHCCC	34.52	19608861
162	Succinylation	SELKTVLKSFLSQGQ HHHHHHHHHHHHCCC	34.52	-
162	Ubiquitination	SELKTVLKSFLSQGQ HHHHHHHHHHHHCCC	34.52	23000965
162	2-Hydroxyisobutyrylation	SELKTVLKSFLSQGQ HHHHHHHHHHHHCCC	34.52	-
163	Phosphorylation	ELKTVLKSFLSQGQV HHHHHHHHHHHCCCE	27.53	21406692
166	Phosphorylation	TVLKSFLSQGQVLKL HHHHHHHHCCCEEEE	30.19	21406692
172	Acetylation	LSQGQVLKLEAKTDP HHCCCEEEEEECCCH	45.48	19608861
172	Ubiquitination	LSQGQVLKLEAKTDP HHCCCEEEEEECCCH	45.48	22817900
172	2-Hydroxyisobutyrylation	LSQGQVLKLEAKTDP HHCCCEEEEEECCCH	45.48	-
172	Malonylation	LSQGQVLKLEAKTDP HHCCCEEEEEECCCH	45.48	26320211
176	Acetylation	QVLKLEAKTDPSILG CEEEEEECCCHHHHH	44.05	25038526
176	Ubiquitination	QVLKLEAKTDPSILG CEEEEEECCCHHHHH	44.05	22817900
176	Malonylation	QVLKLEAKTDPSILG CEEEEEECCCHHHHH	44.05	26320211
177	Phosphorylation	VLKLEAKTDPSILGG EEEEEECCCHHHHHH	61.26	21406692
180	Phosphorylation	LEAKTDPSILGGMIV EEECCCHHHHHHEEE	33.00	21406692
185	Sulfoxidation	DPSILGGMIVRIGEK CHHHHHHEEEEECCC	2.13	21406390
192	Ubiquitination	MIVRIGEKYVDMSVK EEEEECCCCCCCCHH	45.41	22817900
192	Malonylation	MIVRIGEKYVDMSVK EEEEECCCCCCCCHH	45.41	26320211
192	2-Hydroxyisobutyrylation	MIVRIGEKYVDMSVK EEEEECCCCCCCCHH	45.41	-
192	Acetylation	MIVRIGEKYVDMSVK EEEEECCCCCCCCHH	45.41	19608861
193	Phosphorylation	IVRIGEKYVDMSVKT EEEECCCCCCCCHHH	9.44	25367160
197	Phosphorylation	GEKYVDMSVKTKIQK CCCCCCCCHHHHHHH	18.92	24719451
199	Malonylation	KYVDMSVKTKIQKLG CCCCCCHHHHHHHHH	36.47	26320211
199	2-Hydroxyisobutyrylation	KYVDMSVKTKIQKLG CCCCCCHHHHHHHHH	36.47	-
199	Ubiquitination	KYVDMSVKTKIQKLG CCCCCCHHHHHHHHH	36.47	21890473
199	Succinylation	KYVDMSVKTKIQKLG CCCCCCHHHHHHHHH	36.47	-
199	Succinylation	KYVDMSVKTKIQKLG CCCCCCHHHHHHHHH	36.47	-
199	Acetylation	KYVDMSVKTKIQKLG CCCCCCHHHHHHHHH	36.47	25953088
200	Phosphorylation	YVDMSVKTKIQKLGR CCCCCHHHHHHHHHH	31.09	22461510
201	Ubiquitination	VDMSVKTKIQKLGRA CCCCHHHHHHHHHHH	37.10	22817900
204	Ubiquitination	SVKTKIQKLGRAMRE CHHHHHHHHHHHHHH	57.28	22817900

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 ATPO_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
162	K	Acetylation		19608861
Acetylation at Lys-162 decreases ATP production.

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 ATPO_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NDUS4_HUMAN	NDUFS4	physical	22939629
NDUB9_HUMAN	NDUFB9	physical	22939629
QCR2_HUMAN	UQCRC2	physical	22939629
RS10_HUMAN	RPS10	physical	22939629
K1C13_HUMAN	KRT13	physical	25416956
K1C15_HUMAN	KRT15	physical	25416956
TRIP6_HUMAN	TRIP6	physical	25416956
ZBT14_HUMAN	ZBTB14	physical	25416956
PNMA1_HUMAN	PNMA1	physical	25416956
NDC80_HUMAN	NDC80	physical	25416956
5NTC_HUMAN	NT5C2	physical	25416956
TFP11_HUMAN	TFIP11	physical	25416956
CC136_HUMAN	CCDC136	physical	25416956
HMBX1_HUMAN	HMBOX1	physical	25416956
CEP70_HUMAN	CEP70	physical	25416956
USBP1_HUMAN	USHBP1	physical	25416956
MIPO1_HUMAN	MIPOL1	physical	25416956
ANXA7_HUMAN	ANXA7	physical	26344197
ATPA_HUMAN	ATP5A1	physical	26344197
ATPD_HUMAN	ATP5D	physical	26344197
AT5F1_HUMAN	ATP5F1	physical	26344197
ATP5I_HUMAN	ATP5I	physical	26344197
VPP1_HUMAN	ATP6V0A1	physical	26344197
COX41_HUMAN	COX4I1	physical	26344197
MTCH1_HUMAN	MTCH1	physical	26344197
MTCH2_HUMAN	MTCH2	physical	26344197
NDUA8_HUMAN	NDUFA8	physical	26344197
NDUS4_HUMAN	NDUFS4	physical	26344197
RER1_HUMAN	RER1	physical	26344197
SGPL1_HUMAN	SGPL1	physical	26344197
TSPO_HUMAN	TSPO	physical	26344197
PNMA1_HUMAN	PNMA1	physical	21516116
STOM_HUMAN	STOM	physical	27173435

Drug and Disease Associations

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

Regulatory Network of ATPO_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-54; LYS-60; LYS-70; LYS-162;LYS-172 AND LYS-192, AND MASS SPECTROMETRY.	19608861 [Abstract]

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