dbPTM

ATPG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATPG_HUMAN
UniProt AC	P36542
Protein Name	ATP synthase subunit gamma, mitochondrial {ECO:0000305}
Gene Name	ATP5F1C {ECO:0000312\|HGNC:HGNC:833}
Organism	Homo sapiens (Human).
Sequence Length	298
Subcellular Localization	Mitochondrion inner membrane Peripheral membrane protein Matrix side .
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 the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). 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..
Protein Sequence	MFSRAGVAGLSAWTLQPQWIQVRNMATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARIYGLGSLALYEKADIKGPEDKKKHLLIGVSSDRGLCGAIHSSIAKQMKSEVATLTAAGKEVMLVGIGDKIRGILYRTHSDQFLVAFKEVGRKPPTFGDASVIALELLNSGYEFDEGSIIFNKFRSVISYKTEEKPIFSLNTVASADSMSIYDDIDADVLQNYQEYNLANIIYYSLKESTTSEQSARMTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEIISGAAALD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
32	Phosphorylation	MATLKDITRRLKSIK HHHHHHHHHHHHHHH	21.63	26074081
33	Methylation	ATLKDITRRLKSIKN HHHHHHHHHHHHHHC	42.12	-
37	Phosphorylation	DITRRLKSIKNIQKI HHHHHHHHHHCHHHH	43.30	26074081
39	2-Hydroxyisobutyrylation	TRRLKSIKNIQKITK HHHHHHHHCHHHHHH	55.90	-
39	Acetylation	TRRLKSIKNIQKITK HHHHHHHHCHHHHHH	55.90	25953088
39	Ubiquitination	TRRLKSIKNIQKITK HHHHHHHHCHHHHHH	55.90	-
39	Succinylation	TRRLKSIKNIQKITK HHHHHHHHCHHHHHH	55.90	27452117
43	Ubiquitination	KSIKNIQKITKSMKM HHHHCHHHHHHHHHH	48.85	-
43	Acetylation	KSIKNIQKITKSMKM HHHHCHHHHHHHHHH	48.85	25953088
45 (in isoform 2)	Phosphorylation	-	24.89	-
45	Phosphorylation	IKNIQKITKSMKMVA HHCHHHHHHHHHHHH	24.89	20068231
47	Phosphorylation	NIQKITKSMKMVAAA CHHHHHHHHHHHHHH	18.26	26074081
49	Ubiquitination	QKITKSMKMVAAAKY HHHHHHHHHHHHHHH	37.00	21890473
49 (in isoform 1)	Ubiquitination	-	37.00	21890473
49 (in isoform 2)	Ubiquitination	-	37.00	21890473
49	Succinylation	QKITKSMKMVAAAKY HHHHHHHHHHHHHHH	37.00	27452117
49	Succinylation	QKITKSMKMVAAAKY HHHHHHHHHHHHHHH	37.00	-
49	Ubiquitination	QKITKSMKMVAAAKY HHHHHHHHHHHHHHH	37.00	21890473
49	2-Hydroxyisobutyrylation	QKITKSMKMVAAAKY HHHHHHHHHHHHHHH	37.00	-
55 (in isoform 2)	Ubiquitination	-	34.41	21890473
55	Ubiquitination	MKMVAAAKYARAERE HHHHHHHHHHHHHHH	34.41	21890473
55 (in isoform 2)	Acetylation	-	34.41	-
55	Acetylation	MKMVAAAKYARAERE HHHHHHHHHHHHHHH	34.41	19608861
55	2-Hydroxyisobutyrylation	MKMVAAAKYARAERE HHHHHHHHHHHHHHH	34.41	-
55	Ubiquitination	MKMVAAAKYARAERE HHHHHHHHHHHHHHH	34.41	21890473
55 (in isoform 1)	Ubiquitination	-	34.41	21890473
64	Succinylation	ARAERELKPARIYGL HHHHHHCCCCEEECC	31.70	23954790
69	Phosphorylation	ELKPARIYGLGSLAL HCCCCEEECCHHHHH	10.76	28152594
73	Phosphorylation	ARIYGLGSLALYEKA CEEECCHHHHHHHCC	18.60	28857561
77	Phosphorylation	GLGSLALYEKADIKG CCHHHHHHHCCCCCC	15.13	28152594
79	Acetylation	GSLALYEKADIKGPE HHHHHHHCCCCCCCH	37.49	25953088
83	Acetylation	LYEKADIKGPEDKKK HHHCCCCCCCHHHCC	69.80	25953088
88	Acetylation	DIKGPEDKKKHLLIG CCCCCHHHCCEEEEE	63.16	6567975
89	Acetylation	IKGPEDKKKHLLIGV CCCCHHHCCEEEEEE	58.72	155895
90	Acetylation	KGPEDKKKHLLIGVS CCCHHHCCEEEEEEC	45.27	25825284
97	Phosphorylation	KHLLIGVSSDRGLCG CEEEEEECCCCCHHH	22.70	23312004
98	Phosphorylation	HLLIGVSSDRGLCGA EEEEEECCCCCHHHH	28.99	23312004
100	Methylation	LIGVSSDRGLCGAIH EEEECCCCCHHHHHH	41.76	-
103	S-palmitoylation	VSSDRGLCGAIHSSI ECCCCCHHHHHHHHH	3.73	21044946
108	Phosphorylation	GLCGAIHSSIAKQMK CHHHHHHHHHHHHHH	19.82	27080861
109	Phosphorylation	LCGAIHSSIAKQMKS HHHHHHHHHHHHHHH	16.65	23312004
112 (in isoform 1)	Ubiquitination	-	49.62	21890473
112	Ubiquitination	AIHSSIAKQMKSEVA HHHHHHHHHHHHHHH	49.62	21890473
112 (in isoform 2)	Ubiquitination	-	49.62	21890473
112	Acetylation	AIHSSIAKQMKSEVA HHHHHHHHHHHHHHH	49.62	25953088
112	Malonylation	AIHSSIAKQMKSEVA HHHHHHHHHHHHHHH	49.62	26320211
112	Ubiquitination	AIHSSIAKQMKSEVA HHHHHHHHHHHHHHH	49.62	21890473
115	Succinylation	SSIAKQMKSEVATLT HHHHHHHHHHHHHHH	40.76	-
115	Succinylation	SSIAKQMKSEVATLT HHHHHHHHHHHHHHH	40.76	-
115	Ubiquitination	SSIAKQMKSEVATLT HHHHHHHHHHHHHHH	40.76	-
115	2-Hydroxyisobutyrylation	SSIAKQMKSEVATLT HHHHHHHHHHHHHHH	40.76	-
115	Acetylation	SSIAKQMKSEVATLT HHHHHHHHHHHHHHH	40.76	23236377
115	Malonylation	SSIAKQMKSEVATLT HHHHHHHHHHHHHHH	40.76	26320211
116	Phosphorylation	SIAKQMKSEVATLTA HHHHHHHHHHHHHHH	31.77	20068231
116 (in isoform 2)	Phosphorylation	-	31.77	-
120	Phosphorylation	QMKSEVATLTAAGKE HHHHHHHHHHHCCCE	29.80	21406692
122 (in isoform 2)	Phosphorylation	-	15.31	-
122	Phosphorylation	KSEVATLTAAGKEVM HHHHHHHHHCCCEEE	15.31	20068231
126	2-Hydroxyisobutyrylation	ATLTAAGKEVMLVGI HHHHHCCCEEEEEEC	42.27	-
126	Acetylation	ATLTAAGKEVMLVGI HHHHHCCCEEEEEEC	42.27	25038526
129	Sulfoxidation	TAAGKEVMLVGIGDK HHCCCEEEEEECCHH	2.35	21406390
136	Ubiquitination	MLVGIGDKIRGILYR EEEECCHHHCEEEEE	29.14	21890473
136 (in isoform 1)	Ubiquitination	-	29.14	21890473
136 (in isoform 2)	Ubiquitination	-	29.14	21890473
136	Ubiquitination	MLVGIGDKIRGILYR EEEECCHHHCEEEEE	29.14	21890473
136	2-Hydroxyisobutyrylation	MLVGIGDKIRGILYR EEEECCHHHCEEEEE	29.14	-
144	Phosphorylation	IRGILYRTHSDQFLV HCEEEEECCCCCEEE	16.51	30266825
146 (in isoform 2)	Phosphorylation	-	32.28	-
146	Phosphorylation	GILYRTHSDQFLVAF EEEEECCCCCEEEEE	32.28	30266825
154	Succinylation	DQFLVAFKEVGRKPP CCEEEEEECCCCCCC	41.58	23954790
154 (in isoform 2)	Acetylation	-	41.58	-
154 (in isoform 2)	Ubiquitination	-	41.58	-
154	Succinylation	DQFLVAFKEVGRKPP CCEEEEEECCCCCCC	41.58	-
154	Acetylation	DQFLVAFKEVGRKPP CCEEEEEECCCCCCC	41.58	19608861
154	Malonylation	DQFLVAFKEVGRKPP CCEEEEEECCCCCCC	41.58	26320211
197 (in isoform 2)	Acetylation	-	42.54	-
197	Acetylation	FRSVISYKTEEKPIF CCCCCEEECCCCCCE	42.54	19608861
197	Ubiquitination	FRSVISYKTEEKPIF CCCCCEEECCCCCCE	42.54	19608861
197	Succinylation	FRSVISYKTEEKPIF CCCCCEEECCCCCCE	42.54	23954790
241	Phosphorylation	LANIIYYSLKESTTS HHHHHHHCCCCCCCC	18.92	24719451
245	Phosphorylation	IYYSLKESTTSEQSA HHHCCCCCCCCHHHH	35.08	28102081
246	Phosphorylation	YYSLKESTTSEQSAR HHCCCCCCCCHHHHH	35.12	28102081
247	Phosphorylation	YSLKESTTSEQSARM HCCCCCCCCHHHHHH	39.27	28102081
248	Phosphorylation	SLKESTTSEQSARMT CCCCCCCCHHHHHHH	33.45	28102081
251	Phosphorylation	ESTTSEQSARMTAMD CCCCCHHHHHHHHHH	17.50	28102081
262 (in isoform 1)	Ubiquitination	-	54.87	21890473
262	Ubiquitination	TAMDNASKNASEMID HHHHHHCCCHHHHHH	54.87	21906983
262 (in isoform 2)	Ubiquitination	-	54.87	21890473
265	Phosphorylation	DNASKNASEMIDKLT HHHCCCHHHHHHHHH	36.77	21406692
270	2-Hydroxyisobutyrylation	NASEMIDKLTLTFNR CHHHHHHHHHHHCCC	32.23	-
270	Ubiquitination	NASEMIDKLTLTFNR CHHHHHHHHHHHCCC	32.23	21890473
270 (in isoform 2)	Ubiquitination	-	32.23	21890473
270 (in isoform 1)	Ubiquitination	-	32.23	21890473
270	Ubiquitination	NASEMIDKLTLTFNR CHHHHHHHHHHHCCC	32.23	21890473
270	Succinylation	NASEMIDKLTLTFNR CHHHHHHHHHHHCCC	32.23	21890473
270	Succinylation	NASEMIDKLTLTFNR CHHHHHHHHHHHCCC	32.23	-
272	Phosphorylation	SEMIDKLTLTFNRTR HHHHHHHHHHCCCHH	29.50	21406692
274	Phosphorylation	MIDKLTLTFNRTRQA HHHHHHHHCCCHHCC	17.39	21406692
284	Phosphorylation	RTRQAVITKELIEII CHHCCHHCHHHHHHH	16.33	-

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
146	S	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ATPG_HUMAN !!

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 ATPG_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAH12_HUMAN	CA12	physical	16169070
CHM2B_HUMAN	CHMP2B	physical	16169070
DPP3_HUMAN	DPP3	physical	16169070
EGFR_HUMAN	EGFR	physical	16169070
ITIH2_HUMAN	ITIH2	physical	16169070
NDUB3_HUMAN	NDUFB3	physical	16169070
NGEF_HUMAN	NGEF	physical	16169070
GDPD2_HUMAN	GDPD2	physical	16169070
CCND3_HUMAN	CCND3	physical	16169070
TCPH_HUMAN	CCT7	physical	16169070
ELOF1_HUMAN	ELOF1	physical	16169070
MED15_HUMAN	MED15	physical	16169070
PJA1_HUMAN	PJA1	physical	16169070
PNO1_HUMAN	PNO1	physical	16169070
DPOA2_HUMAN	POLA2	physical	16169070
PTN_HUMAN	PTN	physical	16169070
EM55_HUMAN	MPP1	physical	16169070
A4_HUMAN	APP	physical	21832049
QCR1_HUMAN	UQCRC1	physical	22939629
NDUAC_HUMAN	NDUFA12	physical	22939629
NDUB9_HUMAN	NDUFB9	physical	22939629
NDUS1_HUMAN	NDUFS1	physical	22939629
MIC60_HUMAN	IMMT	physical	22939629
VATA_HUMAN	ATP6V1A	physical	22939629
VATB1_HUMAN	ATP6V1B1	physical	22939629
SSBP_HUMAN	SSBP1	physical	22939629
A1AT_HUMAN	SERPINA1	physical	21988832
ATPO_HUMAN	ATP5O	physical	26344197
OST48_HUMAN	DDOST	physical	26344197
COX2_HUMAN	COX2	physical	26344197
SSRD_HUMAN	SSR4	physical	26344197
VDAC1_HUMAN	VDAC1	physical	26344197
VDAC2_HUMAN	VDAC2	physical	26344197
ATPB_HUMAN	ATP5B	physical	28514442
ATIF1_HUMAN	ATPIF1	physical	28514442

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 ATPG_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-55; LYS-154 AND LYS-197, ANDMASS SPECTROMETRY.	19608861 [Abstract]