ATP5J_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATP5J_HUMAN
• UniProt AC: P18859
• Protein Name: ATP synthase-coupling factor 6, mitochondrial
• Gene Name: ATP5J
• Organism: Homo sapiens (Human).
• Sequence Length: 108
• 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. Also involved in the restoration of oligomycin-sensitive ATPase activity to depleted F1-F0 complexes..
• Protein Sequence: MILQRLFRFSSVIRSAVSVHLRRNIGVTAVAFNKELDPIQKLFVDKIREYKSKRQTSGGPVDASSEYQQELERELFKLKQMFGNADMNTFPTFKFEDPKFEVIEKPQA

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
41	Ubiquitination	KELDPIQKLFVDKIR CCCCHHHHHHHHHHH	44.61	21890473
41	Acetylation	KELDPIQKLFVDKIR CCCCHHHHHHHHHHH	44.61	19608861
46	Acetylation	IQKLFVDKIREYKSK HHHHHHHHHHHHHHH	38.06	19608861
46	Ubiquitination	IQKLFVDKIREYKSK HHHHHHHHHHHHHHH	38.06	21890473
46	Succinylation	IQKLFVDKIREYKSK HHHHHHHHHHHHHHH	38.06	27452117
46	2-Hydroxyisobutyrylation	IQKLFVDKIREYKSK HHHHHHHHHHHHHHH	38.06	-
49	Ubiquitination	LFVDKIREYKSKRQT HHHHHHHHHHHHCCC	61.87	19608861
49	Acetylation	LFVDKIREYKSKRQT HHHHHHHHHHHHCCC	61.87	19608861
51	Succinylation	VDKIREYKSKRQTSG HHHHHHHHHHCCCCC	44.76	23954790
54	Ubiquitination	IREYKSKRQTSGGPV HHHHHHHCCCCCCCC	52.69	19608861
54	Acetylation	IREYKSKRQTSGGPV HHHHHHHCCCCCCCC	52.69	19608861
56	Phosphorylation	EYKSKRQTSGGPVDA HHHHHCCCCCCCCCC	33.11	30266825
57	Phosphorylation	YKSKRQTSGGPVDAS HHHHCCCCCCCCCCC	33.15	30266825
64	Phosphorylation	SGGPVDASSEYQQEL CCCCCCCCHHHHHHH	21.17	26657352
65	Phosphorylation	GGPVDASSEYQQELE CCCCCCCHHHHHHHH	41.88	30266825
67	Phosphorylation	PVDASSEYQQELERE CCCCCHHHHHHHHHH	19.90	28450419
72	Phosphorylation	SEYQQELERELFKLK HHHHHHHHHHHHHHH	43.27	24719451
73	Phosphorylation	EYQQELERELFKLKQ HHHHHHHHHHHHHHH	59.55	27251275
79	Malonylation	ERELFKLKQMFGNAD HHHHHHHHHHHCCCC	40.06	26320211
79	Acetylation	ERELFKLKQMFGNAD HHHHHHHHHHHCCCC	40.06	23236377
79	Ubiquitination	ERELFKLKQMFGNAD HHHHHHHHHHHCCCC	40.06	21890473
94	Succinylation	MNTFPTFKFEDPKFE CCCCCCCCCCCCCCE	50.77	-
94	Acetylation	MNTFPTFKFEDPKFE CCCCCCCCCCCCCCE	50.77	26822725
94	Succinylation	MNTFPTFKFEDPKFE CCCCCCCCCCCCCCE	50.77	-
94	Ubiquitination	MNTFPTFKFEDPKFE CCCCCCCCCCCCCCE	50.77	-
99	Succinylation	TFKFEDPKFEVIEKP CCCCCCCCCEEEECC	67.49	23954790
99	Acetylation	TFKFEDPKFEVIEKP CCCCCCCCCEEEECC	67.49	19608861
99	Succinylation	TFKFEDPKFEVIEKP CCCCCCCCCEEEECC	67.49	-
99	Ubiquitination	TFKFEDPKFEVIEKP CCCCCCCCCEEEECC	67.49	21890473
105	Acetylation	PKFEVIEKPQA---- CCCEEEECCCC----	31.16	19608861
105	Malonylation	PKFEVIEKPQA---- CCCEEEECCCC----	31.16	26320211
107	Acetylation	FEVIEKPQA------ CEEEECCCC------	71.43	19608861
107	Ubiquitination	FEVIEKPQA------ CEEEECCCC------	71.43	19608861
113	Acetylation	PQA------------ CCC------------		19608861

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

Oops, there are no upstream regulatory protein records of ATP5J_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATP5J_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 ATP5J_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATPK_HUMAN	ATP5J2	physical	22939629
ATPO_HUMAN	ATP5O	physical	22939629
QCR2_HUMAN	UQCRC2	physical	22939629
COA6_HUMAN	COA6	physical	22939629
PARK7_HUMAN	PARK7	physical	22939629
ATP5I_HUMAN	ATP5I	physical	26344197
ATPO_HUMAN	ATP5O	physical	26344197
FABP5_HUMAN	FABP5	physical	26344197
GSTO1_HUMAN	GSTO1	physical	26344197
PRDX3_HUMAN	PRDX3	physical	26344197
UCRI_HUMAN	UQCRFS1	physical	26344197
ATPB_HUMAN	ATP5B	physical	16230521

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.

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-41; LYS-46; LYS-99 ANDLYS-105, AND MASS SPECTROMETRY.
PubMed: 19608861