ATP5J_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATP5J_RAT
• UniProt AC: P21571
• Protein Name: ATP synthase-coupling factor 6, mitochondrial
• Gene Name: Atp5j
• Organism: Rattus norvegicus (Rat).
• 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 (By similarity)..
• Protein Sequence: MTVQRIFRLSSVLRSAVSVHLRRNIGVTAVAFNKELDPVQKLFLDKIREYKAKRLASGGPVDTGPEYQQEVDRELFKLKQMYGKGEMDKFPTFNFEDPKFEVLDKPQS

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
34	Acetylation	VTAVAFNKELDPVQK CEEEEECCCCCHHHH	53.88	26302492
41	Acetylation	KELDPVQKLFLDKIR CCCCHHHHHHHHHHH	41.25	22902405
46	Acetylation	VQKLFLDKIREYKAK HHHHHHHHHHHHHHH	45.90	25786129
51	Acetylation	LDKIREYKAKRLASG HHHHHHHHHHHHHCC	42.55	22902405
57	Phosphorylation	YKAKRLASGGPVDTG HHHHHHHCCCCCCCC	49.20	22817900
57	O-linked_Glycosylation	YKAKRLASGGPVDTG HHHHHHHCCCCCCCC	49.20	27213235
79	Acetylation	DRELFKLKQMYGKGE HHHHHHHHHHHCCCC	33.34	22902405
84	Acetylation	KLKQMYGKGEMDKFP HHHHHHCCCCCCCCC	33.92	22902405
84	Succinylation	KLKQMYGKGEMDKFP HHHHHHCCCCCCCCC	33.92	-
84	Succinylation	KLKQMYGKGEMDKFP HHHHHHCCCCCCCCC	33.92	-
89	Acetylation	YGKGEMDKFPTFNFE HCCCCCCCCCCCCCC	52.51	22902405
89	Succinylation	YGKGEMDKFPTFNFE HCCCCCCCCCCCCCC	52.51	26843850
99	Succinylation	TFNFEDPKFEVLDKP CCCCCCCCCEECCCC	67.49	-
99	Succinylation	TFNFEDPKFEVLDKP CCCCCCCCCEECCCC	67.49	-
99	Acetylation	TFNFEDPKFEVLDKP CCCCCCCCCEECCCC	67.49	22902405
105	Acetylation	PKFEVLDKPQS---- CCCEECCCCCC----	40.57	22902405
105	Succinylation	PKFEVLDKPQS---- CCCEECCCCCC----	40.57	26843850
108	Phosphorylation	EVLDKPQS------- EECCCCCC-------	51.20	22673903

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
57	S	Phosphorylation	Kinase	PRKACA	P00517	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATP5J_RAT !!

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_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of ATP5J_RAT !!

Drug and Disease Associations

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