ATP5L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATP5L_HUMAN
• UniProt AC: O75964
• Protein Name: ATP synthase subunit g, mitochondrial
• Gene Name: ATP5L
• Organism: Homo sapiens (Human).
• Sequence Length: 103
• 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. Minor subunit located with subunit a in the membrane..
• Protein Sequence: MAQFVRNLVEKTPALVNAAVTYSKPRLATFWYYAKVELVPPTPAEIPRAIQSLKKIVNSAQTGSFKQLTVKEAVLNGLVATEVLMWFYVGEIIGKRGIIGYDV

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	------MAQFVRNLV ------CHHHHHHHH	16.12	19413330
11	Acetylation	FVRNLVEKTPALVNA HHHHHHHHCHHHHHH	52.94	-
11	Ubiquitination	FVRNLVEKTPALVNA HHHHHHHHCHHHHHH	52.94	29967540
12	Phosphorylation	VRNLVEKTPALVNAA HHHHHHHCHHHHHHH	10.57	24719451
21	Phosphorylation	ALVNAAVTYSKPRLA HHHHHHHHCCCCCEE	19.83	28152594
22	Phosphorylation	LVNAAVTYSKPRLAT HHHHHHHCCCCCEEE	14.22	28152594
23	Phosphorylation	VNAAVTYSKPRLATF HHHHHHCCCCCEEEE	27.15	28152594
24	Ubiquitination	NAAVTYSKPRLATFW HHHHHCCCCCEEEEE	24.60	22817900
24	Malonylation	NAAVTYSKPRLATFW HHHHHCCCCCEEEEE	24.60	26320211
24	Acetylation	NAAVTYSKPRLATFW HHHHHCCCCCEEEEE	24.60	19608861
29	Phosphorylation	YSKPRLATFWYYAKV CCCCCEEEEEEEEEE	21.20	-
32	Phosphorylation	PRLATFWYYAKVELV CCEEEEEEEEEEEEC	6.86	28152594
33	Phosphorylation	RLATFWYYAKVELVP CEEEEEEEEEEEECC	7.19	28152594
35	Acetylation	ATFWYYAKVELVPPT EEEEEEEEEEECCCC	21.81	-
42	Phosphorylation	KVELVPPTPAEIPRA EEEECCCCHHHHHHH	29.12	-
52	Phosphorylation	EIPRAIQSLKKIVNS HHHHHHHHHHHHHHH	35.72	26437602
54	Acetylation	PRAIQSLKKIVNSAQ HHHHHHHHHHHHHHC	45.78	25953088
54	Ubiquitination	PRAIQSLKKIVNSAQ HHHHHHHHHHHHHHC	45.78	29967540
55	Acetylation	RAIQSLKKIVNSAQT HHHHHHHHHHHHHCC	58.12	26051181
55	Malonylation	RAIQSLKKIVNSAQT HHHHHHHHHHHHHCC	58.12	26320211
55	Succinylation	RAIQSLKKIVNSAQT HHHHHHHHHHHHHCC	58.12	27452117
55	Ubiquitination	RAIQSLKKIVNSAQT HHHHHHHHHHHHHCC	58.12	16196087
59	Phosphorylation	SLKKIVNSAQTGSFK HHHHHHHHHCCCCCC	15.74	20860994
62	Phosphorylation	KIVNSAQTGSFKQLT HHHHHHCCCCCCCCH	34.21	20860994
64	Phosphorylation	VNSAQTGSFKQLTVK HHHHCCCCCCCCHHH	32.43	20860994
66	Ubiquitination	SAQTGSFKQLTVKEA HHCCCCCCCCHHHHH	46.20	22817900
66	Acetylation	SAQTGSFKQLTVKEA HHCCCCCCCCHHHHH	46.20	2560005
66	2-Hydroxyisobutyrylation	SAQTGSFKQLTVKEA HHCCCCCCCCHHHHH	46.20	-
66	Methylation	SAQTGSFKQLTVKEA HHCCCCCCCCHHHHH	46.20	-
71	Ubiquitination	SFKQLTVKEAVLNGL CCCCCHHHHHHHHHH	34.42	22817900

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

Oops, there are no upstream regulatory protein records of ATP5L_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATP5L_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 ATP5L_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AL3A2_HUMAN	ALDH3A2	physical	26344197
ATD3A_HUMAN	ATAD3A	physical	26344197
ATPA_HUMAN	ATP5A1	physical	26344197
ATPG_HUMAN	ATP5C1	physical	26344197
ATPD_HUMAN	ATP5D	physical	26344197
AT5F1_HUMAN	ATP5F1	physical	26344197
ATP5H_HUMAN	ATP5H	physical	26344197
ATP5I_HUMAN	ATP5I	physical	26344197
ATPO_HUMAN	ATP5O	physical	26344197
CPT2_HUMAN	CPT2	physical	26344197
CY1_HUMAN	CYC1	physical	26344197
OST48_HUMAN	DDOST	physical	26344197
ILVBL_HUMAN	ILVBL	physical	26344197
LMAN1_HUMAN	LMAN1	physical	26344197
MTCH1_HUMAN	MTCH1	physical	26344197
MTCH2_HUMAN	MTCH2	physical	26344197
MYH9_HUMAN	MYH9	physical	26344197
NDUB8_HUMAN	NDUFB8	physical	26344197
PHB_HUMAN	PHB	physical	26344197
PHB2_HUMAN	PHB2	physical	26344197
RER1_HUMAN	RER1	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
SCAM2_HUMAN	SCAMP2	physical	26344197
SCAM3_HUMAN	SCAMP3	physical	26344197
SFXN1_HUMAN	SFXN1	physical	26344197
SSRA_HUMAN	SSR1	physical	26344197
SSRG_HUMAN	SSR3	physical	26344197
STX12_HUMAN	STX12	physical	26344197
STX7_HUMAN	STX7	physical	26344197
TSPO_HUMAN	TSPO	physical	26344197
QCR8_HUMAN	UQCRQ	physical	26344197

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

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330

"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-24, AND MASS SPECTROMETRY.
PubMed: 19608861