ATPK_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATPK_HUMAN
• UniProt AC: P56134
• Protein Name: ATP synthase subunit f, mitochondrial
• Gene Name: ATP5J2
• Organism: Homo sapiens (Human).
• Sequence Length: 94
• Subcellular Localization: Mitochondrion. Mitochondrion inner membrane ; Single-pass membrane protein .
• 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: MASVGECPAPVPVKDKKLLEVKLGELPSWILMRDFSPSGIFGAFQRGYYRYYNKYINVKKGSISGITMVLACYVLFSYSFSYKHLKHERLRKYH

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	------MASVGECPA ------CCCCCCCCC	16.96	22223895
3	Phosphorylation	-----MASVGECPAP -----CCCCCCCCCC	29.38	23401153
3 (in isoform 4)	Phosphorylation	-	29.38	-
3 (in isoform 2)	Phosphorylation	-	29.38	-
14	Ubiquitination	CPAPVPVKDKKLLEV CCCCCCCCCCCEEEE	58.73	33845483
22	Acetylation	DKKLLEVKLGELPSW CCCEEEEECCCCCCE	41.20	25038526
28	Phosphorylation	VKLGELPSWILMRDF EECCCCCCEEEECCC	39.10	25338102
32 (in isoform 4)	Phosphorylation	-	2.58	30087585
36	Phosphorylation	WILMRDFSPSGIFGA EEEECCCCCCCCCHH	23.57	27499020
38	Phosphorylation	LMRDFSPSGIFGAFQ EECCCCCCCCCHHHH	43.24	21712546
38 (in isoform 3)	Phosphorylation	-	43.24	30087585
54	Acetylation	GYYRYYNKYINVKKG HHHHHCCCEECCCCC	31.24	25825284

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATPK_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 ATPK_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARL8B_HUMAN	ARL8B	physical	16169070
CPNS1_HUMAN	CAPNS1	physical	16169070
LPP_HUMAN	LPP	physical	16169070
PRP4_HUMAN	PRPF4	physical	16169070
NECT2_HUMAN	PVRL2	physical	16169070
ZFPL1_HUMAN	ZFPL1	physical	16169070
KDM1A_HUMAN	KDM1A	physical	16169070
CREL1_HUMAN	CRELD1	physical	16169070
F16P1_HUMAN	FBP1	physical	16169070
CC137_HUMAN	CCDC137	physical	16169070
NDUA6_HUMAN	NDUFA6	physical	16169070
HAP1_HUMAN	HAP1	physical	16169070
RLA1_HUMAN	RPLP1	physical	16169070
QCR8_HUMAN	UQCRQ	physical	22939629
NDUB9_HUMAN	NDUFB9	physical	22939629
RT34_HUMAN	MRPS34	physical	22939629

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