dbPTM

ATP5H_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATP5H_HUMAN
UniProt AC	O75947
Protein Name	ATP synthase subunit d, mitochondrial
Gene Name	ATP5H
Organism	Homo sapiens (Human).
Sequence Length	161
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..
Protein Sequence	MAGRKLALKTIDWVAFAEIIPQNQKAIASSLKSWNETLTSRLAALPENPPAIDWAYYKANVAKAGLVDDFEKKFNALKVPVPEDKYTAQVDAEEKEDVKSCAEWVSLSKARIVEYEKEMEKMKNLIPFDQMTIEDLNEAFPETKLDKKKYPYWPHQPIENL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGRKLALK ------CCCCHHHHH	26.88	25944712
5	Acetylation	---MAGRKLALKTID ---CCCCHHHHHHHC	36.87	25038526
9	Acetylation	AGRKLALKTIDWVAF CCCHHHHHHHCHHHH	37.52	25038526
30	Phosphorylation	NQKAIASSLKSWNET CHHHHHHHHHHHHHH	30.69	22817900
32	Ubiquitination	KAIASSLKSWNETLT HHHHHHHHHHHHHHH	56.21	21890473
32	Acetylation	KAIASSLKSWNETLT HHHHHHHHHHHHHHH	56.21	25953088
32 (in isoform 1)	Ubiquitination	-	56.21	21890473
32 (in isoform 2)	Ubiquitination	-	56.21	21890473
32	Ubiquitination	KAIASSLKSWNETLT HHHHHHHHHHHHHHH	56.21	21890473
39	Phosphorylation	KSWNETLTSRLAALP HHHHHHHHHHHHCCC	21.15	-
56	Phosphorylation	PPAIDWAYYKANVAK CCCCCHHHHHHHHHH	10.97	28152594
57	Phosphorylation	PAIDWAYYKANVAKA CCCCHHHHHHHHHHH	8.90	28176486
58 (in isoform 2)	Ubiquitination	-	22.32	21890473
58	Ubiquitination	AIDWAYYKANVAKAG CCCHHHHHHHHHHHC	22.32	-
58 (in isoform 1)	Ubiquitination	-	22.32	21890473
58	Acetylation	AIDWAYYKANVAKAG CCCHHHHHHHHHHHC	22.32	23954790
58	Succinylation	AIDWAYYKANVAKAG CCCHHHHHHHHHHHC	22.32	23954790
63	Malonylation	YYKANVAKAGLVDDF HHHHHHHHHCCCHHH	38.41	26320211
63	2-Hydroxyisobutyrylation	YYKANVAKAGLVDDF HHHHHHHHHCCCHHH	38.41	-
63	Ubiquitination	YYKANVAKAGLVDDF HHHHHHHHHCCCHHH	38.41	-
63	Succinylation	YYKANVAKAGLVDDF HHHHHHHHHCCCHHH	38.41	27452117
63	Acetylation	YYKANVAKAGLVDDF HHHHHHHHHCCCHHH	38.41	23954790
72	2-Hydroxyisobutyrylation	GLVDDFEKKFNALKV CCCHHHHHHHCCCCC	63.76	-
72 (in isoform 2)	Ubiquitination	-	63.76	-
72	Ubiquitination	GLVDDFEKKFNALKV CCCHHHHHHHCCCCC	63.76	19608861
72	Acetylation	GLVDDFEKKFNALKV CCCHHHHHHHCCCCC	63.76	25825284
72	Malonylation	GLVDDFEKKFNALKV CCCHHHHHHHCCCCC	63.76	26320211
73	Ubiquitination	LVDDFEKKFNALKVP CCHHHHHHHCCCCCC	36.33	-
73	Acetylation	LVDDFEKKFNALKVP CCHHHHHHHCCCCCC	36.33	7614613
76 (in isoform 2)	Phosphorylation	-	16.34	29116813
78	Malonylation	EKKFNALKVPVPEDK HHHHCCCCCCCCCCC	41.92	32601280
78	2-Hydroxyisobutyrylation	EKKFNALKVPVPEDK HHHHCCCCCCCCCCC	41.92	-
78	Succinylation	EKKFNALKVPVPEDK HHHHCCCCCCCCCCC	41.92	27452117
78	Acetylation	EKKFNALKVPVPEDK HHHHCCCCCCCCCCC	41.92	23236377
82 (in isoform 2)	Phosphorylation	-	37.69	29116813
84 (in isoform 2)	Phosphorylation	-	43.10	29116813
85	Malonylation	KVPVPEDKYTAQVDA CCCCCCCCCEEECCH	42.72	26320211
85	Succinylation	KVPVPEDKYTAQVDA CCCCCCCCCEEECCH	42.72	27452117
85	2-Hydroxyisobutyrylation	KVPVPEDKYTAQVDA CCCCCCCCCEEECCH	42.72	-
85 (in isoform 1)	Ubiquitination	-	42.72	21890473
85	Ubiquitination	KVPVPEDKYTAQVDA CCCCCCCCCEEECCH	42.72	19608861
85	Acetylation	KVPVPEDKYTAQVDA CCCCCCCCCEEECCH	42.72	19608861
86	Nitration	VPVPEDKYTAQVDAE CCCCCCCCEEECCHH	21.45	-
86	Phosphorylation	VPVPEDKYTAQVDAE CCCCCCCCEEECCHH	21.45	20886841
93	Acetylation	YTAQVDAEEKEDVKS CEEECCHHHHHHHHH	66.20	19608861
95	Succinylation	AQVDAEEKEDVKSCA EECCHHHHHHHHHHH	51.20	23954790
95	Acetylation	AQVDAEEKEDVKSCA EECCHHHHHHHHHHH	51.20	19608861
99	Ubiquitination	AEEKEDVKSCAEWVS HHHHHHHHHHHHHHH	52.73	-
99	Succinylation	AEEKEDVKSCAEWVS HHHHHHHHHHHHHHH	52.73	23954790
99	Acetylation	AEEKEDVKSCAEWVS HHHHHHHHHHHHHHH	52.73	23954790
100	Phosphorylation	EEKEDVKSCAEWVSL HHHHHHHHHHHHHHH	20.57	25159151
101	S-nitrosylation	EKEDVKSCAEWVSLS HHHHHHHHHHHHHHH	3.09	2212679
106	Phosphorylation	KSCAEWVSLSKARIV HHHHHHHHHHHHHHH	28.18	30108239
108	Phosphorylation	CAEWVSLSKARIVEY HHHHHHHHHHHHHHH	19.43	25627689
109	Malonylation	AEWVSLSKARIVEYE HHHHHHHHHHHHHHH	47.15	26320211
109	2-Hydroxyisobutyrylation	AEWVSLSKARIVEYE HHHHHHHHHHHHHHH	47.15	-
109	Succinylation	AEWVSLSKARIVEYE HHHHHHHHHHHHHHH	47.15	27452117
109	Acetylation	AEWVSLSKARIVEYE HHHHHHHHHHHHHHH	47.15	25953088
115	Nitration	SKARIVEYEKEMEKM HHHHHHHHHHHHHHH	22.77	-
117	Acetylation	ARIVEYEKEMEKMKN HHHHHHHHHHHHHHH	62.55	19608861
117	Succinylation	ARIVEYEKEMEKMKN HHHHHHHHHHHHHHH	62.55	27452117
117	Malonylation	ARIVEYEKEMEKMKN HHHHHHHHHHHHHHH	62.55	26320211
117	2-Hydroxyisobutyrylation	ARIVEYEKEMEKMKN HHHHHHHHHHHHHHH	62.55	-
119	Sulfoxidation	IVEYEKEMEKMKNLI HHHHHHHHHHHHHCC	9.94	21406390
121	Acetylation	EYEKEMEKMKNLIPF HHHHHHHHHHHCCCH	54.59	30583895
124	Acetylation	KEMEKMKNLIPFDQM HHHHHHHHCCCHHHC	39.44	19608861
125 (in isoform 2)	Ubiquitination	-	4.37	21890473
125	Ubiquitination	EMEKMKNLIPFDQMT HHHHHHHCCCHHHCC	4.37	19608861
125	Acetylation	EMEKMKNLIPFDQMT HHHHHHHCCCHHHCC	4.37	19608861
144	Succinylation	NEAFPETKLDKKKYP HHHCCCCCCCCCCCC	53.69	23954790
144	Acetylation	NEAFPETKLDKKKYP HHHCCCCCCCCCCCC	53.69	23954790
144	Malonylation	NEAFPETKLDKKKYP HHHCCCCCCCCCCCC	53.69	26320211
147	Acetylation	FPETKLDKKKYPYWP CCCCCCCCCCCCCCC	62.70	2401967
148	Acetylation	PETKLDKKKYPYWPH CCCCCCCCCCCCCCC	58.15	19608861
149	Acetylation	ETKLDKKKYPYWPHQ CCCCCCCCCCCCCCC	58.14	19608861
149	Ubiquitination	ETKLDKKKYPYWPHQ CCCCCCCCCCCCCCC	58.14	21890473
149	2-Hydroxyisobutyrylation	ETKLDKKKYPYWPHQ CCCCCCCCCCCCCCC	58.14	-
149	Succinylation	ETKLDKKKYPYWPHQ CCCCCCCCCCCCCCC	58.14	-
149	Malonylation	ETKLDKKKYPYWPHQ CCCCCCCCCCCCCCC	58.14	26320211
149 (in isoform 1)	Ubiquitination	-	58.14	21890473
149	Ubiquitination	ETKLDKKKYPYWPHQ CCCCCCCCCCCCCCC	58.14	21890473
150	Phosphorylation	TKLDKKKYPYWPHQP CCCCCCCCCCCCCCC	15.50	25884760
152	Phosphorylation	LDKKKYPYWPHQPIE CCCCCCCCCCCCCCC	28.60	20090780

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
Oops, there are no upstream regulatory protein records of ATP5H_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ATP5H_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 ATP5H_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
ATPO_HUMAN	ATP5O	physical	22939629
NDUAC_HUMAN	NDUFA12	physical	22939629
QCR8_HUMAN	UQCRQ	physical	22939629
STML2_HUMAN	STOML2	physical	22939629
ATPD_HUMAN	ATP5D	physical	26344197
AT5F1_HUMAN	ATP5F1	physical	26344197
ATP5I_HUMAN	ATP5I	physical	26344197
ATPO_HUMAN	ATP5O	physical	26344197
CHCH2_HUMAN	CHCHD2	physical	26344197
CISD1_HUMAN	CISD1	physical	26344197
CY1_HUMAN	CYC1	physical	26344197
PDIA3_HUMAN	PDIA3	physical	26344197
RER1_HUMAN	RER1	physical	26344197
STOM_HUMAN	STOM	physical	27173435

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 ATP5H_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-85; LYS-95; LYS-117 ANDLYS-149, AND MASS SPECTROMETRY.	19608861 [Abstract]