ATPA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATPA_HUMAN
• UniProt AC: P25705
• Protein Name: ATP synthase subunit alpha, mitochondrial {ECO:0000305}
• Gene Name: ATP5F1A {ECO:0000312|HGNC:HGNC:823}
• Organism: Homo sapiens (Human).
• Sequence Length: 553
• Subcellular Localization: Mitochondrion inner membrane ; Peripheral membrane protein ; Matrix side . Cell membrane ; Peripheral membrane protein ; Extracellular side . Colocalizes with HRG on the cell surface of T-cells (PubMed:19285951).
• 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. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity)..
• Protein Sequence: MLSVRVAAAVVRALPRRAGLVSRNALGSSFIAARNFHASNTHLQKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGSDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRADGKISEQSDAKLKEIVTNFLAGFEA

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
28	Phosphorylation	VSRNALGSSFIAARN CCCCCCCCHHHHHHC	23.95	23828894
29	Phosphorylation	SRNALGSSFIAARNF CCCCCCCHHHHHHCC	20.90	23828894
44	Pyrrolidone_carboxylic_acid	HASNTHLQKTGTAEM CCCCCCCCCCCCCCH	33.39	-
45	Ubiquitination	ASNTHLQKTGTAEMS CCCCCCCCCCCCCHH	56.11	-
45	Ubiquitination	ASNTHLQKTGTAEMS CCCCCCCCCCCCCHH	56.11	-
46	O-linked_Glycosylation	SNTHLQKTGTAEMSS CCCCCCCCCCCCHHH	27.14	26374642
46	Phosphorylation	SNTHLQKTGTAEMSS CCCCCCCCCCCCHHH	27.14	30108239
48	O-linked_Glycosylation	THLQKTGTAEMSSIL CCCCCCCCCCHHHHH	25.36	26374642
48	Phosphorylation	THLQKTGTAEMSSIL CCCCCCCCCCHHHHH	25.36	30108239
51	Sulfoxidation	QKTGTAEMSSILEER CCCCCCCHHHHHHHH	3.36	21406390
52	Phosphorylation	KTGTAEMSSILEERI CCCCCCHHHHHHHHH	13.01	25072903
53	Phosphorylation	TGTAEMSSILEERIL CCCCCHHHHHHHHHC	29.86	23911959
64	Phosphorylation	ERILGADTSVDLEET HHHCCCCCEECHHHH	30.07	30266825
65	Phosphorylation	RILGADTSVDLEETG HHCCCCCEECHHHHC	17.74	30266825
71	Phosphorylation	TSVDLEETGRVLSIG CEECHHHHCCEEEEC	22.40	30266825
76	O-linked_Glycosylation	EETGRVLSIGDGIAR HHHCCEEEECCCHHH	22.97	UniProtKB CARBOHYD
76	Phosphorylation	EETGRVLSIGDGIAR HHHCCEEEECCCHHH	22.97	30266825
88	Methylation	IARVHGLRNVQAEEM HHHHCCCCCCCHHHH	45.96	-
99	Phosphorylation	AEEMVEFSSGLKGMS HHHHHHHCCCCCCCC	15.25	20363803
100	Phosphorylation	EEMVEFSSGLKGMSL HHHHHHCCCCCCCCC	54.16	20363803
105	Sulfoxidation	FSSGLKGMSLNLEPD HCCCCCCCCCCCCCC	3.83	28183972
106	Phosphorylation	SSGLKGMSLNLEPDN CCCCCCCCCCCCCCC	23.83	-
111	Acetylation	GMSLNLEPDNVGVVV CCCCCCCCCCEEEEE	41.46	19608861
111	Ubiquitination	GMSLNLEPDNVGVVV CCCCCCCCCCEEEEE	41.46	19608861
123	2-Hydroxyisobutyrylation	VVVFGNDKLIKEGDI EEEECCCCEECCCCC	56.99	-
123	Acetylation	VVVFGNDKLIKEGDI EEEECCCCEECCCCC	56.99	23954790
123	Ubiquitination	VVVFGNDKLIKEGDI EEEECCCCEECCCCC	56.99	-
126	Ubiquitination	FGNDKLIKEGDIVKR ECCCCEECCCCCCCC	67.11	21906983
126	2-Hydroxyisobutyrylation	FGNDKLIKEGDIVKR ECCCCEECCCCCCCC	67.11	-
126	Acetylation	FGNDKLIKEGDIVKR ECCCCEECCCCCCCC	67.11	-
126	Malonylation	FGNDKLIKEGDIVKR ECCCCEECCCCCCCC	67.11	26320211
126	Ubiquitination	FGNDKLIKEGDIVKR ECCCCEECCCCCCCC	67.11	21906983
132	2-Hydroxyisobutyrylation	IKEGDIVKRTGAIVD ECCCCCCCCCCCEEE	44.57	-
132	Acetylation	IKEGDIVKRTGAIVD ECCCCCCCCCCCEEE	44.57	23749302
134	Phosphorylation	EGDIVKRTGAIVDVP CCCCCCCCCCEEEEE	25.83	28857561
153	Ubiquitination	LLGRVVDALGNAIDG HHHHHHHHHHHCCCC	13.03	21890473
161	Ubiquitination	LGNAIDGKGPIGSKT HHHCCCCCCCCCCCH	58.74	21890473
161	2-Hydroxyisobutyrylation	LGNAIDGKGPIGSKT HHHCCCCCCCCCCCH	58.74	-
161	Acetylation	LGNAIDGKGPIGSKT HHHCCCCCCCCCCCH	58.74	19608861
161	Malonylation	LGNAIDGKGPIGSKT HHHCCCCCCCCCCCH	58.74	26320211
161	Succinylation	LGNAIDGKGPIGSKT HHHCCCCCCCCCCCH	58.74	-
161	Succinylation	LGNAIDGKGPIGSKT HHHCCCCCCCCCCCH	58.74	-
161	Ubiquitination	LGNAIDGKGPIGSKT HHHCCCCCCCCCCCH	58.74	21890473
166	Phosphorylation	DGKGPIGSKTRRRVG CCCCCCCCCHHCCCC	31.41	22617229
167	2-Hydroxyisobutyrylation	GKGPIGSKTRRRVGL CCCCCCCCHHCCCCC	40.62	-
167	Acetylation	GKGPIGSKTRRRVGL CCCCCCCCHHCCCCC	40.62	-
167	Malonylation	GKGPIGSKTRRRVGL CCCCCCCCHHCCCCC	40.62	26320211
167	Succinylation	GKGPIGSKTRRRVGL CCCCCCCCHHCCCCC	40.62	-
167	Succinylation	GKGPIGSKTRRRVGL CCCCCCCCHHCCCCC	40.62	-
167	Ubiquitination	GKGPIGSKTRRRVGL CCCCCCCCHHCCCCC	40.62	-
168	Phosphorylation	KGPIGSKTRRRVGLK CCCCCCCHHCCCCCC	30.98	28857561
172	Ubiquitination	GSKTRRRVGLKAPGI CCCHHCCCCCCCCCC	11.33	21890473
172	Ubiquitination	GSKTRRRVGLKAPGI CCCHHCCCCCCCCCC	11.33	21906983
175	Ubiquitination	TRRRVGLKAPGIIPR HHCCCCCCCCCCCCC	46.75	21890473
175	Malonylation	TRRRVGLKAPGIIPR HHCCCCCCCCCCCCC	46.75	32601280
175	Ubiquitination	TRRRVGLKAPGIIPR HHCCCCCCCCCCCCC	46.75	21890473
184	Phosphorylation	PGIIPRISVREPMQT CCCCCCEECCCCCCC	19.19	30108239
189	Acetylation	RISVREPMQTGIKAV CEECCCCCCCCCCHH	4.82	19608861
191	Phosphorylation	SVREPMQTGIKAVDS ECCCCCCCCCCHHHH	34.32	20068231
194	Ubiquitination	EPMQTGIKAVDSLVP CCCCCCCCHHHHCCC	43.64	21890473
194	2-Hydroxyisobutyrylation	EPMQTGIKAVDSLVP CCCCCCCCHHHHCCC	43.64	-
194	Acetylation	EPMQTGIKAVDSLVP CCCCCCCCHHHHCCC	43.64	21466224
194	Ubiquitination	EPMQTGIKAVDSLVP CCCCCCCCHHHHCCC	43.64	21890473
198	Phosphorylation	TGIKAVDSLVPIGRG CCCCHHHHCCCCCCC	25.35	20068231
204	Methylation	DSLVPIGRGQRELII HHCCCCCCCCCEEEE	38.50	-
207	Methylation	VPIGRGQRELIIGDR CCCCCCCCEEEEECC	43.44	-
208	Ubiquitination	PIGRGQRELIIGDRQ CCCCCCCEEEEECCC	36.11	21890473
208	Ubiquitination	PIGRGQRELIIGDRQ CCCCCCCEEEEECCC	36.11	21906983
211	Acetylation	RGQRELIIGDRQTGK CCCCEEEEECCCCCC	7.99	19608861
211	Ubiquitination	RGQRELIIGDRQTGK CCCCEEEEECCCCCC	7.99	19608861
214	Methylation	RELIIGDRQTGKTSI CEEEEECCCCCCEEE	30.65	-
217	Acetylation	IIGDRQTGKTSIAID EEECCCCCCEEEEHH	23.94	19608861
218	Ubiquitination	IGDRQTGKTSIAIDT EECCCCCCEEEEHHH	42.35	-
219	Phosphorylation	GDRQTGKTSIAIDTI ECCCCCCEEEEHHHH	27.06	20068231
220	Phosphorylation	DRQTGKTSIAIDTII CCCCCCEEEEHHHHH	17.32	20068231
225	O-linked_Glycosylation	KTSIAIDTIINQKRF CEEEEHHHHHCCCCC	20.04	26374642
225	Phosphorylation	KTSIAIDTIINQKRF CEEEEHHHHHCCCCC	20.04	20068231
230	Ubiquitination	IDTIINQKRFNDGSD HHHHHCCCCCCCCCH	55.24	21890473
230	2-Hydroxyisobutyrylation	IDTIINQKRFNDGSD HHHHHCCCCCCCCCH	55.24	-
230	Acetylation	IDTIINQKRFNDGSD HHHHHCCCCCCCCCH	55.24	23954790
230	Succinylation	IDTIINQKRFNDGSD HHHHHCCCCCCCCCH	55.24	-
230	Succinylation	IDTIINQKRFNDGSD HHHHHCCCCCCCCCH	55.24	27452117
230	Ubiquitination	IDTIINQKRFNDGSD HHHHHCCCCCCCCCH	55.24	21890473
236	Phosphorylation	QKRFNDGSDEKKKLY CCCCCCCCHHHCEEE	45.52	26437602
239	Ubiquitination	FNDGSDEKKKLYCIY CCCCCHHHCEEEEEE	61.26	21906983
239	Acetylation	FNDGSDEKKKLYCIY CCCCCHHHCEEEEEE	61.26	23749302
239	Succinylation	FNDGSDEKKKLYCIY CCCCCHHHCEEEEEE	61.26	-
239	Succinylation	FNDGSDEKKKLYCIY CCCCCHHHCEEEEEE	61.26	23954790
240	Acetylation	NDGSDEKKKLYCIYV CCCCHHHCEEEEEEE	46.06	25953088
241	Acetylation	DGSDEKKKLYCIYVA CCCHHHCEEEEEEEE	56.61	26051181
243	Phosphorylation	SDEKKKLYCIYVAIG CHHHCEEEEEEEECC	5.91	23401153
244	S-nitrosylation	DEKKKLYCIYVAIGQ HHHCEEEEEEEECCC	2.34	24105792
244	S-palmitoylation	DEKKKLYCIYVAIGQ HHHCEEEEEEEECCC	2.34	29575903
246	Phosphorylation	KKKLYCIYVAIGQKR HCEEEEEEEECCCCH	4.73	28152594
254	Phosphorylation	VAIGQKRSTVAQLVK EECCCCHHHHHHHHH	33.98	28258704
255	Acetylation	AIGQKRSTVAQLVKR ECCCCHHHHHHHHHH	24.72	19608861
255	Phosphorylation	AIGQKRSTVAQLVKR ECCCCHHHHHHHHHH	24.72	28258704
255	Ubiquitination	AIGQKRSTVAQLVKR ECCCCHHHHHHHHHH	24.72	19608861
261	2-Hydroxyisobutyrylation	STVAQLVKRLTDADA HHHHHHHHHCCHHHH	50.73	-
261	Acetylation	STVAQLVKRLTDADA HHHHHHHHHCCHHHH	50.73	19608861
261	Malonylation	STVAQLVKRLTDADA HHHHHHHHHCCHHHH	50.73	26320211
261	Succinylation	STVAQLVKRLTDADA HHHHHHHHHCCHHHH	50.73	-
261	Succinylation	STVAQLVKRLTDADA HHHHHHHHHCCHHHH	50.73	-
261	Ubiquitination	STVAQLVKRLTDADA HHHHHHHHHCCHHHH	50.73	19608861
264	Phosphorylation	AQLVKRLTDADAMKY HHHHHHCCHHHHCCE	32.92	21406692
270	Acetylation	LTDADAMKYTIVVSA CCHHHHCCEEEEEEE	40.75	25038526
283	Ubiquitination	SATASDAAPLQYLAP EEECCCCCCCHHHHC	15.44	21906983
283	Acetylation	SATASDAAPLQYLAP EEECCCCCCCHHHHC	15.44	19608861
283	Ubiquitination	SATASDAAPLQYLAP EEECCCCCCCHHHHC	15.44	19608861
294	Ubiquitination	YLAPYSGCSMGEYFR HHHCCCCCCHHHHHH	1.76	21890473
294	Ubiquitination	YLAPYSGCSMGEYFR HHHCCCCCCHHHHHH	1.76	-
294	Glutathionylation	YLAPYSGCSMGEYFR HHHCCCCCCHHHHHH	1.76	22833525
299	Phosphorylation	SGCSMGEYFRDNGKH CCCCHHHHHHHCCCE	9.74	-
305	2-Hydroxyisobutyrylation	EYFRDNGKHALIIYD HHHHHCCCEEEEEEE	31.77	-
305	Acetylation	EYFRDNGKHALIIYD HHHHHCCCEEEEEEE	31.77	23954790
305	Succinylation	EYFRDNGKHALIIYD HHHHHCCCEEEEEEE	31.77	-
305	Succinylation	EYFRDNGKHALIIYD HHHHHCCCEEEEEEE	31.77	19608861
305	Ubiquitination	EYFRDNGKHALIIYD HHHHHCCCEEEEEEE	31.77	19608861
311	Phosphorylation	GKHALIIYDDLSKQA CCEEEEEEECHHHHH	9.08	28152594
315	Phosphorylation	LIIYDDLSKQAVAYR EEEEECHHHHHHHHH	29.71	28152594
316	Ubiquitination	IIYDDLSKQAVAYRQ EEEECHHHHHHHHHH	49.96	21890473
316	Ubiquitination	IIYDDLSKQAVAYRQ EEEECHHHHHHHHHH	49.96	21890473
337	Phosphorylation	RPPGREAYPGDVFYL CCCCCCCCCCCHHHH	11.73	28152594
343	Phosphorylation	AYPGDVFYLHSRLLE CCCCCHHHHHHHHHH	11.89	28152594
346	Phosphorylation	GDVFYLHSRLLERAA CCHHHHHHHHHHHHH	23.25	23186163
363	Phosphorylation	NDAFGGGSLTALPVI CCCCCCCCCCEECEE	26.31	20068231
383	O-linked_Glycosylation	DVSAYIPTNVISITD CEEEEECCCEEEECC	32.34	26374642
384	Acetylation	VSAYIPTNVISITDG EEEEECCCEEEECCC	24.62	19608861
384	Ubiquitination	VSAYIPTNVISITDG EEEEECCCEEEECCC	24.62	19608861
405	Ubiquitination	ELFYKGIRPAINVGL HHHHCCCHHHHCCCC	24.22	-
412	Ubiquitination	RPAINVGLSVSRVGS HHHHCCCCCHHHCCH	3.88	21890473
412	Acetylation	RPAINVGLSVSRVGS HHHHCCCCCHHHCCH	3.88	-
412	Ubiquitination	RPAINVGLSVSRVGS HHHHCCCCCHHHCCH	3.88	-
412	Acetylation	RPAINVGLSVSRVGS HHHHCCCCCHHHCCH	3.88	19608861
412	Ubiquitination	RPAINVGLSVSRVGS HHHHCCCCCHHHCCH	3.88	19608861
413	Phosphorylation	PAINVGLSVSRVGSA HHHCCCCCHHHCCHH	16.47	20068231
415	Phosphorylation	INVGLSVSRVGSAAQ HCCCCCHHHCCHHHH	20.20	20068231
419	Phosphorylation	LSVSRVGSAAQTRAM CCHHHCCHHHHHHHH	19.99	20068231
423	Phosphorylation	RVGSAAQTRAMKQVA HCCHHHHHHHHHHHH	18.70	21406692
427	2-Hydroxyisobutyrylation	AAQTRAMKQVAGTMK HHHHHHHHHHHHCHH	40.41	-
427	Acetylation	AAQTRAMKQVAGTMK HHHHHHHHHHHHCHH	40.41	25953088
427	Malonylation	AAQTRAMKQVAGTMK HHHHHHHHHHHHCHH	40.41	26320211
427	Succinylation	AAQTRAMKQVAGTMK HHHHHHHHHHHHCHH	40.41	-
427	Succinylation	AAQTRAMKQVAGTMK HHHHHHHHHHHHCHH	40.41	27452117
427	Ubiquitination	AAQTRAMKQVAGTMK HHHHHHHHHHHHCHH	40.41	-
432	O-linked_Glycosylation	AMKQVAGTMKLELAQ HHHHHHHCHHHHHHH	11.03	26374642
432	Phosphorylation	AMKQVAGTMKLELAQ HHHHHHHCHHHHHHH	11.03	20068231
434	Ubiquitination	KQVAGTMKLELAQYR HHHHHCHHHHHHHHH	38.35	21890473
434	2-Hydroxyisobutyrylation	KQVAGTMKLELAQYR HHHHHCHHHHHHHHH	38.35	-
434	Acetylation	KQVAGTMKLELAQYR HHHHHCHHHHHHHHH	38.35	19608861
434	Malonylation	KQVAGTMKLELAQYR HHHHHCHHHHHHHHH	38.35	26320211
434	Ubiquitination	KQVAGTMKLELAQYR HHHHHCHHHHHHHHH	38.35	21890473
440	Nitration	MKLELAQYREVAAFA HHHHHHHHHHHHHHH	11.79	-
440	Phosphorylation	MKLELAQYREVAAFA HHHHHHHHHHHHHHH	11.79	30387612
448	Acetylation	REVAAFAQFGSDLDA HHHHHHHCCCCCHHH	36.46	19608861
448	Ubiquitination	REVAAFAQFGSDLDA HHHHHHHCCCCCHHH	36.46	19608861
450	Ubiquitination	VAAFAQFGSDLDAAT HHHHHCCCCCHHHHH	14.26	-
451	Phosphorylation	AAFAQFGSDLDAATQ HHHHCCCCCHHHHHH	35.97	28450419
456	Acetylation	FGSDLDAATQQLLSR CCCCHHHHHHHHHHH	12.95	19608861
457	Phosphorylation	GSDLDAATQQLLSRG CCCHHHHHHHHHHHC	20.69	28450419
462	Phosphorylation	AATQQLLSRGVRLTE HHHHHHHHHCCHHHH	35.26	28450419
472	Ubiquitination	VRLTELLKQGQYSPM CHHHHHHHCCCCCCC	66.07	-
476	Ubiquitination	ELLKQGQYSPMAIEE HHHHCCCCCCCCHHH	22.90	21890473
476	Acetylation	ELLKQGQYSPMAIEE HHHHCCCCCCCCHHH	22.90	-
476	Ubiquitination	ELLKQGQYSPMAIEE HHHHCCCCCCCCHHH	22.90	-
476	Acetylation	ELLKQGQYSPMAIEE HHHHCCCCCCCCHHH	22.90	19608861
476	Phosphorylation	ELLKQGQYSPMAIEE HHHHCCCCCCCCHHH	22.90	26503514
476	Ubiquitination	ELLKQGQYSPMAIEE HHHHCCCCCCCCHHH	22.90	19608861
477	Phosphorylation	LLKQGQYSPMAIEEQ HHHCCCCCCCCHHHH	10.58	26503514
484	Ubiquitination	SPMAIEEQVAVIYAG CCCCHHHHHHHHHHH	18.71	-
484	Acetylation	SPMAIEEQVAVIYAG CCCCHHHHHHHHHHH	18.71	19608861
489	Acetylation	EEQVAVIYAGVRGYL HHHHHHHHHHHHHHH	7.24	19608861
489	Phosphorylation	EEQVAVIYAGVRGYL HHHHHHHHHHHHHHH	7.24	26503514
489	Ubiquitination	EEQVAVIYAGVRGYL HHHHHHHHHHHHHHH	7.24	19608861
495	Phosphorylation	IYAGVRGYLDKLEPS HHHHHHHHHHHCCHH	10.93	28152594
498	Ubiquitination	GVRGYLDKLEPSKIT HHHHHHHHCCHHHCH	52.75	21890473
498	2-Hydroxyisobutyrylation	GVRGYLDKLEPSKIT HHHHHHHHCCHHHCH	52.75	-
498	Acetylation	GVRGYLDKLEPSKIT HHHHHHHHCCHHHCH	52.75	19608861
498	Malonylation	GVRGYLDKLEPSKIT HHHHHHHHCCHHHCH	52.75	26320211
498	Succinylation	GVRGYLDKLEPSKIT HHHHHHHHCCHHHCH	52.75	-
498	Succinylation	GVRGYLDKLEPSKIT HHHHHHHHCCHHHCH	52.75	-
498	Ubiquitination	GVRGYLDKLEPSKIT HHHHHHHHCCHHHCH	52.75	21890473
502	Phosphorylation	YLDKLEPSKITKFEN HHHHCCHHHCHHHHH	27.58	23312004
503	Acetylation	LDKLEPSKITKFENA HHHCCHHHCHHHHHH	66.17	25038526
503	Malonylation	LDKLEPSKITKFENA HHHCCHHHCHHHHHH	66.17	26320211
505	Phosphorylation	KLEPSKITKFENAFL HCCHHHCHHHHHHHH	33.16	23312004
506	2-Hydroxyisobutyrylation	LEPSKITKFENAFLS CCHHHCHHHHHHHHH	54.90	-
506	Acetylation	LEPSKITKFENAFLS CCHHHCHHHHHHHHH	54.90	19608861
506	Succinylation	LEPSKITKFENAFLS CCHHHCHHHHHHHHH	54.90	-
506	Succinylation	LEPSKITKFENAFLS CCHHHCHHHHHHHHH	54.90	-
506	Ubiquitination	LEPSKITKFENAFLS CCHHHCHHHHHHHHH	54.90	19608861
509	Acetylation	SKITKFENAFLSHVV HHCHHHHHHHHHHHH	38.84	-
509	Ubiquitination	SKITKFENAFLSHVV HHCHHHHHHHHHHHH	38.84	21906983
513	Phosphorylation	KFENAFLSHVVSQHQ HHHHHHHHHHHHHHH	14.05	24247654
517	Acetylation	AFLSHVVSQHQALLG HHHHHHHHHHHHHHH	22.36	-
517	Ubiquitination	AFLSHVVSQHQALLG HHHHHHHHHHHHHHH	22.36	21906983
517	Acetylation	AFLSHVVSQHQALLG HHHHHHHHHHHHHHH	22.36	19608861
517	Phosphorylation	AFLSHVVSQHQALLG HHHHHHHHHHHHHHH	22.36	26437602
517	Ubiquitination	AFLSHVVSQHQALLG HHHHHHHHHHHHHHH	22.36	19608861
519	Ubiquitination	LSHVVSQHQALLGTI HHHHHHHHHHHHHHH	13.84	-
525	Phosphorylation	QHQALLGTIRADGKI HHHHHHHHHHCCCCC	13.78	26437602
531	Acetylation	GTIRADGKISEQSDA HHHHCCCCCCCCCHH	43.54	23954790
531	Malonylation	GTIRADGKISEQSDA HHHHCCCCCCCCCHH	43.54	26320211
531	Succinylation	GTIRADGKISEQSDA HHHHCCCCCCCCCHH	43.54	-
531	Succinylation	GTIRADGKISEQSDA HHHHCCCCCCCCCHH	43.54	-
531	Ubiquitination	GTIRADGKISEQSDA HHHHCCCCCCCCCHH	43.54	21906983
539	2-Hydroxyisobutyrylation	ISEQSDAKLKEIVTN CCCCCHHHHHHHHHH	66.15	-
539	Acetylation	ISEQSDAKLKEIVTN CCCCCHHHHHHHHHH	66.15	19608861
539	Succinylation	ISEQSDAKLKEIVTN CCCCCHHHHHHHHHH	66.15	-
539	Succinylation	ISEQSDAKLKEIVTN CCCCCHHHHHHHHHH	66.15	27452117
539	Ubiquitination	ISEQSDAKLKEIVTN CCCCCHHHHHHHHHH	66.15	19608861
541	2-Hydroxyisobutyrylation	EQSDAKLKEIVTNFL CCCHHHHHHHHHHHH	44.69	-
541	Acetylation	EQSDAKLKEIVTNFL CCCHHHHHHHHHHHH	44.69	25038526
541	Ubiquitination	EQSDAKLKEIVTNFL CCCHHHHHHHHHHHH	44.69	-

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATPA_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 ATPA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
A4_HUMAN	APP	physical	21832049
ATPB_HUMAN	ATP5B	physical	22939629
ATPG_HUMAN	ATP5C1	physical	22939629
ATPD_HUMAN	ATP5D	physical	22939629
ATPO_HUMAN	ATP5O	physical	22939629
CY1_HUMAN	CYC1	physical	22939629
VATA_HUMAN	ATP6V1A	physical	22939629
RL18_HUMAN	RPL18	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
HS90B_HUMAN	HSP90AB1	physical	22939629
PDIA1_HUMAN	P4HB	physical	22939629
STML2_HUMAN	STOML2	physical	22939629
RS3_HUMAN	RPS3	physical	22939629
MDHM_HUMAN	MDH2	physical	22939629
PAIRB_HUMAN	SERBP1	physical	22939629
PGK1_HUMAN	PGK1	physical	22939629
MYH9_HUMAN	MYH9	physical	22939629
FLOT1_HUMAN	FLOT1	physical	22939629
RPN2_HUMAN	RPN2	physical	22939629
GRP78_HUMAN	HSPA5	physical	22939629
HS71L_HUMAN	HSPA1L	physical	22939629
RS15A_HUMAN	RPS15A	physical	22939629
BASP1_HUMAN	BASP1	physical	22939629
PABP1_HUMAN	PABPC1	physical	22939629
IF4A1_HUMAN	EIF4A1	physical	22939629
KS6B2_HUMAN	RPS6KB2	physical	21988832
ATPB_HUMAN	ATP5B	physical	25416956
ATPG_HUMAN	ATP5C1	physical	26344197
AT5F1_HUMAN	ATP5F1	physical	26344197
ATP5H_HUMAN	ATP5H	physical	26344197
ATP5I_HUMAN	ATP5I	physical	26344197
ATPK_HUMAN	ATP5J2	physical	26344197
HNRPU_HUMAN	HNRNPU	physical	26344197
MATR3_HUMAN	MATR3	physical	26344197
MTCH1_HUMAN	MTCH1	physical	26344197
MTCH2_HUMAN	MTCH2	physical	26344197
NDUS4_HUMAN	NDUFS4	physical	26344197
RER1_HUMAN	RER1	physical	26344197
RPN1_HUMAN	RPN1	physical	26344197
SSRD_HUMAN	SSR4	physical	26344197
TSPO_HUMAN	TSPO	physical	26344197
ATPF2_HUMAN	ATPAF2	physical	27499296
NRDC_HUMAN	NRD1	physical	27499296
USMG5_HUMAN	USMG5	physical	27499296
ATP5I_HUMAN	ATP5I	physical	27499296
ATP5H_HUMAN	ATP5H	physical	27499296
MPPB_HUMAN	PMPCB	physical	27499296
ATP5E_HUMAN	ATP5E	physical	27499296
OPA3_HUMAN	OPA3	physical	27499296
ATPO_HUMAN	ATP5O	physical	27499296
AT5F1_HUMAN	ATP5F1	physical	27499296
MPPA_HUMAN	PMPCA	physical	27499296
ECH1_HUMAN	ECH1	physical	27499296
ATPG_HUMAN	ATP5C1	physical	27499296
ATPA_HUMAN	ATP5A1	physical	27499296
ATP5J_HUMAN	ATP5J	physical	27499296
PDIP2_HUMAN	POLDIP2	physical	27499296
RM46_HUMAN	MRPL46	physical	27499296
CHCH2_HUMAN	CHCHD2	physical	27499296
CLPX_HUMAN	CLPX	physical	27499296
BACH_HUMAN	ACOT7	physical	27499296
SFXN1_HUMAN	SFXN1	physical	27499296
GLRX5_HUMAN	GLRX5	physical	27499296
ODBA_HUMAN	BCKDHA	physical	27499296
DDAH1_HUMAN	DDAH1	physical	27499296
MIC60_HUMAN	IMMT	physical	27499296
C1QBP_HUMAN	C1QBP	physical	27499296
ETFA_HUMAN	ETFA	physical	27499296
ACPM_HUMAN	NDUFAB1	physical	27499296
IDE_HUMAN	IDE	physical	27499296
FACD2_HUMAN	FANCD2	physical	28687786

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 616045: Combined oxidative phosphorylation deficiency 22 (COXPD22)
• 615228: Mitochondrial complex V deficiency, nuclear 4 (MC5DN4)
• 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-161; LYS-261; LYS-305;LYS-434; LYS-498; LYS-506 AND LYS-539, AND MASS SPECTROMETRY.
PubMed: 19608861