dbPTM

ATPA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATPA_MOUSE
UniProt AC	Q03265
Protein Name	ATP synthase subunit alpha, mitochondrial {ECO:0000305}
Gene Name	Atp5f1a {ECO:0000250\|UniProtKB:P25705}
Organism	Mus musculus (Mouse).
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.
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	MLSVRVAAAVARALPRRAGLVSKNALGSSFVGARNLHASNTRLQKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDVVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDSFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQSLLGNIRSDGKISEQSDAKLKEIVTNFLAGFEP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
44	Pyrrolidone_carboxylic_acid	HASNTRLQKTGTAEM CCCCCCCCCCCCCHH	37.66	-
45	Succinylation	ASNTRLQKTGTAEMS CCCCCCCCCCCCHHH	54.22	24315375
45	Ubiquitination	ASNTRLQKTGTAEMS CCCCCCCCCCCCHHH	54.22	-
46	Phosphorylation	SNTRLQKTGTAEMSS CCCCCCCCCCCHHHH	27.14	20495213
48	Phosphorylation	TRLQKTGTAEMSSIL CCCCCCCCCHHHHHH	25.36	27180971
52	Phosphorylation	KTGTAEMSSILEERI CCCCCHHHHHHHHHH	13.01	27742792
53	Phosphorylation	TGTAEMSSILEERIL CCCCHHHHHHHHHHC	29.86	25521595
64	Phosphorylation	ERILGADTSVDLEET HHHCCCCCEECHHHH	30.07	26525534
65	Phosphorylation	RILGADTSVDLEETG HHCCCCCEECHHHHC	17.74	26824392
71	Phosphorylation	TSVDLEETGRVLSIG CEECHHHHCCEEEEC	22.40	28066266
76	O-linked_Glycosylation	EETGRVLSIGDGIAR HHHCCEEEECCCHHH	22.97	-
76	Phosphorylation	EETGRVLSIGDGIAR HHHCCEEEECCCHHH	22.97	26824392
106	Phosphorylation	SSGLKGMSLNLEPDN CCCCCCCCCCCCCCC	23.83	20495213
123	Acetylation	VVVFGNDKLIKEGDV EEEECCCCEECCCCE	56.99	23576753
123	Succinylation	VVVFGNDKLIKEGDV EEEECCCCEECCCCE	56.99	24315375
123	Ubiquitination	VVVFGNDKLIKEGDV EEEECCCCEECCCCE	56.99	-
126	Acetylation	FGNDKLIKEGDVVKR ECCCCEECCCCEEEE	67.11	23576753
126	Malonylation	FGNDKLIKEGDVVKR ECCCCEECCCCEEEE	67.11	26320211
126	Succinylation	FGNDKLIKEGDVVKR ECCCCEECCCCEEEE	67.11	26388266
126	Ubiquitination	FGNDKLIKEGDVVKR ECCCCEECCCCEEEE	67.11	27667366
132	Acetylation	IKEGDVVKRTGAIVD ECCCCEEEECCCEEE	44.05	23576753
132	Succinylation	IKEGDVVKRTGAIVD ECCCCEEEECCCEEE	44.05	26388266
132	Ubiquitination	IKEGDVVKRTGAIVD ECCCCEEEECCCEEE	44.05	27667366
134	Phosphorylation	EGDVVKRTGAIVDVP CCCEEEECCCEEEEE	25.83	-
161	Acetylation	LGNAIDGKGPIGSKT HHHHCCCCCCCCCCH	58.74	23576753
161	Glutarylation	LGNAIDGKGPIGSKT HHHHCCCCCCCCCCH	58.74	24703693
161	Malonylation	LGNAIDGKGPIGSKT HHHHCCCCCCCCCCH	58.74	26320211
161	Succinylation	LGNAIDGKGPIGSKT HHHHCCCCCCCCCCH	58.74	-
161	Succinylation	LGNAIDGKGPIGSKT HHHHCCCCCCCCCCH	58.74	23806337
161	Ubiquitination	LGNAIDGKGPIGSKT HHHHCCCCCCCCCCH	58.74	27667366
166	Phosphorylation	DGKGPIGSKTRRRVG CCCCCCCCCHHCCCC	31.41	25266776
167	Acetylation	GKGPIGSKTRRRVGL CCCCCCCCHHCCCCC	40.62	23576753
167	Malonylation	GKGPIGSKTRRRVGL CCCCCCCCHHCCCCC	40.62	26320211
167	Succinylation	GKGPIGSKTRRRVGL CCCCCCCCHHCCCCC	40.62	-
167	Succinylation	GKGPIGSKTRRRVGL CCCCCCCCHHCCCCC	40.62	23806337
167	Ubiquitination	GKGPIGSKTRRRVGL CCCCCCCCHHCCCCC	40.62	27667366
168	Phosphorylation	KGPIGSKTRRRVGLK CCCCCCCHHCCCCCC	30.98	19060867
175	Acetylation	TRRRVGLKAPGIIPR HHCCCCCCCCCCCCC	46.75	24062335
175	Succinylation	TRRRVGLKAPGIIPR HHCCCCCCCCCCCCC	46.75	26388266
175	Ubiquitination	TRRRVGLKAPGIIPR HHCCCCCCCCCCCCC	46.75	27667366
184	Phosphorylation	PGIIPRISVREPMQT CCCCCCEECCCCCCC	19.19	25521595
194	Acetylation	EPMQTGIKAVDSLVP CCCCCCCCHHHHCCC	43.64	22826441
194	Succinylation	EPMQTGIKAVDSLVP CCCCCCCCHHHHCCC	43.64	26388266
194	Ubiquitination	EPMQTGIKAVDSLVP CCCCCCCCHHHHCCC	43.64	27667366
204	Methylation	DSLVPIGRGQRELII HHCCCCCCCCCEEEE	38.50	24129315
218	Ubiquitination	IGDRQTGKTSIAIDT EECCCCCCEEEEHHH	42.35	22790023
219	Phosphorylation	GDRQTGKTSIAIDTI ECCCCCCEEEEHHHH	27.06	21183079
230	Acetylation	IDTIINQKRFNDGTD HHHHHCCCCCCCCCC	55.24	23576753
230	Succinylation	IDTIINQKRFNDGTD HHHHHCCCCCCCCCC	55.24	-
230	Succinylation	IDTIINQKRFNDGTD HHHHHCCCCCCCCCC	55.24	23806337
230	Ubiquitination	IDTIINQKRFNDGTD HHHHHCCCCCCCCCC	55.24	-
236	Phosphorylation	QKRFNDGTDEKKKLY CCCCCCCCCHHCEEE	43.80	22817900
239	Acetylation	FNDGTDEKKKLYCIY CCCCCCHHCEEEEEE	59.00	23576753
239	Glutarylation	FNDGTDEKKKLYCIY CCCCCCHHCEEEEEE	59.00	24703693
239	Succinylation	FNDGTDEKKKLYCIY CCCCCCHHCEEEEEE	59.00	-
239	Succinylation	FNDGTDEKKKLYCIY CCCCCCHHCEEEEEE	59.00	23806337
240	Acetylation	NDGTDEKKKLYCIYV CCCCCHHCEEEEEEE	46.06	23576753
240	Succinylation	NDGTDEKKKLYCIYV CCCCCHHCEEEEEEE	46.06	26388266
241	Acetylation	DGTDEKKKLYCIYVA CCCCHHCEEEEEEEE	56.61	24062335
243	Phosphorylation	TDEKKKLYCIYVAIG CCHHCEEEEEEEECC	5.91	25195567
244	S-nitrosocysteine	DEKKKLYCIYVAIGQ CHHCEEEEEEEECCC	2.34	-
244	S-nitrosylation	DEKKKLYCIYVAIGQ CHHCEEEEEEEECCC	2.34	22178444
244	S-palmitoylation	DEKKKLYCIYVAIGQ CHHCEEEEEEEECCC	2.34	28526873
246	Phosphorylation	KKKLYCIYVAIGQKR HCEEEEEEEECCCCH	4.73	-
254	Phosphorylation	VAIGQKRSTVAQLVK EECCCCHHHHHHHHH	33.98	24899341
255	Phosphorylation	AIGQKRSTVAQLVKR ECCCCHHHHHHHHHH	24.72	24899341
261	Acetylation	STVAQLVKRLTDADA HHHHHHHHHCCHHHH	50.73	23576753
261	Glutarylation	STVAQLVKRLTDADA HHHHHHHHHCCHHHH	50.73	24703693
261	Malonylation	STVAQLVKRLTDADA HHHHHHHHHCCHHHH	50.73	26320211
261	Succinylation	STVAQLVKRLTDADA HHHHHHHHHCCHHHH	50.73	-
261	Succinylation	STVAQLVKRLTDADA HHHHHHHHHCCHHHH	50.73	23806337
261	Ubiquitination	STVAQLVKRLTDADA HHHHHHHHHCCHHHH	50.73	-
264	Phosphorylation	AQLVKRLTDADAMKY HHHHHHCCHHHHCCE	32.92	24899341
270	Acetylation	LTDADAMKYTIVVSA CCHHHHCCEEEEEEE	40.75	23864654
271	Nitration	TDADAMKYTIVVSAT CHHHHCCEEEEEEEE	6.65	-
294	S-nitrosocysteine	YLAPYSGCSMGEYFR HHHCCCCCCHHHHHH	1.76	-
294	S-nitrosylation	YLAPYSGCSMGEYFR HHHCCCCCCHHHHHH	1.76	21278135
305	Acetylation	EYFRDNGKHALIIYD HHHHHCCCEEEEEEE	31.77	23576753
305	Succinylation	EYFRDNGKHALIIYD HHHHHCCCEEEEEEE	31.77	-
305	Succinylation	EYFRDNGKHALIIYD HHHHHCCCEEEEEEE	31.77	23806337
305	Ubiquitination	EYFRDNGKHALIIYD HHHHHCCCEEEEEEE	31.77	-
311	Nitration	GKHALIIYDDLSKQA CCEEEEEEECHHHHH	9.08	-
315	Phosphorylation	LIIYDDLSKQAVAYR EEEEECHHHHHHHHH	29.71	22817900
316	Acetylation	IIYDDLSKQAVAYRQ EEEECHHHHHHHHHH	49.96	23864654
337	Phosphorylation	RPPGREAYPGDVFYL CCCCCCCCCCCHHHH	11.73	-
343	Phosphorylation	AYPGDVFYLHSRLLE CCCCCHHHHHHHHHH	11.89	25195567
419	Phosphorylation	LSVSRVGSAAQTRAM CCHHHCCHHHHHHHH	19.99	24899341
427	Acetylation	AAQTRAMKQVAGTMK HHHHHHHHHHHHCHH	40.41	23576753
427	Glutarylation	AAQTRAMKQVAGTMK HHHHHHHHHHHHCHH	40.41	24703693
427	Malonylation	AAQTRAMKQVAGTMK HHHHHHHHHHHHCHH	40.41	26320211
427	Succinylation	AAQTRAMKQVAGTMK HHHHHHHHHHHHCHH	40.41	-
427	Succinylation	AAQTRAMKQVAGTMK HHHHHHHHHHHHCHH	40.41	23806337
427	Ubiquitination	AAQTRAMKQVAGTMK HHHHHHHHHHHHCHH	40.41	27667366
432	Phosphorylation	AMKQVAGTMKLELAQ HHHHHHHCHHHHHHH	11.03	22817900
434	Acetylation	KQVAGTMKLELAQYR HHHHHCHHHHHHHHH	38.35	23576753
434	Ubiquitination	KQVAGTMKLELAQYR HHHHHCHHHHHHHHH	38.35	22790023
451	Phosphorylation	AAFAQFGSDLDAATQ HHHHCCCCCHHHHHH	35.97	23737553
457	Phosphorylation	GSDLDAATQQLLSRG CCCHHHHHHHHHHHC	20.69	20415495
472	Acetylation	VRLTELLKQGQYSPM CHHHHHHHCCCCCCC	66.07	23864654
476	Nitration	ELLKQGQYSPMAIEE HHHHCCCCCCCCHHH	22.90	-
498	Acetylation	GVRGYLDKLEPSKIT HHHHHHHHCCHHHCH	52.75	23806337
498	Glutarylation	GVRGYLDKLEPSKIT HHHHHHHHCCHHHCH	52.75	24703693
498	Malonylation	GVRGYLDKLEPSKIT HHHHHHHHCCHHHCH	52.75	26320211
498	Succinylation	GVRGYLDKLEPSKIT HHHHHHHHCCHHHCH	52.75	-
498	Succinylation	GVRGYLDKLEPSKIT HHHHHHHHCCHHHCH	52.75	23806337
498	Ubiquitination	GVRGYLDKLEPSKIT HHHHHHHHCCHHHCH	52.75	27667366
502	Phosphorylation	YLDKLEPSKITKFEN HHHHCCHHHCHHHHH	27.58	23140645
503	Acetylation	LDKLEPSKITKFENA HHHCCHHHCHHHHHH	66.17	23864654
503	Ubiquitination	LDKLEPSKITKFENA HHHCCHHHCHHHHHH	66.17	22790023
506	Acetylation	LEPSKITKFENAFLS CCHHHCHHHHHHHHH	54.90	23576753
506	Succinylation	LEPSKITKFENAFLS CCHHHCHHHHHHHHH	54.90	-
506	Succinylation	LEPSKITKFENAFLS CCHHHCHHHHHHHHH	54.90	23806337
513	Phosphorylation	KFENAFLSHVISQHQ HHHHHHHHHHHHHCH	14.84	23140645
517	Phosphorylation	AFLSHVISQHQSLLG HHHHHHHHHCHHHHC	22.11	21743459
521	Phosphorylation	HVISQHQSLLGNIRS HHHHHCHHHHCCCCC	24.36	21082442
528	Phosphorylation	SLLGNIRSDGKISEQ HHHCCCCCCCCCCCC	47.09	21183079
531	Acetylation	GNIRSDGKISEQSDA CCCCCCCCCCCCCHH	48.31	23806337
531	Glutarylation	GNIRSDGKISEQSDA CCCCCCCCCCCCCHH	48.31	24703693
531	Malonylation	GNIRSDGKISEQSDA CCCCCCCCCCCCCHH	48.31	26073543
531	Succinylation	GNIRSDGKISEQSDA CCCCCCCCCCCCCHH	48.31	-
531	Succinylation	GNIRSDGKISEQSDA CCCCCCCCCCCCCHH	48.31	23806337
531	Ubiquitination	GNIRSDGKISEQSDA CCCCCCCCCCCCCHH	48.31	27667366
533	Phosphorylation	IRSDGKISEQSDAKL CCCCCCCCCCCHHHH	32.82	27742792
539	Acetylation	ISEQSDAKLKEIVTN CCCCCHHHHHHHHHH	66.15	23806337
539	Glutarylation	ISEQSDAKLKEIVTN CCCCCHHHHHHHHHH	66.15	24703693
539	Malonylation	ISEQSDAKLKEIVTN CCCCCHHHHHHHHHH	66.15	26073543
539	Succinylation	ISEQSDAKLKEIVTN CCCCCHHHHHHHHHH	66.15	-
539	Succinylation	ISEQSDAKLKEIVTN CCCCCHHHHHHHHHH	66.15	23806337
539	Ubiquitination	ISEQSDAKLKEIVTN CCCCCHHHHHHHHHH	66.15	27667366
541	Acetylation	EQSDAKLKEIVTNFL CCCHHHHHHHHHHHH	44.69	23576753
541	Succinylation	EQSDAKLKEIVTNFL CCCHHHHHHHHHHHH	44.69	26388266

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 ATPA_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
132	K	Acetylation	23576753
Acetylation of Lys-132, Lys-230 and Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice.
230	K	Acetylation	23806337
Acetylation of Lys-132, Lys-230 and Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice.
498	K	Acetylation	23806337
Acetylation of Lys-132, Lys-230 and Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice.

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 ATPA_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATPB_HUMAN	ATP5B	physical	26496610
ATPG_HUMAN	ATP5C1	physical	26496610
ATPD_HUMAN	ATP5D	physical	26496610
ATP5E_HUMAN	ATP5E	physical	26496610
AT5F1_HUMAN	ATP5F1	physical	26496610
ATP5J_HUMAN	ATP5J	physical	26496610
ATPO_HUMAN	ATP5O	physical	26496610
ATP5H_HUMAN	ATP5H	physical	26496610
NDUBB_HUMAN	NDUFB11	physical	26496610
E41LB_HUMAN	EPB41L4B	physical	26496610
MIC19_HUMAN	CHCHD3	physical	26496610
ATIF1_HUMAN	ATPIF1	physical	26496610

Drug and Disease Associations

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

Regulatory Network of ATPA_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132; LYS-230; LYS-239;LYS-261; LYS-305; LYS-427; LYS-498; LYS-531 AND LYS-539, AND MASSSPECTROMETRY.	16916647 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative analysis of both protein expression and serine /threonine post-translational modifications through stable isotopelabeling with dithiothreitol."; Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,Hart G.W., Burlingame A.L.; Proteomics 5:388-398(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASSSPECTROMETRY.	15648052 [Abstract]

show

show

show