ATPA_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATPA_ARATH
• UniProt AC: P56757
• Protein Name: ATP synthase subunit alpha, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01346}
• Gene Name: atpA {ECO:0000255|HAMAP-Rule:MF_01346}
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 507
• Subcellular Localization: Plastid, chloroplast thylakoid membrane ; Peripheral membrane protein .
• Protein Description: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit..
• Protein Sequence: MVTIRADEISNIIRERIEQYNREVTIVNTGTVLQVGDGIARIYGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVINALANPIDGRGKISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVAQVVTSLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYREQHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQLGEGSMTALPIVETQSGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAAQIKAMKQVAGKLKLELAQFAELEAFSQFSSDLDKATQNQLARGQRLRELLKQSQSAPLTVEEQIMTIYTGTNGYLDGLEIGQVRKFLVQLRTYLKTNKPQFQEIIASTKTLTAEAESFLKEGIQEQLERFLLQEKV

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
10	Phosphorylation	TIRADEISNIIRERI EECHHHHHHHHHHHH	21.67	30291188
20	Nitration	IRERIEQYNREVTIV HHHHHHHHCCEEEEE	11.91	-
101	Phosphorylation	KIAQIPVSEAYLGRV EEEECCCCHHHHHHH	15.91	30291188
104	Nitration	QIPVSEAYLGRVINA ECCCCHHHHHHHHHH	12.97	-
123	Phosphorylation	IDGRGKISASESRLI CCCCCCCCHHHHHHH	29.27	29654922
125	Phosphorylation	GRGKISASESRLIES CCCCCCHHHHHHHCC	29.34	19376835
127	Phosphorylation	GKISASESRLIESPA CCCCHHHHHHHCCCC	29.86	28295753
132	Phosphorylation	SESRLIESPAPGIIS HHHHHHCCCCCCCCC	21.26	22092075
139	Phosphorylation	SPAPGIISRRSVYEP CCCCCCCCCCCCCCC	21.52	29654922
144	Nitration	IISRRSVYEPLQTGL CCCCCCCCCCCCCCC	17.05	-
204	Phosphorylation	VAIGQKASSVAQVVT EEECCHHHHHHHHHH	32.17	25561503
205	Phosphorylation	AIGQKASSVAQVVTS EECCHHHHHHHHHHH	26.74	29654922
252	Nitration	ALAEYFMYREQHTLI HHHHHHHHHHCCEEE	10.91	-
257	Phosphorylation	FMYREQHTLIIYDDL HHHHHCCEEEEECCH	21.24	22092075
261	Nitration	EQHTLIIYDDLSKQA HCCEEEEECCHHHHH	9.08	-
271	Nitration	LSKQAQAYRQMSLLL HHHHHHHHHHHHHHH	6.84	-
275	Phosphorylation	AQAYRQMSLLLRRPP HHHHHHHHHHHCCCC	13.92	29654922
287	Nitration	RPPGREAYPGDVFYL CCCCCCCCCCCHHHH	11.73	-
287	Phosphorylation	RPPGREAYPGDVFYL CCCCCCCCCCCHHHH	11.73	22092075
293	Nitration	AYPGDVFYLHSRLLE CCCCCHHHHHHHHHH	11.89	-
478	Phosphorylation	QFQEIIASTKTLTAE HHHHHHHHCCCCHHH	21.74	25561503
479	Phosphorylation	FQEIIASTKTLTAEA HHHHHHHCCCCHHHH	21.01	25561503
488	Phosphorylation	TLTAEAESFLKEGIQ CCHHHHHHHHHHHHH	42.82	30291188

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATPA_ARATH !!

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_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ATPB_ARATH	atpB	physical	25775508

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY.
PubMed: 19376835