ATPBM_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ATPBM_ARATH
• UniProt AC: P83483
• Protein Name: ATP synthase subunit beta-1, mitochondrial
• Gene Name: At5g08670
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 556
• Subcellular Localization: Mitochondrion . Mitochondrion inner membrane . Peripheral 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. 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..
• Protein Sequence: MASRRVLSSLLRSSSGRSAAKLGNRNPRLPSPSPARHAAPCSYLLGRVAEYATSSPASSAAPSSAPAKDEGKKTYDYGGKGAIGRVCQVIGAIVDVRFEDQEGLPPIMTSLEVQDHPTRLVLEVSHHLGQNVVRTIAMDGTEGLVRGRKVLNTGAPITVPVGRATLGRIMNVLGEPIDERGEIKTEHYLPIHRDAPALVDLATGQEILATGIKVVDLLAPYQRGGKIGLFGGAGVGKTVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKLGEKQSESKCALVYGQMNEPPGARARVGLTGLTVAEYFRDAEGQDVLLFIDNIFRFTQANSEVSALLGRIPSAVGYQPTLASDLGALQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRQISELGIYPAVDPLDSTSRMLSPHILGEEHYNTARGVQKVLQNYKNLQDIIAILGMDELSEDDKLTVARARKIQRFLSQPFHVAEIFTGAPGKYVDLKENINSFQGLLDGKYDDLSEQSFYMVGGIDEVVAKAEKIAKESAA

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
31	Phosphorylation	NRNPRLPSPSPARHA CCCCCCCCCCHHHCC	42.47	23328941
54	Phosphorylation	RVAEYATSSPASSAA HHHHHHHCCCCCCCC	26.59	23111157
58	Phosphorylation	YATSSPASSAAPSSA HHHCCCCCCCCCCCC	24.72	19880383
59	Phosphorylation	ATSSPASSAAPSSAP HHCCCCCCCCCCCCC	30.47	-
63	Phosphorylation	PASSAAPSSAPAKDE CCCCCCCCCCCCCCC	34.11	23111157
64	Phosphorylation	ASSAAPSSAPAKDEG CCCCCCCCCCCCCCC	36.89	-
108	Sulfoxidation	QEGLPPIMTSLEVQD CCCCCCCEEEEEECC	2.28	23289948
170	Sulfoxidation	RATLGRIMNVLGEPI HHHHHHHHHHHCCCC	2.46	23289948
184	Acetylation	IDERGEIKTEHYLPI CCCCCCCCCCEECCC	43.49	24727099
238	Phosphorylation	GGAGVGKTVLIMELI CCCCCCHHHHHHHHH	18.02	25368622
282	Acetylation	MIESGVIKLGEKQSE HHHHCCCCCCCCCCC	48.29	24727099
286	Acetylation	GVIKLGEKQSESKCA CCCCCCCCCCCCCEE	58.27	24727099
354	Phosphorylation	ALLGRIPSAVGYQPT HHHCCCCCHHCCCCC	32.96	30407730
358	Phosphorylation	RIPSAVGYQPTLASD CCCCHHCCCCCHHHH	12.53	30407730
361	Phosphorylation	SAVGYQPTLASDLGA CHHCCCCCHHHHHHH	21.30	29654922
417	Phosphorylation	TVLSRQISELGIYPA HHHHHHHHHHCCCCC	20.59	19880383
422	Phosphorylation	QISELGIYPAVDPLD HHHHHCCCCCCCCCC	5.37	30407730
434	Sulfoxidation	PLDSTSRMLSPHILG CCCCCCCCCCHHHHC	4.32	23289948
453	Acetylation	NTARGVQKVLQNYKN HHHHHHHHHHHHCCC	42.37	24727099
470	Sulfoxidation	DIIAILGMDELSEDD HHHHHHCCCCCCCCC	3.03	23289948
517	Phosphorylation	DLKENINSFQGLLDG CHHHHHHHHHHHHCC	18.36	29797451

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ATPBM_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 ATPBM_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of ATPBM_ARATH !!

Drug and Disease Associations

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