dbPTM

ATPB_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ATPB_ARATH
UniProt AC	P19366
Protein Name	ATP synthase subunit beta, chloroplastic {ECO:0000255\|HAMAP-Rule:MF_01347}
Gene Name	atpB {ECO:0000255\|HAMAP-Rule:MF_01347}
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	498
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 catalytic sites are hosted primarily by the beta subunits..
Protein Sequence	MRTNPTTSNPEVSIREKKNLGRIAQIIGPVLDVAFPPGKMPNIYNALVVKGRDTLGQEINVTCEVQQLLGNNRVRAVAMSATEGLKRGMDVVDMGNPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHKSAPAFIELDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEQNLAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKKGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQQVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFNLILSGEFDSLPEQAFYLVGNIDEATAKATNLEMESKLKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MRTNPTTSNP -----CCCCCCCCCC	44.23	19376835
6	Phosphorylation	--MRTNPTTSNPEVS --CCCCCCCCCCCCC	44.95	19376835
7	Phosphorylation	-MRTNPTTSNPEVSI -CCCCCCCCCCCCCH	27.97	19376835
8	Phosphorylation	MRTNPTTSNPEVSIR CCCCCCCCCCCCCHH	53.52	30291188
13	Phosphorylation	TTSNPEVSIREKKNL CCCCCCCCHHHCCCH	17.80	30291188
40	Sulfoxidation	VAFPPGKMPNIYNAL EECCCCCCCCCEEEE	3.68	25693801
54	Phosphorylation	LVVKGRDTLGQEINV EEEECCCCCCCEEEE	31.28	23172892
62	Phosphorylation	LGQEINVTCEVQQLL CCCEEEEEEEHHHHH	9.84	23172892
126	Phosphorylation	DNLGPVDTRTTSPIH CCCCCCCCCCCCCCC	30.10	30291188
135	Phosphorylation	TTSPIHKSAPAFIEL CCCCCCCCCCEEEEC	25.89	30291188
144	Phosphorylation	PAFIELDTKLSIFET CEEEECCCCCCHHHH	46.65	25561503
154	Acetylation	SIFETGIKVVDLLAP CHHHHCCEEHHHCCC	37.23	21311031
162	Nitration	VVDLLAPYRRGGKIG EHHHCCCCCCCCEEE	13.82	-
178	Acetylation	FGGAGVGKTVLIMEL ECCCCCCHHHHHHHH	32.81	21311030
213	Nitration	TREGNDLYMEMKESG CCCCCEEEHHHHHHC	8.22	-
219	Phosphorylation	LYMEMKESGVINEQN EEHHHHHHCCCCCCH	32.61	28295753
236	Nitration	ESKVALVYGQMNEPP HHHEEEEEECCCCCC	11.51	-
252	Phosphorylation	ARMRVGLTALTMAEY CCHHHHHHHHHHHHH	17.43	22092075
259	Nitration	TALTMAEYFRDVNEQ HHHHHHHHHCCCCHH	8.38	-
283	Phosphorylation	FRFVQAGSEVSALLG HHHHHCCHHHHHHHC	37.53	29797451
294	Phosphorylation	ALLGRMPSAVGYQPT HHHCCCCCCCCCCCE	26.66	29797451
298	Nitration	RMPSAVGYQPTLSTE CCCCCCCCCCEEECC	12.53	-
303	Phosphorylation	VGYQPTLSTEMGTLQ CCCCCEEECCCCHHH	25.46	29797451
308	Phosphorylation	TLSTEMGTLQERITS EEECCCCHHHHHHHC	24.77	30291188
362	Nitration	GLAAKGIYPAVDPLD HHHHCCCCCCCCCCC	8.20	-
362	Phosphorylation	GLAAKGIYPAVDPLD HHHHCCCCCCCCCCC	8.20	29797451
385	Nitration	RIVGEEHYETAQQVK EECCHHHHHHHHHHH	20.46	-
387	Phosphorylation	VGEEHYETAQQVKQT CCHHHHHHHHHHHHH	23.70	22092075
492	Sulfoxidation	AKATNLEMESKLKK- HHHHHHHHHHHHCC-	8.75	25693801
494	Phosphorylation	ATNLEMESKLKK--- HHHHHHHHHHCC---	41.81	25561503

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 ATPB_ARATH !!

Functions of PTM Sites

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

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 ATPB_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ATPB_ARATH !!

Drug and Disease Associations

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

Regulatory Network of ATPB_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-8 AND SER-13, AND MASSSPECTROMETRY.	19376835 [Abstract]