dbPTM

PMA3_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PMA3_ARATH
UniProt AC	P20431
Protein Name	ATPase 3, plasma membrane-type
Gene Name	AHA3
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	949
Subcellular Localization	Cell membrane Multi-pass membrane protein .
Protein Description	The plasma membrane H(+) ATPase of plants and fungi generates a proton gradient that drives the active transport of nutrients by H(+)-symport. The resulting external acidification and/or internal alkinization may mediate growth responses..
Protein Sequence	MASGLEDIVNENVDLEKIPIEEVFQQLKCSREGLSGAEGENRLQIFGPNKLEEKKESKLLKFLGFMWNPLSWVMEAAAIMAIALANGGGKPPDWQDFVGIVCLLVINSTISFVEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEASILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPATKGPGEEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTAIGNFCICSIAVGIAIEIVVMYPIQRRHYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHKLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLIEVYCKGVEKDEVLLFAARASRVENQDAIDAAMVGMLADPKEARAGIREIHFLPFNPVDKRTALTFIDSNGNWHRVSKGAPEQILDLCNARADLRKRVHSTIDKYAERGLRSLAVSRQTVPEKTKESSGSPWEFVGVLPLFDPPRHDSAETIRRALDLGVNVKMITGDQLAIAKETGRRLGMGSNMYPSSSLLGKHKDEAMAHIPVEDLIEKADGFAGVFPEHKYEIVKKLQERKHICGMTGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFMLIALIWKFDFSPFMVLIIAILNDGTIMTISKDRVKPSPTPDSWKLKEIFATGVVLGGYMAIMTVVFFWAAYKTDFFPRTFHVRDLRGSEHEMMSALYLQVSIVSQALIFVTRSRSWSFTERPGYFLLIAFWVAQLIATAIAVYGNWEFARIKGIGWGWAGVIWLYSIVFYFPLDIMKFAIRYILAGTAWKNIIDNRTAFTTKQNYGIEEREAQWAHAQRTLHGLQNTETANVVPERGGYRELSEIANQAKRRAEIARLRELHTLKGHVESVVKLKGLDIETAGHYTV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MASGLEDIVN -----CCCCHHHHHH	42.48	19880383
292	Phosphorylation	GIPIAMPTVLSVTMA CCCCCCHHHHHHHHH	22.46	15308754
316	Phosphorylation	GAITKRMTAIEEMAG CCHHHHHHHHHHHHC	28.63	19880383
329	Phosphorylation	AGMDVLCSDKTGTLT HCCCEEECCCCCCEE	37.67	19880383
882	Phosphorylation	QWAHAQRTLHGLQNT HHHHHHHHHHHHCCC	15.83	30291188
889	Phosphorylation	TLHGLQNTETANVVP HHHHHCCCCCCCCCC	23.04	19376835
891	Phosphorylation	HGLQNTETANVVPER HHHCCCCCCCCCCCC	22.84	19376835
932	Phosphorylation	TLKGHVESVVKLKGL HHHCHHHEEEEECCC	30.99	17483306
943	Phosphorylation	LKGLDIETAGHYTV- ECCCCCEECCCCCC-	37.97	19376835
947	Phosphorylation	DIETAGHYTV----- CCEECCCCCC-----	14.31	23776212
948	Phosphorylation	IETAGHYTV------ CEECCCCCC------	17.67	30291188

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 PMA3_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PMA3_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 PMA3_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PMA3_ARATH !!

Drug and Disease Associations

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

Regulatory Network of PMA3_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 THR-882, AND MASSSPECTROMETRY.	19376835 [Abstract]
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-882, AND MASSSPECTROMETRY.	19245862 [Abstract]
"Quantitative phosphoproteomic analysis of plasma membrane proteinsreveals regulatory mechanisms of plant innate immune responses."; Nuehse T.S., Bottrill A.R., Jones A.M.E., Peck S.C.; Plant J. 51:931-940(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-882, AND MASSSPECTROMETRY.	17651370 [Abstract]
"Phosphoproteomics of the Arabidopsis plasma membrane and a newphosphorylation site database."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Plant Cell 16:2394-2405(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-948, SUBCELLULARLOCATION, AND MASS SPECTROMETRY.	15308754 [Abstract]
"Binding of 14-3-3 protein to the plasma membrane H(+)-ATPase AHA2involves the three C-terminal residues Tyr(946)-Thr-Val and requiresphosphorylation of Thr(947)."; Fuglsang A.T., Visconti S., Drumm K., Jahn T., Stensballe A.,Mattei B., Jensen O.N., Aducci P., Palmgren M.G.; J. Biol. Chem. 274:36774-36780(1999). Cited for: PHOSPHORYLATION AT THR-948, INTERACTION WITH 14-3-3 PROTEINS, ANDMUTAGENESIS OF TYR-947; THR-948 AND VAL-949.	10593986 [Abstract]