PMA11_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PMA11_ARATH
• UniProt AC: Q9LV11
• Protein Name: ATPase 11, plasma membrane-type
• Gene Name: AHA11
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 956
• Subcellular Localization: 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 (By similarity)..
• Protein Sequence: MGDKEEVLEAVLKETVDLENVPIEEVFESLRCSREGLTTEAADERLALFGHNKLEEKKESKFLKFLGFMWNPLSWVMEAAAIMAIALANGGGKPPDWQDFVGIITLLVINSTISFIEENNAGNAAAALMARLAPKAKVLRDGRWGEQDAAILVPGDIISIKLGDIVPADARLLEGDPLKIDQSSLTGESLPVTKGPGDGVYSGSTCKQGELEAVVIATGVHTFFGKAAHLVDTTNHVGHFQQVLTAIGNFCICSIAVGMIIEIVVMYPIQHRAYRPGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLTVDKNLIEVFTKGVDADTVVLMAAQASRLENQDAIDAAIVGMLADPKEARAGVREVHFLPFNPTDKRTALTYIDSDGKMHRVSKGAPEQILNLAHNRAEIERRVHAVIDKFAERGLRSLAVAYQEVPEGTKESAGGPWQFMGLMPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMYPSSALLGQHKDESIGALPIDDLIEKADGFAGVFPEHKYEIVKRLQARKHICGMTGDGVNDAPALKKADIGIAVADATDAARSASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVLGFMLLALIWKFDFPPFMVLIIAILNDGTIMTISKDRVKPSPLPDSWKLSEIFATGVVFGSYMAMMTVIFFWAAYKTDFFPRTFGVSTLEKTAHDDFRKLASAIYLQVSIISQALIFVTRSRSWSYVERPGMLLVVAFILAQLVATLIAVYANWSFAAIEGIGWGWAGVIWLYNIVFYIPLDIIKFLIRYALSGRAWDLVIEQRVAFTRQKDFGKEQRELQWAHAQRTLHGLQAPDAKMFPERTHFNELSQMAEEAKRRAEIARLRELHTLKGHVESVVRLKGLDIETIQQAYTV

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
295	Phosphorylation	GIPIAMPTVLSVTMA CCCCCCHHHHHHHHH	22.46	15308754
305	Phosphorylation	SVTMAIGSHRLSQQG HHHHHHCCHHHHHCC	10.18	29797451
319	Phosphorylation	GAITKRMTAIEEMAG CCHHHHHHHHHHHHC	28.63	19880383
332	Phosphorylation	AGMDVLCSDKTGTLT HCCCEEECCCCCEEE	37.67	19880383
515	Phosphorylation	GVNVKMITGDQLAIG CCCEEEECCCCEEEC	31.07	17317660
549	Phosphorylation	LGQHKDESIGALPID HCCCCCCCCCCEEHH	36.13	25368622
889	Phosphorylation	QWAHAQRTLHGLQAP HHHHHHHHHCCCCCC	15.83	30291188
938	Phosphorylation	TLKGHVESVVRLKGL HHHCHHHEEEEECCC	25.48	25561503
949	Phosphorylation	LKGLDIETIQQAYTV ECCCCHHHHHHHHCC	25.15	23776212
954	Phosphorylation	IETIQQAYTV----- HHHHHHHHCC-----	12.05	23776212
955	Phosphorylation	ETIQQAYTV------ HHHHHHHCC------	23.82	30291188

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

Oops, there are no upstream regulatory protein records of PMA11_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PMA11_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 PMA11_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of PMA11_ARATH !!

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 THR-889, AND MASSSPECTROMETRY.
PubMed: 19376835

"Temporal analysis of sucrose-induced phosphorylation changes inplasma membrane proteins of Arabidopsis.";
Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B.,Schulze W.X.;
Mol. Cell. Proteomics 6:1711-1726(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-889, AND MASSSPECTROMETRY.
PubMed: 17586839