dbPTM

PMA1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PMA1_ARATH
UniProt AC	P20649
Protein Name	ATPase 1, plasma membrane-type {ECO:0000303\|PubMed:2521951}
Gene Name	AHA1 {ECO:0000303\|PubMed:2521951}
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. Forms a functional cation-translocating unit with CNGC17 that is activated by PSKR1/BAK1 and possibly other BAK1/RLK complexes. [PubMed: 26071421]
Protein Sequence	MSGLEDIKNETVDLEKIPIEEVFQQLKCTREGLTTQEGEDRIVIFGPNKLEEKKESKILKFLGFMWNPLSWVMEAAALMAIALANGDNRPPDWQDFVGIICLLVINSTISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTSIGNFCICSIAIGIAIEIVVMYPIQHRKYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVEVFCKGVEKDQVLLFAAMASRVENQDAIDAAMVGMLADPKEARAGIREVHFLPFNPVDKRTALTYIDSDGNWHRVSKGAPEQILDLANARPDLRKKVLSCIDKYAERGLRSLAVARQVVPEKTKESPGGPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMYPSAALLGTDKDSNIASIPVEELIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFMLIALIWEFDFSAFMVLIIAILNDGTIMTISKDRVKPSPTPDSWKLKEIFATGIVLGGYQAIMSVIFFWAAHKTDFFSDKFGVRSIRDNNDELMGAVYLQVSIISQALIFVTRSRSWSFVERPGALLMIAFVIAQLVATLIAVYADWTFAKVKGIGWGWAGVIWIYSIVTYFPQDILKFAIRYILSGKAWASLFDNRTAFTTKKDYGIGEREAQWAQAQRTLHGLQPKEDVNIFPEKGSYRELSEIAEQAKRRAEIARLRELHTLKGHVESVAKLKGLDIDTAGHHYTV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSGLEDIKN ------CCCHHHHCC	52.68	-
2	Phosphorylation	------MSGLEDIKN ------CCCHHHHCC	52.68	17317660
35	Phosphorylation	CTREGLTTQEGEDRI CCCCCCCCCCCCCEE	29.66	19880383
291	Phosphorylation	GIPIAMPTVLSVTMA CCCCCCHHHHHHHHH	22.46	15308754
301	Phosphorylation	SVTMAIGSHRLSQQG HHHHHHCCHHHHHCC	10.18	29797451
315	Phosphorylation	GAITKRMTAIEEMAG CCHHHHHHHHHHHHC	28.63	19880383
328	Phosphorylation	AGMDVLCSDKTGTLT HCCCEEECCCCCCEE	37.67	19880383
469	Phosphorylation	RQVVPEKTKESPGGP HHHCCCCCCCCCCCC	38.08	26811356
511	Phosphorylation	GVNVKMITGDQLAIG CCCEEEECCCCEEEC	31.07	17317660
544	Phosphorylation	LLGTDKDSNIASIPV HCCCCCCCCCCCCCH	35.56	17317660
881	Phosphorylation	QWAQAQRTLHGLQPK HHHHHHHHHCCCCCH	15.83	30291188
899	Phosphorylation	NIFPEKGSYRELSEI CCCCCCCCHHHHHHH	31.89	30291188
900	Phosphorylation	IFPEKGSYRELSEIA CCCCCCCHHHHHHHH	19.44	24243849
904	Phosphorylation	KGSYRELSEIAEQAK CCCHHHHHHHHHHHH	23.39	15308754
931	Phosphorylation	TLKGHVESVAKLKGL HHHHHHHHHHHHCCC	26.70	19880383
942	Phosphorylation	LKGLDIDTAGHHYTV HCCCCCCCCCCCCCC	34.57	23776212
947	Phosphorylation	IDTAGHHYTV----- CCCCCCCCCC-----	11.97	23776212
948	Phosphorylation	DTAGHHYTV------ CCCCCCCCC------	18.51	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 PMA1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PMA1_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 PMA1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PPI1_ARATH	PPI1	physical	16279950
CNG10_ARATH	CNGC10	physical	22737156
CDPK5_ARATH	CPK5	physical	23609608

Drug and Disease Associations

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

Regulatory Network of PMA1_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-881; SER-899 ANDTHR-948, AND MASS SPECTROMETRY.	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 SER-899 AND THR-948,SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.	15308754 [Abstract]
"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-881 AND THR-948, ANDMASS SPECTROMETRY.	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-948, AND MASSSPECTROMETRY.	19245862 [Abstract]
"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis."; de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.; J. Proteome Res. 7:2458-2470(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-948, AND MASSSPECTROMETRY.	18433157 [Abstract]
"Quantitative phosphoproteomics of early elicitor signaling inArabidopsis."; Benschop J.J., Mohammed S., O'Flaherty M., Heck A.J.R., Slijper M.,Menke F.L.H.; Mol. Cell. Proteomics 6:1198-1214(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-948, AND MASSSPECTROMETRY.	17317660 [Abstract]
"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-881 AND THR-948, ANDMASS SPECTROMETRY.	17586839 [Abstract]