dbPTM

PMA2_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PMA2_ARATH
UniProt AC	P19456
Protein Name	ATPase 2, plasma membrane-type {ECO:0000303\|PubMed:2143186}
Gene Name	AHA2 {ECO:0000303\|PubMed:2143186}
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	948
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. [PubMed: 10748244]
Protein Sequence	MSSLEDIKNETVDLEKIPIEEVFQQLKCSREGLTTQEGEDRIQIFGPNKLEEKKESKLLKFLGFMWNPLSWVMEMAAIMAIALANGDGRPPDWQDFVGIICLLVINSTISFIEENNAGNAAAALMAGLAPKTKVLRDGKWSEQEAAILVPGDIVSIKLGDIIPADARLLEGDPLKVDQSALTGESLPVTKHPGQEVFSGSTCKQGEIEAVVIATGVHTFFGKAAHLVDSTNQVGHFQKVLTAIGNFCICSIAIGMVIEIIVMYPIQRRKYRDGIDNLLVLLIGGIPIAMPTVLSVTMAIGSHRLSQQGAITKRMTAIEEMAGMDVLCSDKTGTLTLNKLSVDKNLVEVFCKGVEKDQVLLFAAMASRVENQDAIDAAMVGMLADPKEARAGIREVHFLPFNPVDKRTALTYIDGSGNWHRVSKGAPEQILELAKASNDLSKKVLSIIDKYAERGLRSLAVARQVVPEKTKESPGAPWEFVGLLPLFDPPRHDSAETIRRALNLGVNVKMITGDQLAIGKETGRRLGMGTNMYPSSALLGTHKDANLASIPVEELIEKADGFAGVFPEHKYEIVKKLQERKHIVGMTGDGVNDAPALKKADIGIAVADATDAARGASDIVLTEPGLSVIISAVLTSRAIFQRMKNYTIYAVSITIRIVFGFMLIALIWEFDFSAFMVLIIAILNDGTIMTISKDRVKPSPTPDSWKLKEIFATGVVLGGYQAIMTVIFFWAAHKTDFFSDTFGVRSIRDNNHELMGAVYLQVSIISQALIFVTRSRSWSFVERPGALLMIAFLIAQLIATLIAVYANWEFAKIRGIGWGWAGVIWLYSIVTYFPLDVFKFAIRYILSGKAWLNLFENKTAFTMKKDYGKEEREAQWALAQRTLHGLQPKEAVNIFPEKGSYRELSEIAEQAKRRAEIARLRELHTLKGHVESVVKLKGLDIETPSHYTV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSLEDIKN ------CCCHHHHHH	43.56	22223895
2	Phosphorylation	------MSSLEDIKN ------CCCHHHHHH	43.56	19880383
3	Phosphorylation	-----MSSLEDIKNE -----CCCHHHHHHC	34.18	19880383
35	Phosphorylation	CSREGLTTQEGEDRI CCCCCCCCCCCCCCE	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	RQVVPEKTKESPGAP HHHCCCCCCCCCCCC	38.08	26811356
511	Phosphorylation	GVNVKMITGDQLAIG CCCEEEECCCCEEEC	31.07	17317660
548	Phosphorylation	HKDANLASIPVEELI CCCCCCCCCCHHHHH	30.50	30407730
881	Phosphorylation	QWALAQRTLHGLQPK 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	TLKGHVESVVKLKGL HHHCHHHEEEEECCC	30.99	17483306
942	Phosphorylation	LKGLDIETPSHYTV- ECCCCCCCCCCCCC-	30.35	23776212
944	Phosphorylation	GLDIETPSHYTV--- CCCCCCCCCCCC---	36.22	19880383
946	Phosphorylation	DIETPSHYTV----- CCCCCCCCCC-----	17.34	23776212
947	Phosphorylation	IETPSHYTV------ CCCCCCCCC------	17.83	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
931	S	Phosphorylation	Kinase	CIPK11	O22932	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
881	T	Phosphorylation	17651370
Phosphorylation at Thr-881 by PSY1R.
899	S	Phosphorylation	17651370
Phosphorylation at Ser-899 is specifically induced by RALF1, thus leading to the inhibition of proton transport.
931	S	Phosphorylation	17483306
Phosphorylation of Thr-947 induces the binding to 14-3-3 proteins, but phosphorylation of Ser-931 interfers with this binding no matter whether Thr-947 is phosphorylated or not.
947	T	Phosphorylation	10593986
Phosphorylation of Thr-947 induces the binding to 14-3-3 proteins, but phosphorylation of Ser-931 interfers with this binding no matter whether Thr-947 is phosphorylated or not.

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 PMA2_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
14334_ARATH	GF14 PHI	physical	9368417
CNG10_ARATH	CNGC10	physical	22737156
P2C67_ARATH	AT5G02760	physical	24858935
SMO12_ARATH	SMO1-2	physical	24833385
PSKR2_ARATH	PSKR2	physical	24833385
HHP2_ARATH	HHP2	physical	24833385
HHP4_ARATH	HHP4	physical	24833385
UBC32_ARATH	UBC32	physical	24833385
UBC34_ARATH	UBC34	physical	24833385
CLH1_ARATH	CLH1	physical	24833385
BCA1_ARATH	CA1	physical	24833385
CNIH1_ARATH	AT3G12180	physical	24833385
WNK3_ARATH	WNK3	physical	24833385
NEK3_ARATH	NEK3	physical	24833385
CP21D_ARATH	AT3G66654	physical	24833385
BET12_ARATH	ATBET12	physical	24833385
PSYR1_ARATH	AT1G72300	physical	25267325

Drug and Disease Associations

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

Regulatory Network of PMA2_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-947, AND MASS SPECTROMETRY.	17651370 [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 SER-944, AND MASSSPECTROMETRY.	17317660 [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; SER-904 ANDTHR-947, 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-947, 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-947, AND MASSSPECTROMETRY.	19245862 [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-947, AND MASSSPECTROMETRY.	17586839 [Abstract]
"Large-scale analysis of in vivo phosphorylated membrane proteins byimmobilized metal ion affinity chromatography and mass spectrometry."; Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.; Mol. Cell. Proteomics 2:1234-1243(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-946 AND THR-947, ANDMASS SPECTROMETRY.	14506206 [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-947.	10593986 [Abstract]

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