dbPTM

AMT11_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	AMT11_ARATH
UniProt AC	P54144
Protein Name	Ammonium transporter 1 member 1
Gene Name	AMT1-1
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	501
Subcellular Localization	Cell membrane Multi-pass membrane protein .
Protein Description	High affinity ammonium transporter probably involved in ammonium uptake from the soil, long-distance transport to the shoots and re-uptake of apoplastic ammonium that derives from photorespiration in shoots. Contributes with AMT1-3 to the overall ammonium uptake capacity in roots under nitrogen-deficiency conditions..
Protein Sequence	MSCSATDLAVLLGPNATAAANYICGQLGDVNNKFIDTAFAIDNTYLLFSAYLVFSMQLGFAMLCAGSVRAKNTMNIMLTNVLDAAAGGLFYYLFGYAFAFGSPSNGFIGKHYFGLKDIPTASADYSNFLYQWAFAIAAAGITSGSIAERTQFVAYLIYSSFLTGFVYPVVSHWFWSVDGWASPFRTDGDLLFSTGAIDFAGSGVVHMVGGIAGLWGALIEGPRLGRFDNGGRAIALRGHSASLVVLGTFLLWFGWYGFNPGSFNKILVTYETGTYNGQWSAVGRTAVTTTLAGCTAALTTLFGKRLLSGHWNVTDVCNGLLGGFAAITGGCSVVEPWAAIICGFVAALVLLGCNKLAEKLKYDDPLEAAQLHGGCGAWGLIFTALFAQEKYLNQIYGNKPGRPHGLFMGGGGKLLGAQLIQIIVITGWVSATMGTLFFILKKMKLLRISSEDEMAGMDMTRHGGFAYMYFDDDESHKAIQLRRVEPRSPSPSGANTTPTPV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
454	Sulfoxidation	RISSEDEMAGMDMTR CCCCCCHHCCCCCCC	6.38	23289948
457	Sulfoxidation	SEDEMAGMDMTRHGG CCCHHCCCCCCCCCC	2.01	23289948
459	Sulfoxidation	DEMAGMDMTRHGGFA CHHCCCCCCCCCCEE	2.35	23289948
460	Phosphorylation	EMAGMDMTRHGGFAY HHCCCCCCCCCCEEE	18.43	30291188
475	Phosphorylation	MYFDDDESHKAIQLR EEECCCHHCEEEEEE	36.96	27532006
488	Phosphorylation	LRRVEPRSPSPSGAN EEEECCCCCCCCCCC	40.21	27532006
490	Phosphorylation	RVEPRSPSPSGANTT EECCCCCCCCCCCCC	32.70	27532006
492	Phosphorylation	EPRSPSPSGANTTPT CCCCCCCCCCCCCCC	55.67	19880383
496	Phosphorylation	PSPSGANTTPTPV-- CCCCCCCCCCCCC--	33.35	17317660
497	Phosphorylation	SPSGANTTPTPV--- CCCCCCCCCCCC---	25.60	23111157
499	Phosphorylation	SGANTTPTPV----- CCCCCCCCCC-----	34.29	25368622

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 AMT11_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of AMT11_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 AMT11_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AMT13_ARATH	AMT1;3	physical	23463773
GCR1_ARATH	GCR1	physical	21423366
SUC9_ARATH	SUC9	physical	21423366
WAXS6_ARATH	AT5G55330	physical	21423366
Y2899_ARATH	AT2G28990	physical	21423366
AMT11_ARATH	AMT1;1	physical	21423366
HHP2_ARATH	HHP2	physical	24833385
HHP4_ARATH	HHP4	physical	24833385
UBC32_ARATH	UBC32	physical	24833385
UBC34_ARATH	UBC34	physical	24833385
ACBP6_ARATH	ACBP6	physical	24833385
CNIH1_ARATH	AT3G12180	physical	24833385
MSBP2_ARATH	MAPR3	physical	24833385
CP21D_ARATH	AT3G66654	physical	24833385
SPCS1_ARATH	AT2G22425	physical	24833385
RAC8_ARATH	ROP10	physical	24833385
BETL2_ARATH	AT1G29060	physical	24833385
BET12_ARATH	ATBET12	physical	24833385

Drug and Disease Associations

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

Regulatory Network of AMT11_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-488, AND MASSSPECTROMETRY.	19376835 [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 SER-475, 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 SER-475, AND MASSSPECTROMETRY.	17317660 [Abstract]
"Novel subsets of the Arabidopsis plasmalemma phosphoproteome identifyphosphorylation sites in secondary active transporters."; Hem S., Rofidal V., Sommerer N., Rossignol M.; Biochem. Biophys. Res. Commun. 363:375-380(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460; SER-488; SER-490AND SER-492, AND MASS SPECTROMETRY.	17869214 [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-460, AND MASSSPECTROMETRY.	19245862 [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-460, SUBCELLULARLOCATION, AND MASS SPECTROMETRY.	15308754 [Abstract]