Y5659_ARATH - dbPTM
Y5659_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID Y5659_ARATH
UniProt AC Q9FMD7
Protein Name Probable inactive receptor kinase At5g16590
Gene Name At5g16590
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 625
Subcellular Localization Cell membrane
Single-pass membrane protein .
Protein Description Might be involved in early recognition of growth promoting fungi. Appears to be specific for P.indica..
Protein Sequence MKNKTNLGLSVFFFFICLVSVTSDLEADRRALIALRDGVHGRPLLWNLTAPPCTWGGVQCESGRVTALRLPGVGLSGPLPIAIGNLTKLETLSFRFNALNGPLPPDFANLTLLRYLYLQGNAFSGEIPSFLFTLPNIIRINLAQNNFLGRIPDNVNSATRLATLYLQDNQLTGPIPEIKIKLQQFNVSSNQLNGSIPDPLSGMPKTAFLGNLLCGKPLDACPVNGTGNGTVTPGGKGKSDKLSAGAIVGIVIGCFVLLLVLFLIVFCLCRKKKKEQVVQSRSIEAAPVPTSSAAVAKESNGPPAVVANGASENGVSKNPAAVSKDLTFFVKSFGEFDLDGLLKASAEVLGKGTFGSSYKASFDHGLVVAVKRLRDVVVPEKEFREKLQVLGSISHANLVTLIAYYFSRDEKLVVFEYMSRGSLSALLHGNKGSGRSPLNWETRANIALGAARAISYLHSRDATTSHGNIKSSNILLSESFEAKVSDYCLAPMISPTSTPNRIDGYRAPEVTDARKISQKADVYSFGVLILELLTGKSPTHQQLHEEGVDLPRWVSSITEQQSPSDVFDPELTRYQSDSNENMIRLLNIGISCTTQYPDSRPTMPEVTRLIEEVSRSPASPGPLSD
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 Orthologous
Protein Cluster
282PhosphorylationEQVVQSRSIEAAPVP
HHHHHCCCEEECCCC		29.9927532006
332PhosphorylationDLTFFVKSFGEFDLD
CCEEEEHHCCCCCHH		32.9330291188
345PhosphorylationLDGLLKASAEVLGKG
HHHHHHHHHHHHCCC		24.3130291188
422PhosphorylationFEYMSRGSLSALLHG
EEEECCCCHHHHHCC		20.31-
433PhosphorylationLLHGNKGSGRSPLNW
HHCCCCCCCCCCCCH		32.4229654922
442PhosphorylationRSPLNWETRANIALG
CCCCCHHHHHHHHHH		27.05-
496PhosphorylationLAPMISPTSTPNRID
ECCCCCCCCCCCCCC		38.14-
517PhosphorylationVTDARKISQKADVYS
CCCHHHHHHHHCHHH		28.76-
555PhosphorylationVDLPRWVSSITEQQS
CCHHHHHHHHCCCCC		14.7315308754
556PhosphorylationDLPRWVSSITEQQSP
CHHHHHHHHCCCCCH		24.7415308754
558PhosphorylationPRWVSSITEQQSPSD
HHHHHHHCCCCCHHH		29.6823328941
562PhosphorylationSSITEQQSPSDVFDP
HHHCCCCCHHHCCCH		26.5115308754
564PhosphorylationITEQQSPSDVFDPEL
HCCCCCHHHCCCHHH		52.2126811356
593PhosphorylationLNIGISCTTQYPDSR
HEEEEEEECCCCCCC		15.33-
616PhosphorylationLIEEVSRSPASPGPL
HHHHHHCCCCCCCCC		19.8123660473
619PhosphorylationEVSRSPASPGPLSD-
HHHCCCCCCCCCCC-		33.5015308754
624PhosphorylationPASPGPLSD------
CCCCCCCCC------		44.3930291188
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 Y5659_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of Y5659_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 Y5659_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLE26_ARATHCLE26physical
21423366
PRA1E_ARATHPRA1.Ephysical
24833385
HHP2_ARATHHHP2physical
24833385
UBC32_ARATHUBC32physical
24833385
KSG4_ARATHSK42physical
24833385
ACBP6_ARATHACBP6physical
24833385
CNIH1_ARATHAT3G12180physical
24833385
CP21D_ARATHAT3G66654physical
24833385
SPCS1_ARATHAT2G22425physical
24833385
PPA3_ARATHPAP3physical
24833385
PAM74_ARATHAT5G59650physical
24833385
BETL2_ARATHAT1G29060physical
24833385
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of Y5659_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-619 AND SER-624, ANDMASS SPECTROMETRY.
"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 SER-345, AND MASSSPECTROMETRY.
"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-345; SER-619 ANDSER-624, AND MASS SPECTROMETRY.
"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 SER-619 AND SER-624, ANDMASS SPECTROMETRY.

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