Y2165_ARATH - dbPTM
Y2165_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID Y2165_ARATH
UniProt AC C0LGK4
Protein Name Probable LRR receptor-like serine/threonine-protein kinase At2g16250
Gene Name At2g16250
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 915
Subcellular Localization Membrane
Single-pass type I membrane protein .
Protein Description
Protein Sequence MVDQRRSALGFVLLLLCLVLFFDCVVVGQTQSRFSEKLILLNLRSSLGLRGTDWPIKGDPCVDWRGIQCENGSIIGINISGFRRTRIGKLNPQFSVDPLRNLTRLSYFNASGLALPGTIPEWFGVSLLALEVLDLSSCSVNGVVPFTLGNLTSLRTLNLSQNSLTSLVPSSLGQLLNLSQLDLSRNSFTGVLPQSFSSLKNLLTLDVSSNYLTGPIPPGLGALSKLIHLNFSSNSFSSPIPSELGDLVNLVDFDLSINSLSGSVPQELRKLSKLQLMAIGDNLLSGTLPVDLFSAESQLQTLVLRENGFSGSLPDVCWSLPKLRILDIAKNNFTGLLPYSSYDSDQIAEMVDISSNTFYGELTPILRRFRIMDLSGNYFEGKLPDYVTGENVSVTSNCLRNERRQKPSAICAAFYKSRGLDFDDFGRPNLTQPTSKNASSGISRRTVIILAAVGGGVAFILLFVILPIILVLCMRHRRRAAQRGNNDRPKPAGEASQQPPKGAQTFDLSRLGNAFSYEQLLQATEEFNDANLIKRGHSGNLFRGFLENGIPVVIKKIDVREGKSEGYISELELFSKAGHQRLVPFLGHCLENESQKFLVYKFMRHGDLASSLFRKSENEGDGLKSLDWITRLKIALGAAEGLSYLHHECSPPLVHRDVQASSILLDDKFEVRLGSLSEAYAQGDAYQSRISRLLRLPQSSEPSSSGVTNAICSYDVYCFGKVLLELVTGKLGISSPDNALAKEYMEEALPYISTNEKELVTKILDPSLMVDEDLLEEVWAMAIIAKSCLNPKPTRRPLMRHIVNALENPLKVVREDTNSGSGSSRLRTNSSRGSWNAAIFGSWRQSASDVTAVQAGATTSGGGGGGGGNGLRNSGSQGSSGRNNNNNGNSSSSRRRQSSEIVPEPAAYGVVEDNL
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
71N-linked_GlycosylationWRGIQCENGSIIGIN
CCCEEEECCCEEEEE		58.08-
78N-linked_GlycosylationNGSIIGINISGFRRT
CCCEEEEEECCCCCC		19.70-
101N-linked_GlycosylationFSVDPLRNLTRLSYF
CCCCHHHCCCEEEEE		54.14-
109N-linked_GlycosylationLTRLSYFNASGLALP
CCEEEEECCCCCCCC		25.59-
150N-linked_GlycosylationVVPFTLGNLTSLRTL
CCCEECCCCCCCEEE		43.17-
158N-linked_GlycosylationLTSLRTLNLSQNSLT
CCCCEEEECCCCCHH		36.71-
177N-linked_GlycosylationSSLGQLLNLSQLDLS
CHHHHHHCHHHHCCC		46.36-
204PhosphorylationSSLKNLLTLDVSSNY
HHHHCCCCEECCCCC		24.8723111157
224PhosphorylationPPGLGALSKLIHLNF
CCCHHHHHHHHHCCC		25.5323111157
230N-linked_GlycosylationLSKLIHLNFSSNSFS
HHHHHHCCCCCCCCC		22.16-
332N-linked_GlycosylationILDIAKNNFTGLLPY
EHHHHHCCCCCCCCC		34.84-
391N-linked_GlycosylationPDYVTGENVSVTSNC
CCCCCCCCEECCCHH		32.48-
429N-linked_GlycosylationFDDFGRPNLTQPTSK
CCCCCCCCCCCCCCC		55.12-
437N-linked_GlycosylationLTQPTSKNASSGISR
CCCCCCCCCCCCCCH		44.84-
842PhosphorylationWNAAIFGSWRQSASD
EEEEEEECHHCCCCC		14.3415308754
898PhosphorylationSSSRRRQSSEIVPEP
CCCCHHCCCCCCCCH		28.2915308754
899PhosphorylationSSRRRQSSEIVPEPA
CCCHHCCCCCCCCHH		24.0115308754
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 Y2165_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of Y2165_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 Y2165_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NIP71_ARATHNIP7;1physical
21423366
Y5838_ARATHBIR1physical
21423366
Y3804_ARATHAT3G28040physical
21423366
Y5639_ARATHAT5G63930physical
21423366
PXC3_ARATHAT2G41820physical
21423366
MLO2_ARATHMLO2physical
21423366
Y5129_ARATHAT5G10290physical
21423366
PRA1E_ARATHPRA1.Ephysical
24833385
PR1B2_ARATHPRA1.B2physical
24833385
PSKR2_ARATHPSKR2physical
24833385
TRXH5_ARATHTRX5physical
24833385
TRXH3_ARATHTRX3physical
24833385
CALX2_ARATHAT5G07340physical
24833385
CNIH1_ARATHAT3G12180physical
24833385
RAH1C_ARATHRABH1cphysical
24833385
RAB1B_ARATHGB2physical
24833385
CRK40_ARATHCRK40physical
24833385
BETL2_ARATHAT1G29060physical
24833385
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of Y2165_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 AT SER-898 AND SER-899, IDENTIFICATION BY MASSSPECTROMETRY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
"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-842; SER-898 ANDSER-899, 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-898 AND SER-899, ANDMASS SPECTROMETRY.

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