Y3288_ARATH - dbPTM
Y3288_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID Y3288_ARATH
UniProt AC Q9M8T0
Protein Name Probable inactive receptor kinase At3g02880
Gene Name At3g02880
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 627
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MKYKRKLSLSVVFLFVFYLAAVTSDLESDRRALLAVRNSVRGRPLLWNMSASSPCNWHGVHCDAGRVTALRLPGSGLFGSLPIGGIGNLTQLKTLSLRFNSLSGPIPSDFSNLVLLRYLYLQGNAFSGEIPSLLFTLPSIIRINLGENKFSGRIPDNVNSATRLVTLYLERNQLSGPIPEITLPLQQFNVSSNQLNGSIPSSLSSWPRTAFEGNTLCGKPLDTCEAESPNGGDAGGPNTPPEKKDSDKLSAGAIVGIVIGCVVGLLLLLLILFCLCRKRKKEENVPSRNVEAPVAAATSSAAIPKETVVVVPPAKATGSESGAVNKDLTFFVKSFGEFDLDGLLKASAEVLGKGTVGSSYKASFEHGLVVAVKRLRDVVVPEKEFRERLHVLGSMSHANLVTLIAYYFSRDEKLLVFEYMSKGSLSAILHGNKGNGRTPLNWETRAGIALGAARAISYLHSRDGTTSHGNIKSSNILLSDSYEAKVSDYGLAPIISSTSAPNRIDGYRAPEITDARKISQKADVYSFGVLILELLTGKSPTHQQLNEEGVDLPRWVQSVTEQQTPSDVLDPELTRYQPEGNENIIRLLKIGMSCTAQFPDSRPSMAEVTRLIEEVSHSSGSPNPVSD
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
300PhosphorylationPVAAATSSAAIPKET
CHHHHHCCCCCCCCE		19.8417317660
317PhosphorylationVVPPAKATGSESGAV
EECCCCCCCCCCCCC		40.3025561503
319PhosphorylationPPAKATGSESGAVNK
CCCCCCCCCCCCCCC		25.0019880383
321PhosphorylationAKATGSESGAVNKDL
CCCCCCCCCCCCCCC		33.4830407730
334PhosphorylationDLTFFVKSFGEFDLD
CCEEEEEECCCCCHH		32.9330291188
347PhosphorylationLDGLLKASAEVLGKG
HHHHHHHHHHHHCCC		24.3130291188
424PhosphorylationFEYMSKGSLSAILHG
EEECCCCCCCHHHCC		23.92-
444PhosphorylationRTPLNWETRAGIALG
CCCCCHHHHHHHHHH		19.89-
519PhosphorylationITDARKISQKADVYS
CCCHHHHHHHHCHHH		28.76-
595PhosphorylationLKIGMSCTAQFPDSR
HHHCCCCEECCCCCC		19.04-
616PhosphorylationTRLIEEVSHSSGSPN
HHHHHHHHCCCCCCC		22.4123776212
618PhosphorylationLIEEVSHSSGSPNPV
HHHHHHCCCCCCCCC		28.9624924143
619PhosphorylationIEEVSHSSGSPNPVS
HHHHHCCCCCCCCCC		37.5519880383
621PhosphorylationEVSHSSGSPNPVSD-
HHHCCCCCCCCCCC-		24.3730291188
626PhosphorylationSGSPNPVSD------
CCCCCCCCC------		38.5730291188
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 Y3288_ARATH !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of Y3288_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 Y3288_ARATH !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUB_ARATHSUBphysical
21423366
PXC3_ARATHAT2G41820physical
21423366
HHP2_ARATHHHP2physical
24833385
HHP4_ARATHHHP4physical
24833385
UBC32_ARATHUBC32physical
24833385
UBC34_ARATHUBC34physical
24833385
CNIH1_ARATHAT3G12180physical
24833385
MSBP2_ARATHMAPR3physical
24833385
CP21D_ARATHAT3G66654physical
24833385
PPA3_ARATHPAP3physical
24833385
PAM74_ARATHAT5G59650physical
24833385
BETL2_ARATHAT1G29060physical
24833385
BET12_ARATHATBET12physical
24833385
TBL18_ARATHTBL18physical
24833385
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of Y3288_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-621 AND SER-626, ANDMASS SPECTROMETRY.
"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 SER-621, AND MASSSPECTROMETRY.
"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-347, AND MASSSPECTROMETRY.
"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 SER-621 AND SER-626, ANDMASS SPECTROMETRY.
"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-347, AND MASSSPECTROMETRY.
"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; SER-621 ANDSER-626, AND MASS SPECTROMETRY.

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