Y1719_ARATH - dbPTM
Y1719_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID Y1719_ARATH
UniProt AC O04567
Protein Name Probable inactive receptor kinase At1g27190
Gene Name At1g27190
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 601
Subcellular Localization Membrane
Single-pass membrane protein .
Protein Description
Protein Sequence MKKIFITLLWLLFISSFLCSSSSAEDDVLCLQGLKNSLIDPSSRLSSWSFPNSSASSICKLTGVSCWNEKENRIISLQLQSMQLAGEIPESLKLCRSLQSLDLSGNDLSGSIPSQICSWLPYLVTLDLSGNKLGGSIPTQIVECKFLNALILSDNKLSGSIPSQLSRLDRLRRLSLAGNDLSGTIPSELARFGGDDFSGNNGLCGKPLSRCGALNGRNLSIIIVAGVLGAVGSLCVGLVIFWWFFIREGSRKKKGYGAGKSKDDSDWIGLLRSHKLVQVTLFQKPIVKIKLGDLMAATNNFSSGNIDVSSRTGVSYKADLPDGSALAVKRLSACGFGEKQFRSEMNKLGELRHPNLVPLLGYCVVEDERLLVYKHMVNGTLFSQLHNGGLCDAVLDWPTRRAIGVGAAKGLAWLHHGCQPPYLHQFISSNVILLDDDFDARITDYGLAKLVGSRDSNDSSFNNGDLGELGYVAPEYSSTMVASLKGDVYGFGIVLLELVTGQKPLSVINGVEGFKGSLVDWVSQYLGTGRSKDAIDRSICDKGHDEEILQFLKIACSCVVSRPKERPTMIQVYESLKNMADKHGVSEHYDEFPLVFNKQEA
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
52N-linked_GlycosylationLSSWSFPNSSASSIC
CCCCCCCCCCHHHHH
46.73-
139PhosphorylationKLGGSIPTQIVECKF
CCCCCCCCHHHCCCC
29.2919880383
265PhosphorylationAGKSKDDSDWIGLLR
CCCCCCCCCHHHHHH
45.0030291188
298PhosphorylationLGDLMAATNNFSSGN
HHHHHHHCCCCCCCC
22.58-
383PhosphorylationMVNGTLFSQLHNGGL
HHCCCHHHHHHCCCC
34.64-
399PhosphorylationDAVLDWPTRRAIGVG
CEECCCCCHHHHCCC
28.65-
456PhosphorylationKLVGSRDSNDSSFNN
HHHCCCCCCCCCCCC
41.2319880383
459PhosphorylationGSRDSNDSSFNNGDL
CCCCCCCCCCCCCCC
40.8719880383
460PhosphorylationSRDSNDSSFNNGDLG
CCCCCCCCCCCCCCC
34.5519880383
476PhosphorylationLGYVAPEYSSTMVAS
HHEECCCCCCCCHHH
13.58-
478PhosphorylationYVAPEYSSTMVASLK
EECCCCCCCCHHHCC
21.44-
479PhosphorylationVAPEYSSTMVASLKG
ECCCCCCCCHHHCCC
15.10-
483PhosphorylationYSSTMVASLKGDVYG
CCCCCHHHCCCCEEE
21.14-
586PhosphorylationMADKHGVSEHYDEFP
HHHHCCCCCCCCCCC
24.2123111157
589PhosphorylationKHGVSEHYDEFPLVF
HCCCCCCCCCCCCEE
17.0825561503

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 Y1719_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of Y1719_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 Y1719_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HHP2_ARATHHHP2physical
24833385
UBC32_ARATHUBC32physical
24833385
UBC34_ARATHUBC34physical
24833385
AB12I_ARATHAT3G21580physical
24833385
CNIH1_ARATHAT3G12180physical
24833385
CP21D_ARATHAT3G66654physical
24833385
WAK3_ARATHWAK3physical
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 Y1719_ARATH

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-586, AND MASSSPECTROMETRY.
"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-586, AND MASSSPECTROMETRY.

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