LRK32_ARATH - dbPTM
LRK32_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRK32_ARATH
UniProt AC Q9ZW11
Protein Name Putative inactive L-type lectin-domain containing receptor kinase III.2 {ECO:0000303|PubMed:19773388}
Gene Name LECRK32 {ECO:0000303|PubMed:19773388}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 623
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici..
Protein Sequence MANTYKSIAVSIIFLLYFSCVSSQQQTKFLNHGFLEANLLKSGSSKIHPSGHLELTNTSMRQIGQAFHGFPIPFLNPNSSNLVSFPTSFVFAITPGPGAPGHGLAFVISPSLDFSGALPSNYLGLFNTSNNGNSLNCILAVEFDTVQAVELNDIDDNHVGIDLNGVISIESTSAEYFDDREAKNISLRLASGKPIRVWIEYNATETMLNVTLAPLDRPKPKLPLLSRKLNLSGIISEENYVGFSAATGTVTSSHFVLGWSFSIEGKASDFDITKLPSLPDPLPPLSPSPSPPVSVMKNSSNTMLIIIIAASAIFGILILSFLAVCFFRRTENFTGGARKFSHQTISSATGGFDNSKLLGEGNSGSFYKGQLAPTEIIAVKRITCNTRQEKTALIAEIDAISKVKQRNLVDLHGYCSKGNEIYLVYEYVINRSLDRFLFSNDLPVLKWVHRFCIIKGIASALQHLHAEVQKPLIHGNVKASNVLLDGELNARLGDYGHGSRHSTTGHVAPELVNTGKATCATDVFEFGVLIMEIVCGRRAIEPTKEPVEISLVNWVLRGVKSGNLLRRCDKRIKKKNLVSEEVLLVLKTGLLCVRRSPEDRPMMKKVLEYLNGTEHLPHDDYVV
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
57N-linked_GlycosylationSGHLELTNTSMRQIG
CCCEEECCCCHHHHH
42.66-
78N-linked_GlycosylationPIPFLNPNSSNLVSF
CCCCCCCCCCCCEEC
57.93-
127N-linked_GlycosylationSNYLGLFNTSNNGNS
CCEEEEEECCCCCCC
47.87-
184N-linked_GlycosylationFDDREAKNISLRLAS
CCHHHHCCEEEEECC
35.81-
202N-linked_GlycosylationIRVWIEYNATETMLN
EEEEEEECCCCEEEE
27.83-
209N-linked_GlycosylationNATETMLNVTLAPLD
CCCCEEEEEEECCCC
17.57-
230N-linked_GlycosylationPLLSRKLNLSGIISE
CHHHCCCCCCCCCCC
34.88-
298N-linked_GlycosylationPPVSVMKNSSNTMLI
CCCEEEECCCCCEEH
32.35-

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 LRK32_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRK32_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 LRK32_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HHP4_ARATHHHP4physical
24833385
UBC34_ARATHUBC34physical
24833385
UBC32_ARATHUBC32physical
24833385
ACBP6_ARATHACBP6physical
24833385
GSTUJ_ARATHGSTU19physical
24833385
TRXH5_ARATHTRX5physical
24833385
TPIS_ARATHTPIphysical
24833385
CNIH1_ARATHAT3G12180physical
24833385
SBP3_ARATHMAPR2physical
24833385
CP21D_ARATHAT3G66654physical
24833385
SPCS1_ARATHAT2G22425physical
24833385
LRK32_ARATHAT2G29250physical
24833385
WAK3_ARATHWAK3physical
24833385
PAM74_ARATHAT5G59650physical
24833385
BETL2_ARATHAT1G29060physical
24833385
VAP21_ARATHAT5G47180physical
24833385

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRK32_ARATH

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Related Literatures of Post-Translational Modification

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