Y5838_ARATH - dbPTM
Y5838_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID Y5838_ARATH
UniProt AC Q9ASS4
Protein Name Probably inactive leucine-rich repeat receptor-like protein kinase At5g48380
Gene Name At5g48380
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 620
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description
Protein Sequence MMMGRLVFVIWLYNCLCLLLLSSLVDADQANIDCLRTFKSQVEDPNRYLSTWVFGNETAGYICKFSGVTCWHDDENRVLSIKLSGYGLRGVFPPAVKLCADLTGLDLSRNNFSGPLPANISTLIPLVTILDLSYNSFSGEIPMLISNITFLNTLMLQHNQFTGTLPPQLAQLGRLKTFSVSDNRLVGPIPNFNQTLQFKQELFANNLDLCGKPLDDCKSASSSRGKVVIIAAVGGLTAAALVVGVVLFFYFRKLGAVRKKQDDPEGNRWAKSLKGQKGVKVFMFKKSVSKMKLSDLMKATEEFKKDNIIATGRTGTMYKGRLEDGSLLMIKRLQDSQRSEKEFDAEMKTLGSVKNRNLVPLLGYCVANKERLLMYEYMANGYLYDQLHPADEESFKPLDWPSRLKIAIGTAKGLAWLHHSCNPRIIHRNISSKCILLTAEFEPKISDFGLARLMNPIDTHLSTFVNGEFGDFGYVAPEYSRTMVATPKGDVYSFGVVLLELVTGQKATSVTKVSEEKAEEENFKGNLVEWITKLSSESKLQEAIDRSLLGNGVDDEIFKVLKVACNCVLPEIAKQRPTMFEVYQLLRAIGESYNFTADDDILIPSESGEGDFIEELIVAR
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
56N-linked_GlycosylationLSTWVFGNETAGYIC
EEEEECCCCCCEEEE
31.79-
111N-linked_GlycosylationGLDLSRNNFSGPLPA
CCCCCCCCCCCCCCC
31.20-
119N-linked_GlycosylationFSGPLPANISTLIPL
CCCCCCCCHHHHHHH
27.14-
147N-linked_GlycosylationEIPMLISNITFLNTL
CCCHHHHHHHHHHHH
30.26-
177PhosphorylationAQLGRLKTFSVSDNR
HHHCCCEEEECCCCE
26.2425561503
179PhosphorylationLGRLKTFSVSDNRLV
HCCCEEEECCCCEEE
26.4125561503
193N-linked_GlycosylationVGPIPNFNQTLQFKQ
ECCCCCCCHHHHHHH
40.33-
300PhosphorylationLSDLMKATEEFKKDN
HHHHHHHHHHHHHCC
30.45-
463PhosphorylationPIDTHLSTFVNGEFG
CCHHHHHHHCCCCCC
37.65-
479PhosphorylationFGYVAPEYSRTMVAT
CCEECCCCEEEEEEC
11.46-
482PhosphorylationVAPEYSRTMVATPKG
ECCCCEEEEEECCCC
15.28-
547PhosphorylationLQEAIDRSLLGNGVD
HHHHHHHHHHCCCCC
24.97-

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 Y5838_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of Y5838_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 Y5838_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BON1_ARATHBON1physical
21623975
BON3_ARATHBON3physical
21623975
PAM74_ARATHAT5G59650physical
21423366
Y5838_ARATHBIR1physical
21423366
Y5659_ARATHLRR1physical
21423366
Y5129_ARATHAT5G10290physical
21423366
BLUS1_ARATHAT4G14480physical
21423366
TET11_ARATHTET11physical
21423366
Y3804_ARATHAT3G28040physical
21423366
Y5639_ARATHAT5G63930physical
21423366
Y2289_ARATHAT2G28960physical
21423366
MLO2_ARATHMLO2physical
21423366
HHP2_ARATHHHP2physical
24833385
UBC34_ARATHUBC34physical
24833385
NAC89_ARATHNAC089physical
24833385
DHAR1_ARATHDHAR1physical
24833385
TRXH3_ARATHTRX3physical
24833385
CALX2_ARATHAT5G07340physical
24833385
CNIH1_ARATHAT3G12180physical
24833385
MSBP2_ARATHMAPR3physical
24833385
CP21D_ARATHAT3G66654physical
24833385
PPA3_ARATHPAP3physical
24833385
PAM74_ARATHAT5G59650physical
24833385
RUS3_ARATHRUS3physical
24833385
BET12_ARATHATBET12physical
24833385
TBL18_ARATHTBL18physical
24833385
BAK1_ARATHBAK1genetic
25944825

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of Y5838_ARATH

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-547, SUBCELLULARLOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.

TOP