dbPTM

LRK81_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LRK81_ARATH
UniProt AC	Q9LFH9
Protein Name	L-type lectin-domain containing receptor kinase VIII.1
Gene Name	LECRK81
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	715
Subcellular Localization	Cell membrane Single-pass type I membrane protein .
Protein Description
Protein Sequence	MSLFLSFFISILLCFFNGATTTQFDFSTLAISNLKLLGDARLSNGIVGLTRDLSVPNSGAGKVLYSNPIRFRQPGTHFPTSFSSFFSFSITNVNPSSIGGGLAFVISPDANSIGIAGGSLGLTGPNGSGSKFVAVEFDTLMDVDFKDINSNHVGFDVNGVVSSVSGDLGTVNIDLKSGNTINSWIEYDGLTRVFNVSVSYSNLKPKVPILSFPLDLDRYVNDFMFVGFSGSTQGSTEIHSIEWWSFSSSFGSSLGSGSGSPPPRANLMNPKANSVKSPPPLASQPSSSAIPISSNTQLKTSSSSSCHSRFCKENPGTIAGVVTAGAFFLALFAGALFWVYSKKFKRVERSDSFASEIIKAPKEFSYKELKAGTKNFNESRIIGHGAFGVVYRGILPETGDIVAVKRCSHSSQDKKNEFLSELSIIGSLRHRNLVRLQGWCHEKGEILLVYDLMPNGSLDKALFESRFTLPWDHRKKILLGVASALAYLHRECENQVIHRDVKSSNIMLDESFNAKLGDFGLARQIEHDKSPEATVAAGTMGYLAPEYLLTGRASEKTDVFSYGAVVLEVVSGRRPIEKDLNVQRHNVGVNPNLVEWVWGLYKEGKVSAAADSRLEGKFDEGEMWRVLVVGLACSHPDPAFRPTMRSVVQMLIGEADVPVVPKSRPTMSFSTSHLLLSLQDTLSDCNTVALNSSRSSSWSVPEHNVIIRSDDDHLV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
126	N-linked_Glycosylation	SLGLTGPNGSGSKFV CCCCCCCCCCCCEEE	59.62	-
195	N-linked_Glycosylation	DGLTRVFNVSVSYSN CCCEEEEEEEEECCC	23.46	-
350	Phosphorylation	KFKRVERSDSFASEI HCCCCCCCCCHHHHH	24.89	25561503
352	Phosphorylation	KRVERSDSFASEIIK CCCCCCCCHHHHHHH	24.78	15308754
355	Phosphorylation	ERSDSFASEIIKAPK CCCCCHHHHHHHCCC	27.58	15308754

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 LRK81_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LRK81_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 LRK81_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of LRK81_ARATH !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LRK81_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-352, IDENTIFICATION BY MASS SPECTROMETRY, ANDSUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].	17317660 [Abstract]
"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-352 AND SER-355,SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.	15308754 [Abstract]
"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-352 AND SER-355,SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.	14506206 [Abstract]