dbPTM

CRN_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CRN_ARATH
UniProt AC	Q9LYU7
Protein Name	Inactive leucine-rich repeat receptor-like protein kinase CORYNE
Gene Name	CRN
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	401
Subcellular Localization	Cell membrane Single-pass type I membrane protein . Requires CLV2 for export from the endoplasmic reticulum and localization to the plasma membrane.
Protein Description	Involved in the perception of CLV3 and CLV3-like (CLE) peptides, that acts as a extracellular signals regulating meristems maintenance. Modulates root, shoot and flower apical meristems maintenance and floral organ development regulation, probably via CLAVATA (CLV)-like pathways involving at least CLV3 and CLE19. In complex with CLV2, perceives secreted CLV3-like effector proteins from plant-parasitic cyst nematodes as ligand mimics of the plant CLE signaling pathway. [PubMed: 21265896 This recognition is required for proper feeding structure (syncytium) development and ultimately successful nematode infection]
Protein Sequence	MKQRRRRNGCSSSNTISLLLLFFLVFFSRTSTSTSCRRRTVKHLSTTSTSSTPLESRITSKVIVISIVSGILTGLVSALVLAFLVRSIVKFMKQTPILKGPVVFSPKITPKSLHAALSNGIQLLGSDLNGKYYKMVLDNGLVVAVKRLGSLEGVGSPESSSSKSVKRRLQKELELLAGLRHRNLMSLRAYVRESDEFSLVYDYMPNGSLEDVMNKVRTKEVELGWEIRLRVAVGIVKGLQYLHFSCETQILHYNLKPTNVMLDSEFEPRLADCGLAKIMPSSHTAVSCYSAPESSQSNRYTDKSDIFSFGMILGVLLTGRDPTHPFCEESASGGSLGQWLKHLQQSGEAREALDKTILGEEVEEDEMLMALRITIICLSDFPADRPSSDELVHMLTQLHSF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference	Orthologous Protein Cluster
150	Phosphorylation	VAVKRLGSLEGVGSP EEEEECCCCCCCCCC	28.04	30407730
156	Phosphorylation	GSLEGVGSPESSSSK CCCCCCCCCCCCCCH	24.08	30291188

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 CRN_ARATH !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CLV2_ARATH	CLV2	physical	19843317
CRN_ARATH	CRN	physical	19933383
CLV2_ARATH	CLV2	physical	19933383
CLV2_ARATH	CLV2	physical	20978082
P2C70_ARATH	KAPP	physical	21214859
CCI1_ARATH	CPI1	physical	23776660

Drug and Disease Associations

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

Regulatory Network of CRN_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-156, SUBCELLULARLOCATION, 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-156, SUBCELLULARLOCATION, AND MASS SPECTROMETRY.	14506206 [Abstract]