Y5815_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: Y5815_ARATH
• UniProt AC: Q9LVN2
• Protein Name: Probably inactive leucine-rich repeat receptor-like protein kinase At5g58150
• Gene Name: At5g58150
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 785
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein .
• Protein Sequence: MRLSLWGSLLFFSFFVKHLTSLDPNTDAYHLSSFFSAMRLPNSPQAHTFSSLCSWPGVVVCDSSENVLHISASGLDLSGSIPDNTIGKMSKLQTLDLSGNKITSLPSDLWSLSLLESLNLSSNRISEPLPSNIGNFMSLHTLDLSFNSISGKIPAAISNLVNLTTLKLHNNDFQFGVPPELVHCRSLLSIDLSSNRLNESLPVGFGSAFPLLKSLNLSRNLFQGSLIGVLHENVETVDLSENRFDGHILQLIPGHKHNWSSLIHLDLSDNSFVGHIFNGLSSAHKLGHLNLACNRFRAQEFPEIGKLSALHYLNLSRTNLTNIIPREISRLSHLKVLDLSSNNLTGHVPMLSVKNIEVLDLSLNKLDGDIPRPLLEKLAMMQRFNFSFNNLTFCNPNFSQETIQRSFINIRNNCPFAAKPIITKGKKVNKKNTGLKIGLGLAISMAFLLIGLLLILVALRVRRKSRTWATKLAINNTEPNSPDQHDSTTDIKQATQIPVVMIDKPLMKMTLADLKAATFNFDRGTMLWEGKSGPTYGAVLPGGFRAALKVIPSGTTLTDTEVSIAFERLARINHPNLFPLCGYCIATEQRIAIYEDLDMVNLQSLLHNNGDDSAPWRLRHKIALGTARALAFLHHGCIPPMVHGEVKAATILLDSSQEPRLADFGLVKLLDEQFPGSESLDGYTPPEQERNASPTLESDVYSFGVVLLELVSGKKPEGDLVNWVRGLVRQGQGLRAIDPTMQETVPEDEIAEAVKIGYLCTADLPWKRPTMQQVVGLLKDISPNY

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
119	N-linked_Glycosylation	LSLLESLNLSSNRIS HHHHHHCCCCCCCCC	47.35	-
162	N-linked_Glycosylation	AAISNLVNLTTLKLH HHHHHHHCCCEEEEC	34.53	-
198	N-linked_Glycosylation	DLSSNRLNESLPVGF ECCCCCCCCCCCCCC	33.31	-
216	N-linked_Glycosylation	FPLLKSLNLSRNLFQ HHHHHHCCCCCCHHC	42.96	-
258	N-linked_Glycosylation	LIPGHKHNWSSLIHL ECCCCCCCCCCEEEE	45.16	-
312	Phosphorylation	GKLSALHYLNLSRTN HHHHHHHHHCCCCCC	9.72	19880383
314	N-linked_Glycosylation	LSALHYLNLSRTNLT HHHHHHHCCCCCCCC	28.89	-
319	N-linked_Glycosylation	YLNLSRTNLTNIIPR HHCCCCCCCCCCCCH	43.70	-
343	N-linked_Glycosylation	VLDLSSNNLTGHVPM EEECCCCCCCCCCCE	40.71	-
352	Phosphorylation	TGHVPMLSVKNIEVL CCCCCEEEECCCEEE	25.45	19880383
385	N-linked_Glycosylation	LAMMQRFNFSFNNLT HHHHHHCCCEECCCC	33.56	-
390	N-linked_Glycosylation	RFNFSFNNLTFCNPN HCCCEECCCCCCCCC	38.15	-
397	N-linked_Glycosylation	NLTFCNPNFSQETIQ CCCCCCCCCCHHHHH	34.90	-
477	Phosphorylation	TKLAINNTEPNSPDQ HEEEECCCCCCCCCC	48.62	15308754
481	Phosphorylation	INNTEPNSPDQHDST ECCCCCCCCCCCCCC	40.34	15308754
510	Phosphorylation	DKPLMKMTLADLKAA CCCCHHCCHHHHHHH	17.18	-
518	Phosphorylation	LADLKAATFNFDRGT HHHHHHHEEECCCCC	24.79	-
594	Phosphorylation	TEQRIAIYEDLDMVN HCHHHHHHCCCCCCC	8.38	-
679	Phosphorylation	EQFPGSESLDGYTPP CCCCCCCCCCCCCCC	33.20	-
683	Phosphorylation	GSESLDGYTPPEQER CCCCCCCCCCCHHHC	18.75	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of Y5815_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of Y5815_ARATH !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of Y5815_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HHP2_ARATH	HHP2	physical	24833385
HHP4_ARATH	HHP4	physical	24833385
UBC34_ARATH	UBC34	physical	24833385
CNIH1_ARATH	AT3G12180	physical	24833385
CP21D_ARATH	AT3G66654	physical	24833385
PAM74_ARATH	AT5G59650	physical	24833385
BETL2_ARATH	AT1G29060	physical	24833385
BET12_ARATH	ATBET12	physical	24833385

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-481, SUBCELLULARLOCATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
PubMed: 14506206