Y2393_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: Y2393_ARATH
• UniProt AC: O80623
• Protein Name: Probable receptor-like protein kinase At2g39360
• Gene Name: At2g39360
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 815
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein .
• Protein Sequence: MINLKLFLELKLCFLITLLCSSHISSVSDTFFINCGSPTNVTVNNRTFVSDNNLVQGFSVGTTDSNSGDESTLFQTARVFSDESSSTYRFPIEEHGWFLIRIYFLPLVSASQDLTTARFSVSAQNFTLIREYKPSTTSVVREYILNVTTDSLLLQFLPRTGSVSFINALEVLRLPETLIPEDAKLIGTQKDLKLSSHAMETVSRVNMGNLSVSRDQDKLWRQWDSDSAYKAHFGTPVMNLKAVNFSAGGITDDIAPVYVYGTATRLNSDLDPNTNANLTWTFKVEPGFDYFVRFHFCNIIVDPFGFERQIRFDIFVNSEKVRTIDMTEVLNGTFGAPFFVDAVMRKAKSREGFLNLSIGLVMDVSSYPVSFINGFEISKLSNDKRSLDAFDAILPDGSSSNKSSNTSVGLIAGLSAALCVALVFGVVVSWWCIRKRRRRNRQMQTVHSRGDDHQIKKNETGESLIFSSSKIGYRYPLALIKEATDDFDESLVIGVGGFGKVYKGVLRDKTEVAVKRGAPQSRQGLAEFKTEVEMLTQFRHRHLVSLIGYCDENSEMIIVYEYMEKGTLKDHLYDLDDKPRLSWRQRLEICVGAARGLHYLHTGSTRAIIHRDVKSANILLDDNFMAKVADFGLSKTGPDLDQTHVSTAVKGSFGYLDPEYLTRQQLTEKSDVYSFGVVMLEVVCGRPVIDPSLPREKVNLIEWAMKLVKKGKLEDIIDPFLVGKVKLEEVKKYCEVTEKCLSQNGIERPAMGDLLWNLEFMLQVQAKDEKAAMVDDKPEASVVGSTMQFSVNGVGDIAGVSMSKVFAQMVREETR

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
40	N-linked_Glycosylation	INCGSPTNVTVNNRT EECCCCCEEEECCEE	30.74	-
45	N-linked_Glycosylation	PTNVTVNNRTFVSDN CCEEEECCEEEECCC	39.78	-
125	N-linked_Glycosylation	RFSVSAQNFTLIREY CEEEECCCEEEEEEC	31.42	-
146	N-linked_Glycosylation	VVREYILNVTTDSLL HHHHHHHHCCCCCHH	21.38	-
209	N-linked_Glycosylation	VSRVNMGNLSVSRDQ HHHCCCCCCCCCCCH	20.55	-
244	N-linked_Glycosylation	VMNLKAVNFSAGGIT CCCEEEEEECCCCCC	29.98	-
277	N-linked_Glycosylation	LDPNTNANLTWTFKV CCCCCCCCEEEEEEE	39.82	-
331	N-linked_Glycosylation	IDMTEVLNGTFGAPF EECHHHHCCCCCCCH	53.27	-
355	N-linked_Glycosylation	KSREGFLNLSIGLVM HCCCCCCCEEEEEEE	29.49	-
401	N-linked_Glycosylation	LPDGSSSNKSSNTSV CCCCCCCCCCCCCHH	50.61	-
405	N-linked_Glycosylation	SSSNKSSNTSVGLIA CCCCCCCCCHHHHHH	43.39	-
469	Phosphorylation	ESLIFSSSKIGYRYP CCEEEECCCCCCCCC	27.39	17317660
646	Phosphorylation	DLDQTHVSTAVKGSF CCCCHHHHHHHHCCC	11.75	23111157
647	Phosphorylation	LDQTHVSTAVKGSFG CCCHHHHHHHHCCCC	34.09	23111157
652	Phosphorylation	VSTAVKGSFGYLDPE HHHHHHCCCCCCCHH	15.13	15308754

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

Oops, there are no upstream regulatory protein records of Y2393_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of Y2393_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 Y2393_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HHP2_ARATH	HHP2	physical	24833385
UBC32_ARATH	UBC32	physical	24833385
UBC34_ARATH	UBC34	physical	24833385
CNIH1_ARATH	AT3G12180	physical	24833385
CP21D_ARATH	AT3G66654	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

"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-469, IDENTIFICATION BY MASS SPECTROMETRY [LARGESCALE ANALYSIS], AND SUBCELLULAR LOCATION.
PubMed: 17317660