dbPTM

Y1733_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	Y1733_ARATH
UniProt AC	Q8RY60
Protein Name	DUF21 domain-containing protein At1g47330
Gene Name	CBSDUF7
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	527
Subcellular Localization	Membrane Multi-pass membrane protein .
Protein Description
Protein Sequence	MSSDIPCCGTTFSLYVVIIIALVAFAGLMAGLTLGLMSLGLVDLEVLIKSGRPQDRINAGKIFPVVKNQHLLLCTLLIGNSMAMEALPIFLDKIVPPWLAILLSVTLILVFGEIMPQAVCTRYGLKVGAIMAPFVRVLLVLFFPISYPISKVLDWMLGKGHGVLLRRAELKTFVNFHGNEAGKGGDLTTDETSIITGALELTEKTAKDAMTPISNAFSLELDTPLNLETLNTIMSVGHSRVPVYFRNPTHIIGLILVKNLLAVDARKEVPLRKMSMRKIPRVSETMPLYDILNEFQKGHSHIAVVYKDLDEQEQSPETSENGIERRKNKKTKDELFKDSCRKPKAQFEVSEKEVFKIETGDAKSGKSENGEEQQGSGKTSLLAAPAKKRHRGCSFCILDIENTPIPDFPTNEEVVGVITMEDVIEELLQEEILDETDEYVNIHNRIRVNMHASPENLPSVITSITQSSSGSTSPNQTSHMATPDSSPTTKPSNSSPTRKPSVSSPTREPSDSSHSMAPKHEESTQTL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
315	Phosphorylation	DLDEQEQSPETSENG CCCHHHCCCCCCHHH	24.77	17317660
318	Phosphorylation	EQEQSPETSENGIER HHHCCCCCCHHHHHH	44.73	25561503
319	Phosphorylation	QEQSPETSENGIERR HHCCCCCCHHHHHHH	27.66	25561503
475	N-linked_Glycosylation	SSGSTSPNQTSHMAT CCCCCCCCCCCCCCC	58.49	-
506	Phosphorylation	KPSVSSPTREPSDSS CCCCCCCCCCCCCCC	50.00	23111157

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 Y1733_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of Y1733_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 Y1733_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of Y1733_ARATH !!

Drug and Disease Associations

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

Regulatory Network of Y1733_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND MASSSPECTROMETRY.	19245862 [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-315, AND MASSSPECTROMETRY.	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-315, AND MASSSPECTROMETRY.	14506206 [Abstract]