SPY_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SPY_ARATH
• UniProt AC: Q96301
• Protein Name: Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY
• Gene Name: SPY
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 914
• Subcellular Localization: Cytoplasm . Nucleus .
• Protein Description: Probable O-linked N-acetylglucosamine transferase (OGT) involved in various processes such as gibberellin (GA) signaling pathway and circadian clock. OGTs catalyze the addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. Probably acts by adding O-linked sugars to yet unknown proteins. Acts as a repressor of GA signaling pathway to inhibit hypocotyl elongation. Functions with GIGANTEA (GI) in pathways controlling flowering, circadian cotyledon movements and hypocotyl elongation. Acts as a light-regulated promoter of elongation via its interaction with GI. Acts as an activator of cytokinin signaling. Required with SEC for gamete and seed development. Its OGT activity has been proved in vitro but not in vivo..
• Protein Sequence: MVGLEDDTERERSPVVENGFSNGSRSSSSSAGVLSPSRKVTQGNDTLSYANILRARNKFADALALYEAMLEKDSKNVEAHIGKGICLQTQNKGNLAFDCFSEAIRLDPHNACALTHCGILHKEEGRLVEAAESYQKALMADASYKPAAECLAIVLTDLGTSLKLAGNTQEGIQKYYEALKIDPHYAPAYYNLGVVYSEMMQYDNALSCYEKAALERPMYAEAYCNMGVIYKNRGDLEMAITCYERCLAVSPNFEIAKNNMAIALTDLGTKVKLEGDVTQGVAYYKKALYYNWHYADAMYNLGVAYGEMLKFDMAIVFYELAFHFNPHCAEACNNLGVLYKDRDNLDKAVECYQMALSIKPNFAQSLNNLGVVYTVQGKMDAAASMIEKAILANPTYAEAFNNLGVLYRDAGNITMAIDAYEECLKIDPDSRNAGQNRLLAMNYINEGLDDKLFEAHRDWGWRFTRLHPQYTSWDNLKDPERPITIGYISPDFFTHSVSYFIEAPLTHHDYTKYKVVVYSAVVKADAKTYRFRDKVLKKGGVWKDIYGIDEKKIASMVREDKIDILVELTGHTANNKLGTMACRPAPVQVTWIGYPNTTGLPTVDYRITDSLADPPDTKQKQVEELVRLPDCFLCYTPSPEAGPVCPTPALSNGFVTFGSFNNLAKITPKVLQVWARILCAVPNSRLVVKCKPFCCDSIRQRFLTTLEQLGLESKRVDLLPLILFNHDHMQAYSLMDISLDTFPYAGTTTTCESLYMGVPCVTMAGSVHAHNVGVSLLTKVGLGHLVAKNEDEYVQLSVDLASDVTALSKLRMSLRDLMAGSPVCNGPSFAVGLESAYRNMWKKYCKGEVPSLRRMEMLQKEVHDDPLISKDLGPSRVSVTGEATPSLKANGSAPVPSSLPTQSPQLSKRMDSTS

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
13	Phosphorylation	DDTERERSPVVENGF CCCCCCCCCCCCCCC	19.79	25561503
26	Phosphorylation	GFSNGSRSSSSSAGV CCCCCCCCCCCCCCE	35.95	19376835
27	Phosphorylation	FSNGSRSSSSSAGVL CCCCCCCCCCCCCEE	32.88	19376835
28	Phosphorylation	SNGSRSSSSSAGVLS CCCCCCCCCCCCEEC	29.56	19376835
29	Phosphorylation	NGSRSSSSSAGVLSP CCCCCCCCCCCEECC	26.59	19376835
30	Phosphorylation	GSRSSSSSAGVLSPS CCCCCCCCCCEECCC	30.87	19376835
35	Phosphorylation	SSSAGVLSPSRKVTQ CCCCCEECCCCEEEC	20.58	23111157
37	Phosphorylation	SAGVLSPSRKVTQGN CCCEECCCCEEECCC	41.16	19376835
518	Phosphorylation	TKYKVVVYSAVVKAD CCCEEEEEEEEEECC	4.55	19880383
519	Phosphorylation	KYKVVVYSAVVKADA CCEEEEEEEEEECCC	11.72	19880383
555	Phosphorylation	IDEKKIASMVREDKI CCHHHHHHHHHHCCC	22.68	19880383

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SPY_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 SPY_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GIGAN_ARATH	GI	physical	15155885
SPY_ARATH	SPY	physical	11457975
TCP14_ARATH	TCP14	physical	22267487
TCP15_ARATH	AT1G69690	physical	22267487
SWI3C_ARATH	SWI3C	physical	23893173

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale Arabidopsis phosphoproteome profiling reveals novelchloroplast kinase substrates and phosphorylation networks.";
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,Grossmann J., Gruissem W., Baginsky S.;
Plant Physiol. 150:889-903(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASSSPECTROMETRY.
PubMed: 19376835

"Site-specific phosphorylation profiling of Arabidopsis proteins bymass spectrometry and peptide chip analysis.";
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,Hirt H.;
J. Proteome Res. 7:2458-2470(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASSSPECTROMETRY.
PubMed: 18433157