dbPTM

Y1515_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	Y1515_ARATH
UniProt AC	O23052
Protein Name	Uncharacterized TPR repeat-containing protein At1g05150
Gene Name	At1g05150
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	808
Subcellular Localization
Protein Description
Protein Sequence	MATRGSRSEKVKRIFQQFDGNHDGGLNREEMAALVVAVNPRVKFSDEQINAILDEVFRTYAEFIDPNKGLTYDGLLRTYDDGAGDVDRDFDALGLELNADETTIKGSEAASSSSITDERAVEAQKKQRTAAWAVSPNHGIVFDETWKLVDDLEILVKRLKSKQEKDGKLKADNNNNNVDAFSDAGWSRELGPSSEISEKRIYWEESSHDYGVFVKELGVLRSKADGARSREEAFDGHMAIGRVLYEHQLFKEALVSFKRACELQPTDVRPHFKAGNCLYVLGKCKESKDEFLLALEAAESGGNQWAYLLPQIYVNLGIALEGEGMVLSACEYYREAAILCPTHFRALKLLGSALFGVGEYRAAVKALEEAIYLKPDYADAHCDLASSLHSMGEDERAIEVFQRAIDLKPGHVDALYNLGGLYMDLGRFQRASEMYTRVLTVWPNHWRAQLNKAVSLLGAGETEEAKRALKEALKLTNRVELHDAISHLKHLQKKKGKNNGNGNGGEGPFIVVEPSKFKTVGEKTTLRPDLATALQIRAFQRVTRLGKCDVEAVRKEMRDNDVPVSYSGSGGPTKSIRKPNLEEILRRLLSSLKPDTFQGAIKAINEKILALLDDSGSGRVDMGMFYAVIAPLCGGHSDKRKRVAFDALLWRPVNEGSSQITKTDAVKYIKLLRAIYIPSHGMSEMLEVHGEEEAESSVTVTFNQFLAMFDDPDWGFGIMSTILKLEANDRNRHGNQVCSVCRYPVIGSRFKEVKARFSLCNQCYGEGKVPPSFKQEEYKFREYESEAEAMKAKCVCFSMQSHKKAIAT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
111	Phosphorylation	IKGSEAASSSSITDE ECCCHHCCCCCCCCH	37.49	30407730
112	Phosphorylation	KGSEAASSSSITDER CCCHHCCCCCCCCHH	24.31	29654922
113	Phosphorylation	GSEAASSSSITDERA CCHHCCCCCCCCHHH	24.22	29654922
114	Phosphorylation	SEAASSSSITDERAV CHHCCCCCCCCHHHH	31.30	30407730
116	Phosphorylation	AASSSSITDERAVEA HCCCCCCCCHHHHHH	33.48	25561503
135	Phosphorylation	RTAAWAVSPNHGIVF CCHHEECCCCCCEEE	16.55	30291188
182	Phosphorylation	NNNVDAFSDAGWSRE CCCCHHHHCCCCCCC	28.42	17317660
187	Phosphorylation	AFSDAGWSRELGPSS HHHCCCCCCCCCCCC	18.24	30291188
193	Phosphorylation	WSRELGPSSEISEKR CCCCCCCCCHHCCCC	38.51	27288362
194	Phosphorylation	SRELGPSSEISEKRI CCCCCCCCHHCCCCE	41.92	30407730
197	Phosphorylation	LGPSSEISEKRIYWE CCCCCHHCCCCEECC	32.77	30407730
416	Phosphorylation	PGHVDALYNLGGLYM CCCHHHHHHCCCHHH	15.29	28295753
422	Phosphorylation	LYNLGGLYMDLGRFQ HHHCCCHHHHHHHHH	7.58	28295753
565	Phosphorylation	RDNDVPVSYSGSGGP HCCCCCCCCCCCCCC	13.91	27532006
566	Phosphorylation	DNDVPVSYSGSGGPT CCCCCCCCCCCCCCC	19.79	27532006
567	Phosphorylation	NDVPVSYSGSGGPTK CCCCCCCCCCCCCCC	20.98	30291188
569	Phosphorylation	VPVSYSGSGGPTKSI CCCCCCCCCCCCCCC	34.34	27532006
573	Phosphorylation	YSGSGGPTKSIRKPN CCCCCCCCCCCCCCC	40.47	23776212

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 Y1515_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of Y1515_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 Y1515_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of Y1515_ARATH !!

Drug and Disease Associations

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

Regulatory Network of Y1515_ARATH

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-567, AND MASSSPECTROMETRY.	19376835 [Abstract]
"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 [LARGE SCALE ANALYSIS] AT SER-182, AND MASSSPECTROMETRY.	17317660 [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-187, 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-567, AND MASSSPECTROMETRY.	14506206 [Abstract]