dbPTM

Y2245_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	Y2245_ARATH
UniProt AC	Q8S8L9
Protein Name	Uncharacterized TPR repeat-containing protein At2g32450
Gene Name	At2g32450
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	802
Subcellular Localization
Protein Description
Protein Sequence	MTTRGSRSEKVKRIFQQFDGNLDGGLSREEMSALVVAVNPRVKFSDEQISAILDEVFRTYAEFIDGDKGLTFDGLLRTYDDGAGDVDRDFDALGIEFNEETKGASEASSSSITDERAVEAQKQQRTAAWAVSPNHGIVFDETWKLVDDLEILVKRLKSKQEKDGKLKVDNNNVDAFSEAGWSRELGPSSDISDKRIYWEESSHDYGVFVKELGVLRSKADGARSREEAFDGHMAIGKVLYEHQLFKEALVSFKRACELQPTDVRPHFKAGNCLYVLGKYKESKDEFLLALEAAESGGNQWAYLLPQIYVNLGISLEGEGMVLSACEYYREAAILCPTHYRALKLLGSALFGVGEYRAAVKALEEAIYLKPDYADAHCDLASSLHAMGEDERAIEVFQRAIDLKPGHVDALYNLGGLYMDLGRFQRASEMYTRVLAVWPNHWRAQLNKAVSLLGAGETEEAKRALKEALKMTNRVELHDAVSHLKQLQKKKKVKKGNSANEEGPFIVVESSKFKTVGEKTTLRPDLAIALQVRAFQRVTRLWKCDVEALRREMRDNNVPVSYSGNGIPTKSIRRPNLEEILRRLLNVLKPETFQGAIKAINEKILSVLDDSGSGRVDLGMFYAVIAPLCGGHPDKRKRVAFDALLWKPVNEGSSQITKMEAVKYIKLLRAIYIPSQGMSEMLEVHGESDDTSTVTFNQFLEMYDDSEWGFGIMSTVFKLETRDRNRHGNQVCSVCRYPIIGSRFKEVKTGFSLCNQCYSEGKIPPTFKQQEEYKFREYASEVEAMKAKCVCFSMQSHKKTIAT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
101	Phosphorylation	GIEFNEETKGASEAS CCEECHHCCCCCCCC	28.71	19880383
109	Phosphorylation	KGASEASSSSITDER CCCCCCCCCCCCCHH	34.84	30407730
110	Phosphorylation	GASEASSSSITDERA CCCCCCCCCCCCHHH	24.22	30407730
111	Phosphorylation	ASEASSSSITDERAV CCCCCCCCCCCHHHH	31.30	30407730
113	Phosphorylation	EASSSSITDERAVEA CCCCCCCCCHHHHHH	33.48	19880383
132	Phosphorylation	RTAAWAVSPNHGIVF HHHHHHCCCCCCEEE	16.55	30291188
177	Phosphorylation	NNNVDAFSEAGWSRE CCCCHHHHHCCCCCC	28.40	25561503
182	Phosphorylation	AFSEAGWSRELGPSS HHHHCCCCCCCCCCC	18.24	17317660
189	Phosphorylation	SRELGPSSDISDKRI CCCCCCCCCCCCCEE	41.94	25561503
192	Phosphorylation	LGPSSDISDKRIYWE CCCCCCCCCCEEEEE	41.91	26811356
411	Phosphorylation	PGHVDALYNLGGLYM CCCHHHHHHCCCHHH	15.29	28295753
417	Phosphorylation	LYNLGGLYMDLGRFQ HHHCCCHHHHHCHHH	7.58	28295753
560	Phosphorylation	RDNNVPVSYSGNGIP HHCCCCCCCCCCCCC	13.91	15308754
561	Phosphorylation	DNNVPVSYSGNGIPT HCCCCCCCCCCCCCC	22.34	23111157
562	Phosphorylation	NNVPVSYSGNGIPTK CCCCCCCCCCCCCCC	20.48	30291188
568	Phosphorylation	YSGNGIPTKSIRRPN CCCCCCCCCCCCCCC	35.19	19376835
605	Phosphorylation	AINEKILSVLDDSGS HHHHHHHHHHCCCCC	24.90	24894044
612	Phosphorylation	SVLDDSGSGRVDLGM HHHCCCCCCCCCHHH	27.64	24894044

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 Y2245_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of Y2245_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 Y2245_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of Y2245_ARATH !!

Drug and Disease Associations

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

Regulatory Network of Y2245_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-562, 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-560, 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-560, AND MASSSPECTROMETRY.	14506206 [Abstract]