dbPTM

Y1044_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	Y1044_ARATH
UniProt AC	Q9S9Q9
Protein Name	BTB/POZ domain-containing protein At1g30440
Gene Name	At1g30440
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	665
Subcellular Localization
Protein Description	May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins..
Protein Sequence	MACMKLGSKSDAFQRQGQAWFCTTGLPSDIVVEVGEMSFHLHKFPLLSRSGVMERRIAEASKEGDDKCLIEISDLPGGDKTFELVAKFCYGVKLELTASNVVYLRCAAEHLEMTEEHGEGNLISQTETFFNQVVLKSWKDSIKALHSCDEVLEYADELNITKKCIESLAMRASTDPNLFGWPVVEHGGPMQSPGGSVLWNGISTGARPKHTSSDWWYEDASMLSFPLFKRLITVMESRGIREDIIAGSLTYYTRKHLPGLKRRRGGPESSGRFSTPLGSGNVLSEEEQKNLLEEIQELLRMQKGLVPTKFFVDMLRIAKILKASPDCIANLEKRIGMQLDQAALEDLVMPSFSHTMETLYDVDSVQRILDHFLGTDQIMPGGVGSPCSSVDDGNLIGSPQSITPMTAVAKLIDGYLAEVAPDVNLKLPKFQALAASIPEYARLLDDGLYRAIDIYLKHHPWLAETERENLCRLLDCQKLSLEACTHAAQNERLPLRIIVQVLFFEQLQLRTSVAGCFLVSDNLDGGSRQLRSGGYVGGPNEGGGGGGGWATAVRENQVLKVGMDSMRMRVCELEKECSNMRQEIEKLGKTTKGGGSASNGVGSKTWENVSKKLGFGFKLKSHQMCSAQEGSVSKSNNENVKIEKLKDVKERRGKHKKASSISSER

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
8	Phosphorylation	MACMKLGSKSDAFQR CCCCCCCCCCHHHHH	39.15	25561503
10	Phosphorylation	CMKLGSKSDAFQRQG CCCCCCCCHHHHHHC	35.55	25561503
248	Phosphorylation	REDIIAGSLTYYTRK CCCHHHHHHHHHHHC	14.44	28295753
250	Phosphorylation	DIIAGSLTYYTRKHL CHHHHHHHHHHHCCC	19.04	28295753
251	Phosphorylation	IIAGSLTYYTRKHLP HHHHHHHHHHHCCCC	14.24	28295753
253	Phosphorylation	AGSLTYYTRKHLPGL HHHHHHHHHCCCCCC	23.87	28295753
269	Phosphorylation	RRRGGPESSGRFSTP CCCCCCCCCCCCCCC	41.02	23111157
270	Phosphorylation	RRGGPESSGRFSTPL CCCCCCCCCCCCCCC	32.12	23111157
274	Phosphorylation	PESSGRFSTPLGSGN CCCCCCCCCCCCCCC	27.96	23776212
275	Phosphorylation	ESSGRFSTPLGSGNV CCCCCCCCCCCCCCC	21.59	23776212
279	Phosphorylation	RFSTPLGSGNVLSEE CCCCCCCCCCCCCHH	34.57	30291188
284	Phosphorylation	LGSGNVLSEEEQKNL CCCCCCCCHHHHHHH	38.38	23776212
449	Phosphorylation	RLLDDGLYRAIDIYL HHHHCHHHHHHHHHH	11.97	-
527	Phosphorylation	SDNLDGGSRQLRSGG ECCCCCCCCCCCCCC	23.53	30291188
532	Phosphorylation	GGSRQLRSGGYVGGP CCCCCCCCCCCCCCC	45.20	17317660
535	Phosphorylation	RQLRSGGYVGGPNEG CCCCCCCCCCCCCCC	10.23	23660473
565	Phosphorylation	VLKVGMDSMRMRVCE EEEEEHHHHHHHHHH	10.21	30407730
631	Phosphorylation	MCSAQEGSVSKSNNE CCCCCCCCCCCCCCC	23.59	23111157
633	Phosphorylation	SAQEGSVSKSNNENV CCCCCCCCCCCCCCC	31.87	25561503
659	Phosphorylation	RGKHKKASSISSER- CCCCCCCCCCCCCC-	36.76	25561503
660	Phosphorylation	GKHKKASSISSER-- CCCCCCCCCCCCC--	31.20	25561503
662	Phosphorylation	HKKASSISSER---- CCCCCCCCCCC----	28.26	25561503
663	Phosphorylation	KKASSISSER----- CCCCCCCCCC-----	35.40	25561503

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 Y1044_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of Y1044_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 Y1044_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of Y1044_ARATH !!

Drug and Disease Associations

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

Regulatory Network of Y1044_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-279, AND MASSSPECTROMETRY.	19376835 [Abstract]
"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-279, AND MASSSPECTROMETRY.	19245862 [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-532, AND MASSSPECTROMETRY.	17317660 [Abstract]