dbPTM

RCA_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RCA_ARATH
UniProt AC	P10896
Protein Name	Ribulose bisphosphate carboxylase/oxygenase activase, chloroplastic
Gene Name	RCA
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	474
Subcellular Localization	Plastid, chloroplast stroma. Plastid, chloroplast, plastoglobule .
Protein Description	Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure..
Protein Sequence	MAAAVSTVGAINRAPLSLNGSGSGAVSAPASTFLGKKVVTVSRFAQSNKKSNGSFKVLAVKEDKQTDGDRWRGLAYDTSDDQQDITRGKGMVDSVFQAPMGTGTHHAVLSSYEYVSQGLRQYNLDNMMDGFYIAPAFMDKLVVHITKNFLTLPNIKVPLILGIWGGKGQGKSFQCELVMAKMGINPIMMSAGELESGNAGEPAKLIRQRYREAADLIKKGKMCCLFINDLDAGAGRMGGTTQYTVNNQMVNATLMNIADNPTNVQLPGMYNKEENARVPIICTGNDFSTLYAPLIRDGRMEKFYWAPTREDRIGVCKGIFRTDKIKDEDIVTLVDQFPGQSIDFFGALRARVYDDEVRKFVESLGVEKIGKRLVNSREGPPVFEQPEMTYEKLMEYGNMLVMEQENVKRVQLAETYLSQAALGDANADAIGRGTFYGKGAQQVNLPVPEGCTDPVAENFDPTARSDDGTCVYNF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
27	Phosphorylation	GSGSGAVSAPASTFL CCCCCCCCCCCHHCC	28.18	29654922
31	Phosphorylation	GAVSAPASTFLGKKV CCCCCCCHHCCCCEE	20.73	29654922
32	Phosphorylation	AVSAPASTFLGKKVV CCCCCCHHCCCCEEE	25.61	29654922
51	Phosphorylation	FAQSNKKSNGSFKVL HHHCCCCCCCCEEEE	48.29	19880383
76	Phosphorylation	DRWRGLAYDTSDDQQ CCCCEEEECCCCCHH	25.46	23776212
78	Phosphorylation	WRGLAYDTSDDQQDI CCEEEECCCCCHHHH	22.75	30291188
79	Phosphorylation	RGLAYDTSDDQQDIT CEEEECCCCCHHHHH	35.97	30291188
86	Phosphorylation	SDDQQDITRGKGMVD CCCHHHHHCCCCCHH	41.48	23776212
94	Phosphorylation	RGKGMVDSVFQAPMG CCCCCHHEEEECCCC	17.27	29654922
167	Acetylation	ILGIWGGKGQGKSFQ EEEECCCCCCCHHHH	44.09	21311031
172	Phosphorylation	GGKGQGKSFQCELVM CCCCCCHHHHHHHHH	27.63	30291188
175	S-nitrosylation	GQGKSFQCELVMAKM CCCHHHHHHHHHHHC	4.04	22115780
182	Sulfoxidation	CELVMAKMGINPIMM HHHHHHHCCCCCEEE	4.77	25693801
188	Sulfoxidation	KMGINPIMMSAGELE HCCCCCEEEECCCCC	1.51	25693801
190	Phosphorylation	GINPIMMSAGELESG CCCCEEEECCCCCCC	18.75	30291188
241	Phosphorylation	AGRMGGTTQYTVNNQ CCCCCCCEEEEECCE	23.89	25368622
243	Phosphorylation	RMGGTTQYTVNNQMV CCCCCEEEEECCEEE	15.57	25368622
244	Phosphorylation	MGGTTQYTVNNQMVN CCCCEEEEECCEEEE	13.62	25368622
253	Phosphorylation	NNQMVNATLMNIADN CCEEEEEEEEECCCC	22.72	25368622
283	Phosphorylation	ARVPIICTGNDFSTL CCCCEEEECCCCHHC	28.72	14593172
376	Phosphorylation	IGKRLVNSREGPPVF HHHHHCCCCCCCCCC	24.99	30291188
388	Sulfoxidation	PVFEQPEMTYEKLME CCCCCCCCCHHHHHH	6.51	25693801
394	Sulfoxidation	EMTYEKLMEYGNMLV CCCHHHHHHHCCEEE	5.74	25693801
399	Sulfoxidation	KLMEYGNMLVMEQEN HHHHHCCEEEEECHH	2.31	25693801
415	Phosphorylation	KRVQLAETYLSQAAL HHHHHHHHHHHHHHH	24.93	24243849
416	Phosphorylation	RVQLAETYLSQAALG HHHHHHHHHHHHHHC	8.89	24243849
418	Phosphorylation	QLAETYLSQAALGDA HHHHHHHHHHHHCCC	13.83	30291188
434 (in isoform 2)	Phosphorylation	-	16.60	22074104
436 (in isoform 2)	Phosphorylation	-	20.12	22074104
445 (in isoform 2)	Phosphorylation	-	4.80	25561503
465	Phosphorylation	NFDPTARSDDGTCVY CCCCCCCCCCCCEEE	37.27	19880383
469	Phosphorylation	TARSDDGTCVYNF-- CCCCCCCCEEECC--	13.04	23572148

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
78	T	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
78	T	Phosphorylation		27064346
Phosphorylated at Thr-78 by CK2.

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 RCA_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CPNB1_ARATH	CPN60B	physical	18353762

Drug and Disease Associations

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

Regulatory Network of RCA_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 THR-78, 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 THR-78, AND MASSSPECTROMETRY.	19245862 [Abstract]

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