dbPTM

CAPP1_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CAPP1_ARATH
UniProt AC	Q9MAH0
Protein Name	Phosphoenolpyruvate carboxylase 1
Gene Name	PPC1
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	967
Subcellular Localization	Cytoplasm.
Protein Description	Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. Contributes probably to the adaptation to inorganic phosphate (Pi) deprivation..
Protein Sequence	MANRKLEKMASIDVHLRQLVPGKVSEDDKLVEYDALLLDRFLDILQDLHGEDLRETVQELYEHSAEYEGKHEPKKLEELGSVLTSLDPGDSIVIAKAFSHMLNLANLAEEVQIAYRRRIKKLKKGDFVDESSATTESDLEETFKKLVGDLNKSPEEIFDALKNQTVDLVLTAHPTQSVRRSLLQKHGRIRDCLAQLYAKDITPDDKQELDEALQREIQAAFRTDEIKRTPPTPQDEMRAGMSYFHETIWKGVPKFLRRVDTALKNIGIEERVPYNAPLIQFSSWMGGDRDGNPRVTPEVTRDVCLLARMMAATMYFNQIEDLMFEMSMWRCNDELRARADEVHANSRKDAAKHYIEFWKSIPTTEPYRVILGDVRDKLYHTRERAHQLLSNGHSDVPVEATFINLEQFLEPLELCYRSLCSCGDRPIADGSLLDFLRQVSTFGLSLVRLDIRQESDRHTDVLDAITTHLDIGSYREWSEERRQEWLLSELSGKRPLFGSDLPKTEEIADVLDTFHVIAELPADSFGAYIISMATAPSDVLAVELLQRECRVKQPLRVVPLFEKLADLEAAPAAVARLFSVDWYKNRINGKQEVMIGYSDSGKDAGRLSAAWQLYKAQEELVKVAKEYGVKLTMFHGRGGTVGRGGGPTHLAILSQPPDTINGSLRVTVQGEVIEQSFGEEHLCFRTLQRFTAATLEHGMRPPISPKPEWRALLDEMAVVATEEYRSVVFQEPRFVEYFRLATPELEYGRMNIGSRPSKRKPSGGIESLRAIPWIFAWTQTRFHLPVWLGFGSAIRHVIEKDVRNLHMLQDMYQHWPFFRVTIDLIEMVFAKGDPGIAALYDKLLVSEELWPFGEKLRANFEETKKLILQTAGHKDLLEGDPYLKQRLRLRDSYITTLNVCQAYTLKRIRDPSYHVTLRPHISKEIAESSKPAKELIELNPTSEYAPGLEDTLILTMKGIAAGLQNTG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Sulfoxidation	ANRKLEKMASIDVHL CCHHHHHHHHCCHHH	2.30	23289948
11	Phosphorylation	RKLEKMASIDVHLRQ HHHHHHHHCCHHHHH	18.80	30291188
135	Phosphorylation	VDESSATTESDLEET CCCCCCCCHHHHHHH	32.96	23776212
137	Phosphorylation	ESSATTESDLEETFK CCCCCCHHHHHHHHH	45.46	23776212
142	Phosphorylation	TESDLEETFKKLVGD CHHHHHHHHHHHHHH	31.23	23776212
153	Phosphorylation	LVGDLNKSPEEIFDA HHHHHCCCHHHHHHH	36.15	24894044
232	Phosphorylation	EIKRTPPTPQDEMRA HHCCCCCCCHHHHHH	34.48	23328941
694	Phosphorylation	LQRFTAATLEHGMRP HHHHHHHHHHCCCCC	30.16	27643528
704	Phosphorylation	HGMRPPISPKPEWRA CCCCCCCCCCHHHHH	32.42	18433157
754	Phosphorylation	YGRMNIGSRPSKRKP HCCCCCCCCCCCCCC	36.90	25561503
762	Phosphorylation	RPSKRKPSGGIESLR CCCCCCCCCCHHHHH	53.32	30291188
767	Phosphorylation	KPSGGIESLRAIPWI CCCCCHHHHHHHHHH	22.64	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 CAPP1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
11	S	Phosphorylation		18433157
The phosphorylation of Ser-11 is reversibly promoted by inorganic phosphate (Pi) deprivation.

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 CAPP1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CAPP1_ARATH !!

Drug and Disease Associations

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

Regulatory Network of CAPP1_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-11, 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-11, AND MASSSPECTROMETRY.	19245862 [Abstract]
"In vivo regulatory phosphorylation of the phosphoenolpyruvatecarboxylase AtPPC1 in phosphate-starved Arabidopsis thaliana."; Gregory A.L., Hurley B.A., Tran H.T., Valentine A.J., She Y.-M.,Knowles V.L., Plaxton W.C.; Biochem. J. 420:57-65(2009). Cited for: FUNCTION, PHOSPHORYLATION AT SER-11, INDUCTION BY PHOSPHATEDEPRIVATION, ENZYME REGULATION, SUBUNIT, TISSUE SPECIFICITY,IDENTIFICATION BY MASS SPECTROMETRY, BIOPHYSICOCHEMICAL PROPERTIES,AND COFACTOR.	19228119 [Abstract]
"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-11 AND SER-704, AND MASSSPECTROMETRY.	18433157 [Abstract]

show