BCA1_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BCA1_ARATH
• UniProt AC: P27140
• Protein Name: Beta carbonic anhydrase 1, chloroplastic {ECO:0000303|PubMed:17407539}
• Gene Name: BCA1 {ECO:0000303|PubMed:17407539}
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 347
• Subcellular Localization: Plastid, chloroplast stroma . Cell membrane ; Peripheral membrane protein .
• Protein Description: Reversible hydration of carbon dioxide. Required for photosynthesis in cotyledons. Binds salicylic acid. Together with BCA4, involved in the CO(2) signaling pathway which controls gas-exchange between plants and the atmosphere by modulating stomatal development and movements. Promotes water use efficiency..
• Protein Sequence: MSTAPLSGFFLTSLSPSQSSLQKLSLRTSSTVACLPPASSSSSSSSSSSSRSVPTLIRNEPVFAAPAPIIAPYWSEEMGTEAYDEAIEALKKLLIEKEELKTVAAAKVEQITAALQTGTSSDKKAFDPVETIKQGFIKFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFQPGDAFVVRNIANMVPPFDKVKYGGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFPLDGNNSTDFIEDWVKICLPAKSKVISELGDSAFEDQCGRCEREAVNVSLANLLTYPFVREGLVKGTLALKGGYYDFVKGAFELWGLEFGLSETSSVKDVATILHWKL

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
112	Phosphorylation	AAKVEQITAALQTGT HHHHHHHHHHHHHCC		19376835
114	Acetylation	KVEQITAALQTGTSS HHHHHHHHHHHCCCC		22223895
117	Phosphorylation	QITAALQTGTSSDKK HHHHHHHHCCCCCCC		19376835
119	Phosphorylation	TAALQTGTSSDKKAF HHHHHHCCCCCCCCC		19376835
120	Phosphorylation	AALQTGTSSDKKAFD HHHHHCCCCCCCCCC		19376835
121	Phosphorylation	ALQTGTSSDKKAFDP HHHHCCCCCCCCCCH		19376835
131	Phosphorylation	KAFDPVETIKQGFIK CCCCHHHHHHHHHCH		25561503
144	Phosphorylation	IKFKKEKYETNPALY CHHCHHHHCCCHHHH		24299221
146	Phosphorylation	FKKEKYETNPALYGE HCHHHHCCCHHHHHH		24299221
151	Phosphorylation	YETNPALYGELAKGQ HCCCHHHHHHHHCCC		24299221
159	Phosphorylation	GELAKGQSPKYMVFA HHHHCCCCCCEEEEE		27545962
162	Phosphorylation	AKGQSPKYMVFACSD HCCCCCCEEEEEECC		24299221
175	Phosphorylation	SDSRVCPSHVLDFQP CCCCCCCCHHCCCCC		30291188
203	Phosphorylation	PPFDKVKYGGVGAAI CCCCCCCCCCHHHHH		22092075
246	Phosphorylation	FPLDGNNSTDFIEDW CCCCCCCCCCHHHHH		30291188
266	Phosphorylation	PAKSKVISELGDSAF HHCCHHHHHHCHHHH		30291188
271	Phosphorylation	VISELGDSAFEDQCG HHHHHCHHHHHHCCC		30291188
280	S-nitrosylation	FEDQCGRCEREAVNV HHHCCCCCHHHHHHH		19017644
288	Phosphorylation	EREAVNVSLANLLTY HHHHHHHHHHHHHHC		22092075
294	Phosphorylation	VSLANLLTYPFVREG HHHHHHHHCHHHHCC		19880383
295	Phosphorylation	SLANLLTYPFVREGL HHHHHHHCHHHHCCC		19880383
306	Phosphorylation	REGLVKGTLALKGGY HCCCCCEEEEECCCH		24299221

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of BCA1_ARATH !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
280	C	S-nitrosylation	S-nitrosylation at Cys-280 is up-regulated during nitrosative burst and suppresses both binding of salicylic acid and carbonic anhydrase activity.	19017644

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of BCA1_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BT4_ARATH	BT4	physical	21798944

Drug and Disease Associations

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