CAN_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CAN_SCHPO
• UniProt AC: O94255
• Protein Name: Carbonic anhydrase
• Gene Name: SPBP8B7.05c
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 328
• Subcellular Localization: Cytoplasm. Nucleus .
• Protein Description: Catalyzes the reversible hydration of CO(2) to H(2)CO(3). The main role may be to provide inorganic carbon for the bicarbonate-dependent carboxylation reactions catalyzed by pyruvate carboxylase, acetyl-CoA carboxylase and carbamoyl-phosphate synthetase (By similarity)..
• Protein Sequence: MLPPFGALTTTKIPLPKTILQSTFNQIKSSSYSIIAAPRLTSRFIRFPCNYNSCLQSISFSSLGRKRLFFSSSQLLEKSDKKKKMPDRLKRRIEEIDHQDEIIDREASTASPVSGAGKIDQNGEIKDLLERNLTWSQQTSRKYPSFFTATKDIQTPQVLWIGCSDSRVPETTILNLLPGEVFVHRNIANVVPRSDINALAVMEYSVTVLKVKHIIVCGHYGCGGVAAALGPNLNNLLDHWLRHIRDVIEDNREELDAIEDPQLRRLKLAELNTRAQAISVTRVGFVREAMEKRGLQVHGWIYDLSNGQIKKLDITDAIKKAKYGTYDS

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
108	Phosphorylation	EIIDREASTASPVSG HHCCCCCCCCCCCCC	26.27	21712547
109	Phosphorylation	IIDREASTASPVSGA HCCCCCCCCCCCCCC	35.04	25720772
111	Phosphorylation	DREASTASPVSGAGK CCCCCCCCCCCCCCC	39.17	28889911
114	Phosphorylation	ASTASPVSGAGKIDQ CCCCCCCCCCCCCCC	9.38	21712547
134	Phosphorylation	DLLERNLTWSQQTSR HHHHHCCCHHHHHHC	13.22	25720772
136	Phosphorylation	LERNLTWSQQTSRKY HHHCCCHHHHHHCCC	10.21	28889911
139	Phosphorylation	NLTWSQQTSRKYPSF CCCHHHHHHCCCCCC	29.28	21712547
140	Phosphorylation	LTWSQQTSRKYPSFF CCHHHHHHCCCCCCE	15.23	29996109
328	Phosphorylation	AKYGTYDS------- HHCCCCCC-------		21712547

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CAN_SCHPO !!

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAN_SCHPO	nce103	physical	26771498
MU123_SCHPO	mug123	physical	26771498
YCX5_SCHPO	dbl1	physical	26771498

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND MASSSPECTROMETRY.
PubMed: 18257517