PSBC_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PSBC_ARATH
• UniProt AC: P56778
• Protein Name: Photosystem II CP43 reaction center protein {ECO:0000255|HAMAP-Rule:MF_01496}
• Gene Name: psbC {ECO:0000255|HAMAP-Rule:MF_01496}
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 473
• Subcellular Localization: Plastid, chloroplast thylakoid membrane ; Multi-pass membrane protein .
• Protein Description: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plastoquinone oxidoreductase, using light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation..
• Protein Sequence: MKTLYSLRRFYHVETLFNGTLALAGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEVIDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWKDRNKMTTILGIHLILLGVGAFLLVFKALYFGGVYDTWAPGGGDVRKITNLTLSPSVIFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGSICIFGGIWHILTKPFAWARRALVWSGEAYLSYSLAALSVCGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVRDQRLGANVGSAQGPTGLGKYLMRSPTGEVIFGGETMRFWDLRAPWLEPLRGPNGLDLSRLKKDIQPWQERRSAEYMTHAPLGSLNSVGGVATEINAVNYVSPRSWLSTSHFVLGFFLFVGHLWHAGRARAAAAGFEKGIDRDFEPVLSMTPLN

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
15	Acetylation	RRFYHVETLFNGTLA HCCEEHHHHCCCEEE	35.24	22223895
15	Phosphorylation	RRFYHVETLFNGTLA HCCEEHHHHCCCEEE	35.24	19376835
18	Deamidated asparagine	YHVETLFNGTLALAG EEHHHHCCCEEEECC	45.73	-
18	Deamidation	YHVETLFNGTLALAG EEHHHHCCCEEEECC	45.73	11113141
20	Phosphorylation	VETLFNGTLALAGRD HHHHCCCEEEECCCC	15.23	29654922
212	Nitration	SPSVIFGYLLKSPFG CHHHHHHHHHCCCCC	9.71	-
344	Phosphorylation	LGKYLMRSPTGEVIF HHHHHCCCCCCCEEE	16.91	19376835
346	Phosphorylation	KYLMRSPTGEVIFGG HHHCCCCCCCEEECC	47.42	19376835
355	Phosphorylation	EVIFGGETMRFWDLR CEEECCEEEEEECCC	19.54	19376835
468	Phosphorylation	RDFEPVLSMTPLN-- CCCCCCCCCCCCC--	22.35	19376835
470	Phosphorylation	FEPVLSMTPLN---- CCCCCCCCCCC----	22.65	29654922

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ALB3_ARATH	ALB3	physical	15988575
LPA2_ARATH	LPA2	physical	17601825
LPA3_ARATH	LPA3	physical	20605914
SCO2_ARATH	SCO2	physical	22572242

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"Mass spectrometric resolution of reversible protein phosphorylationin photosynthetic membranes of Arabidopsis thaliana.";
Vener A.V., Harms A., Sussman M.R., Vierstra R.D.;
J. Biol. Chem. 276:6959-6966(2001).
Cited for: PROTEIN SEQUENCE OF 15-26, DEAMIDATION AT ASN-18, PHOSPHORYLATION ATTHR-15, AND ACETYLATION AT THR-15.
PubMed: 11113141

Deamidation

"Mass spectrometric resolution of reversible protein phosphorylationin photosynthetic membranes of Arabidopsis thaliana.";
Vener A.V., Harms A., Sussman M.R., Vierstra R.D.;
J. Biol. Chem. 276:6959-6966(2001).
Cited for: PROTEIN SEQUENCE OF 15-26, DEAMIDATION AT ASN-18, PHOSPHORYLATION ATTHR-15, AND ACETYLATION AT THR-15.
PubMed: 11113141

Phosphorylation

"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-15 AND SER-468, AND MASSSPECTROMETRY.
PubMed: 19376835

"Mass spectrometric resolution of reversible protein phosphorylationin photosynthetic membranes of Arabidopsis thaliana.";
Vener A.V., Harms A., Sussman M.R., Vierstra R.D.;
J. Biol. Chem. 276:6959-6966(2001).
Cited for: PROTEIN SEQUENCE OF 15-26, DEAMIDATION AT ASN-18, PHOSPHORYLATION ATTHR-15, AND ACETYLATION AT THR-15.
PubMed: 11113141