PSBA_ARATH - dbPTM
PSBA_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PSBA_ARATH
UniProt AC P83755
Protein Name Photosystem II protein D1 {ECO:0000255|HAMAP-Rule:MF_01379}
Gene Name psbA {ECO:0000255|HAMAP-Rule:MF_01379}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 353
Subcellular Localization Plastid, chloroplast thylakoid membrane
Multi-pass membrane protein .
Protein Description Photosystem II (PSII) is a light-driven water: plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors..
Protein Sequence MTAILERRESESLWGRFCNWITSTENRLYIGWFGVLMIPTLLTATSVFIIAFIAAPPVDIDGIREPVSGSLLYGNNIISGAIIPTSAAIGLHFYPIWEAASVDEWLYNGGPYELIVLHFLLGVACYMGREWELSFRLGMRPWIAVAYSAPVAAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLIRETTENESANEGYRFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLAAWPVVGIWFTALGISTMAFNLNGFNFNQSVVDSQGRVINTWADIINRANLGMEVMHERNAHNFPLDLAAVEAPSTNG
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 Orthologous
Protein Cluster
2Acetylation------MTAILERRE
------CCCHHHHHH
23.5411113141
2Phosphorylation------MTAILERRE
------CCCHHHHHH
23.5427531888
227PhosphorylationTSSLIRETTENESAN
HHHHHHHHCCCCCCC
29.5728295753
228PhosphorylationSSLIRETTENESANE
HHHHHHHCCCCCCCC
31.8728295753
232PhosphorylationRETTENESANEGYRF
HHHCCCCCCCCCCCC
48.2325561503
237NitrationNESANEGYRFGQEEE
CCCCCCCCCCCCHHH
9.15-
262NitrationFGRLIFQYASFNNSR
HHHHHHEHHCCCCCC
8.08-

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 PSBA_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 PSBA_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ALB3_ARATHALB3physical
15988575
PSBA_ARATHpsbAphysical
15988575

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PSBA_ARATH

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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 2-7, PHOSPHORYLATION AT THR-2, ACETYLATION ATTHR-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 2-7, PHOSPHORYLATION AT THR-2, ACETYLATION ATTHR-2, AND MASS SPECTROMETRY.

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