Gene Ontology annotation through association of InterPro records with GO terms.
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.
An essential role of a TatC homologue of a Delta pH- dependent protein transporter in thylakoid membrane formation during chloroplast development in Arabidopsis thaliana.
Proteome map of the chloroplast lumen of Arabidopsis thaliana.
Central functions of the lumenal and peripheral thylakoid proteome of Arabidopsis determined by experimentation and genome-wide prediction.
Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis.
In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database.
New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy.
The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts.
High light response of the thylakoid proteome in arabidopsis wild type and the ascorbate-deficient mutant vtc2-2. A comparative proteomics study.
Identification of proteins expressed at extremely low level in Arabidopsis leaves.
Sorting signals, N-terminal modifications and abundance of the chloroplast proteome.
Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study.
Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis.
AT_CHLORO, a comprehensive chloroplast proteome database with subplastidial localization and curated information on envelope proteins.
A split-ubiquitin yeast two-hybrid screen to examine the substrate specificity of atToc159 and atToc132, two Arabidopsis chloroplast preprotein import receptors.
A proteomic strategy for global analysis of plant protein complexes.
Identification of multiple salicylic acid-binding proteins using two high throughput screens.
Global Analysis of Membrane-associated Protein Oligomerization Using Protein Correlation Profiling.
Discovering the RNA-Binding Proteome of Plant Leaves with an Improved RNA Interactome Capture Method.
Nucleotide sequence of the psbP gene encoding precursor of 23-kDa polypeptide of oxygen-evolving complex in Arabidopsis thaliana and its expression in the wild-type and a constitutively photomorphogenic mutant.
Structure and function of the PsbP protein of photosystem II from higher plants.
PsbP protein, but not PsbQ protein, is essential for the regulation and stabilization of photosystem II in higher plants.
D139N mutation of PsbP enhances the oxygen-evolving activity of photosystem II through stabilized binding of a chloride ion.
Falcon (Edison Scientific) deep research report on Arabidopsis PSBP1 (AT1G06680 / Q42029)
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PsbP1 (At1g06680) is curated as a thylakoid-lumen protein assigned to the PSII oxygen-evolving complex (OEC) category.
"a curated thylakoid-lumen protein table explicitly lists **At1g06680 = PsbP1** and assigns it to **PSII/OEC**"
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PsbP (OEE2) is an extrinsic, lumen-facing component of photosystem II that contributes to oxygen-evolving complex function and stability.
"**PsbP (OEE2)** is an **extrinsic component of PSII** on the **lumenal side**, contributing to OEC/PSII function and stability."
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The plant oxygen-evolving complex is supported by three extrinsic lumenal proteins, classically PsbO, PsbP, and PsbQ.
"the OEC is functionally supported/stabilized by **extrinsic proteins located on the lumenal side of the thylakoid membrane**, classically **PsbO, PsbP, and PsbQ**."
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PsbP1 functions as an extrinsic lumenal PSII subunit associated with the oxygen-evolving complex, supporting PSII stability and oxygen evolution capacity.
"PSBP1/PsbP1 functions as an **extrinsic lumenal PSII subunit** associated with the **oxygen-evolving complex** and is implicated in maintaining **PSII stability and oxygen evolution capacity** in higher plants."
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PsbP1 is treated as a structural/functional PSII extrinsic subunit rather than an enzyme or transporter catalyzing an independent reaction.
"PsbP1 is described and treated as a **structural/functional PSII extrinsic subunit** (supporting OEC function and PSII stability/repair), rather than catalyzing an independent metabolic reaction or transporting a substrate."
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PsbP1 localizes to the chloroplast thylakoid lumen, with both a soluble lumen pool and a membrane-associated lumen pool near the PSII supercomplex.
"PsbP1 is placed in the **chloroplast thylakoid lumen**, with evidence for both a **soluble lumen pool** and a **membrane-associated lumen pool**"
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In Arabidopsis PSII, the small subunit PsbR is positioned to stabilize the luminal extrinsic protein PsbP.
"**PsbR** (a small PSII subunit) is positioned to **stabilize the luminal extrinsic protein PsbP**"
Electronic Gene Ontology annotations created by ARBA machine learning models