Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae.
Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry.
Cell cycle-dependent assembly of a Gin4-septin complex.
A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B.
Genome-wide expression analysis of NAP1 in Saccharomyces cerevisiae.
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In a single microarray experiment, about 10% of yeast open reading frames
changed expression by more than 2-fold in the Deltanap1 strain relative
to wild type, and the affected genes were clustered, suggesting that Nap1
helps maintain cumulative nucleosome formation in vivo.
"About 10% of all yeast open reading frames changed the transcription level more than 2-fold in the Deltanap1 strain, compared with wild-type strain, in one experiment."
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Nap1 reportedly interacts functionally with the mitotic regulators Clb2 (B-type
cyclin) and Gin4, linking histone-chaperone activity to mitotic functions and
suppression of polar bud growth.
"additional functions have been ascribed to Nap1, as it has been shown to interact with Clb2 (B type cyclin) and Gin4 (septum formation)"
Saccharomyces cerevisiae Ats1p interacts with Nap1p, a cytoplasmic protein that controls bud morphogenesis.
Functional analysis of nucleosome assembly protein, NAP-1. The negatively charged COOH-terminal region is not necessary for the intrinsic assembly activity.
ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex.
High-definition macromolecular composition of yeast RNA-processing complexes.
A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin.
A phosphatase complex that dephosphorylates gammaH2AX regulates DNA damage checkpoint recovery.
Proteome survey reveals modularity of the yeast cell machinery.
The structure of nucleosome assembly protein 1.
Chromatin remodeling by nucleosome disassembly in vitro.
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae.
Chz1, a nuclear chaperone for histone H2AZ.
An in vivo map of the yeast protein interactome.
High-quality binary protein interaction map of the yeast interactome network.
Histone chaperone specificity in Rtt109 activation.
An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell.
Identification and molecular cloning of yeast homolog of nucleosome assembly protein I which facilitates nucleosome assembly in vitro.
A global protein kinase and phosphatase interaction network in yeast.
Defining the budding yeast chromatin-associated interactome.
Assembly states of the nucleosome assembly protein 1 (NAP-1) revealed by sedimentation velocity and non-denaturing MS.
Histone density is maintained during transcription mediated by the chromatin remodeler RSC and histone chaperone NAP1 in vitro.
A safeguard mechanism regulates Rho GTPases to coordinate cytokinesis with the establishment of cell polarity.
A memory system of negative polarity cues prevents replicative aging.
Structural evidence for Nap1-dependent H2A-H2B deposition and nucleosome assembly.
Septin-associated proteins Aim44 and Nis1 traffic between the bud neck and the nucleus in the yeast Saccharomyces cerevisiae.
Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME.
Histone chaperone Nap1 dismantles an H2A/H2B dimer from a partially unwrapped nucleosome.
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Nap1 can dismantle an H2A-H2B dimer from a partially unwrapped nucleosome;
partial unwrapping by a translocase dramatically facilitates this Nap1-mediated
dimer removal.
"partial unwrapping of a nucleosome by an RNA polymerase dramatically facilitates an H2A/H2B dimer dismantling from the nucleosome by Nucleosome Assembly Protein 1 (Nap1)"
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The acidic C-terminal flexible tails of Nap1 engage an H2A-H2B interface that
is normally buried in the nucleosome and inaccessible to Nap1's globular domains,
consistent with a 'penetrating fuzzy binding' chaperone mechanism.
"the highly acidic C-terminal flexible tails of Nap1 contribute to the H2A/H2B binding by associating with the binding interface buried and not accessible to Nap1 globular domains, supporting the penetrating fuzzy binding mechanism seemingly shared across various histone chaperones"
The social and structural architecture of the yeast protein interactome.
Glutamylation of Npm2 and Nap1 acidic disordered regions increases DNA mimicry and histone chaperone efficiency.
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Post-translational glutamylation of the Nap1/NAP1-like acidic disordered regions
can increase DNA mimicry and histone chaperone efficiency, reinforcing the
functional importance of the acidic disordered regions in the chaperone mechanism.
"glutamylation of these chaperone polyelectrolyte acidic stretches functions to enhance DNA electrostatic mimicry, promoting the binding and stabilization of H2A/H2B heterodimers and facilitating nucleosome assembly"
Nap1 and Kap114 co-chaperone H2A-H2B and facilitate targeted histone release in the nucleus.
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Nap1 is the principal cytosolic H2A-H2B chaperone; it is mostly cytoplasmic but
also functions in the nucleus, implying nucleocytoplasmic shuttling.
"mostly localized to the yeast cytoplasm where it chaperones newly synthesized and folded H2A-H2B"
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Kap114, H2A-H2B, and the Nap1 dimer form equimolar complexes, including a
quaternary Nap1_2-H2A-H2B-Kap114-RanGTP assembly resolved by cryo-EM.
"Nap12•H2A-H2B•Kap114•RanGTP complex explains how both Kap114 and Nap12 interact"
Members of the NAP/SET family of proteins interact specifically with B-type cyclins.
NAP1 acts with Clb1 to perform mitotic functions and to suppress polar bud growth in budding yeast.
Control of mitotic events by Nap1 and the Gin4 kinase.
The septins are required for the mitosis-specific activation of the Gin4 kinase.
Falcon (Edison) deep research report: Saccharomyces cerevisiae NAP1 (P25293) functional annotation.
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Yeast NAP1 (YKR048C; P25293) encodes a dimeric H2A-H2B histone chaperone whose
primary molecular function is to bind and shield the H2A-H2B dimer and mediate
its correct delivery into nucleosomes, including a Kap114/RanGTP-coordinated
handoff pathway for targeted nuclear release and nucleosome assembly; Nap1 also
enables H2A-H2B eviction from partially unwrapped nucleosomes.
"Nap1’s primary molecular function is to bind/shield H2A–H2B and mediate their correct delivery into nucleosomes, including a Kap114/RanGTP-coordinated handoff pathway for targeted nuclear release and nucleosome assembly. Nap1 also participates in transcription-coupled chromatin dynamics by enabling H2A–H2B eviction from partially unwrapped nucleosomes via acidic disordered tails."
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
Phosphorylation by casein kinase 2 regulates Nap1 localization and function.
The histone chaperones Nap1 and Vps75 bind histones H3 and H4 in a tetrameric conformation.
Chaperone Nap1 shields histone surfaces used in a nucleosome and can put H2A-H2B in an unconventional tetrameric form.