Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Crystal structure of human ornithine decarboxylase at 2.1 A resolution: structural insights to antizyme binding.
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Human ODC crystal structure at 2.1 A; describes the C-terminal basal degradation elements and antizyme-binding surface, establishing the dimeric enzyme and antizyme-mediated degradation model.
"Ornithine decarboxylase (ODC, EC 4.1.1.17) performs the first step in polyamine biosynthesis, the decarboxylation of ornithine to putrescine."
Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection.
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ODC1 protein and transcript are differentially expressed (down-regulated) in rhabdomyosarcoma cells infected with enterovirus 71; basis of the response-to-virus IEP annotation.
"Western blot analyses of APOB, CLU, DCAMKL1 and ODC1 proteins correlated protein and transcript levels."
A structural insight into the inhibition of human and Leishmania donovani ornithine decarboxylases by 1-amino-oxy-3-aminopropane.
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Structural and kinetic characterization of human ODC (KM 0.08 mM for L-ornithine; EC 4.1.1.17). Two active sites at the dimer interface with Lys69 and Cys360 from opposite monomers; PLP-dependent enzyme.
"The two active sites are found at the dimer interface, between the N-terminal domain of one monomer and the C-terminal domain of the other, with Lys 69 and Cys 360 contributing to each active site from opposite monomers"
Human ornithine decarboxylase paralogue (ODCp) is an antizyme inhibitor but not an arginine decarboxylase.
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Uses ODC-activity and ODC-degradation assays with human ODC to establish that the ODC paralogue is an antizyme inhibitor (AZIN2); reaffirms ODC as the rate-limiting polyamine-biosynthesis enzyme regulated by antizymes.
"ODC (ornithine decarboxylase), the rate-limiting enzyme in polyamine biosynthesis, is regulated by specific inhibitors, AZs (antizymes)"
Expression of human chromosome 2 ornithine decarboxylase gene in ornithine decarboxylase-deficient Chinese hamster ovary cells.
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The human chromosome-2 ODC gene encodes functional ODC: expression in ODC-deficient CHO cells restored 70-400-fold ODC activity and increased growth, showing ODC/putrescine is required for cell proliferation.
"the ODC gene from human chromosome 2 encodes functional ODC protein"
A proteome-scale map of the human interactome network.
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High-throughput binary interactome map; source of a bare "protein binding" IPI annotation (partner KAT5). No specific functional interpretation for ODC1.
"a systematic map of ?14,000 high-quality human binary protein-protein interactions"
Architecture of the human interactome defines protein communities and disease networks.
An interactome perturbation framework prioritizes damaging missense mutations for developmental disorders.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Antizyme OAZ binds to Ornithine decarboxylase
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Antizymes (OAZ) bind ODC monomers, preventing dimerization into active ODC; AZIN1 negatively regulates the OAZ-ODC interaction by binding OAZ.
"Members of the OAZ (Ornithine decarboxylase antizyme) protein family bind ODC (ornithine decarboxylase) monomers"
NQO1 interaction with ODC
Metabolism of polyamines
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Polyamines are derived from ornithine by decarboxylation; polyamine levels are tightly regulated at the level of ODC.
"Polyamine levels are tightly regulated at the level of the enzyme ornithine decarboxylase (ODC)"
26S proteosome degrades ODC holoenzyme complex
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ODC turnover by the 26S proteasome is ubiquitin-independent; antizyme association (not ubiquitination) directs ODC to the proteasome.
"Proteolytic processing of ODC is highly unusual in that ubiquitination is not required for this degradation."
ornithine => putrescine + CO2
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Cytosolic ODC, conjugated with pyridoxal phosphate and active as a dimer, converts L-ornithine into putrescine.
"L-ornithine is converted into putrescine by cytosolic ornithine decarboxylase (ODC). The enzyme, conjugated with pyridoxal phosphate, is active as a dimer"
UniProt entry P11926 (DCOR_HUMAN), Ornithine decarboxylase
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Authoritative UniProt record: catalytic activity (L-ornithine + H+ = putrescine + CO2, EC 4.1.1.17), PLP cofactor, obligate homodimer with shared active sites, antizyme-mediated ubiquitin-independent degradation, and Bachmann-Bupp syndrome gain-of-function truncating variants.
"Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine"