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
Gene Ontology annotation based on curation of immunofluorescence data
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Combined Automated Annotation using Multiple IEA Methods
Huntingtin interacting proteins are genetic modifiers of neurodegeneration.
Defining the membrane proteome of NK cells.
The structural motifs for substrate binding and dimerization of the α subunit of collagen prolyl 4-hydroxylase.
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The C-P4H alpha subunit comprises an N domain (1-143), a peptide-substrate-binding (PSB) domain (144-244) and a catalytic domain (245-517); the N domain forms an antiparallel coiled-coil four-helix bundle that drives alpha-alpha dimerization and tetramer assembly, and the PSB domain binds substrate peptides in a poly-(L)-proline-II conformation.
Molecular cloning of the alpha-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts.
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Prolyl 4-hydroxylase is an alpha2-beta2 tetramer that catalyzes 4-hydroxyproline formation in collagens; the alpha subunit lacks a C-terminal KDEL, so ER retention of the tetramer is conferred by the beta (PDI) subunit. The single alpha gene yields two mRNA types by mutually exclusive alternative splicing.
Histone Interaction Landscapes Visualized by Crosslinking Mass Spectrometry in Intact Cell Nuclei.
Multimodal cell maps as a foundation for structural and functional genomics.
Mannose Binding Lectin Is Hydroxylated by Collagen Prolyl-4-hydroxylase and Inhibited by Some PHD Inhibitors.
Lactate supports cell-autonomous ECM production to sustain metastatic behavior in prostate cancer.
P4HA1 expression and function in esophageal squamous cell carcinoma.
Collagen prolyl 4-hydroxylase subunit alpha member-induced head and neck squamous cell carcinoma aggressiveness is antagonized by LLGL2 via reduced expression of occludin.
IL-10 mediates pleural remodeling in systemic lupus erythematosus.
P4HA1: an important target for treating fibrosis related diseases and cancer.
Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer.
Prolyl 4-hydroxylase converts collagen prolines to 4-hydroxyprolines
Proline hydroxylases hydroxylate Polyprotein
UniProt entry P13674 (P4HA1_HUMAN), Prolyl 4-hydroxylase subunit alpha-1