GO_REF:0000024
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
GO_REF:0000033
Annotation inferences using phylogenetic trees
GO_REF:0000044
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
GO_REF:0000107
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
GO_REF:0000117
Electronic Gene Ontology annotations created by ARBA machine learning models
GO_REF:0000120
Combined Automated Annotation using Multiple IEA Methods
file:human/FECH/FECH-uniprot.txt
UniProtKB entry P22830 (HEMH_HUMAN), Ferrochelatase, mitochondrial
PMID:1376018
A molecular defect in human protoporphyria.
PMID:15123683
Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis.
PMID:17261801
Substrate interactions with human ferrochelatase.
PMID:1729699
The molecular defect of ferrochelatase in a patient with erythropoietic protoporphyria.
PMID:2260980
Molecular cloning and sequence analysis of cDNA encoding human ferrochelatase.
PMID:27599036
A Novel Role for Progesterone Receptor Membrane Component 1 (PGRMC1): A Partner and Regulator of Ferrochelatase.
PMID:30765471
Dimeric ferrochelatase bridges ABCB7 and ABCB10 homodimers in an architecturally defined molecular complex required for heme biosynthesis.
PMID:33961781
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
PMID:34800366
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
PMID:36836934
Proteomic Analysis of Ferrochelatase Interactome in Erythroid and Non-Erythroid Cells.
PMID:8276824
Mammalian ferrochelatase. Expression and characterization of normal and two human protoporphyric ferrochelatases.
PMID:8973195
Site-directed mutagenesis and spectroscopic characterization of human ferrochelatase: identification of residues coordinating the [2Fe-2S] cluster.
Reactome:R-HSA-189465
FECH binds Fe2+ to PRIN9 to form heme
Reactome:R-HSA-9838035
CLPXP binds mitochondrial matrix proteins
Reactome:R-HSA-9838081
LONP1 degrades mitochondrial matrix proteins
Reactome:R-HSA-9838093
LONP1 binds mitochondrial matrix proteins
Reactome:R-HSA-9838289
CLPXP degrades mitochondrial matrix proteins