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

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Combined Automated Annotation using Multiple IEA Methods

Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia.

The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis.

Erythroid-specific 5-aminolevulinate synthase protein is stabilized by low oxygen and proteasomal inhibition.

Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA.

New mutation in erythroid-specific delta-aminolevulinate synthase as the cause of X-linked sideroblastic anemia responsive to pyridoxine.

Sideroblastic anemia: molecular analysis of the ALAS2 gene in a series of 29 probands and functional studies of 10 missense mutations.

ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria.

A proteome-scale map of the human interactome network.

Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release.

The immunometabolite itaconate inhibits heme synthesis and remodels cellular metabolism in erythroid precursors.

Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.

ALAS condenses SUCC-CoA and Gly to form dALA

UniProtKB P22557 (HEM0_HUMAN) 5-aminolevulinate synthase, erythroid-specific, mitochondrial

Heme deficiency in erythroid lineage causes differentiation arrest and cytoplasmic iron overload.

Deficient heme and globin synthesis in embryonic stem cells lacking the erythroid-specific delta-aminolevulinate synthase gene.