Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Alas2. (This text reflects annotations as of Wednesday, January 23, 2013.) MGI curation of this mouse gene is considered complete, including annotations derived from the biomedical literature as of October 15, 2007. If you know of any additional information regarding this mouse gene please let us know. Please supply mouse gene symbol and a PubMed ID.

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] The product of this gene specifies an erythroid-specific mitochondrially located enzyme. The encoded protein catalyzes the first step in the heme biosynthetic pathway. Defects in this gene cause X-linked pyridoxine-responsive sideroblastic anemia. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Alas2
  • is located in the following cellular components:
    • mitochondrion ^{[3, 5]}
• Researchers have inferred, based on phenotypic analysis of mouse mutants, that the gene product of Alas2
  • participates in the following biological processes:
    • cellular iron ion homeostasis ^[4]
    • erythrocyte differentiation ^[1]
    • heme biosynthetic process ^[1]
    • hemoglobin biosynthetic process ^[1]
  • performs the following molecular functions:
    • 5-aminolevulinate synthase activity ^[2]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Alas2:
  • participates in the following biological processes:
    • metabolic process
    • response to hypoxia
  • performs the following molecular functions:
    • 5-aminolevulinate synthase activity
    • coenzyme binding
    • glycine binding
  • is located in the following cellular components:
    • mitochondrial inner membrane
    • mitochondrion

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Summary text based on GO annotations supported by structural data

• Alas2 encodes a protein or proteins that contain the following InterPro domains: 5-aminolevulinate synthase presequence, Aminotransferase, class I/classII, Aminotransferase, class-II, pyridoxal-phosphate binding site, Pyridoxal phosphate-dependent transferase, major domain, Pyridoxal phosphate-dependent transferase, major region, subdomain 1, Pyridoxal phosphate-dependent transferase, major region, subdomain 2, Tetrapyrrole biosynthesis, 5-aminolevulinic acid synthase, indicating that the gene product:
  • participates in the following biological processes:
    • biosynthetic process
    • porphyrin-containing compound metabolic process
    • tetrapyrrole biosynthetic process
  • performs the following molecular functions:
    • catalytic activity
    • pyridoxal phosphate binding
    • transferase activity
  • is located in the following cellular components:
    • mitochondrial matrix

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Alas2 indicates that it:
  • performs the following molecular functions:
    • transferase activity
    • transferase activity, transferring acyl groups

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References

1. Harigae H et al. (1998) Deficient heme and globin synthesis in embryonic stem cells lacking the erythroid-specific delta-aminolevulinate synthase gene. Blood, 91:798-805. (PubMed:9446639)
2. Meguro K et al. (1995) The role of the erythroid-specific delta-aminolevulinate synthase gene expression in erythroid heme synthesis. Blood, 86:940-8. (PubMed:7620186)
3. Mootha VK et al. (2003) Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria. Cell, 115:629-40. (PubMed:14651853)
4. Nakajima O et al. (1999) Heme deficiency in erythroid lineage causes differentiation arrest and cytoplasmic iron overload. EMBO J, 18:6282-9. (PubMed:10562540)
5. Pagliarini DJ et al. (2008) A mitochondrial protein compendium elucidates complex I disease biology. Cell, 134:112-23. (PubMed:18614015)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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