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MGI:Alas2

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Contents

Species (Taxon ID) Mus musculus (house mouse) (taxon:10090)
Gene Name(s) Alas2 ( synonyms: 5-aminolevulinate synthase, ALAS, Alas-2, ALAS-E, ALASE, erythroid-specific ALAS )
Protein Name(s) aminolevulinic acid synthase 2, erythroid,
External Links
MGI MGI:87990

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0001666

response to hypoxia

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P22557

P

From MGI

GO:0003824

catalytic activity

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR015421
InterPro:IPR015422

F

From MGI

GO:0003870

5-aminolevulinate synthase activity

MGI:MGI:2154458

ISO: Inferred from Sequence Orthology

EMBL:AF068624

F

From MGI

GO:0003870

5-aminolevulinate synthase activity

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:Q63147

F

From MGI

GO:0003870

5-aminolevulinate synthase activity

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P22557

F

From MGI

GO:0003870

5-aminolevulinate synthase activity

MGI:MGI:75768
PMID:7620186[1]

IMP: Inferred from Mutant Phenotype

F

From MGI

GO:0005739

mitochondrion

MGI:MGI:2154458

ISO: Inferred from Sequence Orthology

EMBL:AF068624

C

From MGI

GO:0005739

mitochondrion

MGI:MGI:2682130
PMID:14651853[2]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005739

mitochondrion

MGI:MGI:3852644
PMID:18614015[3]

IDA: Inferred from Direct Assay

C

From MGI

GO:0005739

mitochondrion

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:Q63147

C

From MGI

GO:0005739

mitochondrion

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P22557

C

From MGI

GO:0005743

mitochondrial inner membrane

MGI:MGI:4834177

ISO: Inferred from Sequence Orthology

UniProtKB:P22557

C

From MGI

GO:0005759

mitochondrial matrix

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR015118

C

From MGI

GO:0006778

porphyrin-containing compound metabolic process

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR015118

P

From MGI

GO:0006783

heme biosynthetic process

MGI:MGI:3694153
PMID:9446639[4]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0006879

cellular iron ion homeostasis

MGI:MGI:1347738
PMID:10562540[5]

IMP: Inferred from Mutant Phenotype

MGI:MGI:2180151

P

From MGI

GO:0009058

biosynthetic process

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR004839

P

From MGI

GO:0016594

glycine binding

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:Q63147

F

From MGI

GO:0016740

transferase activity

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0808

F

From MGI

GO:0016740

transferase activity

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR001917
InterPro:IPR004839

F

From MGI

GO:0016746

transferase activity, transferring acyl groups

MGI:MGI:1354194

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0012

F

From MGI

GO:0030170

pyridoxal phosphate binding

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR010961
InterPro:IPR015118
InterPro:IPR004839
InterPro:IPR015421
InterPro:IPR015422

F

From MGI

GO:0030218

erythrocyte differentiation

MGI:MGI:3694153
PMID:9446639[4]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0033014

tetrapyrrole biosynthetic process

MGI:MGI:2152098

IEA: Inferred from Electronic Annotation

InterPro:IPR010961

P

From MGI

GO:0042541

hemoglobin biosynthetic process

MGI:MGI:3694153
PMID:9446639[4]

IMP: Inferred from Mutant Phenotype

P

From MGI

GO:0050662

coenzyme binding

MGI:MGI:4417868

ISO: Inferred from Sequence Orthology

UniProtKB:Q63147

F

From MGI


Notes

References

See Help:References for how to manage references in GONUTS.
  1. 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 GONUTS page
  2. Mootha VK et al. (2003) Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria. Cell 115: 629-40 PubMed GONUTS page
  3. Pagliarini DJ et al. (2008) A mitochondrial protein compendium elucidates complex I disease biology. Cell 134: 112-23 PubMed GONUTS page
  4. 4.0 4.1 4.2 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 GONUTS page
  5. Nakajima O et al. (1999) Heme deficiency in erythroid lineage causes differentiation arrest and cytoplasmic iron overload. EMBO J 18: 6282-9 PubMed GONUTS page
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