ALAS1

ALAS1
Identifiers
Aliases	ALAS1, ALAS, ALAS3, ALASH, MIG4, ALAS-H, 5'-aminolevulinate synthase 1
External IDs	OMIM: 125290 MGI: 87989 HomoloGene: 55478 GeneCards: ALAS1
Gene location (Human)
Chr.	Chromosome 3 (human)[1]
End	52,214,327 bp[1]
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)[2]
End	106,248,654 bp[2]
Gene ontology
Molecular function	• transferase activity; • pyridoxal phosphate binding; • transferase activity, transferring acyl groups; • GO:0001948 protein binding; • catalytic activity; • 5-aminolevulinate synthase activity; • identical protein binding;
Cellular component	• mitochondrial matrix; • mitochondrion; • nucleoplasm; • cytosol;
Biological process	• heme biosynthetic process; • mitochondrion organization; • metabolism; • protoporphyrinogen IX biosynthetic process; • biosynthetic process; • tetrapyrrole biosynthetic process; • porphyrin-containing compound metabolic process; • regulation of lipid metabolic process;
	Sources:Amigo / QuickGO
Orthologs
	211
	11655
	ENSG00000023330
	ENSMUSG00000032786
	P13196
	Q8VC19
	NM_000688; NM_001304443; NM_001304444; NM_199166
	NM_001291835; NM_020559
	NP_000679; NP_001291372; NP_001291373; NP_954635
	NP_001278764; NP_065584
	Wikidata
View/Edit Human	View/Edit Mouse

Delta-aminolevulinate synthase 1 also known as ALAS1 is a protein that in humans is encoded by the ALAS1 gene.[5][6] ALAS1 is an aminolevulinic acid synthase.

Delta-aminolevulinate synthase catalyzes the condensation of glycine with succinyl-CoA to form delta-aminolevulinic acid. This nuclear-encoded mitochondrial enzyme is the first and rate-limiting enzyme in the mammalian heme biosynthetic pathway. There are 2 tissue-specific isozymes: a housekeeping enzyme encoded by the ALAS1 gene and an erythroid tissue-specific enzyme encoded by ALAS2.[6]

References

GRCh38: Ensembl release 89: ENSG00000023330 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000032786 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Bishop DF, Henderson AS, Astrin KH (June 1990). "Human delta-aminolevulinate synthase: assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X chromosome". Genomics. 7 (2): 207–14. doi:10.1016/0888-7543(90)90542-3. PMID 2347585.
"Entrez Gene: Delta-aminolevulinate synthase 1".

External links

Human ALAS1 genome location and ALAS1 gene details page in the UCSC Genome Browser.

Goodfellow BJ, Dias JS, Ferreira GC, et al. (2001). "The solution structure and heme binding of the presequence of murine 5-aminolevulinate synthase". FEBS Lett. 505 (2): 325–31. doi:10.1016/S0014-5793(01)02818-6. PMID 11566198. S2CID 34879759.
Cortesão E, Vidan J, Pereira J, et al. (2004). "Onset of X-linked sideroblastic anemia in the fourth decade". Haematologica. 89 (10): 1261–3. PMID 15477213.
May BK, Bhasker CR, Bawden MJ, Cox TC (1990). "Molecular regulation of 5-aminolevulinate synthase. Diseases related to heme biosynthesis". Mol. Biol. Med. 7 (5): 405–21. PMID 2095458.
Dwyer BE, Smith MA, Richardson SL, et al. (2009). "Down-Regulation of Aminolevulinate Synthase, the Rate-Limiting Enzyme for Heme Biosynthesis in Alzheimer's Disease". Neurosci. Lett. 460 (2): 180–4. doi:10.1016/j.neulet.2009.05.058. PMC 2743886. PMID 19477221.
Furuyama K, Sassa S (2002). "Multiple mechanisms for hereditary sideroblastic anemia". Cell. Mol. Biol. (Noisy-le-grand). 48 (1): 5–10. PMID 11929048.
Guberman AS, Scassa ME, Cánepa ET (2005). "Repression of 5-aminolevulinate synthase gene by the potent tumor promoter, TPA, involves multiple signal transduction pathways". Arch. Biochem. Biophys. 436 (2): 285–96. doi:10.1016/j.abb.2005.02.011. PMID 15797241.
Roberts AG, Elder GH (2001). "Alternative splicing and tissue-specific transcription of human and rodent ubiquitous 5-aminolevulinate synthase (ALAS1) genes". Biochim. Biophys. Acta. 1518 (1–2): 95–105. doi:10.1016/s0167-4781(01)00187-7. PMID 11267664.
Szafranski K, Schindler S, Taudien S, et al. (2007). "Violating the splicing rules: TG dinucleotides function as alternative 3' splice sites in U2-dependent introns". Genome Biol. 8 (8): R154. doi:10.1186/gb-2007-8-8-r154. PMC 2374985. PMID 17672918.
Scassa ME, Guberman AS, Ceruti JM, Cánepa ET (2004). "Hepatic nuclear factor 3 and nuclear factor 1 regulate 5-aminolevulinate synthase gene expression and are involved in insulin repression". J. Biol. Chem. 279 (27): 28082–92. doi:10.1074/jbc.M401792200. PMID 15123725.
Imabayashi H, Mori T, Gojo S, et al. (2003). "Redifferentiation of dedifferentiated chondrocytes and chondrogenesis of human bone marrow stromal cells via chondrosphere formation with expression profiling by large-scale cDNA analysis". Exp. Cell Res. 288 (1): 35–50. doi:10.1016/S0014-4827(03)00130-7. PMID 12878157.
Fujii H, Takahashi T, Matsumi M, et al. (2004). "Increased heme oxygenase-1 and decreased delta-aminolevulinate synthase expression in the liver of patients with acute liver failure". Int. J. Mol. Med. 14 (6): 1001–5. doi:10.3892/ijmm.14.6.1001. PMID 15547665.
Zheng J, Shan Y, Lambrecht RW, et al. (2008). "Differential regulation of human ALAS1 mRNA and protein levels by heme and cobalt protoporphyrin". Mol. Cell. Biochem. 319 (1–2): 153–61. doi:10.1007/s11010-008-9888-0. PMID 18719978. S2CID 33770538.
Roberts AG, Redding SJ, Llewellyn DH (2005). "An alternatively-spliced exon in the 5'-UTR of human ALAS1 mRNA inhibits translation and renders it resistant to haem-mediated decay". FEBS Lett. 579 (5): 1061–6. doi:10.1016/j.febslet.2004.12.080. PMID 15710391. S2CID 32462861.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Jung M, Ohl F, Stephan C, et al. (2007). "[Quantifying gene expression in prostate carcinoma. Which endogenous reference genes are suitable?]". Urologe A. 46 (9): 1083–4. doi:10.1007/s00120-007-1436-0. PMID 17628775. S2CID 11640176.
Guberman AS, Scassa ME, Giono LE, et al. (2003). "Inhibitory effect of AP-1 complex on 5-aminolevulinate synthase gene expression through sequestration of cAMP-response element protein (CRE)-binding protein (CBP) coactivator". J. Biol. Chem. 278 (4): 2317–26. doi:10.1074/jbc.M205057200. PMID 12433930.
Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Ferreira GC, Cheltsov AV (2002). "Circular permutation of 5-aminolevulinate synthase as a tool to evaluate folding, structure and function". Cell. Mol. Biol. (Noisy-le-grand). 48 (1): 11–6. PMID 11929042.
Tsang HT, Connell JW, Brown SE, et al. (2006). "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex". Genomics. 88 (3): 333–46. doi:10.1016/j.ygeno.2006.04.003. PMID 16730941.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000023330 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000032786 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid2347585-5] Bishop DF, Henderson AS, Astrin KH (June 1990). "Human delta-aminolevulinate synthase: assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X chromosome". Genomics. 7 (2): 207–14. doi:10.1016/0888-7543(90)90542-3. PMID 2347585.

[entrez-6] "Entrez Gene: Delta-aminolevulinate synthase 1".

ALAS1

References

External links

Further reading