ALAS2 | ENSG00000158578 | NCBI 212

Details for: ALAS2

Gene ID: 212

Symbol: ALAS2

Ensembl ID: ENSG00000158578

Description: 5'-aminolevulinate synthase 2

Associated with

Heme biosynthesis
(R-HSA-189451)
Metabolism
(R-HSA-1430728)
Metabolism of porphyrins
(R-HSA-189445)
5-aminolevulinate synthase activity
(GO:0003870)
Erythrocyte development
(GO:0048821)
Erythrocyte differentiation
(GO:0030218)
Heme biosynthetic process
(GO:0006783)
Hemoglobin biosynthetic process
(GO:0042541)
Intracellular iron ion homeostasis
(GO:0006879)
Intracellular oxygen homeostasis
(GO:0032364)
Mitochondrial inner membrane
(GO:0005743)
Mitochondrial matrix
(GO:0005759)
Mitochondrion
(GO:0005739)
Protein binding
(GO:0005515)
Protoporphyrinogen ix biosynthetic process
(GO:0006782)
Pyridoxal phosphate binding
(GO:0030170)
Response to hypoxia
(GO:0001666)

Other Information

Proteins

5-aminolevulinate synthase, erythroid-specific, mitochondrial

Genular Protein ID: 1196948901

Symbol: HEM0_HUMAN

Name: 5-aminolevulinate synthase, erythroid-specific, mitochondrial

UniProtKB Accession Codes:

P22557 A8K3F0 A8K6C4 Q13735 Q5JZF5 Q8N6H3

Database IDs:

Citations:

PubMed ID: 2263504

Title: Two different genes encode delta-aminolevulinate synthase in humans: nucleotide sequences of cDNAs for the housekeeping and erythroid genes.

PubMed ID: 2263504

DOI: 10.1093/nar/18.23.7187

PubMed ID: 2050125

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

PubMed ID: 2050125

DOI: 10.1002/j.1460-2075.1991.tb07715.x

PubMed ID: 9642238

Title: Identification and characterization of a conserved erythroid-specific enhancer located in intron 8 of the human 5-aminolevulinate synthase 2 gene.

PubMed ID: 9642238

DOI: 10.1074/jbc.273.27.16798

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15772651

Title: The DNA sequence of the human X chromosome.

PubMed ID: 15772651

DOI: 10.1038/nature03440

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 14643893

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

PubMed ID: 14643893

DOI: 10.1016/s1357-2725(03)00246-2

PubMed ID: 32499479

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

PubMed ID: 32499479

DOI: 10.1038/s41467-020-16586-x

PubMed ID: 8107717

Title: X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase.

PubMed ID: 8107717

DOI: 10.1056/nejm199403103301004

PubMed ID: 1570328

Title: Enzymatic defect in 'X-linked' sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency.

PubMed ID: 1570328

DOI: 10.1073/pnas.89.9.4028

PubMed ID: 9858242

Title: R411C mutation of the ALAS2 gene encodes a pyridoxine-responsive enzyme with low activity.

PubMed ID: 9858242

DOI: 10.1046/j.1365-2141.1998.01050.x

PubMed ID: 10577279

Title: A novel mutation of the erythroid-specific gamma-aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia.

PubMed ID: 10577279

DOI: 10.1002/(sici)1096-8652(199910)62:2<112::aid-ajh9>3.0.co;2-l

PubMed ID: 10029606

Title: Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis.

PubMed ID: 10029606

PubMed ID: 12393718

Title: Absent phenotypic expression of X-linked sideroblastic anemia in one of 2 brothers with a novel ALAS2 mutation.

PubMed ID: 12393718

DOI: 10.1182/blood-2002-03-0685

PubMed ID: 12031592

Title: A novel mutation in exon 5 of the ALAS2 gene results in X-linked sideroblastic anemia.

PubMed ID: 12031592

DOI: 10.1016/s0009-8981(02)00095-5

PubMed ID: 16446107

Title: Three kinships with ALAS2 P520L (c. 1559 C --> T) mutation, two in association with severe iron overload, and one with sideroblastic anemia and severe iron overload.

PubMed ID: 16446107

DOI: 10.1016/j.bcmd.2005.12.004

PubMed ID: 18760763

Title: C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload.

PubMed ID: 18760763

DOI: 10.1016/j.ajhg.2008.08.003

PubMed ID: 19731322

Title: Systematic molecular genetic analysis of congenital sideroblastic anemia: evidence for genetic heterogeneity and identification of novel mutations.

PubMed ID: 19731322

DOI: 10.1002/pbc.22244

PubMed ID: 21252495

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

PubMed ID: 21252495

DOI: 10.1159/000322870

PubMed ID: 21653323

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

PubMed ID: 21653323

DOI: 10.1182/blood-2011-03-342873

PubMed ID: 21309041

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

PubMed ID: 21309041

DOI: 10.1002/humu.21455

Sequence Information:

Length: 587
Mass: 64633
Checksum: FD821BE245C440B5
Sequence:

MVTAAMLLQC CPVLARGPTS LLGKVVKTHQ FLFGIGRCPI LATQGPNCSQ IHLKATKAGG 
DSPSWAKGHC PFMLSELQDG KSKIVQKAAP EVQEDVKAFK TDLPSSLVSV SLRKPFSGPQ 
EQEQISGKVT HLIQNNMPGN YVFSYDQFFR DKIMEKKQDH TYRVFKTVNR WADAYPFAQH 
FSEASVASKD VSVWCSNDYL GMSRHPQVLQ ATQETLQRHG AGAGGTRNIS GTSKFHVELE 
QELAELHQKD SALLFSSCFV ANDSTLFTLA KILPGCEIYS DAGNHASMIQ GIRNSGAAKF 
VFRHNDPDHL KKLLEKSNPK IPKIVAFETV HSMDGAICPL EELCDVSHQY GALTFVDEVH 
AVGLYGSRGA GIGERDGIMH KIDIISGTLG KAFGCVGGYI ASTRDLVDMV RSYAAGFIFT 
TSLPPMVLSG ALESVRLLKG EEGQALRRAH QRNVKHMRQL LMDRGLPVIP CPSHIIPIRV 
GNAALNSKLC DLLLSKHGIY VQAINYPTVP RGEELLRLAP SPHHSPQMME DFVEKLLLAW 
TAVGLPLQDV SVAACNFCRR PVHFELMSEW ERSYFGNMGP QYVTTYA

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: ALAS2

Associated with

Other Information

Two different genes encode delta-aminolevulinate synthase in humans: nucleotide sequences of cDNAs for the housekeeping and erythroid genes. PubMed ID: 2263504

Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA. PubMed ID: 2050125

Identification and characterization of a conserved erythroid-specific enhancer located in intron 8 of the human 5-aminolevulinate synthase 2 gene. PubMed ID: 9642238

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The DNA sequence of the human X chromosome. PubMed ID: 15772651

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

The major splice variant of human 5-aminolevulinate synthase-2 contributes significantly to erythroid heme biosynthesis. PubMed ID: 14643893

Human aminolevulinate synthase structure reveals a eukaryotic-specific autoinhibitory loop regulating substrate binding and product release. PubMed ID: 32499479

X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase. PubMed ID: 8107717

Enzymatic defect in 'X-linked' sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency. PubMed ID: 1570328

R411C mutation of the ALAS2 gene encodes a pyridoxine-responsive enzyme with low activity. PubMed ID: 9858242

A novel mutation of the erythroid-specific gamma-aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia. PubMed ID: 10577279

Four new mutations in the erythroid-specific 5-aminolevulinate synthase (ALAS2) gene causing X-linked sideroblastic anemia: increased pyridoxine responsiveness after removal of iron overload by phlebotomy and coinheritance of hereditary hemochromatosis. PubMed ID: 10029606

Absent phenotypic expression of X-linked sideroblastic anemia in one of 2 brothers with a novel ALAS2 mutation. PubMed ID: 12393718

A novel mutation in exon 5 of the ALAS2 gene results in X-linked sideroblastic anemia. PubMed ID: 12031592

Three kinships with ALAS2 P520L (c. 1559 C --&gt; T) mutation, two in association with severe iron overload, and one with sideroblastic anemia and severe iron overload. PubMed ID: 16446107

C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload. PubMed ID: 18760763

Systematic molecular genetic analysis of congenital sideroblastic anemia: evidence for genetic heterogeneity and identification of novel mutations. PubMed ID: 19731322

New mutation in erythroid-specific delta-aminolevulinate synthase as the cause of X-linked sideroblastic anemia responsive to pyridoxine. PubMed ID: 21252495

ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria. PubMed ID: 21653323

Sideroblastic anemia: molecular analysis of the ALAS2 gene in a series of 29 probands and functional studies of 10 missense mutations. PubMed ID: 21309041