Alas2 (5'-aminolevulinate synthase 2) - Rat Genome Database

Send us a Message



 Submit Data |  Help |  Video Tutorials |  News |  Publications |  Download |  REST API |  Citing RGD |  Contact   
Search RGD Grant Resources Citing RGD About Us Contact Us
Genes QTLs Strains Markers Community Projects Genome Information Ontologies Cell Lines References Download Submit Data
OntoMate (Literature Search) JBrowse (Genome Browser) Synteny Browser (VCMap)  (beta) Variant Visualizer Multi-Ontology Enrichment (MOET) Gene-Ortholog Location Finder (GOLF) InterViewer (Protein-Protein Interactions) PhenoMiner (Quatitative Phenotypes) Gene Annotator OLGA (Gene List Generator) AllianceMine GViewer (Genome Viewer)
Aging & Age-Related Disease Cancer & Neoplastic Disease Cardiovascular Disease COVID-19 Developmental Disease Diabetes Hematologic Disease Immune & Inflammatory Disease Infectious Disease Liver Disease Neurological Disease Obesity & Metabolic Syndrome Renal Disease Respiratory Disease Sensory Organ Disease
Find Models   new Genetic Models Autism Models Rat PhenoMiner (Quantitative Phenotypes) Chinchilla PhenoMiner Expected Ranges (Quantitative Phenotype) PhenoMiner Term Comparison Hybrid Rat Diversity Panel Phenotypes GERRC (Gene Editing Rat Resource Center) Phenotypes in Other Animal Models Animal Husbandry Strain Medical Records Phylogenetics Strain Availability Calendar Rats 101 Submissions Photo Archive
Pathways
Rat Community Forum Directory of Rat Laboratories Video Tutorials News RGD Publications RGD Presentations Archive Nomenclature Guidelines Resource Links Laboratory Resources Employment Resources
Gene: Alas2 (5'-aminolevulinate synthase 2) Rattus norvegicus
Analyze
Symbol: Alas2
Name: 5'-aminolevulinate synthase 2
RGD ID: 2084
Description: Enables 5-aminolevulinate synthase activity and coenzyme A binding activity. Involved in several processes, including lactation; liver regeneration; and response to benzene. Predicted to be located in mitochondrial inner membrane. Predicted to be active in mitochondrion. Biomarker of anemia; bilirubin metabolic disorder; and hemolytic anemia. Human ortholog(s) of this gene implicated in cutaneous porphyria; erythropoietic protoporphyria; hemochromatosis; sideroblastic anemia; and sideroblastic anemia 1. Orthologous to human ALAS2 (5'-aminolevulinate synthase 2); PARTICIPATES IN heme biosynthetic pathway; glycine, serine and threonine metabolic pathway; porphyrin and chlorophyll metabolic pathway; INTERACTS WITH 17beta-estradiol; 2,3,7,8-tetrachlorodibenzodioxine; 2,6-dinitrotoluene.
Type: protein-coding
RefSeq Status: PROVISIONAL
Previously known as: 5-aminolevulinate synthase, erythroid-specific, mitochondrial; 5-aminolevulinic acid synthase 2; ALAS-E; Aminolevulinate synthase 2 delta; Aminolevulinate synthase 2, delta; aminolevulinate, delta-, synthase 2; aminolevulinic acid synthase 2; aminolevulinic acid synthase 2, erythroid; aminolevulinic acid synthase 2, erythroid-like; delta-ALA synthase 2; delta-ALA synthetase; delta-aminolevulinate synthase 2; erythroid-specific delta-aminolevulinate synthase ALAS-E; erythroid-specific delta-aminolevulinate synthase, ALAS-E; LOC100363476
RGD Orthologs
Human
Mouse
Chinchilla
Bonobo
Dog
Squirrel
Pig
Green Monkey
Naked Mole-Rat
Alliance Genes
More Info more info ...
Latest Assembly: mRatBN7.2 - mRatBN7.2 Assembly
Position:
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
mRatBN7.2X19,463,146 - 19,486,526 (+)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 EnsemblX19,463,171 - 19,486,519 (+)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_UtxX16,897,530 - 16,916,114 (+)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0X23,208,808 - 23,227,392 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0X19,981,156 - 19,999,751 (+)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0X23,167,576 - 23,187,356 (-)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 EnsemblX23,167,696 - 23,187,341 (-)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0X23,587,683 - 23,605,753 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.1X39,853,992 - 39,864,053 (+)NCBI
CeleraX19,742,070 - 19,760,615 (+)NCBICelera
Cytogenetic MapXq12NCBI
JBrowse: View Region in Genome Browser (JBrowse)
Model


Gene-Chemical Interaction Annotations     Click to see Annotation Detail View
(1->4)-beta-D-glucan  (ISO)
1,2-dichloroethane  (ISO)
17alpha-ethynylestradiol  (ISO)
17beta-estradiol  (EXP,ISO)
2,2',4,4',5,5'-hexachlorobiphenyl  (ISO)
2,3,7,8-tetrachlorodibenzodioxine  (EXP,ISO)
2,6-dinitrotoluene  (EXP)
3,3',4,4',5-pentachlorobiphenyl  (EXP)
3H-1,2-dithiole-3-thione  (EXP,ISO)
4,4'-sulfonyldiphenol  (ISO)
4-hydroxyphenyl retinamide  (ISO)
6-propyl-2-thiouracil  (EXP)
7,12-dimethyltetraphene  (EXP)
acetamide  (EXP)
aflatoxin B1  (ISO)
amiodarone  (ISO)
antirheumatic drug  (ISO)
arsenous acid  (ISO)
astemizole  (EXP)
benzene  (EXP,ISO)
benzo[a]pyrene  (ISO)
benzo[b]fluoranthene  (ISO)
beta-naphthoflavone  (EXP)
bisphenol A  (EXP,ISO)
bisphenol F  (ISO)
butyric acid  (ISO)
cadmium dichloride  (EXP)
cantharidin  (ISO)
carbamazepine  (ISO)
carbon nanotube  (ISO)
carbonyl sulfide  (EXP)
carboplatin  (EXP)
carmustine  (EXP)
catechol  (ISO)
CGP 52608  (ISO)
chloroprene  (EXP)
cisplatin  (EXP)
clofibrate  (ISO)
copper atom  (EXP,ISO)
copper(0)  (EXP,ISO)
crocidolite asbestos  (ISO)
Cuprizon  (EXP)
diarsenic trioxide  (ISO)
dibutyl phthalate  (ISO)
dichloroacetic acid  (ISO)
diclofenac  (ISO)
dimethyl sulfoxide  (ISO)
dioxygen  (ISO)
doxorubicin  (EXP,ISO)
epoxiconazole  (ISO)
ethanol  (ISO)
ferroheme b  (ISO)
gentamycin  (EXP)
heme b  (ISO)
hemin  (ISO)
hexachlorobenzene  (EXP)
indole-3-methanol  (EXP)
indometacin  (EXP)
inulin  (ISO)
irinotecan  (ISO)
iron atom  (ISO)
iron(0)  (ISO)
lead diacetate  (EXP)
linalool  (EXP)
linezolid  (EXP)
maneb  (ISO)
metformin  (EXP)
methimazole  (EXP)
methotrexate  (EXP)
N-nitrosodiethylamine  (EXP,ISO)
nitrofen  (EXP)
ozone  (ISO)
paracetamol  (EXP,ISO)
paraquat  (ISO)
parathion  (ISO)
perfluorohexanesulfonic acid  (ISO)
perfluorononanoic acid  (ISO)
perfluorooctane-1-sulfonic acid  (ISO)
perfluorooctanoic acid  (ISO)
phenacetin  (EXP)
phenformin  (EXP)
phenol  (ISO)
phenylhydrazine  (EXP)
pirinixic acid  (EXP,ISO)
potassium dichromate  (ISO)
progesterone  (ISO)
raloxifene  (EXP)
rotenone  (EXP)
S-adenosyl-L-homocysteine  (ISO)
S-adenosyl-L-methioninate  (ISO)
S-adenosyl-L-methionine  (ISO)
sodium arsenate  (ISO)
sodium arsenite  (ISO)
sodium dichromate  (ISO)
T-2 toxin  (ISO)
testosterone  (ISO)
tetrachloromethane  (EXP,ISO)
thioacetamide  (EXP)
tioguanine  (EXP)
trichloroethene  (EXP)
triphenyl phosphate  (EXP)
tungsten  (ISO)
valproic acid  (ISO)
vinclozolin  (EXP)

Gene Ontology Annotations     Click to see Annotation Detail View

Cellular Component

Molecular Function

Molecular Pathway Annotations     Click to see Annotation Detail View
References

References - curated
# Reference Title Reference Citation
1. Biosynthesis of heme in mammals. Ajioka RS, etal., Biochim Biophys Acta. 2006 Jul;1763(7):723-36. Epub 2006 Jun 3.
2. Effects of chlorinated benzenes of the activities of delta-aminolevulinic acid synthetase and heme oxygenase and on the content of hemoprotein in the liver of rats. Ariyoshi T, etal., J Pharmacobiodyn. 1981 Jan;4(1):69-76.
3. Synthesis, delivery and regulation of eukaryotic heme and Fe-S cluster cofactors. Barupala DP, etal., Arch Biochem Biophys. 2016 Feb 15;592:60-75. doi: 10.1016/j.abb.2016.01.010. Epub 2016 Jan 16.
4. Pregnancy and lactation modulate maternal splenic growth and development of the erythroid lineage in the rat and mouse. Bustamante JJ, etal., Reprod Fertil Dev. 2008;20(2):303-10.
5. Familial-skewed X-chromosome inactivation as a predisposing factor for late-onset X-linked sideroblastic anemia in carrier females. Cazzola M, etal., Blood. 2000 Dec 15;96(13):4363-5.
6. X-linked sideroblastic anemia: identification of the mutation in the erythroid-specific delta-aminolevulinate synthase gene (ALAS2) in the original family described by Cooley. Cotter PD, etal., Blood. 1994 Dec 1;84(11):3915-24.
7. Late-onset X-linked sideroblastic anemia. Missense mutations in the erythroid delta-aminolevulinate synthase (ALAS2) gene in two pyridoxine-responsive patients initially diagnosed with acquired refractory anemia and ringed sideroblasts. Cotter PD, etal., J Clin Invest. 1995 Oct;96(4):2090-6.
8. Nature of heme metabolizing enzymes in a mutant rat with hyperbilirubinuria. Dhar SK, etal., Res Commun Chem Pathol Pharmacol. 1993 Jun;80(3):329-36.
9. Molecular and functional analysis of the C-terminal region of human erythroid-specific 5-aminolevulinic synthase associated with X-linked dominant protoporphyria (XLDPP). Ducamp S, etal., Hum Mol Genet. 2013 Apr 1;22(7):1280-8. doi: 10.1093/hmg/dds531. Epub 2012 Dec 20.
10. Development of a large-scale chemogenomics database to improve drug candidate selection and to understand mechanisms of chemical toxicity and action. Ganter B, etal., J Biotechnol. 2005 Sep 29;119(3):219-44.
11. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Gaudet P, etal., Brief Bioinform. 2011 Sep;12(5):449-62. doi: 10.1093/bib/bbr042. Epub 2011 Aug 27.
12. GenMAPP: Gene Map Annotator and Pathway Profiler GenMAPP
13. Rat ISS GO annotations from GOA human gene data--August 2006 GOA data from the GO Consortium
14. Fish oil feeding up-regulates the expression of 5-aminolevulinate synthase 2 mRNA in rat brain. Haraguchi T, etal., Biosci Biotechnol Biochem. 2011;75(7):1383-5. Epub 2011 Jul 7.
15. PROLACTIN-LIKE PROTEIN-F SUBFAMILY OF PLACENTAL HORMONES/ CYTOKINES: RESPONSIVENESS TO MATERNAL HYPOXIA. Ho-Chen JK, etal., Endocrinology. 2006 Nov 9;.
16. The source of heme for vascular heme oxygenase II: de novo heme biosynthesis in rat aorta. Jaronczyk K, etal., Can J Physiol Pharmacol. 2004 Apr;82(4):218-24.
17. KEGG: Kyoto Encyclopedia of Genes and Genomes KEGG
18. New mutation in erythroid-specific delta-aminolevulinate synthase as the cause of X-linked sideroblastic anemia responsive to pyridoxine. Kucerova J, etal., Acta Haematol. 2011;125(4):193-7. doi: 10.1159/000322870. Epub 2011 Jan 20.
19. Circadian rhythms in acute intermittent porphyria--a pilot study. Larion S, etal., Eur J Clin Invest. 2013 Jul;43(7):727-39. doi: 10.1111/eci.12102. Epub 2013 May 8.
20. 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. Lee PL, etal., Blood Cells Mol Dis. 2006 Mar-Apr;36(2):292-7. Epub 2006 Jan 30.
21. Rat ISS GO annotations from MGI mouse gene data--August 2006 MGD data from the GO Consortium
22. Purification and structure of rat erythroid-specific delta-aminolevulinate synthase. Munakata H, etal., J Biochem (Tokyo) 1993 Jul;114(1):103-11.
23. Role of the heme regulatory motif in the heme-mediated inhibition of mitochondrial import of 5-aminolevulinate synthase. Munakata H, etal., J Biochem (Tokyo). 2004 Aug;136(2):233-8.
24. Electronic Transfer of LocusLink and RefSeq Data NCBI rat LocusLink and RefSeq merged data July 26, 2002
25. OMIM Disease Annotation Pipeline OMIM Disease Annotation Pipeline
26. KEGG Annotation Import Pipeline Pipeline to import KEGG annotations from KEGG into RGD
27. GOA pipeline RGD automated data pipeline
28. ClinVar Automated Import and Annotation Pipeline RGD automated import pipeline for ClinVar variants, variant-to-disease annotations and gene-to-disease annotations
29. Data Import for Chemical-Gene Interactions RGD automated import pipeline for gene-chemical interactions
30. A Toxicogenomic Approach Revealed Hepatic Gene Expression Changes Mechanistically Linked to Drug-Induced Hemolytic Anemia. Rokushima M, etal., Toxicol Sci. 2006 Nov 2;.
31. Changes in brain biogenic amines and haem biosynthesis and their response to combined administration of succimers and Centella asiatica in lead poisoned rats. Saxena G and Flora SJ, J Pharm Pharmacol. 2006 Apr;58(4):547-59.
32. Effects of perphenazine, chlorpromazine or CoCl2 on the activities of delta-aminolevulinic acid synthetase and heme oxygenase and on the content of hemoprotein in rat liver. Senda N, etal., Res Commun Chem Pathol Pharmacol. 1989 Jul;65(1):57-64.
33. Haem and drug-metabolizing enzymes in regenerating rat liver. Srivastava RC, etal., Br J Exp Pathol. 1982 Feb;63(1):1-4.
34. Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Strausberg RL, etal., Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11.
35. ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria. To-Figueras J, etal., Blood. 2011 Aug 11;118(6):1443-51. doi: 10.1182/blood-2011-03-342873. Epub 2011 Jun 7.
36. A toxicogenomic approach for identifying biomarkers for myelosuppressive anemia in rats. Uehara T, etal., Toxicology. 2011 Apr 11;282(3):139-45. doi: 10.1016/j.tox.2011.01.027. Epub 2011 Feb 4.
37. C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload. Whatley SD, etal., Am J Hum Genet. 2008 Sep;83(3):408-14. doi: 10.1016/j.ajhg.2008.08.003. Epub 2008 Sep 4.
Additional References at PubMed
PMID:7620186   PMID:9446639   PMID:10562540   PMID:10727444   PMID:14643893   PMID:14651853   PMID:16234850   PMID:18614015  


Genomics

Comparative Map Data
Alas2
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
mRatBN7.2X19,463,146 - 19,486,526 (+)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 EnsemblX19,463,171 - 19,486,519 (+)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_UtxX16,897,530 - 16,916,114 (+)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.0X23,208,808 - 23,227,392 (-)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.0X19,981,156 - 19,999,751 (+)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.0X23,167,576 - 23,187,356 (-)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 EnsemblX23,167,696 - 23,187,341 (-)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.0X23,587,683 - 23,605,753 (-)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.1X39,853,992 - 39,864,053 (+)NCBI
CeleraX19,742,070 - 19,760,615 (+)NCBICelera
Cytogenetic MapXq12NCBI
ALAS2
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCh38X55,009,055 - 55,030,977 (-)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 EnsemblX55,009,055 - 55,030,977 (-)EnsemblGRCh38hg38GRCh38
GRCh37X55,035,488 - 55,057,410 (-)NCBIGRCh37GRCh37hg19GRCh37
Build 36X55,052,213 - 55,074,136 (-)NCBINCBI36Build 36hg18NCBI36
Build 34X54,918,512 - 54,940,432NCBI
CeleraX58,870,631 - 58,892,640 (-)NCBICelera
Cytogenetic MapXp11.21NCBI
HuRefX52,086,432 - 52,108,437 (-)NCBIHuRef
CHM1_1X55,025,527 - 55,047,534 (-)NCBICHM1_1
T2T-CHM13v2.0X54,302,181 - 54,324,103 (-)NCBIT2T-CHM13v2.0
Alas2
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCm39X149,330,443 - 149,353,614 (+)NCBIGRCm39GRCm39mm39
GRCm39 EnsemblX149,330,371 - 149,353,634 (+)EnsemblGRCm39 Ensembl
GRCm38X150,547,417 - 150,570,622 (+)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 EnsemblX150,547,375 - 150,570,638 (+)EnsemblGRCm38mm10GRCm38
MGSCv37X146,981,960 - 147,005,165 (+)NCBIGRCm37MGSCv37mm9NCBIm37
MGSCv36X145,888,161 - 145,911,335 (+)NCBIMGSCv36mm8
CeleraX133,836,224 - 133,858,249 (-)NCBICelera
Cytogenetic MapXF3NCBI
cM MapX68.46NCBI
Alas2
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChiLan1.0 EnsemblNW_0049554752,362,118 - 2,377,864 (-)EnsemblChiLan1.0
ChiLan1.0NW_0049554752,362,368 - 2,382,680 (-)NCBIChiLan1.0ChiLan1.0
ALAS2
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
NHGRI_mPanPan1X56,408,788 - 56,430,790 (-)NCBINHGRI_mPanPan1
Mhudiblu_PPA_v0X47,219,588 - 47,241,592 (-)NCBIMhudiblu_PPA_v0Mhudiblu_PPA_v0panPan3
PanPan1.1X55,451,669 - 55,468,601 (-)NCBIpanpan1.1PanPan1.1panPan2
PanPan1.1 EnsemblX55,451,794 - 55,473,680 (-)Ensemblpanpan1.1panPan2
ALAS2
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
CanFam3.1X46,703,477 - 46,731,767 (-)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
CanFam3.1 EnsemblX46,703,477 - 46,723,529 (-)EnsemblCanFam3.1canFam3CanFam3.1
Dog10K_Boxer_TashaX38,039,113 - 38,065,286 (-)NCBIDog10K_Boxer_Tasha
ROS_Cfam_1.0X46,992,131 - 47,018,312 (-)NCBIROS_Cfam_1.0
ROS_Cfam_1.0 EnsemblX46,992,147 - 47,018,260 (-)EnsemblROS_Cfam_1.0 Ensembl
UMICH_Zoey_3.1X46,501,907 - 46,528,079 (-)NCBIUMICH_Zoey_3.1
UNSW_CanFamBas_1.0X46,968,475 - 46,994,644 (-)NCBIUNSW_CanFamBas_1.0
UU_Cfam_GSD_1.0X46,910,743 - 46,936,916 (-)NCBIUU_Cfam_GSD_1.0
Alas2
(Ictidomys tridecemlineatus - thirteen-lined ground squirrel)
Squirrel AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HiC_Itri_2X39,478,526 - 39,501,336 (-)NCBIHiC_Itri_2
SpeTri2.0 EnsemblNW_0049367511,814,446 - 1,841,531 (-)EnsemblSpeTri2.0
SpeTri2.0NW_0049367511,818,255 - 1,841,028 (-)NCBISpeTri2.0SpeTri2.0SpeTri2.0
ALAS2
(Sus scrofa - pig)
Pig AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Sscrofa11.1 EnsemblX47,871,523 - 47,896,000 (-)EnsemblSscrofa11.1susScr11Sscrofa11.1
Sscrofa11.1X47,871,519 - 47,896,041 (-)NCBISscrofa11.1Sscrofa11.1susScr11Sscrofa11.1
Sscrofa10.2X53,807,663 - 53,832,189 (-)NCBISscrofa10.2Sscrofa10.2susScr3
ALAS2
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChlSab1.1X51,086,062 - 51,108,564 (-)NCBIChlSab1.1ChlSab1.1chlSab2
ChlSab1.1 EnsemblX51,086,066 - 51,103,505 (-)EnsemblChlSab1.1ChlSab1.1 EnsemblchlSab2
Vero_WHO_p1.0NW_0236660865,064,507 - 5,087,016 (-)NCBIVero_WHO_p1.0Vero_WHO_p1.0
Alas2
(Heterocephalus glaber - naked mole-rat)
Naked Mole-Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HetGla_female_1.0 EnsemblNW_004624910426,032 - 448,325 (-)EnsemblHetGla_female_1.0HetGla_female_1.0 EnsemblhetGla2
HetGla 1.0NW_004624910426,273 - 726,778 (-)NCBIHetGla_female_1.0HetGla 1.0hetGla2

Variants

.
Variants in Alas2
74 total Variants
miRNA Target Status

Predicted Target Of
Summary Value
Count of predictions:60
Count of miRNA genes:55
Interacting mature miRNAs:59
Transcripts:ENSRNOT00000000180
Prediction methods:Miranda, Rnahybrid, Targetscan
Result types:miRGate_prediction

The detailed report is available here: Full Report CSV TAB Printer

miRNA Target Status data imported from miRGate (http://mirgate.bioinfo.cnio.es/).
For more information about miRGate, see PMID:25858286 or access the full paper here.


QTLs in Region (mRatBN7.2)
The following QTLs overlap with this region.    Full Report CSV TAB Printer Gviewer
RGD IDSymbolNameLODP ValueTraitSub TraitChrStartStopSpecies
731181Uae27Urinary albumin excretion QTL 272.70.0059urine albumin amount (VT:0002871)urine albumin excretion rate (CMO:0000757)X143491017Rat
634325Bw13Body weight QTL 130body mass (VT:0001259)body weight (CMO:0000012)X144797220991088Rat
70165Bp64Blood pressure QTL 645.2arterial blood pressure trait (VT:2000000)systolic blood pressure (CMO:0000004)X144812931706553Rat
631204Gluco15Glucose level QTL 150.001blood glucose amount (VT:0000188)blood glucose level area under curve (AUC) (CMO:0000350)X162371522646544Rat
1298071Edpm12Estrogen-dependent pituitary mass QTL 123.2pituitary gland mass (VT:0010496)pituitary gland wet weight (CMO:0000853)X292789847927898Rat
10755455Coatc13Coat color QTL 130coat/hair pigmentation trait (VT:0010463)pigmented ventral coat/hair area to total ventral coat/hair area ratio (CMO:0001812)7440600049406000Rat
631666Iddm5Insulin dependent diabetes mellitus QTL 5blood glucose amount (VT:0000188)plasma glucose level (CMO:0000042)X449454949494549Rat
61430Cia18Collagen induced arthritis QTL 183.1joint integrity trait (VT:0010548)joint inflammation composite score (CMO:0000919)X14843113120568734Rat
71116Niddm16Non-insulin dependent diabetes mellitus QTL 167.81blood glucose amount (VT:0000188)plasma glucose level (CMO:0000042)X1529780260297802Rat

Markers in Region
Alas2  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.2X19,486,282 - 19,486,409 (-)MAPPERmRatBN7.2
Rnor_6.0X23,167,686 - 23,167,812NCBIRnor6.0
Rnor_5.0X23,587,793 - 23,587,919UniSTSRnor5.0
RGSC_v3.4X39,810,348 - 39,810,474UniSTSRGSC3.4
CeleraX19,760,379 - 19,760,505UniSTS
Cytogenetic MapXq21UniSTS
RH130825  
Rat AssemblyChrPosition (strand)SourceJBrowse
Cytogenetic MapXq21UniSTS


Expression


RNA-SEQ Expression
High: > 1000 TPM value   Medium: Between 11 and 1000 TPM
Low: Between 0.5 and 10 TPM   Below Cutoff: < 0.5 TPM

alimentary part of gastrointestinal system circulatory system endocrine system exocrine system hemolymphoid system hepatobiliary system integumental system musculoskeletal system nervous system renal system reproductive system respiratory system appendage
High 6 6 1 6
Medium 1 43 36 28 12 28 1 1 58 28 35 11 1
Low 2 15 7 6 7 7 10 16 7 6 7
Below cutoff

Sequence

Nucleotide Sequences
RefSeq Transcripts NM_013197 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_039099504 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_039099505 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_039099506 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_039099507 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_039099508 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_039099509 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  XM_039099510 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
GenBank Nucleotide AF186775 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  BC081857 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  CH474063 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  D86297 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ227145 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ232108 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  FQ232456 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles
  JACYVU010000368 (Get FASTA)   NCBI Sequence Viewer   Search GEO for Microarray Profiles

Reference Sequences
RefSeq Acc Id: ENSRNOT00000000180   ⟹   ENSRNOP00000000180
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 EnsemblX19,463,171 - 19,486,519 (+)Ensembl
Rnor_6.0 EnsemblX23,167,696 - 23,187,341 (-)Ensembl
RefSeq Acc Id: NM_013197   ⟹   NP_037329
RefSeq Status: PROVISIONAL
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2X19,467,924 - 19,486,519 (+)NCBI
Rnor_6.0X23,167,576 - 23,187,356 (-)NCBI
Rnor_5.0X23,587,683 - 23,605,753 (-)NCBI
CeleraX19,742,070 - 19,760,615 (+)RGD
Sequence:
RefSeq Acc Id: XM_039099504   ⟹   XP_038955432
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2X19,463,146 - 19,486,526 (+)NCBI
RefSeq Acc Id: XM_039099505   ⟹   XP_038955433
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2X19,467,504 - 19,486,526 (+)NCBI
RefSeq Acc Id: XM_039099506   ⟹   XP_038955434
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2X19,466,050 - 19,486,526 (+)NCBI
RefSeq Acc Id: XM_039099507   ⟹   XP_038955435
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2X19,463,146 - 19,486,526 (+)NCBI
RefSeq Acc Id: XM_039099508   ⟹   XP_038955436
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2X19,463,146 - 19,486,526 (+)NCBI
RefSeq Acc Id: XM_039099509   ⟹   XP_038955437
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2X19,466,032 - 19,486,526 (+)NCBI
RefSeq Acc Id: XM_039099510   ⟹   XP_038955438
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2X19,463,146 - 19,486,526 (+)NCBI
Reference Protein Sequences
RefSeq Acc Id: NP_037329   ⟸   NM_013197
- UniProtKB: Q63895 (UniProtKB/Swiss-Prot),   Q63147 (UniProtKB/Swiss-Prot)
- Sequence:
RefSeq Acc Id: ENSRNOP00000000180   ⟸   ENSRNOT00000000180
RefSeq Acc Id: XP_038955432   ⟸   XM_039099504
- Peptide Label: isoform X1
RefSeq Acc Id: XP_038955435   ⟸   XM_039099507
- Peptide Label: isoform X2
- UniProtKB: Q642C1 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_038955436   ⟸   XM_039099508
- Peptide Label: isoform X3
RefSeq Acc Id: XP_038955438   ⟸   XM_039099510
- Peptide Label: isoform X4
- UniProtKB: F1LVW9 (UniProtKB/TrEMBL)
RefSeq Acc Id: XP_038955437   ⟸   XM_039099509
- Peptide Label: isoform X3
RefSeq Acc Id: XP_038955434   ⟸   XM_039099506
- Peptide Label: isoform X1
RefSeq Acc Id: XP_038955433   ⟸   XM_039099505
- Peptide Label: isoform X1
Protein Domains
5-aminolevulinate synthase presequence   Aminotransferase class I/classII

Protein Structures
Name Modeler Protein Id AA Range Protein Structure
AF-Q63147-F1-model_v2 AlphaFold Q63147 1-587 view protein structure

Transcriptome

eQTL   View at Phenogen
WGCNA   View at Phenogen
Tissue/Strain Expression   View at Phenogen


Additional Information

Database Acc Id Source(s)
AGR Gene RGD:2084 AgrOrtholog
BioCyc Gene G2FUF-2811 BioCyc
BioCyc Pathway PWY-5189 [tetrapyrrole biosynthesis II (from glycine)] BioCyc
Ensembl Genes ENSRNOG00000000167 Ensembl, ENTREZGENE, UniProtKB/TrEMBL
Ensembl Transcript ENSRNOT00000000180 ENTREZGENE
  ENSRNOT00000000180.8 UniProtKB/TrEMBL
Gene3D-CATH 3.40.640.10 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  3.90.1150.10 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Aminolevulinic Acid Synthase 2 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
IMAGE_CLONE IMAGE:7133382 IMAGE-MGC_LOAD
InterPro 4pyrrol_synth_NH2levulA_synth UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  5aminolev_synth_preseq UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Aminotrans_II_pyridoxalP_BS UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Aminotransferase_I/II UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  PyrdxlP-dep_Trfase UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  PyrdxlP-dep_Trfase_dom1 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  PyrdxlP-dep_Trfase_major UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
KEGG Report rno:25748 UniProtKB/Swiss-Prot
MGC_CLONE MGC:93657 IMAGE-MGC_LOAD
NCBI Gene 25748 ENTREZGENE
PANTHER 5-AMINOLEVULINATE SYNTHASE, ERYTHROID-SPECIFIC, MITOCHONDRIAL UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Pfam Aminotran_1_2 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  Preseq_ALAS UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PhenoGen Alas2 PhenoGen
PROSITE AA_TRANSFER_CLASS_2 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
RatGTEx ENSRNOG00000000167 RatGTEx
Superfamily-SCOP SSF53383 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
UniProt A6KL69_RAT UniProtKB/TrEMBL
  A6KL71_RAT UniProtKB/TrEMBL
  A6KL73_RAT UniProtKB/TrEMBL
  A6KL74_RAT UniProtKB/TrEMBL
  F1LVW9 ENTREZGENE, UniProtKB/TrEMBL
  HEM0_RAT UniProtKB/Swiss-Prot, ENTREZGENE
  Q63895 ENTREZGENE
  Q642C1 ENTREZGENE, UniProtKB/TrEMBL
UniProt Secondary Q63895 UniProtKB/Swiss-Prot


Nomenclature History
Date Current Symbol Current Name Previous Symbol Previous Name Description Reference Status
2014-12-01 Alas2  5'-aminolevulinate synthase 2  Alas2  aminolevulinate, delta-, synthase 2  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2013-04-12 Alas2  aminolevulinate, delta-, synthase 2  LOC100363476  aminolevulinic acid synthase 2, erythroid-like  Data merged from RGD:2322969 737654 PROVISIONAL
2010-05-06 LOC100363476  aminolevulinic acid synthase 2, erythroid-like      Symbol and Name status set to provisional 70820 PROVISIONAL
2008-09-26 Alas2  aminolevulinate, delta-, synthase 2  Alas2  aminolevulinic acid synthase 2, erythroid  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2008-02-15 Alas2  aminolevulinic acid synthase 2, erythroid  Alas2  aminolevulinic acid synthase 2  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2002-11-06 Alas2  aminolevulinic acid synthase 2    Aminolevulinate synthase 2, delta  Name updated 625702 APPROVED
2002-06-10 Alas2  Aminolevulinate synthase 2, delta      Symbol and Name status set to approved 70586 APPROVED

RGD Curation Notes
Note Type Note Reference
gene_function catalyzes the conversion of glycine and succinyl-CoA to 5-aminolevulinate 632181
gene_other erythroid specific form of aminolevulinic acid synthase is distinct from Alas1, the non-specific form of this enzyme 632181
gene_protein 64.84 kDa protein precursor 632181