Type | Description |
---|---|
Definition | aminolevulinic acid synthase 2, erythroid |
Date | Results | Publications |
---|---|---|
2018-10-27 12:06:00 | we used bioinformatics and computational biology tools to evaluate the role(s) of the C-terminal tail dynamics in the structure and conformational dynamics of the murine ALAS2 homodimer active site loop. | 29958424 |
2018-10-20 11:02:00 | Data indicate that the 5-aminolevulinate synthase (mALAS2) active site loop harboring the simultaneous seven amino acid mutations was less flexible than the wild type loop. | 27928941 |
2016-06-28 11:18:00 | We propose that the N-terminal truncation offers a cell-specific ALAS2 regulatory mechanism without hindering heme synthesis | 26854603 |
2016-05-14 10:45:00 | N150F ALAS variant catalyzes the forward reaction at a mere 1.2-fold faster rate than that of the reverse reaction. | 26511319 |
2015-01-10 12:31:00 | Light treatments revealed that ALAS2 expression results in an increase in cell death in comparison to aminolevulinic acid (ALA) treatment producing a similar amount of protoprophyrin IX. | 24718052 |
Type | IDs |
---|---|
Synonymous | ALAS, ALAS-E, ALASE, Alas-2 |
Gene |
UniProtKB-ID:
HEM0_MOUSE,
A2AFM1_MOUSE,
A2AFM0_MOUSE
UniprotKB:
P08680,
A2AFM1,
A2AFM0
UniParc:
UPI0000EE05A6,
UPI0000004121
EMBL:
BC150870,
AK077610,
M15268,
M63244,
AL808140,
AL672150,
AK002642
Ensembl:
ENSMUSG00000025270
KO:
mmu:11656
|
Nucleutide sequences |
EMBL-CDS:
AAA91866.1,
BAC36898.1,
AAA37207.1,
BAB22254.1,
AAI50871.1
Ensembl_TRS:
ENSMUST00000066337,
ENSMUST00000112715
|
Protein sequencees |
Ensembl_PRO:
ENSMUSP00000066040,
ENSMUSP00000108335
RefSeq:
NP_001095916.1,
NP_033783.1,
XP_030107059.1
|
Others |
UniRef100:
UniRef100_P08680,
UniRef100_A2AFM1
UniRef90:
UniRef90_P08680
UniRef50:
UniRef50_P22557
UniGene:
Mm.302724
CCDS:
CCDS41173.1
|
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Refseq |
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