ALAS1
entrez
211
canonical
uniprot
P13196
canonical
ensembl
ENSG00000023330
resolver
ensp
ENSP00000309259
resolver
ensp
ENSP00000417719
resolver
ensp
ENSP00000418779
resolver
ensp
ENSP00000612159
resolver
genesymbol
ALAS1
resolver
genesymbol_syn
ALAS3
resolver
genesymbol_syn
ALASH
resolver
hgnc
HGNC:396
resolver
uniprot
A0A024R353
resolver
uniprot
B4DVA0
resolver
uniprot
Q5JAM2
resolver
uniprot_entry
B4DVA0_HUMAN
resolver
uniprot_entry
HEM1_HUMAN
resolver
uniprot_entry
Q5JAM2_HUMAN
resolver
uniprot_sec
A0A024R353
resolver
activity_regulation
ACTIVITY REGULATION: Activity increases about 2-fold over 72 hours of hypoxia compared with normoxia (PubMed:16234850). Activity increases in the presence of phenobarbital, chenodeoxycholic and NR1H4/FXR-specific agonist GW4064 (PubMed:17975826). {ECO:0000269|PubMed:16234850, ECO:0000269|PubMed:17975826}.
uniprot
proteins
amino_acid_sequence
MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKETPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGSSVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPERVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLITKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLELKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA
uniprot
proteins
ec_number
2.3.1.37
uniprot
proteins
function
FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products. {ECO:0000269|PubMed:16234850, ECO:0000269|PubMed:17975826}.
uniprot
proteins
mass_dalton
70581
uniprot
proteins
mutagenesis
MUTAGEN 576; /note="P->A: Loss of interaction with VHL."; /evidence="ECO:0000269|PubMed:16234850
uniprot
proteins
pathway_participation
PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1.
uniprot
proteins
post_translational_modification
PTM: In normoxia, is hydroxylated at Pro-576, promoting interaction with VHL, initiating ubiquitination and subsequent degradation via the proteasome. {ECO:0000269|PubMed:16234850}.; PTM: Ubiquitinated; in normoxia following hydroxylation and interaction with VHL, leading to its subsequent degradation via the proteasome. {ECO:0000269|PubMed:16234850}.
uniprot
proteins
protein_family
Class-II pyridoxal-phosphate-dependent aminotransferase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16234850
uniprot
proteins
pubmed
17975826
uniprot
proteins
pubmed
2263504
uniprot
proteins
pubmed
3671094
uniprot
proteins
sequence_length
640
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22557}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22557}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P22557}.
uniprot
proteins