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ALAD aminolevulinate dehydratase [ Homo sapiens (human) ]

Gene ID: 210, updated on 7-Dec-2018

Summary

Official Symbol
ALADprovided by HGNC
Official Full Name
aminolevulinate dehydrataseprovided by HGNC
Primary source
HGNC:HGNC:395
See related
Ensembl:ENSG00000148218 MIM:125270
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
PBGS; ALADH
Summary
The ALAD enzyme is composed of 8 identical subunits and catalyzes the condensation of 2 molecules of delta-aminolevulinate to form porphobilinogen (a precursor of heme, cytochromes and other hemoproteins). ALAD catalyzes the second step in the porphyrin and heme biosynthetic pathway; zinc is essential for enzymatic activity. ALAD enzymatic activity is inhibited by lead and a defect in the ALAD structural gene can cause increased sensitivity to lead poisoning and acute hepatic porphyria. Alternative splicing of this gene results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Dec 2015]
Expression
Ubiquitous expression in adrenal (RPKM 60.0), liver (RPKM 56.7) and 25 other tissues See more
Orthologs

Genomic context

See ALAD in Genome Data Viewer
Location:
9q32
Exon count:
15
Annotation release Status Assembly Chr Location
109 current GRCh38.p12 (GCF_000001405.38) 9 NC_000009.12 (113386312..113401338, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 9 NC_000009.11 (116148592..116163618, complement)

Chromosome 9 - NC_000009.12Genomic Context describing neighboring genes Neighboring gene B-box and SPRY domain containing Neighboring gene haloacid dehalogenase like hydrolase domain containing 3 Neighboring gene chromosome 9 open reading frame 43 Neighboring gene DNA polymerase epsilon 3, accessory subunit Neighboring gene regulator of G protein signaling 3

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

Pathways from BioSystems

  • Heme Biosynthesis, organism-specific biosystem (from WikiPathways)
    Heme Biosynthesis, organism-specific biosystemThe enzymatic process that produces heme is properly called porphyrin synthesis, as all the intermediates are tetrapyrroles that are chemically classified are porphyrins. The process is highly conser...
  • Heme biosynthesis, organism-specific biosystem (from REACTOME)
    Heme biosynthesis, organism-specific biosystemEight enzymes are involved in heme biosynthesis, four each in the mitochondria and the cytosol. The process starts in the mitochondria with the condensation of succinyl CoA (from the TCA cycle) and g...
  • Immune System, organism-specific biosystem (from REACTOME)
    Immune System, organism-specific biosystemHumans are exposed to millions of potential pathogens daily, through contact, ingestion, and inhalation. Our ability to avoid infection depends on the adaptive immune system and during the first crit...
  • Innate Immune System, organism-specific biosystem (from REACTOME)
    Innate Immune System, organism-specific biosystemInnate immunity encompases the nonspecific part of immunity tha are part of an individual's natural biologic makeup
  • Metabolic pathways, organism-specific biosystem (from KEGG)
    Metabolic pathways, organism-specific biosystem
    Metabolic pathways
  • Metabolism, organism-specific biosystem (from REACTOME)
    Metabolism, organism-specific biosystemMetabolic processes in human cells generate energy through the oxidation of molecules consumed in the diet and mediate the synthesis of diverse essential molecules not taken in the diet as well as th...
  • Metabolism of porphyrins, organism-specific biosystem (from REACTOME)
    Metabolism of porphyrins, organism-specific biosystemPorphyrins are heterocyclic macrocycles, consisting of four pyrrole subunits (tetrapyrrole) linked by four methine (=CH-) bridges. The extensive conjugated porphyrin macrocycle is chromatic and the n...
  • Neutrophil degranulation, organism-specific biosystem (from REACTOME)
    Neutrophil degranulation, organism-specific biosystemNeutrophils are the most abundant leukocytes (white blood cells), indispensable in defending the body against invading microorganisms. In response to infection, neutrophils leave the circulation and ...
  • Porphyrin and chlorophyll metabolism, organism-specific biosystem (from KEGG)
    Porphyrin and chlorophyll metabolism, organism-specific biosystem
    Porphyrin and chlorophyll metabolism
  • Porphyrin and chlorophyll metabolism, conserved biosystem (from KEGG)
    Porphyrin and chlorophyll metabolism, conserved biosystem
    Porphyrin and chlorophyll metabolism
  • heme biosynthesis, organism-specific biosystem (from BIOCYC)
    heme biosynthesis, organism-specific biosystemGeneral Background Heme (protoheme, heme b) is an iron-containing porphyrin, that belongs to the family of macrocyclic tetrapyrroles. It has a diverse range of biological functions as a prosthetic g...
  • superpathway of heme biosynthesis from glycine, conserved biosystem (from BIOCYC)
    superpathway of heme biosynthesis from glycine, conserved biosystemGeneral Background Heme (protoheme, heme b) is an iron-containing prosthetic group found in many essential proteins including cytochromes and heme-containing globins. In addition to its role in oxi...
  • tetrapyrrole biosynthesis, organism-specific biosystem (from BIOCYC)
    tetrapyrrole biosynthesis, organism-specific biosystemBackground Tetrapyrroles play a role in a variety of biological processes such as photosynthesis and respiration. They are large macrocyclic compounds derived from a common biosynthetic pathway . Te...
  • tetrapyrrole biosynthesis II (from glycine), conserved biosystem (from BIOCYC)
    tetrapyrrole biosynthesis II (from glycine), conserved biosystemTetrapyrrole compounds include four rings of the pyrrole type, generally linked together by single-atom bridges between the alpha positions of the five-membered pyrrole rings. Tetrapyrroles usually f...

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Clone Names

  • MGC5057

Gene Ontology Provided by GOA

Function Evidence Code Pubs
catalytic activity TAS
Traceable Author Statement
more info
PubMed 
identical protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
porphobilinogen synthase activity IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
porphobilinogen synthase activity IDA
Inferred from Direct Assay
more info
PubMed 
porphobilinogen synthase activity TAS
Traceable Author Statement
more info
 
proteasome core complex binding IEA
Inferred from Electronic Annotation
more info
 
zinc ion binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
zinc ion binding IDA
Inferred from Direct Assay
more info
PubMed 
Process Evidence Code Pubs
cellular response to interleukin-4 IEA
Inferred from Electronic Annotation
more info
 
cellular response to lead ion IEA
Inferred from Electronic Annotation
more info
 
heme biosynthetic process IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
heme biosynthetic process IDA
Inferred from Direct Assay
more info
PubMed 
heme biosynthetic process TAS
Traceable Author Statement
more info
 
negative regulation of proteasomal protein catabolic process IDA
Inferred from Direct Assay
more info
PubMed 
neutrophil degranulation TAS
Traceable Author Statement
more info
 
protein homooligomerization IPI
Inferred from Physical Interaction
more info
PubMed 
protoporphyrinogen IX biosynthetic process IEA
Inferred from Electronic Annotation
more info
 
response to activity IEA
Inferred from Electronic Annotation
more info
 
response to aluminum ion IEA
Inferred from Electronic Annotation
more info
 
response to amino acid IEA
Inferred from Electronic Annotation
more info
 
response to arsenic-containing substance IEA
Inferred from Electronic Annotation
more info
 
response to cadmium ion IEA
Inferred from Electronic Annotation
more info
 
response to cobalt ion IEA
Inferred from Electronic Annotation
more info
 
response to ethanol IEA
Inferred from Electronic Annotation
more info
 
response to fatty acid IEA
Inferred from Electronic Annotation
more info
 
response to glucocorticoid IEA
Inferred from Electronic Annotation
more info
 
response to herbicide IEA
Inferred from Electronic Annotation
more info
 
response to hypoxia IEA
Inferred from Electronic Annotation
more info
 
response to ionizing radiation IEA
Inferred from Electronic Annotation
more info
 
response to iron ion IEA
Inferred from Electronic Annotation
more info
 
response to lipopolysaccharide IEA
Inferred from Electronic Annotation
more info
 
response to mercury ion IEA
Inferred from Electronic Annotation
more info
 
response to methylmercury IEA
Inferred from Electronic Annotation
more info
 
response to oxidative stress IEA
Inferred from Electronic Annotation
more info
 
response to platinum ion IEA
Inferred from Electronic Annotation
more info
 
response to selenium ion IEA
Inferred from Electronic Annotation
more info
 
response to vitamin B1 IEA
Inferred from Electronic Annotation
more info
 
response to vitamin E IEA
Inferred from Electronic Annotation
more info
 
response to zinc ion IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
cytosol IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
cytosol TAS
Traceable Author Statement
more info
 
extracellular exosome HDA PubMed 
extracellular region TAS
Traceable Author Statement
more info
 
ficolin-1-rich granule lumen TAS
Traceable Author Statement
more info
 
nucleus HDA PubMed 
secretory granule lumen TAS
Traceable Author Statement
more info
 

General protein information

Preferred Names
delta-aminolevulinic acid dehydratase
Names
aminolevulinate, delta-, dehydratase
porphobilinogen synthase
testicular tissue protein Li 95
NP_000022.3
NP_001003945.1
NP_001304674.1
XP_011516666.1
XP_024303217.1

NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

  1. NG_008716.1 RefSeqGene

    Range
    5001..20027
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_000031.6NP_000022.3  delta-aminolevulinic acid dehydratase isoform b

    See identical proteins and their annotated locations for NP_000022.3

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) lacks a segment of the coding region and initiates translation from an alternate start codon, compared to variant 1. The resulting isoform (b) has a distinct N-terminus, compared to isoform a.
    Source sequence(s)
    AK131490, AK290490, BC000977, BU625796, DA805310
    Consensus CDS
    CCDS6794.2
    UniProtKB/Swiss-Prot
    P13716
    UniProtKB/TrEMBL
    A0A140VJL9, Q6ZMU0
    Related
    ENSP00000386284.3, ENST00000409155.7
    Conserved Domains (1) summary
    cd04824
    Location:8327
    eu_ALAD_PBGS_cysteine_rich; Porphobilinogen synthase (PBGS), which is also called delta-aminolevulinic acid dehydratase (ALAD), catalyzes the condensation of two 5-aminolevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (PBG), which is the second step in the ...
  2. NM_001003945.2NP_001003945.1  delta-aminolevulinic acid dehydratase isoform a

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) represents the longest transcript, and encodes the longest isoform (a).
    Source sequence(s)
    AK131490, AK290490, BU625796, DA412142
    UniProtKB/Swiss-Prot
    P13716
    UniProtKB/TrEMBL
    Q6ZMU0
    Conserved Domains (1) summary
    cd04824
    Location:68356
    eu_ALAD_PBGS_cysteine_rich; Porphobilinogen synthase (PBGS), which is also called delta-aminolevulinic acid dehydratase (ALAD), catalyzes the condensation of two 5-aminolevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (PBG), which is the second step in the ...
  3. NM_001317745.1NP_001304674.1  delta-aminolevulinic acid dehydratase isoform c

    Status: REVIEWED

    Description
    Transcript Variant: This variant (3) differs in the 5' UTR, lacks an alternate in-frame exon in the 5' coding region and initiates translation from an alternate start codon, compared to variant 1. The resulting isoform (c) has a distinct N-terminus compared to isoform a.
    Source sequence(s)
    AK131490, AK295945, BU625796
    UniProtKB/TrEMBL
    B7Z3I9, Q6ZMU0
    Conserved Domains (1) summary
    cd04824
    Location:17319
    eu_ALAD_PBGS_cysteine_rich; Porphobilinogen synthase (PBGS), which is also called delta-aminolevulinic acid dehydratase (ALAD), catalyzes the condensation of two 5-aminolevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (PBG), which is the second step in the ...

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p12 Primary Assembly

Genomic

  1. NC_000009.12 Reference GRCh38.p12 Primary Assembly

    Range
    113386312..113401338 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_011518364.2XP_011516666.1  delta-aminolevulinic acid dehydratase isoform X2

    See identical proteins and their annotated locations for XP_011516666.1

    UniProtKB/Swiss-Prot
    P13716
    UniProtKB/TrEMBL
    A0A024R877
    Conserved Domains (1) summary
    cd04824
    Location:17336
    eu_ALAD_PBGS_cysteine_rich; Porphobilinogen synthase (PBGS), which is also called delta-aminolevulinic acid dehydratase (ALAD), catalyzes the condensation of two 5-aminolevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (PBG), which is the second step in the ...
  2. XM_024447449.1XP_024303217.1  delta-aminolevulinic acid dehydratase isoform X1

    Conserved Domains (1) summary
    cd04824
    Location:68356
    eu_ALAD_PBGS_cysteine_rich; Porphobilinogen synthase (PBGS), which is also called delta-aminolevulinic acid dehydratase (ALAD), catalyzes the condensation of two 5-aminolevulinic acid (ALA) molecules to form the pyrrole porphobilinogen (PBG), which is the second step in the ...

RNA

  1. XR_002956764.1 RNA Sequence

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