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Entry version 211 (22 Apr 2020)
Sequence version 1 (01 Jan 1990)
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Protein

Delta-aminolevulinic acid dehydratase

Gene

ALAD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+1 PublicationNote: Binds 8 zinc ions per octamer. Requires four zinc ions per octamer for full catalytic activity. Can bind up to 2 zinc ions per subunit.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Can alternate between a fully active homooctamer and a low-activity homohexamer. A bound magnesium ion may promote the assembly of the fully active homooctamer. The magnesium-binding site is absent in the low-activity homohexamer. Inhibited by compounds that favor the hexameric state. Inhibited by divalent lead ions. The lead ions partially displace the zinc cofactor.3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.09 mM for 5-aminolevulinate at pH 71 Publication
  1. Vmax=43 µmol/h/mg enzyme at pH 71 Publication

pH dependencei

Optimum pH is 6.8-7.3.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Delta-aminolevulinic acid dehydratase (ALAD)
  2. Porphobilinogen deaminase (HMBS)
  3. Uroporphyrinogen-III synthase (UROS)
  4. Uroporphyrinogen decarboxylase (UROD), Uroporphyrinogen decarboxylase (UROD), Uroporphyrinogen decarboxylase (UROD)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coproporphyrinogen-III from 5-aminolevulinate, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi122Zinc 1; catalytic1
Metal bindingi124Zinc 1; catalytic1
Metal bindingi131Zinc 21
Metal bindingi132Zinc 1; catalytic1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei199Schiff-base intermediate with substrate1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei209Substrate 11
Binding sitei221Substrate 11
Metal bindingi223Zinc 21
Active sitei252Schiff-base intermediate with substrate1 Publication1
Binding sitei279Substrate 21
Binding sitei318Substrate 21

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • catalytic activity Source: ProtInc
  • identical protein binding Source: UniProtKB
  • porphobilinogen synthase activity Source: UniProtKB
  • proteasome core complex binding Source: Ensembl
  • zinc ion binding Source: UniProtKB

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAllosteric enzyme, Lyase
Biological processHeme biosynthesis, Porphyrin biosynthesis
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS07501-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.1.24 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-189451 Heme biosynthesis
R-HSA-6798695 Neutrophil degranulation

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00251;UER00318

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P13716 Curated

MoonProt database of moonlighting proteins

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MoonProti
P13716

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Delta-aminolevulinic acid dehydratase (EC:4.2.1.24)
Short name:
ALADH
Alternative name(s):
Porphobilinogen synthase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ALAD
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:395 ALAD

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
125270 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P13716

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Acute hepatic porphyria (AHEPP)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. AHP is characterized by attacks of gastrointestinal disturbances, abdominal colic, paralyses and peripheral neuropathy. Most attacks are precipitated by drugs, alcohol, caloric deprivation, infections, or endocrine factors.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_003634133G → R in AHEPP; mixture of about 50% hexamer and 50% octamer; about 10% residual activity. 2 PublicationsCorresponds to variant dbSNP:rs121912980EnsemblClinVar.1
Natural variantiVAR_020974153V → M in AHEPP; about 95% octamer; about 40% residual activity. 2 Publications1
Natural variantiVAR_003635240R → W in AHEPP; mixture of about 80% hexamer and 20% octamer; about 4% residual activity. 3 PublicationsCorresponds to variant dbSNP:rs121912982EnsemblClinVar.1
Natural variantiVAR_003636274A → T in AHEPP; mixture of about 14% hexamer and 86% octamer; about 20% enzyme residual activity. 3 PublicationsCorresponds to variant dbSNP:rs121912983EnsemblClinVar.1
Natural variantiVAR_003637275V → M in AHEPP; mainly octamer; reduced activity. 2 PublicationsCorresponds to variant dbSNP:rs121912981EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi122C → A: Reduces enzyme activity about 1000000-fold; when associated with A-124 and A-132. 1 Publication1
Mutagenesisi124C → A: Reduces enzyme activity about 1000000-fold; when associated with A-122 and A-132. 1 Publication1
Mutagenesisi131H → A: No effect on catalytic activity; when associated with A-223. 1 Publication1
Mutagenesisi132C → A: Reduces enzyme activity about 1000000-fold; when associated with A-122 and A-124. 1 Publication1
Mutagenesisi223C → A: No effect on catalytic activity; when associated with A-131. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
210

MalaCards human disease database

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MalaCardsi
ALAD
MIMi612740 phenotype

Open Targets

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OpenTargetsi
ENSG00000148218

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
100924 Porphyria due to ALA dehydratase deficiency

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24687

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P13716 Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3126

Drug and drug target database

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DrugBanki
DB02878 3-(2-Aminoethyl)-4-(Aminomethyl)Heptanedioic Acid
DB04560 4,7-Dioxosebacic Acid
DB02260 4-Oxosebacic Acid
DB04781 5-hydroxyvaleric acid
DB00855 Aminolevulinic acid
DB02068 Delta-Amino Valeric Acid
DB02239 Laevulinic Acid
DB02272 Porphobilinogen

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ALAD

Domain mapping of disease mutations (DMDM)

More...
DMDMi
122833

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001405261 – 330Delta-aminolevulinic acid dehydrataseAdd BLAST330

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei199N6-succinyllysineBy similarity1
Modified residuei215PhosphoserineBy similarity1
Modified residuei252N6-succinyllysineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P13716

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P13716

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P13716

MaxQB - The MaxQuant DataBase

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MaxQBi
P13716

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P13716

PeptideAtlas

More...
PeptideAtlasi
P13716

PRoteomics IDEntifications database

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PRIDEi
P13716

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
52973 [P13716-1]
52974 [P13716-2]

2D gel databases

USC-OGP 2-DE database

More...
OGPi
P13716

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
P13716

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P13716

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P13716

MetOSite database of methionine sulfoxide sites

More...
MetOSitei
P13716

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P13716

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P13716

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000148218 Expressed in right adrenal gland and 221 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P13716 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P13716 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000148218 Tissue enhanced (liver)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homooctamer; active form. Homohexamer; low activity form.

3 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
106712, 31 interactors

Protein interaction database and analysis system

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IntActi
P13716, 7 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000386284

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P13716

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P13716 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1330
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P13716

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P13716

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the ALAD family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2794 Eukaryota
COG0113 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000006998

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_035731_0_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P13716

KEGG Orthology (KO)

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KOi
K01698

Identification of Orthologs from Complete Genome Data

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OMAi
YQMDYAN

Database of Orthologous Groups

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OrthoDBi
918089at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P13716

TreeFam database of animal gene trees

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TreeFami
TF300665

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.20.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001731 ALAD
IPR030656 ALAD_AS
IPR013785 Aldolase_TIM

The PANTHER Classification System

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PANTHERi
PTHR11458 PTHR11458, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00490 ALAD, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF001415 Porphbilin_synth, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00144 DALDHYDRTASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01004 ALAD, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00169 D_ALA_DEHYDRATASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P13716-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MQPQSVLHSG YFHPLLRAWQ TATTTLNASN LIYPIFVTDV PDDIQPITSL
60 70 80 90 100
PGVARYGVKR LEEMLRPLVE EGLRCVLIFG VPSRVPKDER GSAADSEESP
110 120 130 140 150
AIEAIHLLRK TFPNLLVACD VCLCPYTSHG HCGLLSENGA FRAEESRQRL
160 170 180 190 200
AEVALAYAKA GCQVVAPSDM MDGRVEAIKE ALMAHGLGNR VSVMSYSAKF
210 220 230 240 250
ASCFYGPFRD AAKSSPAFGD RRCYQLPPGA RGLALRAVDR DVREGADMLM
260 270 280 290 300
VKPGMPYLDI VREVKDKHPD LPLAVYHVSG EFAMLWHGAQ AGAFDLKAAV
310 320 330
LEAMTAFRRA GADIIITYYT PQLLQWLKEE
Length:330
Mass (Da):36,295
Last modified:January 1, 1990 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE005F3055F6D9403
GO
Isoform 2 (identifier: P13716-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MQPQSVLHSG...SNLIYPIFVT → MPPTSSTPSL...QSISHPRSCR

Show »
Length:359
Mass (Da):39,034
Checksum:i4AD5F3B2570ACD81
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B7ZBK6B7ZBK6_HUMAN
Delta-aminolevulinic acid dehydrata...
ALAD
120Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B7ZBK7B7ZBK7_HUMAN
Delta-aminolevulinic acid dehydrata...
ALAD
59Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B7ZBK8B7ZBK8_HUMAN
Delta-aminolevulinic acid dehydrata...
ALAD
14Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH00977 differs from that shown. Reason: Erroneous initiation.Curated

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Genetic variation in ALAD influences susceptibility to lead poisoning in individuals exposed to high amount of environmental lead. There are two common alleles: allele ALAD*1 and allele ALAD*2 resulting in 3 isozymes: ALAD 1-1, ALAD 1-2, and ALAD 2-2. Individuals with ALAD 1-2 or ALAD 2-2 isozymes have levels of blood lead higher than those in individuals with ALAD 1-1 isozyme. The sequence shown corresponds to allele ALAD*1.1 Publication2 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02097312F → L in an asymptomatic patient with ALAD deficiency; also found in a hereditary coproporphyria patient carrying the R-279 mutation in CPOX; hexamer with almost no residual activity. 3 PublicationsCorresponds to variant dbSNP:rs121912984EnsemblClinVar.1
Natural variantiVAR_00363359K → N Common polymorphism; allele ALAD*2; ALAD*2 heterozygous or homozygous carriers have significantly higher blood lead levels than ALAD*1 homozygotes when exposed to environmental lead; fully active octamer. 5 PublicationsCorresponds to variant dbSNP:rs1800435EnsemblClinVar.1
Natural variantiVAR_003634133G → R in AHEPP; mixture of about 50% hexamer and 50% octamer; about 10% residual activity. 2 PublicationsCorresponds to variant dbSNP:rs121912980EnsemblClinVar.1
Natural variantiVAR_020974153V → M in AHEPP; about 95% octamer; about 40% residual activity. 2 Publications1
Natural variantiVAR_003635240R → W in AHEPP; mixture of about 80% hexamer and 20% octamer; about 4% residual activity. 3 PublicationsCorresponds to variant dbSNP:rs121912982EnsemblClinVar.1
Natural variantiVAR_003636274A → T in AHEPP; mixture of about 14% hexamer and 86% octamer; about 20% enzyme residual activity. 3 PublicationsCorresponds to variant dbSNP:rs121912983EnsemblClinVar.1
Natural variantiVAR_003637275V → M in AHEPP; mainly octamer; reduced activity. 2 PublicationsCorresponds to variant dbSNP:rs121912981EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0378661 – 38MQPQS…PIFVT → MPPTSSTPSLSRPGLGQAGK PDTGSHPPPTISTSIFLSCF PTIPLSRPRTTGPSHSYQSI SHPRSCR in isoform 2. 1 PublicationAdd BLAST38

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M13928 mRNA Translation: AAA51687.1
X64467 Genomic DNA Translation: CAA45796.1
S99468 mRNA Translation: AAC60581.1
S99471 mRNA Translation: AAC60582.1
AK290490 mRNA Translation: BAF83179.1
AK312552 mRNA Translation: BAG35449.1
AY319481 Genomic DNA Translation: AAP72012.1
AL137066 Genomic DNA No translation available.
BC000977 mRNA Translation: AAH00977.3 Different initiation.

The Consensus CDS (CCDS) project

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CCDSi
CCDS6794.2 [P13716-1]

Protein sequence database of the Protein Information Resource

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PIRi
A26478

NCBI Reference Sequences

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RefSeqi
NP_000022.3, NM_000031.5 [P13716-1]
NP_001003945.1, NM_001003945.2 [P13716-2]
XP_011516666.1, XM_011518364.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000409155; ENSP00000386284; ENSG00000148218 [P13716-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
210

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:210

UCSC genome browser

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UCSCi
uc011lxf.3 human [P13716-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13928 mRNA Translation: AAA51687.1
X64467 Genomic DNA Translation: CAA45796.1
S99468 mRNA Translation: AAC60581.1
S99471 mRNA Translation: AAC60582.1
AK290490 mRNA Translation: BAF83179.1
AK312552 mRNA Translation: BAG35449.1
AY319481 Genomic DNA Translation: AAP72012.1
AL137066 Genomic DNA No translation available.
BC000977 mRNA Translation: AAH00977.3 Different initiation.
CCDSiCCDS6794.2 [P13716-1]
PIRiA26478
RefSeqiNP_000022.3, NM_000031.5 [P13716-1]
NP_001003945.1, NM_001003945.2 [P13716-2]
XP_011516666.1, XM_011518364.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1E51X-ray2.83A/B1-330[»]
1PV8X-ray2.20A/B1-330[»]
5HMSX-ray2.80A/B1-330[»]
5HNRX-ray2.83A/B1-330[»]
SMRiP13716
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi106712, 31 interactors
IntActiP13716, 7 interactors
STRINGi9606.ENSP00000386284

Chemistry databases

BindingDBiP13716
ChEMBLiCHEMBL3126
DrugBankiDB02878 3-(2-Aminoethyl)-4-(Aminomethyl)Heptanedioic Acid
DB04560 4,7-Dioxosebacic Acid
DB02260 4-Oxosebacic Acid
DB04781 5-hydroxyvaleric acid
DB00855 Aminolevulinic acid
DB02068 Delta-Amino Valeric Acid
DB02239 Laevulinic Acid
DB02272 Porphobilinogen

Protein family/group databases

MoonDBiP13716 Curated
MoonProtiP13716

PTM databases

iPTMnetiP13716
MetOSiteiP13716
PhosphoSitePlusiP13716
SwissPalmiP13716

Polymorphism and mutation databases

BioMutaiALAD
DMDMi122833

2D gel databases

OGPiP13716
REPRODUCTION-2DPAGEiP13716
SWISS-2DPAGEiP13716

Proteomic databases

EPDiP13716
jPOSTiP13716
MassIVEiP13716
MaxQBiP13716
PaxDbiP13716
PeptideAtlasiP13716
PRIDEiP13716
ProteomicsDBi52973 [P13716-1]
52974 [P13716-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
15306 228 antibodies

Genome annotation databases

EnsembliENST00000409155; ENSP00000386284; ENSG00000148218 [P13716-1]
GeneIDi210
KEGGihsa:210
UCSCiuc011lxf.3 human [P13716-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
210
DisGeNETi210

GeneCards: human genes, protein and diseases

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GeneCardsi
ALAD
HGNCiHGNC:395 ALAD
HPAiENSG00000148218 Tissue enhanced (liver)
MalaCardsiALAD
MIMi125270 gene
612740 phenotype
neXtProtiNX_P13716
OpenTargetsiENSG00000148218
Orphaneti100924 Porphyria due to ALA dehydratase deficiency
PharmGKBiPA24687

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2794 Eukaryota
COG0113 LUCA
GeneTreeiENSGT00390000006998
HOGENOMiCLU_035731_0_1_1
InParanoidiP13716
KOiK01698
OMAiYQMDYAN
OrthoDBi918089at2759
PhylomeDBiP13716
TreeFamiTF300665

Enzyme and pathway databases

UniPathwayiUPA00251;UER00318
BioCyciMetaCyc:HS07501-MONOMER
BRENDAi4.2.1.24 2681
ReactomeiR-HSA-189451 Heme biosynthesis
R-HSA-6798695 Neutrophil degranulation

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
ALAD human
EvolutionaryTraceiP13716

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
ALAD

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
210
PharosiP13716 Tbio

Protein Ontology

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PROi
PR:P13716
RNActiP13716 protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000148218 Expressed in right adrenal gland and 221 other tissues
ExpressionAtlasiP13716 baseline and differential
GenevisibleiP13716 HS

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR001731 ALAD
IPR030656 ALAD_AS
IPR013785 Aldolase_TIM
PANTHERiPTHR11458 PTHR11458, 1 hit
PfamiView protein in Pfam
PF00490 ALAD, 1 hit
PIRSFiPIRSF001415 Porphbilin_synth, 1 hit
PRINTSiPR00144 DALDHYDRTASE
SMARTiView protein in SMART
SM01004 ALAD, 1 hit
PROSITEiView protein in PROSITE
PS00169 D_ALA_DEHYDRATASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHEM2_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P13716
Secondary accession number(s): A8K375
, B2R6F2, Q16870, Q16871, Q9BVQ9
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 22, 2020
This is version 211 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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