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Protein

Delta-aminolevulinic acid dehydratase

Gene

Alad

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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+By similarityNote: 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.By similarity

<p>This subsection of the ‘Function’ 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 (By similarity).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'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)
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 ‘Function’ 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; catalyticBy similarity1
Metal bindingi124Zinc 1; catalyticBy similarity1
Metal bindingi131Zinc 2By similarity1
Metal bindingi132Zinc 1; catalyticBy similarity1
<p>This subsection of the ‘Function’ 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 substrateBy similarity1
<p>This subsection of the ‘Function’ 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 1By similarity1
Binding sitei221Substrate 1By similarity1
Metal bindingi223Zinc 2By similarity1
Active sitei252Schiff-base intermediate with substrateBy similarity1
Binding sitei279Substrate 2By similarity1
Binding sitei318Substrate 2By similarity1

<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

  • identical protein binding Source: MGI
  • porphobilinogen synthase activity Source: MGI
  • proteasome core complex binding Source: MGI
  • 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

Reactome - a knowledgebase of biological pathways and processes

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

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

More...
UniPathwayi
UPA00251;UER00318

<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_and_taxonomy_section">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_and_taxonomy_section">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
Synonyms:Lv
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 4

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:96853 Alad

<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; Source: COMPARTMENTS

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001405281 – 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-succinyllysineCombined sources1
Modified residuei215PhosphoserineCombined sources1
Modified residuei252N6-succinyllysineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P10518

MaxQB - The MaxQuant DataBase

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MaxQBi
P10518

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

More...
PaxDbi
P10518

PeptideAtlas

More...
PeptideAtlasi
P10518

PRoteomics IDEntifications database

More...
PRIDEi
P10518

2D gel databases

REPRODUCTION-2DPAGE

More...
REPRODUCTION-2DPAGEi
P10518

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

More...
SWISS-2DPAGEi
P10518

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P10518

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

More...
PhosphoSitePlusi
P10518

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P10518

<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

More...
Bgeei
ENSMUSG00000028393 Expressed in 286 organ(s), highest expression level in liver

CleanEx database of gene expression profiles

More...
CleanExi
MM_ALAD

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P10518 MM

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homooctamer; active form. Homohexamer; low activity form (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
201229, 2 interactors

Protein interaction database and analysis system

More...
IntActi
P10518, 6 interactors

Molecular INTeraction database

More...
MINTi
P10518

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000030090

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P10518

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

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SMRi
P10518

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P10518

<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

More...
eggNOGi
KOG2794 Eukaryota
COG0113 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000006998

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000020323

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG001222

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P10518

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

More...
OrthoDBi
EOG091G0FMX

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P10518

TreeFam database of animal gene trees

More...
TreeFami
TF300665

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001731 ALAD
IPR030656 ALAD_AS
IPR013785 Aldolase_TIM

The PANTHER Classification System

More...
PANTHERi
PTHR11458 PTHR11458, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00490 ALAD, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001415 Porphbilin_synth, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00144 DALDHYDRTASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01004 ALAD, 1 hit

PROSITE; a protein domain and family database

More...
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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P10518-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHHQSVLHSG YFHPLLRSWQ TAASTVSASN LIYPIFVTDV PDDVQPIASL
60 70 80 90 100
PGVARYGVNQ LEEMLRPLVE AGLRCVLIFG VPSRVPKDEQ GSAADSEDSP
110 120 130 140 150
TIEAVRLLRK TFPSLLVACD VCLCPYTSHG HCGLLSENGA FLAEESRQRL
160 170 180 190 200
AEVALAYAKA GCQVVAPSDM MDGRVEAIKA ALLKHGLGNR VSVMSYSAKF
210 220 230 240 250
ASCFYGPFRD AAQSSPAFGD RRCYQLPPGA RGLALRAVAR DIQEGADMLM
260 270 280 290 300
VKPGLPYLDM VREVKDKHPE LPLAVYQVSG EFAMLWHGAQ AGAFDLRTAV
310 320 330
LETMTAFRRA GADIIITYFA PQLLKWLKEE
Length:330
Mass (Da):36,024
Last modified:July 1, 1989 - 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:i84052DC911C153EB
GO

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

More...
DDBJi
Links Updated
X13752 mRNA Translation: CAA32015.1
AK032908 mRNA Translation: BAC28080.1
AK167673 mRNA Translation: BAE39722.1
AK168119 mRNA Translation: BAE40090.1
AK168132 mRNA Translation: BAE40101.1
BC055930 mRNA Translation: AAH55930.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS18243.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S03187

NCBI Reference Sequences

More...
RefSeqi
NP_001263375.1, NM_001276446.1
NP_032551.3, NM_008525.4
XP_006537702.1, XM_006537639.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.6988

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000030090; ENSMUSP00000030090; ENSMUSG00000028393
ENSMUST00000107444; ENSMUSP00000103068; ENSMUSG00000028393

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
17025

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:17025

UCSC genome browser

More...
UCSCi
uc008tez.2 mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13752 mRNA Translation: CAA32015.1
AK032908 mRNA Translation: BAC28080.1
AK167673 mRNA Translation: BAE39722.1
AK168119 mRNA Translation: BAE40090.1
AK168132 mRNA Translation: BAE40101.1
BC055930 mRNA Translation: AAH55930.1
CCDSiCCDS18243.1
PIRiS03187
RefSeqiNP_001263375.1, NM_001276446.1
NP_032551.3, NM_008525.4
XP_006537702.1, XM_006537639.2
UniGeneiMm.6988

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2Z0IX-ray3.20A/B1-330[»]
2Z1BX-ray3.30A/B/C/D1-330[»]
ProteinModelPortaliP10518
SMRiP10518
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201229, 2 interactors
IntActiP10518, 6 interactors
MINTiP10518
STRINGi10090.ENSMUSP00000030090

PTM databases

iPTMnetiP10518
PhosphoSitePlusiP10518
SwissPalmiP10518

2D gel databases

REPRODUCTION-2DPAGEiP10518
SWISS-2DPAGEiP10518

Proteomic databases

EPDiP10518
MaxQBiP10518
PaxDbiP10518
PeptideAtlasiP10518
PRIDEiP10518

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030090; ENSMUSP00000030090; ENSMUSG00000028393
ENSMUST00000107444; ENSMUSP00000103068; ENSMUSG00000028393
GeneIDi17025
KEGGimmu:17025
UCSCiuc008tez.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
210
MGIiMGI:96853 Alad

Phylogenomic databases

eggNOGiKOG2794 Eukaryota
COG0113 LUCA
GeneTreeiENSGT00390000006998
HOGENOMiHOG000020323
HOVERGENiHBG001222
InParanoidiP10518
KOiK01698
OMAiYQMDYAN
OrthoDBiEOG091G0FMX
PhylomeDBiP10518
TreeFamiTF300665

Enzyme and pathway databases

UniPathwayi
UPA00251;UER00318

ReactomeiR-MMU-189451 Heme biosynthesis
R-MMU-6798695 Neutrophil degranulation

Miscellaneous databases

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

More...
ChiTaRSi
Alad mouse
EvolutionaryTraceiP10518

Protein Ontology

More...
PROi
PR:P10518

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000028393 Expressed in 286 organ(s), highest expression level in liver
CleanExiMM_ALAD
GenevisibleiP10518 MM

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

More...
ProtoNeti
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_MOUSE
<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: P10518
Secondary accession number(s): Q3THV6
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: December 5, 2018
This is version 159 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

<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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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