Domains within Homo sapiens protein HEM2_HUMAN (P13716)

Delta-aminolevulinic acid dehydratase

Alternative representations: 1 /

Protein length330 aa
Source databaseUniProt
Identifiers HEM2_HUMAN, P13716, ENSP00000386284.3, ENSP00000386284, A8K375, B2R6F2, Q16870, Q16871, Q9BVQ9, A0A024R877_HUMAN, A0A024R877, B7ZBK6_HUMAN, B7ZBK6, B7ZBK7_HUMAN, B7ZBK7, A0A140VJL9_HUMAN, A0A140VJL9
Source gene ENSG00000148218
Alternative splicing HEM2_HUMAN, ENSP00000392748.1, ENSP00000415737.1, ENSP00000398438.1

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

Predicted functional partners

HEM2_HUMAN is shown as ALAD in the network

Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.

The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for ALAD

Protein HEM2_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map00860Porphyrin metabolism iPath3
Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

KONameDescription
K01698hemB, ALADporphobilinogen synthase [EC:4.2.1.24] iPath3
Some of these orthologous groups are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

Post-translational modifications

PTM annotation is taken from PTMcode, a resource of known and predicted functional associations between protein post-translational modifications (PTMs). There are 12 PTMs annotated in this protein:

PTMCount
Phosphorylation4
Ubiquitination4
Nitrosylation3
Acetylation1

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein ALAD.

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 9606.ENSP00000386284 in eggNOG.

OGTaxonomic classDescription
LCOG0113All organisms (root)porphobilinogen synthase [EC:4.2.1.24],DNA polymerase epsilon subunit 3 [EC:2.7.7.7]
KOG2794Eukaryota (superkingdom)porphobilinogen synthase [EC:4.2.1.24],DNA polymerase epsilon subunit 3 [EC:2.7.7.7]
HV37FMetazoa (kingdom)porphobilinogen synthase [EC:4.2.1.24],DNA polymerase epsilon subunit 3 [EC:2.7.7.7]
93VP2Chordata (phylum)porphobilinogen synthase [EC:4.2.1.24],DNA polymerase epsilon subunit 3 [EC:2.7.7.7]
5QBNFSarcopterygii (superclass)porphobilinogen synthase [EC:4.2.1.24],DNA polymerase epsilon subunit 3 [EC:2.7.7.7]
8ZHG1Mammalia (class)porphobilinogen synthase [EC:4.2.1.24],DNA polymerase epsilon subunit 3 [EC:2.7.7.7]
4R7YJEuarchontoglires (superorder)porphobilinogen synthase [EC:4.2.1.24]
4ZN3MPrimates (order)porphobilinogen synthase [EC:4.2.1.24]
98Q7RHaplorrhini (suborder)porphobilinogen synthase [EC:4.2.1.24]
BVE5ESimiiformes (infraorder)porphobilinogen synthase [EC:4.2.1.24]
9EZ26Catarrhini (parvorder)porphobilinogen synthase [EC:4.2.1.24]
H3KHBBilateria (clade)porphobilinogen synthase [EC:4.2.1.24],DNA polymerase epsilon subunit 3 [EC:2.7.7.7]
9FF0PVertebrata (clade)porphobilinogen synthase [EC:4.2.1.24],DNA polymerase epsilon subunit 3 [EC:2.7.7.7]
7NEQJOpisthokonta (clade)porphobilinogen synthase [EC:4.2.1.24],DNA polymerase epsilon subunit 3 [EC:2.7.7.7]
FX540Hominoidea (superfamily)porphobilinogen synthase [EC:4.2.1.24]
5N4TSHominidae (family)porphobilinogen synthase [EC:4.2.1.24]
5XTAUHomininae (subfamily)porphobilinogen synthase [EC:4.2.1.24]

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: