Domains within Homo sapiens protein PGAM4_HUMAN (Q8N0Y7)

Probable phosphoglycerate mutase 4

Alternative representations: 1 /

Protein length254 aa
Source databaseUniProt
Identifiers PGAM4_HUMAN, Q8N0Y7, ENSP00000412189.1, ENSP00000412189, Q5JPN2, Q8NI24, Q8NI25, Q8NI26, O00228_HUMAN, O00228
Source gene ENSG00000226784

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

PGAM4_HUMAN is shown as PGAM4 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 PGAM4

Protein PGAM4_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map00260Glycine, serine and threonine 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
K01834PGAM, gpmA2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11] 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 52 PTMs annotated in this protein:

PTMCount
Phosphorylation19
Acetylation14
Ubiquitination12
N-linked glycosylation3
Glycation3
Nitrosylation1

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein PGAM1.

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.ENSP00000412189 in eggNOG.

OGTaxonomic classDescription
LCOG0588All organisms (root)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11],fructose-2,6-bisphosphatase [EC:3.1.3.46],bisphosphoglycerate/phosphoglycerate mutase [EC:5.4.2.4 5.4.2.11]
KOG0235Eukaryota (superkingdom)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11],fructose-2,6-bisphosphatase [EC:3.1.3.46],bisphosphoglycerate/phosphoglycerate mutase [EC:5.4.2.4 5.4.2.11]
HU2XTMetazoa (kingdom)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11],bisphosphoglycerate/phosphoglycerate mutase [EC:5.4.2.4 5.4.2.11]
9414PChordata (phylum)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11],bisphosphoglycerate/phosphoglycerate mutase [EC:5.4.2.4 5.4.2.11]
5R0VBSarcopterygii (superclass)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11],bisphosphoglycerate/phosphoglycerate mutase [EC:5.4.2.4 5.4.2.11]
8Z8AZMammalia (class)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11]
4RMT6Euarchontoglires (superorder)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11]
4ZJANPrimates (order)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11]
98QQPHaplorrhini (suborder)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11]
BV2CXSimiiformes (infraorder)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11]
9EFZKCatarrhini (parvorder)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11]
7IPJIOpisthokonta (clade)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11],bisphosphoglycerate/phosphoglycerate mutase [EC:5.4.2.4 5.4.2.11]
9FVITVertebrata (clade)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11],bisphosphoglycerate/phosphoglycerate mutase [EC:5.4.2.4 5.4.2.11]
H3GUDBilateria (clade)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11],bisphosphoglycerate/phosphoglycerate mutase [EC:5.4.2.4 5.4.2.11]
FX8S7Hominoidea (superfamily)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11]
5N1WAHominidae (family)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11]
5Y8SFHomininae (subfamily)2,3-bisphosphoglycerate-dependent phosphoglycerate mutase [EC:5.4.2.11]

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: