Domains within Homo sapiens protein PERT_HUMAN (P07202)

Thyroid peroxidase

Alternative representations: 1 /

Protein length933 aa
Source databaseUniProt
Identifiers PERT_HUMAN, P07202, ENSP00000329869.4, ENSP00000329869, ENSP00000318820.7, ENSP00000318820, P09934, P09935, Q8IUL0, Q8NF94, Q8NF95, Q8NF96, Q8NF97, Q8TCI9, Q53QT2_HUMAN, Q53QT2
Source gene ENSG00000115705
Alternative splicing PERT_HUMAN, P07202-2, P07202-5, H0Y6H4_HUMAN, H7C1F5_HUMAN, ENSP00000419461.1, P07202-4

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.

This domain architecture was probably invented with the emergence of Chordata

Predicted functional partners

PERT_HUMAN is shown as TPO 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 TPO

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

KEGG pathways

PathwayDescription
map04918Thyroid hormone synthesis

KEGG orthologous groups

KONameDescription
K19511PXDN, VPO1peroxidase [EC:1.11.1.7]
K00431TPOthyroid peroxidase [EC:1.11.1.8] 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 8 PTMs annotated in this protein:

PTMCount
Phosphorylation5
Acetylation2
N-linked glycosylation1

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

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.ENSP00000329869 in eggNOG.

OGTaxonomic classDescription
LKOG2408All organisms (root)peroxidase [EC:1.11.1.7],prostaglandin-endoperoxide synthase 2 [EC:1.14.99.1],prostaglandin-endoperoxide synthase 1 [EC:1.14.99.1]
KOG2408Eukaryota (superkingdom)peroxidase [EC:1.11.1.7],prostaglandin-endoperoxide synthase 2 [EC:1.14.99.1],prostaglandin-endoperoxide synthase 1 [EC:1.14.99.1]
HV60RMetazoa (kingdom)peroxidase [EC:1.11.1.7],thyroid peroxidase [EC:1.11.1.8],rotatin
93M72Chordata (phylum)thyroid peroxidase [EC:1.11.1.8],myeloperoxidase [EC:1.11.2.2],eosinophil peroxidase [EC:1.11.1.7]
5R34DSarcopterygii (superclass)thyroid peroxidase [EC:1.11.1.8]
8YVWRMammalia (class)thyroid peroxidase [EC:1.11.1.8]
4R541Euarchontoglires (superorder)thyroid peroxidase [EC:1.11.1.8]
4ZKAGPrimates (order)thyroid peroxidase [EC:1.11.1.8]
98ATPHaplorrhini (suborder)thyroid peroxidase [EC:1.11.1.8]
BVCSTSimiiformes (infraorder)thyroid peroxidase [EC:1.11.1.8]
9EWP8Catarrhini (parvorder)thyroid peroxidase [EC:1.11.1.8]
9FRASVertebrata (clade)thyroid peroxidase [EC:1.11.1.8],myeloperoxidase [EC:1.11.2.2],eosinophil peroxidase [EC:1.11.1.7]
7NVKROpisthokonta (clade)peroxidase [EC:1.11.1.7],thyroid peroxidase [EC:1.11.1.8],rotatin
H6EE6Bilateria (clade)peroxidase [EC:1.11.1.7],thyroid peroxidase [EC:1.11.1.8],rotatin
FX11EHominoidea (superfamily)thyroid peroxidase [EC:1.11.1.8]
5N9SWHominidae (family)thyroid peroxidase [EC:1.11.1.8]
5Y4C9Homininae (subfamily)thyroid peroxidase [EC:1.11.1.8]

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: