Domains within Homo sapiens protein Q9UNP9-3

Isoform 3 of Peptidyl-prolyl cis-trans isomerase E

Alternative representations: 1 /

Protein length314 aa
Source databaseUniProt
Identifiers Q9UNP9-3, ENSP00000361918.1, ENSP00000361918
Source gene ENSG00000084072
Alternative splicing ENSP00000436689.1, PPIE_HUMAN, Q9UNP9-2, E9PMH0_HUMAN, ENSP00000433475.1, E9PK21_HUMAN, E9PEQ6_HUMAN, Q9UNP9-3, ENSP00000432396.1, H0YE31_HUMAN

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 cellular organisms

Predicted functional partners

Q9UNP9-3 is shown as PPIE 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 PPIE

Protein Q9UNP9-3 is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map04217Necroptosis
map03040Spliceosome

KEGG orthologous groups

KONameDescription
K09564PPIEpeptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
K03768PPIB, ppiBpeptidyl-prolyl cis-trans isomerase B (cyclophilin B) [EC:5.2.1.8]

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.ENSP00000361918 in eggNOG.

OGTaxonomic classDescription
LCOG0652All organisms (root)peptidyl-prolyl cis-trans isomerase B (cyclophilin B) [EC:5.2.1.8],peptidyl-prolyl cis-trans isomerase A (cyclophilin A) [EC:5.2.1.8],peptidylprolyl isomerase [EC:5.2.1.8]
KOG0111Eukaryota (superkingdom)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8],peptidyl-prolyl cis-trans isomerase A (cyclophilin A) [EC:5.2.1.8]
HVM35Metazoa (kingdom)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
93FZKChordata (phylum)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
5R48QSarcopterygii (superclass)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
8Z4DWMammalia (class)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
4RG0MEuarchontoglires (superorder)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
502CVPrimates (order)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
98K7UHaplorrhini (suborder)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
BVIM2Simiiformes (infraorder)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
9EYFKCatarrhini (parvorder)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
9GFBJVertebrata (clade)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
7M4I9Opisthokonta (clade)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8],peptidyl-prolyl cis-trans isomerase A (cyclophilin A) [EC:5.2.1.8]
H5YV0Bilateria (clade)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
FX4S2Hominoidea (superfamily)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
5NDE6Hominidae (family)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]
5Y2DCHomininae (subfamily)peptidyl-prolyl isomerase E (cyclophilin E) [EC:5.2.1.8]

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: