Domains within Mus musculus protein EGF_MOUSE (P01132)

Pro-epidermal growth factor

Alternative representations: 1 /

Protein length1217 aa
Source databaseUniProt
Identifiers EGF_MOUSE, P01132, ENSMUSP00000029653.2, ENSMUSP00000029653, E9QNX6, Q569W5, Q6P9J2
Source gene ENSMUSG00000028017
Alternative splicing EGF_MOUSE, A0A0G2JF92_MOUSE, A0A0G2JDT8_MOUSE, A0A0G2JFB8_MOUSE

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 Euteleostomi

Predicted functional partners

EGF_MOUSE is shown as Egf 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 Egf

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

KEGG pathways

PathwayDescription
map05219Bladder cancer
map05010Alzheimer disease

KEGG orthologous groups

KONameDescription
K04357EGFepidermal growth factor
K20050LRP3_10_12low-density lipoprotein receptor-related protein 3/10/12

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
Phosphorylation6
O-GalNAc glycosylation2
O-linked glycosylation2
Proteolytic cleavage1
Ubiquitination1

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

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 10090.ENSMUSP00000029653 in eggNOG.

OGTaxonomic classDescription
LKOG1215All organisms (root)low-density lipoprotein receptor-related protein 3/10/12,low density lipoprotein receptor-related protein 5/6,low-density lipoprotein receptor-related protein 4
KOG1215Eukaryota (superkingdom)low-density lipoprotein receptor-related protein 3/10/12,low density lipoprotein receptor-related protein 5/6,low-density lipoprotein receptor-related protein 4
HVUA6Metazoa (kingdom)epidermal growth factor,protocadherin Fat 4,low-density lipoprotein receptor-related protein 4
93TX1Chordata (phylum)epidermal growth factor,visual pigment-like receptor peropsin
5R3ADSarcopterygii (superclass)epidermal growth factor,visual pigment-like receptor peropsin
8Z4BAMammalia (class)epidermal growth factor,visual pigment-like receptor peropsin
4RJZDEuarchontoglires (superorder)epidermal growth factor,visual pigment-like receptor peropsin
AI6W9Rodentia (order)epidermal growth factor,visual pigment-like receptor peropsin
8D8UQMyomorpha (suborder)epidermal growth factor,visual pigment-like receptor peropsin
H55W6Bilateria (clade)epidermal growth factor,low-density lipoprotein receptor-related protein 4,visual pigment-like receptor peropsin
9FT5AVertebrata (clade)epidermal growth factor,visual pigment-like receptor peropsin
7N8RTOpisthokonta (clade)epidermal growth factor,protocadherin Fat 4,low-density lipoprotein receptor-related protein 4
CQAV1Muridae (family)epidermal growth factor
AE3E0Murinae (subfamily)epidermal growth factor
5PR1NMus (genus)epidermal growth factor
HEG0SMus (subgenus)epidermal growth factor

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: