Domains within Homo sapiens protein P02751-15

Isoform 15 of Fibronectin

Alternative representations: 1 /

Protein length2477 aa
Source databaseUniProt
Identifiers P02751-15, ENSP00000346839.4, ENSP00000346839
Source gene ENSG00000115414
Alternative splicing P02751-9, P02751-7, P02751-3, P02751-10, P02751-15, P02751-17, P02751-14, P02751-13, P02751-8, H0Y7Z1_HUMAN, H0Y4K8_HUMAN, P02751-16, FINC_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 Euteleostomi

Predicted functional partners

P02751-15 is shown as FN1 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 FN1

Protein P02751-15 is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map04928Parathyroid hormone synthesis, secretion and action
map05146Amoebiasis

KEGG orthologous groups

KONameDescription
K05717FN1fibronectin 1
K01047PLA2G, SPLA2secretory phospholipase A2 [EC:3.1.1.4] 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 18 PTMs annotated in this protein:

PTMCount
N-linked glycosylation8
Isopeptide bond3
Phosphorylation2
Acetylation2
Oxidation1
Ubiquitination1
Pyrrolidone carboxylic acid formation1

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein DKFZp686B18150.

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.ENSP00000346839 in eggNOG.

OGTaxonomic classDescription
LKOG1565All organisms (root)secretory phospholipase A2 [EC:3.1.1.4],matrix metalloproteinase-14 (membrane-inserted) [EC:3.4.24.80],matrix metalloproteinase-13 (collagenase 3) [EC:3.4.24.-]
KOG1565Eukaryota (superkingdom)secretory phospholipase A2 [EC:3.1.1.4],matrix metalloproteinase-14 (membrane-inserted) [EC:3.4.24.80],matrix metalloproteinase-13 (collagenase 3) [EC:3.4.24.-]
HTIRWMetazoa (kingdom)fibronectin 1
94TW3Chordata (phylum)fibronectin 1
5QHQGSarcopterygii (superclass)fibronectin 1
8Z24VMammalia (class)fibronectin 1
4RBYXEuarchontoglires (superorder)fibronectin 1
4ZMTBPrimates (order)fibronectin 1
98PIIHaplorrhini (suborder)fibronectin 1
BV05USimiiformes (infraorder)fibronectin 1
9F080Catarrhini (parvorder)fibronectin 1
H6ZF9Bilateria (clade)fibronectin 1
7MJ1EOpisthokonta (clade)fibronectin 1
9G3K7Vertebrata (clade)fibronectin 1

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: