Domains within Homo sapiens protein FA11_HUMAN (P03951)

Coagulation factor XI

Alternative representations: 1 /

Protein length625 aa
Source databaseUniProt
Identifiers FA11_HUMAN, P03951, ENSP00000384957.2, ENSP00000384957, D3DP64, Q4W5C2, Q9Y495, Q9UEG0_HUMAN, Q9UEG0
Source gene ENSG00000088926
Alternative splicing FA11_HUMAN, D6RB32_HUMAN, H0Y596_HUMAN, X6R3B1_HUMAN, P03951-2

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 Amniota

Predicted functional partners

FA11_HUMAN is shown as F11 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 F11

Protein FA11_HUMAN is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map05202Transcriptional misregulation in cancer
map04974Protein digestion and absorption
map04080Neuroactive ligand-receptor interaction
map04610Complement and coagulation cascades
map04972Pancreatic secretion

KEGG orthologous groups

KONameDescription
K01353GZMBgranzyme B [EC:3.4.21.79]
K01317ACRacrosin [EC:3.4.21.10]
K01312PRSS1_2_3trypsin [EC:3.4.21.4]
K01323F11coagulation factor XI [EC:3.4.21.27]

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 13 PTMs annotated in this protein:

PTMCount
Phosphorylation7
N-linked glycosylation5
Acetylation1

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein F11.

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.ENSP00000384957 in eggNOG.

OGTaxonomic classDescription
LCOG5640All organisms (root)trypsin [EC:3.4.21.4],chymotrypsin [EC:3.4.21.1],transmembrane protease serine 9 [EC:3.4.21.-]
KOG3627Eukaryota (superkingdom)trypsin [EC:3.4.21.4],chymotrypsin [EC:3.4.21.1],transmembrane protease serine 9 [EC:3.4.21.-]
HTTXHMetazoa (kingdom)trypsin [EC:3.4.21.4],chymotrypsin [EC:3.4.21.1],pancreatic elastase II [EC:3.4.21.71]
93HMSChordata (phylum)trypsin [EC:3.4.21.4],granzyme B [EC:3.4.21.79],granzyme A [EC:3.4.21.78]
5R3FQSarcopterygii (superclass)acrosin [EC:3.4.21.10],transmembrane protease serine 2 [EC:3.4.21.-],plasma kallikrein [EC:3.4.21.34]
8ZM9IMammalia (class)coagulation factor XI [EC:3.4.21.27],plasma kallikrein [EC:3.4.21.34]
4RE68Euarchontoglires (superorder)coagulation factor XI [EC:3.4.21.27]
4ZJE1Primates (order)coagulation factor XI [EC:3.4.21.27]
9868HHaplorrhini (suborder)coagulation factor XI [EC:3.4.21.27]
BVF13Simiiformes (infraorder)coagulation factor XI [EC:3.4.21.27]
9ES9RCatarrhini (parvorder)coagulation factor XI [EC:3.4.21.27]
H50FABilateria (clade)trypsin [EC:3.4.21.4],chymotrypsin [EC:3.4.21.1],pancreatic elastase II [EC:3.4.21.71]
9FFGMVertebrata (clade)granzyme B [EC:3.4.21.79],granzyme A [EC:3.4.21.78],serine protease 27 [EC:3.4.21.-]
7MW1XOpisthokonta (clade)trypsin [EC:3.4.21.4],chymotrypsin [EC:3.4.21.1],pancreatic elastase II [EC:3.4.21.71]
FWYTRHominoidea (superfamily)coagulation factor XI [EC:3.4.21.27]
5N64AHominidae (family)coagulation factor XI [EC:3.4.21.27]
5Y4H5Homininae (subfamily)coagulation factor XI [EC:3.4.21.27]

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: