Gene Symbol | FURIN |
Entrez ID | 5045 |
Uniprot ID | P09958 |
Description | furin (paired basic amino acid cleaving enzyme) |
Chromosomal Location | chr15: 90,868,592-90,883,458 |
Ontology | GO ID | GO Term | Definition | Evidence |
---|---|---|---|---|
BP |
GO:0006465 |
signal peptide processing |
The proteolytic removal of a signal peptide from a protein during or after transport to a specific location in the cell. |
IDA|TAS |
BP |
GO:0007179 |
transforming growth factor beta receptor signaling pathway |
A series of molecular signals initiated by the binding of an extracellular ligand to a transforming growth factor beta receptor on the surface of a target cell, and ending with regulation of a downstream cellular process, e.g. transcription. |
TAS |
BP |
GO:0008283 |
cell proliferation |
The multiplication or reproduction of cells, resulting in the expansion of a cell population. |
IMP |
BP |
GO:0009966 |
regulation of signal transduction |
Any process that modulates the frequency, rate or extent of signal transduction. |
IEA |
BP |
GO:0010951 |
negative regulation of endopeptidase activity |
Any process that decreases the frequency, rate or extent of endopeptidase activity, the endohydrolysis of peptide bonds within proteins. |
IEA |
BP |
GO:0016485 |
protein processing |
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. |
IDA|IMP |
BP |
GO:0016486 |
peptide hormone processing |
The generation of a mature peptide hormone by posttranslational processing of a prohormone. |
IDA |
BP |
GO:0019058 |
viral life cycle |
A set of processes which all viruses follow to ensure survival; includes attachment and entry of the virus particle, decoding of genome information, translation of viral mRNA by host ribosomes, genome replication, and assembly and release of viral particles containing the genome. |
IEP |
BP |
GO:0019082 |
viral protein processing |
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein. |
TAS |
BP |
GO:0022617 |
extracellular matrix disassembly |
A process that results in the breakdown of the extracellular matrix. |
TAS |
BP |
GO:0030198 |
extracellular matrix organization |
A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of an extracellular matrix. |
TAS |
BP |
GO:0030574 |
collagen catabolic process |
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells. |
TAS |
BP |
GO:0032455 |
nerve growth factor processing |
The generation of a mature nerve growth factor (NGF) by proteolysis of a precursor. |
TAS |
BP |
GO:0032804 |
negative regulation of low-density lipoprotein particle receptor catabolic process |
Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of low-density lipoprotein receptors. |
IDA |
BP |
GO:0032902 |
nerve growth factor production |
The appearance of nerve growth factor (NGF) due to biosynthesis or secretion by cells in a neuron's target field, resulting in an increase in its intracellular or extracellular levels. |
IDA |
BP |
GO:0032911 |
negative regulation of transforming growth factor beta1 production |
Any process that stops, prevents, or reduces the frequency, rate, or extent of production of transforming growth factor-beta1. |
IMP |
BP |
GO:0032940 |
secretion by cell |
The controlled release of a substance by a cell. |
IDA |
BP |
GO:0042176 |
regulation of protein catabolic process |
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the breakdown of a protein by the destruction of the native, active configuration, with or without the hydrolysis of peptide bonds. |
IMP |
BP |
GO:0043043 |
peptide biosynthetic process |
The chemical reactions and pathways resulting in the formation of peptides, compounds of 2 or more (but usually less than 100) amino acids where the alpha carboxyl group of one is bound to the alpha amino group of another. This may include the translation of a precursor protein and its subsequent processing into a functional peptide. |
IDA |
BP |
GO:0044267 |
cellular protein metabolic process |
The chemical reactions and pathways involving a specific protein, rather than of proteins in general, occurring at the level of an individual cell. Includes cellular protein modification. |
TAS |
BP |
GO:0045714 |
regulation of low-density lipoprotein particle receptor biosynthetic process |
Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of low-density lipoprotein particle receptors. |
IEA |
BP |
GO:0051044 |
positive regulation of membrane protein ectodomain proteolysis |
Any process that activates or increases the frequency, rate or extent of membrane protein ectodomain peptidolysis. |
IC |
BP |
GO:0052548 |
regulation of endopeptidase activity |
Any process that modulates the frequency, rate or extent of endopeptidase activity, the endohydrolysis of peptide bonds within proteins. |
IDA |
CC |
GO:0000139 |
Golgi membrane |
The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
TAS |
CC |
GO:0005783 |
endoplasmic reticulum |
The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
IGI |
CC |
GO:0005796 |
Golgi lumen |
The volume enclosed by the membranes of any cisterna or subcompartment of the Golgi apparatus, including the cis- and trans-Golgi networks. |
TAS |
CC |
GO:0005802 |
trans-Golgi network |
The network of interconnected tubular and cisternal structures located within the Golgi apparatus on the side distal to the endoplasmic reticulum, from which secretory vesicles emerge. The trans-Golgi network is important in the later stages of protein secretion where it is thought to play a key role in the sorting and targeting of secreted proteins to the correct destination. |
IDA |
CC |
GO:0005886 |
plasma membrane |
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
TAS |
CC |
GO:0009986 |
cell surface |
The external part of the cell wall and/or plasma membrane. |
IDA |
CC |
GO:0016020 |
membrane |
A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
IDA |
CC |
GO:0016021 |
integral component of membrane |
The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
IEA |
CC |
GO:0030140 |
trans-Golgi network transport vesicle |
A vesicle that mediates transport between the trans-Golgi network and other parts of the cell. |
IDA |
CC |
GO:0045121 |
membrane raft |
Any of the small (10-200 nm), heterogeneous, highly dynamic, sterol- and sphingolipid-enriched membrane domains that compartmentalize cellular processes. Small rafts can sometimes be stabilized to form larger platforms through protein-protein and protein-lipid interactions. |
IDA |
CC |
GO:0070062 |
extracellular exosome |
A membrane-bounded vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. |
IDA |
MF |
GO:0002020 |
protease binding |
Interacting selectively and non-covalently with any protease or peptidase. |
IPI |
MF |
GO:0004175 |
endopeptidase activity |
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. |
IDA|TAS |
MF |
GO:0004252 |
serine-type endopeptidase activity |
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine). |
IDA|TAS |
MF |
GO:0004867 |
serine-type endopeptidase inhibitor activity |
Stops, prevents or reduces the activity of serine-type endopeptidases, enzymes that catalyze the hydrolysis of nonterminal peptide bonds in a polypeptide chain; a serine residue (and a histidine residue) are at the active center of the enzyme. |
IDA |
MF |
GO:0008233 |
peptidase activity |
Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. |
IDA |
MF |
GO:0042277 |
peptide binding |
Interacting selectively and non-covalently with peptides, any of a group of organic compounds comprising two or more amino acids linked by peptide bonds. |
IDA |
MF |
GO:0046872 |
metal ion binding |
Interacting selectively and non-covalently with any metal ion. |
IEA |
MF |
GO:0048406 |
nerve growth factor binding |
Interacting selectively and non-covalently with nerve growth factor (NGF). |
IDA |
Domain ID | Description |
---|---|
IPR000209 |
Peptidase S8/S53 domain |
IPR002884 |
Proprotein convertase, P |
IPR006212 |
Furin-like repeat |
IPR008979 |
Galactose-binding domain-like |
IPR009020 |
Protease propeptides/proteinase inhibitor I9 |
IPR009030 |
Growth factor receptor cysteine-rich domain |
IPR015500 |
Peptidase S8, subtilisin-related |
IPR022398 |
Peptidase S8, subtilisin, His-active site |
IPR023827 |
Peptidase S8, subtilisin, Asp-active site |
IPR023828 |
Peptidase S8, subtilisin, Ser-active site |
IPR032815 |
Peptidase S8, pro-domain |
IPR034182 |
Kexin/furin catalytic domain |
Pathway ID | Pathway Term | Pathway Source |
---|---|---|
hsa05164 |
Influenza A |
KEGG |
h_notchpathway |
Proteolysis and Signaling Pathway of Notch |
BioCarta |
UMLS CUI | UMLS Term |
---|---|
C0024667 |
Animal Mammary Neoplasms |
C0024668 |
Mammary Neoplasms, Experimental |
C0036341 |
Schizophrenia |
Tissue | Cell Type |
---|---|
cerebellum |
Purkinje cells |
cerebral cortex |
neuronal cells |
hippocampus |
neuronal cells |
kidney |
cells in tubules |
pancreas |
exocrine glandular cells |
parathyroid gland |
glandular cells |
placenta |
trophoblastic cells |
salivary gland |
glandular cells |
thyroid gland |
glandular cells |
Pubmed ID | Author | Year | Title |
---|---|---|---|
22617121 |
Ouandaogo et al. |
2012 |
Differences in transcriptomic profiles of human cumulus cells isolated from oocytes at GV, MI and MII stages after in vivo andin vitro oocyte maturation |
Gene Symbol | Entrez ID | Uniprot ID | Score |
---|---|---|---|
NOTCH1 |
4851 |
P46531 |
0.52 |
PDGFA |
5154 |
P04085 |
0.52 |
PMCH |
5367 |
P20382 |
0.52 |
PRB4 |
5545 |
P10163 |
0.52 |
SORL1 |
6653 |
Q92673 |
0.52 |
VWF |
7450 |
P04275 |
0.52 |
ZP3 |
7784 |
P21754 |
0.52 |
TNFSF13 |
8741 |
O75888 |
0.52 |
LECT1 |
11061 |
O75829 |
0.52 |
GORASP2 |
26003 |
Q9H8Y8 |
0.52 |
NAGPA |
51172 |
Q9UK23 |
0.52 |
ITM2C |
81618 |
Q9NQX7 |
0.52 |
DSG3 |
1830 |
P32926 |
0.55 |
EDA |
1896 |
Q92838 |
0.55 |
ADAMTS1 |
9510 |
Q9UHI8 |
0.55 |
TGOLN2 |
10618 |
O43493 |
0.55 |
BACE1 |
23621 |
P56817 |
0.55 |
SORCS1 |
114815 |
Q8WY21 |
0.55 |
DDX56 |
54606 |
Q9NY93 |
0.63 |
LRP1 |
4035 |
Q07954 |
0.65 |
ADAM19 |
8728 |
Q9H013 |
0.65 |
FLNC |
2318 |
Q14315 |
0.67 |
MST1R |
4486 |
Q04912 |
0.68 |
FURIN |
5045 |
P09958 |
0.68 |
ADAMTS4 |
9507 |
O75173 |
0.52 |
ZP4 |
57829 |
Q12836 |
0.52 |
COL23A1 |
91522 |
Q86Y22 |
0.55 |
FLNA |
2316 |
P21333 |
0.59 |
ABCC6 |
368 |
O95255 |
0.63 |
ELAVL1 |
1994 |
Q15717 |
0.63 |
MMP14 |
4323 |
P50281 |
0.63 |
MSTN |
2660 |
O14793 |
0.70 |
BAG6 |
7917 |
P46379 |
0.72 |
HUWE1 |
10075 |
Q7Z6Z7 |
0.72 |
SGTB |
54557 |
Q96EQ0 |
0.72 |
SERPINB8 |
5271 |
P50452 |
0.75 |
AP2M1 |
1173 |
Q96CW1 |
0.85 |
PACS1 |
55690 |
Q6VY07 |
0.88 |