HTRA1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0060718Biological processchorionic trophoblast cell differentiation
GO_0030512Biological processnegative regulation of transforming growth factor beta receptor signaling pathway
GO_0012501Biological processprogrammed cell death
GO_0030514Biological processnegative regulation of BMP signaling pathway
GO_0001890Biological processplacenta development
GO_0006508Biological processproteolysis
GO_0043065Biological processpositive regulation of apoptotic process
GO_0005615Cellular componentextracellular space
GO_0005576Cellular componentextracellular region
GO_0005886Cellular componentplasma membrane
GO_0070062Cellular componentextracellular exosome
GO_0062023Cellular componentcollagen-containing extracellular matrix
GO_0005829Cellular componentcytosol
GO_0140677Molecular functionmolecular function activator activity
GO_0042802Molecular functionidentical protein binding
GO_0008236Molecular functionserine-type peptidase activity
GO_0019838Molecular functiongrowth factor binding
GO_0005515Molecular functionprotein binding
GO_0004252Molecular functionserine-type endopeptidase activity

IV. Literature review

[source]
Gene nameHTRA1
Protein nameHtrA serine peptidase 1
HTRA1 protein
Serine protease HTRA1 (EC 3.4.21.-) (High-temperature requirement A serine peptidase 1) (L56) (Serine protease 11)
SynonymsPRSS11
HTRA
DescriptionFUNCTION: Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets. .

AccessionsQ92743
ENST00000648167.1
Q05DJ8
A0A3B3IU24
ENST00000420892.1
H0Y7G9
ENST00000368984.8