UniProt ID | HTRA1_HUMAN | |
---|---|---|
UniProt AC | Q92743 | |
Protein Name | Serine protease HTRA1 | |
Gene Name | HTRA1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 480 | |
Subcellular Localization | Cell membrane . Secreted . Cytoplasm, cytosol . Predominantly secreted (PubMed:15208355). Also found associated with the plasma membrane (PubMed:21297635). | |
Protein Description | 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.. | |
Protein Sequence | MQIPRAALLPLLLLLLAAPASAQLSRAGRSAPLAAGCPDRCEPARCPPQPEHCEGGRARDACGCCEVCGAPEGAACGLQEGPCGEGLQCVVPFGVPASATVRRRAQAGLCVCASSEPVCGSDANTYANLCQLRAASRRSERLHRPPVIVLQRGACGQGQEDPNSLRHKYNFIADVVEKIAPAVVHIELFRKLPFSKREVPVASGSGFIVSEDGLIVTNAHVVTNKHRVKVELKNGATYEAKIKDVDEKADIALIKIDHQGKLPVLLLGRSSELRPGEFVVAIGSPFSLQNTVTTGIVSTTQRGGKELGLRNSDMDYIQTDAIINYGNSGGPLVNLDGEVIGINTLKVTAGISFAIPSDKIKKFLTESHDRQAKGKAITKKKYIGIRMMSLTSSKAKELKDRHRDFPDVISGAYIIEVIPDTPAEAGGLKENDVIISINGQSVVSANDVSDVIKRESTLNMVVRRGNEDIMITVIPEEIDP | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
195 | Phosphorylation | LFRKLPFSKREVPVA HHHCCCCCCCCCCCC | 28.94 | - | |
237 | Phosphorylation | VELKNGATYEAKIKD EEECCCCEEEEEECC | 24.24 | - | |
238 | Phosphorylation | ELKNGATYEAKIKDV EECCCCEEEEEECCC | 17.23 | - | |
305 | Ubiquitination | STTQRGGKELGLRNS EECCCCCEEECCCCC | 53.22 | - | |
357 | Phosphorylation | GISFAIPSDKIKKFL EEEEEECHHHHHHHH | 45.48 | - | |
365 | Phosphorylation | DKIKKFLTESHDRQA HHHHHHHHHHCCHHH | 38.28 | - | |
367 | Phosphorylation | IKKFLTESHDRQAKG HHHHHHHHCCHHHCC | 26.00 | - | |
382 | Phosphorylation | KAITKKKYIGIRMMS CCCCHHHCEEEEEEE | 17.17 | 23403867 | |
393 | Phosphorylation | RMMSLTSSKAKELKD EEEECCCHHHHHHHH | 31.25 | 23403867 | |
444 | Phosphorylation | INGQSVVSANDVSDV ECCEEEEECHHHHHH | 21.14 | 30576142 | |
449 | Phosphorylation | VVSANDVSDVIKRES EEECHHHHHHHHCHH | 29.08 | 30576142 | |
456 | Phosphorylation | SDVIKRESTLNMVVR HHHHHCHHHHHHHEE | 42.08 | - | |
472 | Phosphorylation | GNEDIMITVIPEEID CCCCEEEEECCCCCC | 8.59 | 30243723 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of HTRA1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HTRA1_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of HTRA1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
XIAP_HUMAN | XIAP | physical | 21387310 | |
IMDH1_HUMAN | IMPDH1 | physical | 21988832 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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