HTRA1_HUMAN - dbPTM
HTRA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
195PhosphorylationLFRKLPFSKREVPVA
HHHCCCCCCCCCCCC
28.94-
237PhosphorylationVELKNGATYEAKIKD
EEECCCCEEEEEECC
24.24-
238PhosphorylationELKNGATYEAKIKDV
EECCCCEEEEEECCC
17.23-
305UbiquitinationSTTQRGGKELGLRNS
EECCCCCEEECCCCC
53.22-
357PhosphorylationGISFAIPSDKIKKFL
EEEEEECHHHHHHHH
45.48-
365PhosphorylationDKIKKFLTESHDRQA
HHHHHHHHHHCCHHH
38.28-
367PhosphorylationIKKFLTESHDRQAKG
HHHHHHHHCCHHHCC
26.00-
382PhosphorylationKAITKKKYIGIRMMS
CCCCHHHCEEEEEEE
17.1723403867
393PhosphorylationRMMSLTSSKAKELKD
EEEECCCHHHHHHHH
31.2523403867
444PhosphorylationINGQSVVSANDVSDV
ECCEEEEECHHHHHH
21.1430576142
449PhosphorylationVVSANDVSDVIKRES
EEECHHHHHHHHCHH
29.0830576142
456PhosphorylationSDVIKRESTLNMVVR
HHHHHCHHHHHHHEE
42.08-
472PhosphorylationGNEDIMITVIPEEID
CCCCEEEEECCCCCC
8.5930243723

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HTRA1_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XIAP_HUMANXIAPphysical
21387310
IMDH1_HUMANIMPDH1physical
21988832

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HTRA1_HUMAN

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Related Literatures of Post-Translational Modification

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