UniProt ID | OAS1_HUMAN | |
---|---|---|
UniProt AC | P00973 | |
Protein Name | 2'-5'-oligoadenylate synthase 1 | |
Gene Name | OAS1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 400 | |
Subcellular Localization | Cytoplasm . Mitochondrion . Nucleus . Microsome . Endoplasmic reticulum . Secreted. Associated with different subcellular fractions such as mitochondrial, nuclear, and rough/smooth microsomal fractions. | |
Protein Description | Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes higher oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. The secreted form displays antiviral effect against vesicular stomatitis virus (VSV), herpes simplex virus type 2 (HSV-2), and encephalomyocarditis virus (EMCV) and stimulates the alternative antiviral pathway independent of RNase L.. | |
Protein Sequence | MMDLRNTPAKSLDKFIEDYLLPDTCFRMQINHAIDIICGFLKERCFRGSSYPVCVSKVVKGGSSGKGTTLRGRSDADLVVFLSPLTTFQDQLNRRGEFIQEIRRQLEACQRERAFSVKFEVQAPRWGNPRALSFVLSSLQLGEGVEFDVLPAFDALGQLTGGYKPNPQIYVKLIEECTDLQKEGEFSTCFTELQRDFLKQRPTKLKSLIRLVKHWYQNCKKKLGKLPPQYALELLTVYAWERGSMKTHFNTAQGFRTVLELVINYQQLCIYWTKYYDFKNPIIEKYLRRQLTKPRPVILDPADPTGNLGGGDPKGWRQLAQEAEAWLNYPCFKNWDGSPVSSWILLAESNSADDETDDPRRYQKYGYIGTHEYPHFSHRPSTLQAASTPQAEEDWTCTIL | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
10 | Ubiquitination | DLRNTPAKSLDKFIE CCCCCCCHHHHHHHH | 53.40 | 29967540 | |
19 | Phosphorylation | LDKFIEDYLLPDTCF HHHHHHHHCCCCHHH | 9.43 | 27259358 | |
42 | Acetylation | DIICGFLKERCFRGS HHHHHHHHHHHCCCC | 40.63 | 26051181 | |
49 | Phosphorylation | KERCFRGSSYPVCVS HHHHCCCCCCCEEEE | 23.57 | 30108239 | |
50 | Phosphorylation | ERCFRGSSYPVCVSK HHHCCCCCCCEEEEE | 35.96 | 26657352 | |
50 (in isoform 3) | Phosphorylation | - | 35.96 | 24719451 | |
51 | Phosphorylation | RCFRGSSYPVCVSKV HHCCCCCCCEEEEEE | 11.03 | 23312004 | |
116 (in isoform 3) | Phosphorylation | - | 24.34 | 24719451 | |
116 | Phosphorylation | CQRERAFSVKFEVQA HHHHCCCEEEEEEEC | 24.34 | 24719451 | |
182 | Ubiquitination | EECTDLQKEGEFSTC HHHCHHHHCCCHHHH | 75.00 | 29967540 | |
199 | Ubiquitination | ELQRDFLKQRPTKLK HHHHHHHHHCCHHHH | 44.23 | 29967540 | |
207 | Phosphorylation | QRPTKLKSLIRLVKH HCCHHHHHHHHHHHH | 39.19 | 24719451 | |
213 | Ubiquitination | KSLIRLVKHWYQNCK HHHHHHHHHHHHHHH | 32.77 | 29967540 | |
220 | Ubiquitination | KHWYQNCKKKLGKLP HHHHHHHHHHHCCCC | 61.57 | 29967540 | |
271 | Phosphorylation | NYQQLCIYWTKYYDF CHHHHHHHHHHHCCC | 13.16 | 18083107 | |
279 | Ubiquitination | WTKYYDFKNPIIEKY HHHHCCCCCHHHHHH | 59.94 | 33845483 | |
285 | Ubiquitination | FKNPIIEKYLRRQLT CCCHHHHHHHHHHCC | 38.89 | 33845483 | |
314 | Ubiquitination | NLGGGDPKGWRQLAQ CCCCCCHHHHHHHHH | 75.69 | 29967540 | |
338 | Phosphorylation | CFKNWDGSPVSSWIL CCCCCCCCCCEEEEE | 21.47 | - | |
338 (in isoform 2) | Phosphorylation | - | 21.47 | 25159151 | |
341 | Phosphorylation | NWDGSPVSSWILLAE CCCCCCCEEEEEEEE | 24.28 | 23090842 | |
342 | Phosphorylation | WDGSPVSSWILLAES CCCCCCEEEEEEEEC | 20.54 | 23090842 | |
349 | Phosphorylation | SWILLAESNSADDET EEEEEEECCCCCCCC | 30.40 | 23090842 | |
351 | Phosphorylation | ILLAESNSADDETDD EEEEECCCCCCCCCC | 42.21 | 23090842 | |
356 | Phosphorylation | SNSADDETDDPRRYQ CCCCCCCCCCHHHHH | 53.34 | 23090842 | |
362 | Phosphorylation | ETDDPRRYQKYGYIG CCCCHHHHHHHCEEE | 15.61 | - | |
367 | Phosphorylation | RRYQKYGYIGTHEYP HHHHHHCEEECCCCC | 7.96 | 22461510 |
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 OAS1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of OAS1_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 OAS1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ANM6_HUMAN | PRMT6 | physical | 23455924 | |
BUD23_HUMAN | WBSCR22 | physical | 21988832 | |
RL30_HUMAN | RPL30 | physical | 21988832 | |
TRI27_HUMAN | TRIM27 | physical | 25416956 | |
EXOC5_HUMAN | EXOC5 | physical | 25416956 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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