OAS1_HUMAN - dbPTM
OAS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
10UbiquitinationDLRNTPAKSLDKFIE
CCCCCCCHHHHHHHH
53.4029967540
19PhosphorylationLDKFIEDYLLPDTCF
HHHHHHHHCCCCHHH
9.4327259358
42AcetylationDIICGFLKERCFRGS
HHHHHHHHHHHCCCC
40.6326051181
49PhosphorylationKERCFRGSSYPVCVS
HHHHCCCCCCCEEEE
23.5730108239
50PhosphorylationERCFRGSSYPVCVSK
HHHCCCCCCCEEEEE
35.9626657352
50 (in isoform 3)Phosphorylation-35.9624719451
51PhosphorylationRCFRGSSYPVCVSKV
HHCCCCCCCEEEEEE
11.0323312004
116 (in isoform 3)Phosphorylation-24.3424719451
116PhosphorylationCQRERAFSVKFEVQA
HHHHCCCEEEEEEEC
24.3424719451
182UbiquitinationEECTDLQKEGEFSTC
HHHCHHHHCCCHHHH
75.0029967540
199UbiquitinationELQRDFLKQRPTKLK
HHHHHHHHHCCHHHH
44.2329967540
207PhosphorylationQRPTKLKSLIRLVKH
HCCHHHHHHHHHHHH
39.1924719451
213UbiquitinationKSLIRLVKHWYQNCK
HHHHHHHHHHHHHHH
32.7729967540
220UbiquitinationKHWYQNCKKKLGKLP
HHHHHHHHHHHCCCC
61.5729967540
271PhosphorylationNYQQLCIYWTKYYDF
CHHHHHHHHHHHCCC
13.1618083107
279UbiquitinationWTKYYDFKNPIIEKY
HHHHCCCCCHHHHHH
59.9433845483
285UbiquitinationFKNPIIEKYLRRQLT
CCCHHHHHHHHHHCC
38.8933845483
314UbiquitinationNLGGGDPKGWRQLAQ
CCCCCCHHHHHHHHH
75.6929967540
338PhosphorylationCFKNWDGSPVSSWIL
CCCCCCCCCCEEEEE
21.47-
338 (in isoform 2)Phosphorylation-21.4725159151
341PhosphorylationNWDGSPVSSWILLAE
CCCCCCCEEEEEEEE
24.2823090842
342PhosphorylationWDGSPVSSWILLAES
CCCCCCEEEEEEEEC
20.5423090842
349PhosphorylationSWILLAESNSADDET
EEEEEEECCCCCCCC
30.4023090842
351PhosphorylationILLAESNSADDETDD
EEEEECCCCCCCCCC
42.2123090842
356PhosphorylationSNSADDETDDPRRYQ
CCCCCCCCCCHHHHH
53.3423090842
362PhosphorylationETDDPRRYQKYGYIG
CCCCHHHHHHHCEEE
15.61-
367PhosphorylationRRYQKYGYIGTHEYP
HHHHHHCEEECCCCC
7.9622461510

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 OAS1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OAS1_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 OAS1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANM6_HUMANPRMT6physical
23455924
BUD23_HUMANWBSCR22physical
21988832
RL30_HUMANRPL30physical
21988832
TRI27_HUMANTRIM27physical
25416956
EXOC5_HUMANEXOC5physical
25416956

Drug and Disease Associations
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.
Regulatory Network of OAS1_HUMAN

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Related Literatures of Post-Translational Modification

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