OAS3_HUMAN - dbPTM
OAS3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OAS3_HUMAN
UniProt AC Q9Y6K5
Protein Name 2'-5'-oligoadenylate synthase 3
Gene Name OAS3
Organism Homo sapiens (Human).
Sequence Length 1087
Subcellular Localization Cytoplasm. Nucleus.
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 preferentially dimers 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. Displays antiviral activity against Chikungunya virus (CHIKV), Dengue virus, Sindbis virus (SINV) and Semliki forest virus (SFV)..
Protein Sequence MDLYSTPAAALDRFVARRLQPRKEFVEKARRALGALAAALRERGGRLGAAAPRVLKTVKGGSSGRGTALKGGCDSELVIFLDCFKSYVDQRARRAEILSEMRASLESWWQNPVPGLRLTFPEQSVPGALQFRLTSVDLEDWMDVSLVPAFNVLGQAGSGVKPKPQVYSTLLNSGCQGGEHAACFTELRRNFVNIRPAKLKNLILLVKHWYHQVCLQGLWKETLPPVYALELLTIFAWEQGCKKDAFSLAEGLRTVLGLIQQHQHLCVFWTVNYGFEDPAVGQFLQRQLKRPRPVILDPADPTWDLGNGAAWHWDLLAQEAASCYDHPCFLRGMGDPVQSWKGPGLPRAGCSGLGHPIQLDPNQKTPENSKSLNAVYPRAGSKPPSCPAPGPTGAASIVPSVPGMALDLSQIPTKELDRFIQDHLKPSPQFQEQVKKAIDIILRCLHENCVHKASRVSKGGSFGRGTDLRDGCDVELIIFLNCFTDYKDQGPRRAEILDEMRAQLESWWQDQVPSLSLQFPEQNVPEALQFQLVSTALKSWTDVSLLPAFDAVGQLSSGTKPNPQVYSRLLTSGCQEGEHKACFAELRRNFMNIRPVKLKNLILLVKHWYRQVAAQNKGKGPAPASLPPAYALELLTIFAWEQGCRQDCFNMAQGFRTVLGLVQQHQQLCVYWTVNYSTEDPAMRMHLLGQLRKPRPLVLDPADPTWNVGHGSWELLAQEAAALGMQACFLSRDGTSVQPWDVMPALLYQTPAGDLDKFISEFLQPNRQFLAQVNKAVDTICSFLKENCFRNSPIKVIKVVKGGSSAKGTALRGRSDADLVVFLSCFSQFTEQGNKRAEIISEIRAQLEACQQERQFEVKFEVSKWENPRVLSFSLTSQTMLDQSVDFDVLPAFDALGQLVSGSRPSSQVYVDLIHSYSNAGEYSTCFTELQRDFIISRPTKLKSLIRLVKHWYQQCTKISKGRGSLPPQHGLELLTVYAWEQGGKDSQFNMAEGFRTVLELVTQYRQLCIYWTINYNAKDKTVGDFLKQQLQKPRPIILDPADPTGNLGHNARWDLLAKEAAACTSALCCMGRNGIPIQPWPVKAAV
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
1Acetylation-------MDLYSTPA
-------CCCCCCHH
36.6822814378
4Phosphorylation----MDLYSTPAAAL
----CCCCCCHHHHH
23.8827642862
59AcetylationPRVLKTVKGGSSGRG
CCEECCCCCCCCCCC
63.8930590991
70AcetylationSGRGTALKGGCDSEL
CCCCCCCCCCCCCEE
51.2830590997
119PhosphorylationPVPGLRLTFPEQSVP
CCCCCEEECCCCCCC
30.6123403867
341UbiquitinationGDPVQSWKGPGLPRA
CCCCCCCCCCCCCCC
61.5522505724
351PhosphorylationGLPRAGCSGLGHPIQ
CCCCCCCCCCCCCCC
35.8122167270
364UbiquitinationIQLDPNQKTPENSKS
CCCCCCCCCCCCCCC
73.0929967540
365PhosphorylationQLDPNQKTPENSKSL
CCCCCCCCCCCCCCC
26.5222167270
369PhosphorylationNQKTPENSKSLNAVY
CCCCCCCCCCCCEEC
23.2022167270
370UbiquitinationQKTPENSKSLNAVYP
CCCCCCCCCCCEECC
71.2327667366
371PhosphorylationKTPENSKSLNAVYPR
CCCCCCCCCCEECCC
27.0323090842
376PhosphorylationSKSLNAVYPRAGSKP
CCCCCEECCCCCCCC
5.6522817900
381PhosphorylationAVYPRAGSKPPSCPA
EECCCCCCCCCCCCC
40.7923090842
385PhosphorylationRAGSKPPSCPAPGPT
CCCCCCCCCCCCCCC
41.0627251275
392PhosphorylationSCPAPGPTGAASIVP
CCCCCCCCCCCCCCC
45.4223090842
396PhosphorylationPGPTGAASIVPSVPG
CCCCCCCCCCCCCCC
24.4723090842
400PhosphorylationGAASIVPSVPGMALD
CCCCCCCCCCCCCCC
30.0123090842
409PhosphorylationPGMALDLSQIPTKEL
CCCCCCHHHCCHHHH
26.2323090842
413PhosphorylationLDLSQIPTKELDRFI
CCHHHCCHHHHHHHH
38.4923090842
425UbiquitinationRFIQDHLKPSPQFQE
HHHHHHCCCCHHHHH
39.7829967540
427PhosphorylationIQDHLKPSPQFQEQV
HHHHCCCCHHHHHHH
29.7328102081
435UbiquitinationPQFQEQVKKAIDIIL
HHHHHHHHHHHHHHH
35.8629967540
452UbiquitinationLHENCVHKASRVSKG
HHHCCHHHHHHCCCC
27.8829967540
454PhosphorylationENCVHKASRVSKGGS
HCCHHHHHHCCCCCC
37.7127251275
458UbiquitinationHKASRVSKGGSFGRG
HHHHHCCCCCCCCCC
65.52-
461O-linked_GlycosylationSRVSKGGSFGRGTDL
HHCCCCCCCCCCCCC
32.9430379171
486PhosphorylationFLNCFTDYKDQGPRR
EEECCCCCCCCCHHH
17.26-
571PhosphorylationQVYSRLLTSGCQEGE
HHHHHHHHCCCCCCC
27.8920873877
572PhosphorylationVYSRLLTSGCQEGEH
HHHHHHHCCCCCCCH
37.2320873877
580UbiquitinationGCQEGEHKACFAELR
CCCCCCHHHHHHHHH
42.41-
597AcetylationFMNIRPVKLKNLILL
CCCCCCCCHHHHHHH
57.3225953088
693SumoylationHLLGQLRKPRPLVLD
HHHHCCCCCCCEEEC
54.71-
782PhosphorylationKAVDTICSFLKENCF
HHHHHHHHHHHHHCC
29.7524719451
785UbiquitinationDTICSFLKENCFRNS
HHHHHHHHHHCCCCC
44.8929967540
785AcetylationDTICSFLKENCFRNS
HHHHHHHHHHCCCCC
44.8926051181
792PhosphorylationKENCFRNSPIKVIKV
HHHCCCCCCEEEEEE
24.6025159151
795UbiquitinationCFRNSPIKVIKVVKG
CCCCCCEEEEEEEEC
41.0929967540
804PhosphorylationIKVVKGGSSAKGTAL
EEEEECCCCCCCCCC
35.4722468782
805PhosphorylationKVVKGGSSAKGTALR
EEEECCCCCCCCCCC
36.9622468782
807UbiquitinationVKGGSSAKGTALRGR
EECCCCCCCCCCCCC
59.7627667366
809PhosphorylationGGSSAKGTALRGRSD
CCCCCCCCCCCCCCC
23.0823403867
841PhosphorylationNKRAEIISEIRAQLE
HHHHHHHHHHHHHHH
32.4124719451
892UbiquitinationVDFDVLPAFDALGQL
CCCCCHHHHHHHHHH
15.7027667366
943UbiquitinationISRPTKLKSLIRLVK
HCCCHHHHHHHHHHH
44.7827667366
944PhosphorylationSRPTKLKSLIRLVKH
CCCHHHHHHHHHHHH
39.1924719451
958MethylationHWYQQCTKISKGRGS
HHHHHHHHHHCCCCC
53.2423644510
958UbiquitinationHWYQQCTKISKGRGS
HHHHHHHHHHCCCCC
53.2429967540
963MethylationCTKISKGRGSLPPQH
HHHHHCCCCCCCCCC
34.9554557763
965PhosphorylationKISKGRGSLPPQHGL
HHHCCCCCCCCCCCC
36.0224961811
1021UbiquitinationINYNAKDKTVGDFLK
EECCCCCCCHHHHHH
44.3929967540
1028UbiquitinationKTVGDFLKQQLQKPR
CCHHHHHHHHHCCCC
35.6730230243
1033UbiquitinationFLKQQLQKPRPIILD
HHHHHHCCCCCEEEC
52.1429967540
1059UbiquitinationARWDLLAKEAAACTS
HHHHHHHHHHHHHHH
48.1029967540
1084UbiquitinationPIQPWPVKAAV----
CCCCCCCCCCC----
26.92-

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 OAS3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OAS3_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 OAS3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IF6_HUMANEIF6physical
21903422
LYAR_HUMANLYARphysical
21903422
SPB1_HUMANFTSJ3physical
21903422
DHX30_HUMANDHX30physical
21903422
GNL3_HUMANGNL3physical
21903422
NOG1_HUMANGTPBP4physical
21903422
H12_HUMANHIST1H1Cphysical
21903422
IFRD2_HUMANIFRD2physical
21903422
PABP4_HUMANPABPC4physical
21903422
PPM1G_HUMANPPM1Gphysical
21903422
TOP1_HUMANTOP1physical
21903422
ZN622_HUMANZNF622physical
21903422

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 OAS3_HUMAN

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Related Literatures of Post-Translational Modification

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