OAS2_HUMAN - dbPTM
OAS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OAS2_HUMAN
UniProt AC P29728
Protein Name 2'-5'-oligoadenylate synthase 2
Gene Name OAS2 {ECO:0000312|HGNC:HGNC:8087}
Organism Homo sapiens (Human).
Sequence Length 719
Subcellular Localization Cytoplasm . Cytoplasm, perinuclear region .
Protein Description Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. [PubMed: 10464285]
Protein Sequence MGNGESQLSSVPAQKLGWFIQEYLKPYEECQTLIDEMVNTICDVLQEPEQFPLVQGVAIGGSYGRKTVLRGNSDGTLVLFFSDLKQFQDQKRSQRDILDKTGDKLKFCLFTKWLKNNFEIQKSLDGFTIQVFTKNQRISFEVLAAFNALSLNDNPSPWIYRELKRSLDKTNASPGEFAVCFTELQQKFFDNRPGKLKDLILLIKHWHQQCQKKIKDLPSLSPYALELLTVYAWEQGCRKDNFDIAEGVRTVLELIKCQEKLCIYWMVNYNFEDETIRNILLHQLQSARPVILDPVDPTNNVSGDKICWQWLKKEAQTWLTSPNLDNELPAPSWNVLPAPLFTTPGHLLDKFIKEFLQPNKCFLEQIDSAVNIIRTFLKENCFRQSTAKIQIVRGGSTAKGTALKTGSDADLVVFHNSLKSYTSQKNERHKIVKEIHEQLKAFWREKEEELEVSFEPPKWKAPRVLSFSLKSKVLNESVSFDVLPAFNALGQLSSGSTPSPEVYAGLIDLYKSSDLPGGEFSTCFTVLQRNFIRSRPTKLKDLIRLVKHWYKECERKLKPKGSLPPKYALELLTIYAWEQGSGVPDFDTAEGFRTVLELVTQYQQLCIFWKVNYNFEDETVRKFLLSQLQKTRPVILDPAEPTGDVGGGDRWCWHLLAKEAKEWLSSPCFKDGTGNPIPPWKVPTMQTPGSCGARIHPIVNEMFSSRSHRILNNNSKRNF
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
2N-myristoyl glycine------MGNGESQLS
------CCCCCCHHC		51.34-
2Myristoylation------MGNGESQLS
------CCCCCCHHC		51.342211721
67PhosphorylationGGSYGRKTVLRGNSD
CCCCCCCEEEECCCC		24.3424719451
73PhosphorylationKTVLRGNSDGTLVLF
CEEEECCCCCEEEEE		40.0027499020
76PhosphorylationLRGNSDGTLVLFFSD
EECCCCCEEEEEECC		20.7728348404
112UbiquitinationLKFCLFTKWLKNNFE
HHHHHHHHHHHHCHH		43.10-
134UbiquitinationFTIQVFTKNQRISFE
EEEEEEECCCCEEHH		39.35-
169UbiquitinationELKRSLDKTNASPGE
HHHHHHHCCCCCCCC		49.31-
187UbiquitinationCFTELQQKFFDNRPG
EHHHHHHHHHCCCCC		34.73-
195UbiquitinationFFDNRPGKLKDLILL
HHCCCCCHHHHHHHH		55.86-
212UbiquitinationHWHQQCQKKIKDLPS
HHHHHHHHHHCCCCC		65.18-
250PhosphorylationDIAEGVRTVLELIKC
CHHHHHHHHHHHHHC		27.34-
360AcetylationKEFLQPNKCFLEQID
HHHHCCCCCHHHHHH		32.807406481
360 (in isoform 2)Ubiquitination-32.8021906983
360 (in isoform 1)Ubiquitination-32.8021906983
360UbiquitinationKEFLQPNKCFLEQID
HHHHCCCCCHHHHHH		32.802190698
368PhosphorylationCFLEQIDSAVNIIRT
CHHHHHHHHHHHHHH		35.4330108239
378AcetylationNIIRTFLKENCFRQS
HHHHHHHHHCCCCCC		42.5619608861
378UbiquitinationNIIRTFLKENCFRQS
HHHHHHHHHCCCCCC		42.56-
385PhosphorylationKENCFRQSTAKIQIV
HHCCCCCCCCEEEEE		26.5228348404
388UbiquitinationCFRQSTAKIQIVRGG
CCCCCCCEEEEECCC		34.92-
396PhosphorylationIQIVRGGSTAKGTAL
EEEECCCCCCCCEEC		28.1927067055
399UbiquitinationVRGGSTAKGTALKTG
ECCCCCCCCEECCCC		57.81-
404UbiquitinationTAKGTALKTGSDADL
CCCCEECCCCCCCCE		48.66-
405PhosphorylationAKGTALKTGSDADLV
CCCEECCCCCCCCEE		42.6530108239
407PhosphorylationGTALKTGSDADLVVF
CEECCCCCCCCEEEE		34.5530108239
417PhosphorylationDLVVFHNSLKSYTSQ
CEEEEECCHHHHCCC		28.7130108239
419UbiquitinationVVFHNSLKSYTSQKN
EEEECCHHHHCCCHH		41.03-
423PhosphorylationNSLKSYTSQKNERHK
CCHHHHCCCHHHHHH		30.81-
425UbiquitinationLKSYTSQKNERHKIV
HHHHCCCHHHHHHHH		61.62-
433UbiquitinationNERHKIVKEIHEQLK
HHHHHHHHHHHHHHH		55.1919608861
433AcetylationNERHKIVKEIHEQLK
HHHHHHHHHHHHHHH		55.1919608861
440UbiquitinationKEIHEQLKAFWREKE
HHHHHHHHHHHHHCH		41.03-
466PhosphorylationWKAPRVLSFSLKSKV
CCCCCEEEEECCCCC		15.2122167270
468PhosphorylationAPRVLSFSLKSKVLN
CCCEEEEECCCCCCC		31.3522167270
470UbiquitinationRVLSFSLKSKVLNES
CEEEEECCCCCCCCC		47.21-
472UbiquitinationLSFSLKSKVLNESVS
EEEECCCCCCCCCCC		49.51-
622UbiquitinationFEDETVRKFLLSQLQ
CCCHHHHHHHHHHHH		35.71-
661UbiquitinationHLLAKEAKEWLSSPC
HHHHHHHHHHHCCCC		50.98-
684PhosphorylationIPPWKVPTMQTPGSC
CCCCCCCCCCCCCCC		25.5427251275
687PhosphorylationWKVPTMQTPGSCGAR
CCCCCCCCCCCCCCC		20.8527251275
690PhosphorylationPTMQTPGSCGARIHP
CCCCCCCCCCCCCHH		15.5827251275
704PhosphorylationPIVNEMFSSRSHRIL
HHHHHHHHCCCHHHC		24.4327251275
705PhosphorylationIVNEMFSSRSHRILN
HHHHHHHCCCHHHCC		26.9127251275
715PhosphorylationHRILNNNSKRNF---
HHHCCCCCCCCC---		34.8126714015
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 OAS2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OAS2_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 OAS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
KGP1_HUMANPRKG1physical
28514442
ACACA_HUMANACACAphysical
28514442
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 OAS2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-378 AND LYS-433, AND MASSSPECTROMETRY.
Myristoylation
ReferencePubMed
"Differential expression and distinct structure of 69- and 100-kDaforms of 2-5A synthetase in human cells treated with interferon.";
Marie I., Svab J., Robert N., Galabru J., Hovanessian A.G.;
J. Biol. Chem. 265:18601-18607(1990).
Cited for: MYRISTOYLATION AT GLY-2, AND SUBCELLULAR LOCATION.

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