ISG15_MOUSE - dbPTM
ISG15_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ISG15_MOUSE
UniProt AC Q64339
Protein Name Ubiquitin-like protein ISG15
Gene Name Isg15
Organism Mus musculus (Mouse).
Sequence Length 161
Subcellular Localization Cytoplasm. Secreted. Exists in three distinct states: free within the cell, released into the extracellular space, or conjugated to target proteins..
Protein Description Ubiquitin-like protein which plays a key role in the innate immune response to viral infection either via its conjugation to a target protein (ISGylation) or via its action as a free or unconjugated protein. ISGylation involves a cascade of enzymatic reactions involving E1, E2, and E3 enzymes which catalyze the conjugation of ISG15 to a lysine residue in the target protein. Its target proteins include SERPINA3G/SPI2A, JAK1, MAPK3/ERK1, PLCG1, TRIM25, STAT5A, MAPK1/ERK2 and globin. Can also isgylate: DDX58/RIG-I which inhibits its function in antiviral signaling response and EIF4E2 which enhances its cap structure-binding activity and translation-inhibition activity. Exhibits antiviral activity towards both DNA and RNA viruses, including influenza A and B virus, sindbis virus (SV) and herpes simplex type-1 (HHV-1). Plays a significant role in the control of neonatal Chikungunya virus (CHIKV) infection by acting as a putative immunomodulator of proinflammatory cytokines. Protects mice against the consequences of Chikungunya virus infection by downregulating the pathogenic cytokine response, often denoted as the cytokine storm. Plays a role in erythroid differentiation. The secreted form of ISG15 can: induce natural killer cell proliferation, act as a chemotactic factor for neutrophils and act as a IFN-gamma-inducing cytokine playing an essential role in antimycobacterial immunity..
Protein Sequence MAWDLKVKMLGGNDFLVSVTNSMTVSELKKQIAQKIGVPAFQQRLAHQTAVLQDGLTLSSLGLGPSSTVMLVVQNCSEPLSILVRNERGHSNIYEVFLTQTVDTLKKKVSQREQVHEDQFWLSFEGRPMEDKELLGEYGLKPQCTVIKHLRLRGGGGDQCA
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
6Ubiquitination--MAWDLKVKMLGGN
--CCCEEEEEEECCC
37.02-
6Acetylation--MAWDLKVKMLGGN
--CCCEEEEEEECCC
37.0222826441
20PhosphorylationNDFLVSVTNSMTVSE
CCEEEEEECCCCHHH
17.6728576409
35UbiquitinationLKKQIAQKIGVPAFQ
HHHHHHHHHCCHHHH
32.19-
76S-nitrosocysteineVMLVVQNCSEPLSIL
EEEEEECCCCCEEEE
2.45-
76S-nitrosylationVMLVVQNCSEPLSIL
EEEEEECCCCCEEEE
2.4518606809
106UbiquitinationTQTVDTLKKKVSQRE
HHHHHHHHHHHHHHH
53.28-
141UbiquitinationLLGEYGLKPQCTVIK
HHHHCCCCCCCEEEE
28.78-
141AcetylationLLGEYGLKPQCTVIK
HHHHCCCCCCCEEEE
28.7822826441
144S-nitrosocysteineEYGLKPQCTVIKHLR
HCCCCCCCEEEEEEE
4.44-
144S-nitrosylationEYGLKPQCTVIKHLR
HCCCCCCCEEEEEEE
4.4418606809
148UbiquitinationKPQCTVIKHLRLRGG
CCCCEEEEEEEECCC
32.05-

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 ISG15_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ISG15_MOUSE !!

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 ISG15_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBP5_MOUSEUsp5physical
14673145

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ISG15_MOUSE

loading...

Related Literatures of Post-Translational Modification

TOP