IFI2_MOUSE - dbPTM
IFI2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IFI2_MOUSE
UniProt AC Q9R002
Protein Name Interferon-activable protein 202
Gene Name Ifi202
Organism Mus musculus (Mouse).
Sequence Length 445
Subcellular Localization Cytoplasm . Nucleus . Accumulates first in the cytoplasm, and is translocated to the nucleus after a delay, where it is primarily chromatin-associated.
Protein Description Inhibits the transcriptional activity of several transcription factors, including NF-kappa-B p50 and p65, FOS, JUN, E2F1, E2F4, MYOD1 and myogenin. Has anti-apoptotic effects due to inhibition of the transcriptional activity of p53. Binds dsDNA in the cytosol. Is involved in innate immune response and has anti-inflammatory activity. Inhibits caspase activation in response to cytosolic DNA and inhibits the activation of the AIM2 inflammasome, probably by sequestering cytoplasmic DNA and preventing its being bound by AIM2..
Protein Sequence MSNRNLRSSTNSEFSEGQHQTPSSDSSGHGEDQPQASPGPNKKSHTPKKNISKGAVLHEKPMTVMVLTATEPFNYKEGKENMFHATVATESQYYRVKVFNMDLKEKFTENKFITISKYFNSSGILEINETATVSEAAPNQIIEVPKNIIRSAKETLKISKIKELDSGTLIYGVFAVEKKKVNDKSITFKIKDNEDNIKVVWDKKQHNINYEKGDKLQLFSFHLRKGNGKPILHSGNHSFIKGEKLLKESFEGDGYHKGPKQVVALKATKLFTYDSIKSKKMFHATVATDTEFFRVMVFEENLEKKFIPGNTIALSDYFGMYGSLAIHEYSSVSEVKSQNKEDSSSSDERLIEHLKICDLHLQTKERLVDGEFKVYRKSTGNNCICYGIWDDTGAMKVVVSGQLTSVNCEIGNTIRLVCFELTSNADEWFLRSTRYSYMEVIMPEK
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
8PhosphorylationMSNRNLRSSTNSEFS
CCCCCCCCCCCCCCC
44.6825777480
9PhosphorylationSNRNLRSSTNSEFSE
CCCCCCCCCCCCCCC
25.7725777480
10PhosphorylationNRNLRSSTNSEFSEG
CCCCCCCCCCCCCCC
43.9725777480
12PhosphorylationNLRSSTNSEFSEGQH
CCCCCCCCCCCCCCC
39.8625777480
15PhosphorylationSSTNSEFSEGQHQTP
CCCCCCCCCCCCCCC
36.4425777480
21PhosphorylationFSEGQHQTPSSDSSG
CCCCCCCCCCCCCCC
24.0225777480
23PhosphorylationEGQHQTPSSDSSGHG
CCCCCCCCCCCCCCC
50.6025777480
24PhosphorylationGQHQTPSSDSSGHGE
CCCCCCCCCCCCCCC
42.5925777480
26PhosphorylationHQTPSSDSSGHGEDQ
CCCCCCCCCCCCCCC
39.9225777480
27PhosphorylationQTPSSDSSGHGEDQP
CCCCCCCCCCCCCCC
39.5425777480
37PhosphorylationGEDQPQASPGPNKKS
CCCCCCCCCCCCCCC
25.7423684622
46PhosphorylationGPNKKSHTPKKNISK
CCCCCCCCCCCCCCC
43.8424719451
86PhosphorylationKENMFHATVATESQY
CCCCCEEEEECCCCE
11.3425293948
89PhosphorylationMFHATVATESQYYRV
CCEEEEECCCCEEEE
31.6525293948
91PhosphorylationHATVATESQYYRVKV
EEEEECCCCEEEEEE
21.0925293948
93PhosphorylationTVATESQYYRVKVFN
EEECCCCEEEEEEEC
11.5225293948
94PhosphorylationVATESQYYRVKVFNM
EECCCCEEEEEEECC
10.9925293948
268PhosphorylationQVVALKATKLFTYDS
HEEEEEEEECCCHHH
27.0522817900
272PhosphorylationLKATKLFTYDSIKSK
EEEEECCCHHHHCCC
36.5322817900
275PhosphorylationTKLFTYDSIKSKKMF
EECCCHHHHCCCCEE
22.8524719451
278PhosphorylationFTYDSIKSKKMFHAT
CCHHHHCCCCEEEEE
35.5222817900

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 IFI2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IFI2_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 IFI2_MOUSE !!

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

Oops, there are no PPI records of IFI2_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IFI2_MOUSE

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Related Literatures of Post-Translational Modification

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