PCBP2_MOUSE - dbPTM
PCBP2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCBP2_MOUSE
UniProt AC Q61990
Protein Name Poly(rC)-binding protein 2
Gene Name Pcbp2
Organism Mus musculus (Mouse).
Sequence Length 362
Subcellular Localization Nucleus. Cytoplasm.
Protein Description Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. Major cellular poly(rC)-binding protein. Binds also poly(rU). Negatively regulates cellular antiviral responses mediated by MAVS signaling. It acts as an adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore triggering MAVS ubiquitinationa and degradation (By similarity)..
Protein Sequence MDTGVIEGGLNVTLTIRLLMHGKEVGSIIGKKGESVKKMREESGARINISEGNCPERIITLAGPTNAIFKAFAMIIDKLEEDISSSMTNSTAASRPPVTLRLVVPASQCGSLIGKGGCKIKEIRESTGAQVQVAGDMLPNSTERAITIAGIPQSIIECVKQICVVMLESPPKGVTIPYRPKPSSSPVIFAGGQDRYSTGSDSASFPHTTPSMCLNPDLEGPPLEAYTIQGQYAIPQPDLTKLHQLAMQQSHFPMTHGNTGFSGIESSSPEVKGYWAGLDASAQTTSHELTIPNDLIGCIIGRQGAKINEIRQMSGAQIKIANPVEGSTDRQVTITGSAASISLAQYLINVRLSSETGGMGSS
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
23UbiquitinationIRLLMHGKEVGSIIG
EEHHHCCHHHHHHHC
34.25-
23AcetylationIRLLMHGKEVGSIIG
EEHHHCCHHHHHHHC
34.2521680727
50PhosphorylationSGARINISEGNCPER
HCCCEEECCCCCCCC
34.66-
54S-nitrosocysteineINISEGNCPERIITL
EEECCCCCCCCEEEE
5.64-
54S-nitrosylationINISEGNCPERIITL
EEECCCCCCCCEEEE
5.6420925432
109S-palmitoylationLVVPASQCGSLIGKG
EEEEHHHHHHHHCCC
3.5628526873
109S-nitrosylationLVVPASQCGSLIGKG
EEEEHHHHHHHHCCC
3.5622178444
109GlutathionylationLVVPASQCGSLIGKG
EEEEHHHHHHHHCCC
3.5624333276
109S-nitrosocysteineLVVPASQCGSLIGKG
EEEEHHHHHHHHCCC
3.56-
111PhosphorylationVPASQCGSLIGKGGC
EEHHHHHHHHCCCCC
25.1727566939
115UbiquitinationQCGSLIGKGGCKIKE
HHHHHHCCCCCEEEH
45.17-
115MalonylationQCGSLIGKGGCKIKE
HHHHHHCCCCCEEEH
45.1726320211
115AcetylationQCGSLIGKGGCKIKE
HHHHHHCCCCCEEEH
45.17-
119UbiquitinationLIGKGGCKIKEIRES
HHCCCCCEEEHHHHH
61.15-
154PhosphorylationTIAGIPQSIIECVKQ
HHCCCCHHHHHHHHH
21.8522006019
158S-palmitoylationIPQSIIECVKQICVV
CCHHHHHHHHHHHEE
3.0628526873
158S-nitrosylationIPQSIIECVKQICVV
CCHHHHHHHHHHHEE
3.0622178444
158S-nitrosocysteineIPQSIIECVKQICVV
CCHHHHHHHHHHHEE
3.06-
160UbiquitinationQSIIECVKQICVVML
HHHHHHHHHHHEEEE
45.67-
169PhosphorylationICVVMLESPPKGVTI
HHEEEECCCCCCCCC
42.4126643407
175PhosphorylationESPPKGVTIPYRPKP
CCCCCCCCCCCCCCC
25.5527742792
175 (in isoform 2)Phosphorylation-25.5526239621
178PhosphorylationPKGVTIPYRPKPSSS
CCCCCCCCCCCCCCC
35.3827742792
178 (in isoform 2)Phosphorylation-35.3825777480
181UbiquitinationVTIPYRPKPSSSPVI
CCCCCCCCCCCCCEE
48.83-
181MalonylationVTIPYRPKPSSSPVI
CCCCCCCCCCCCCEE
48.8326320211
181AcetylationVTIPYRPKPSSSPVI
CCCCCCCCCCCCCEE
48.8323806337
183PhosphorylationIPYRPKPSSSPVIFA
CCCCCCCCCCCEEEE
49.9627742792
183 (in isoform 2)Phosphorylation-49.9625777480
184PhosphorylationPYRPKPSSSPVIFAG
CCCCCCCCCCEEEEC
47.3826824392
184 (in isoform 2)Phosphorylation-47.3825777480
185 (in isoform 2)Phosphorylation-27.7625777480
185PhosphorylationYRPKPSSSPVIFAGG
CCCCCCCCCEEEECC
27.7626824392
195 (in isoform 2)Phosphorylation-21.2925777480
196 (in isoform 2)Phosphorylation-20.9025777480
201 (in isoform 2)Phosphorylation-49.9525777480
209 (in isoform 2)Phosphorylation-15.4425777480
232PhosphorylationAYTIQGQYAIPQPDL
EEEEECCCCCCCCCH
17.2122817900
250PhosphorylationHQLAMQQSHFPMTHG
HHHHHHHCCCCCCCC
15.3725619855
255PhosphorylationQQSHFPMTHGNTGFS
HHCCCCCCCCCCCCC
27.2025619855
259PhosphorylationFPMTHGNTGFSGIES
CCCCCCCCCCCCCCC
44.1725619855
262PhosphorylationTHGNTGFSGIESSSP
CCCCCCCCCCCCCCC
39.9625619855
266PhosphorylationTGFSGIESSSPEVKG
CCCCCCCCCCCCCCC
33.9123984901
267PhosphorylationGFSGIESSSPEVKGY
CCCCCCCCCCCCCCE
36.8025521595
268PhosphorylationFSGIESSSPEVKGYW
CCCCCCCCCCCCCEE
34.0726824392
298GlutathionylationIPNDLIGCIIGRQGA
CCCCHHHHHHCCCCC
1.3024333276
306MalonylationIIGRQGAKINEIRQM
HHCCCCCCHHHHHHH
53.5426320211
314PhosphorylationINEIRQMSGAQIKIA
HHHHHHHCCCEEEEC
23.7329514104
319UbiquitinationQMSGAQIKIANPVEG
HHCCCEEEECCCCCC
24.5622790023
353PhosphorylationYLINVRLSSETGGMG
HHHHCCCCCCCCCCC
18.6320415495
354PhosphorylationLINVRLSSETGGMGS
HHHCCCCCCCCCCCC
43.7120415495
356PhosphorylationNVRLSSETGGMGSS-
HCCCCCCCCCCCCC-
40.7729233185
361PhosphorylationSETGGMGSS------
CCCCCCCCC------
24.7925521595
362PhosphorylationETGGMGSS-------
CCCCCCCC-------
38.2125521595

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 PCBP2_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCBP2_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 PCBP2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRIC3_HUMANPRICKLE3physical
26496610
UBP11_HUMANUSP11physical
26496610
FARP1_HUMANFARP1physical
26496610
ARIP4_HUMANRAD54L2physical
26496610
ZFY26_HUMANZFYVE26physical
26496610
PLPL8_HUMANPNPLA8physical
26496610
NOP58_HUMANNOP58physical
26496610
SAV1_HUMANSAV1physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCBP2_MOUSE

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Related Literatures of Post-Translational Modification

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