PABP2_MOUSE - dbPTM
PABP2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PABP2_MOUSE
UniProt AC Q8CCS6
Protein Name Polyadenylate-binding protein 2
Gene Name Pabpn1
Organism Mus musculus (Mouse).
Sequence Length 302
Subcellular Localization Cytoplasm . Nucleus . Nucleus speckle . Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the nucleus and the cytoplasm but predominantly found in the nucleus. Its nuclear import may involve the nucleocytoplasmic
Protein Description Involved in the 3'-end formation of mRNA precursors (pre-mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length. Increases the affinity of poly(A) polymerase for RNA. Is also present at various stages of mRNA metabolism including nucleocytoplasmic trafficking and nonsense-mediated decay (NMD) of mRNA. Cooperates with SKIP to synergistically activate E-box-mediated transcription through MYOD1 and may regulate the expression of muscle-specific genes. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation. Subunit of the trimeric poly(A) tail exosome targeting (PAXT) complex, a complex that directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor MTREX, which links to RNA-binding protein adapters (By similarity)..
Protein Sequence MAAAAAAAAAAGAAGGRGSGPGRRRHLVPGAGGEAGEGDPGGAGDYGNGLESEELEPGELLPEPEPEEEPPRPRAPPGAPGPGPGSGAPGSQEEEEEPGLVEADPGDGAIEDPELEAIKARVREMEEEAEKLKELQNEVEKQMNMSPPPGNAGPVIMSLEEKMEADARSIYVGNVDYGATAEELEAHFHGCGSVNRVTILCDKFSGHPKGFAYIEFSDKESVRTSLALDESLFRGRQIKVIPKRTNRPGISTTDRGFPRSRYRARTTNYNSSRSRFYSGFNSRPRGRIYRGRARATSWYSPY
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
2Acetylation------MAAAAAAAA
------CHHHHHHHH		13.05-
17MethylationAAGAAGGRGSGPGRR
HHHHCCCCCCCCCCC		34.8824129315
19PhosphorylationGAAGGRGSGPGRRRH
HHCCCCCCCCCCCCC		40.2226824392
46PhosphorylationDPGGAGDYGNGLESE
CCCCCCCCCCCCCCC		16.1522802335
52PhosphorylationDYGNGLESEELEPGE
CCCCCCCCCCCCCCC		41.2229514104
86PhosphorylationAPGPGPGSGAPGSQE
CCCCCCCCCCCCCCC		34.6125159016
91PhosphorylationPGSGAPGSQEEEEEP
CCCCCCCCCCCCCCC		33.1027087446
115UbiquitinationGAIEDPELEAIKARV
CCCCCHHHHHHHHHH		7.0127667366
133UbiquitinationEEEAEKLKELQNEVE
HHHHHHHHHHHHHHH		68.40-
146PhosphorylationVEKQMNMSPPPGNAG
HHHHHCCCCCCCCCC		29.2925521595
158PhosphorylationNAGPVIMSLEEKMEA
CCCHHEEEHHHHHHH		22.8525619855
180PhosphorylationGNVDYGATAEELEAH
EECCCCCCHHHHHHH		30.18-
191GlutathionylationLEAHFHGCGSVNRVT
HHHHHCCCCCCCEEE		2.4924333276
231PhosphorylationTSLALDESLFRGRQI
HHHHHCHHHHCCCEE		32.26-
234Asymmetric dimethylarginineALDESLFRGRQIKVI
HHCHHHHCCCEEEEE		44.68-
234MethylationALDESLFRGRQIKVI
HHCHHHHCCCEEEEE		44.6812019541
236MethylationDESLFRGRQIKVIPK
CHHHHCCCEEEEECC		30.6916186507
239UbiquitinationLFRGRQIKVIPKRTN
HHCCCEEEEECCCCC		26.2727667366
255Asymmetric dimethylargininePGISTTDRGFPRSRY
CCCCCCCCCCCCHHC		46.70-
255MethylationPGISTTDRGFPRSRY
CCCCCCCCCCCCHHC		46.7030760601
259MethylationTTDRGFPRSRYRART
CCCCCCCCHHCEEEC		31.3530760595
259Asymmetric dimethylarginineTTDRGFPRSRYRART
CCCCCCCCHHCEEEC		31.35-
261MethylationDRGFPRSRYRARTTN
CCCCCCHHCEEECCC		26.66134973
261Asymmetric dimethylarginineDRGFPRSRYRARTTN
CCCCCCHHCEEECCC		26.66-
263MethylationGFPRSRYRARTTNYN
CCCCHHCEEECCCCC		19.24134979
263Asymmetric dimethylarginineGFPRSRYRARTTNYN
CCCCHHCEEECCCCC		19.24-
265MethylationPRSRYRARTTNYNSS
CCHHCEEECCCCCCC		32.84134985
265Asymmetric dimethylargininePRSRYRARTTNYNSS
CCHHCEEECCCCCCC		32.84-
273MethylationTTNYNSSRSRFYSGF
CCCCCCCHHHCCCCC		31.50-
273Asymmetric dimethylarginineTTNYNSSRSRFYSGF
CCCCCCCHHHCCCCC		31.50-
275MethylationNYNSSRSRFYSGFNS
CCCCCHHHCCCCCCC		33.1518966489
275Asymmetric dimethylarginineNYNSSRSRFYSGFNS
CCCCCHHHCCCCCCC		33.15-
283Asymmetric dimethylarginineFYSGFNSRPRGRIYR
CCCCCCCCCCCCEEC		26.49-
283MethylationFYSGFNSRPRGRIYR
CCCCCCCCCCCCEEC		26.4954557839
285Asymmetric dimethylarginineSGFNSRPRGRIYRGR
CCCCCCCCCCEECCC		46.01-
285MethylationSGFNSRPRGRIYRGR
CCCCCCCCCCEECCC		46.01-
287Asymmetric dimethylarginineFNSRPRGRIYRGRAR
CCCCCCCCEECCCCC		24.84-
287MethylationFNSRPRGRIYRGRAR
CCCCCCCCEECCCCC		24.8454557849
289PhosphorylationSRPRGRIYRGRARAT
CCCCCCEECCCCCCC		12.98-
290Asymmetric dimethylarginineRPRGRIYRGRARATS
CCCCCEECCCCCCCC		26.25-
290MethylationRPRGRIYRGRARATS
CCCCCEECCCCCCCC		26.25135021
292Asymmetric dimethylarginineRGRIYRGRARATSWY
CCCEECCCCCCCCCC		16.35-
292MethylationRGRIYRGRARATSWY
CCCEECCCCCCCCCC		16.35135027
294Asymmetric dimethylarginineRIYRGRARATSWYSP
CEECCCCCCCCCCCC		36.72-
294MethylationRIYRGRARATSWYSP
CEECCCCCCCCCCCC		36.7225058371
297PhosphorylationRGRARATSWYSPY--
CCCCCCCCCCCCC--		24.0324719451
299PhosphorylationRARATSWYSPY----
CCCCCCCCCCC----		10.2724719451
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 PABP2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PABP2_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 PABP2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PABP2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PABP2_MOUSE

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Related Literatures of Post-Translational Modification

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