PABP2_HUMAN - dbPTM
PABP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PABP2_HUMAN
UniProt AC Q86U42
Protein Name Polyadenylate-binding protein 2
Gene Name PABPN1
Organism Homo sapiens (Human).
Sequence Length 306
Subcellular Localization Nucleus . Cytoplasm . Nucleus speckle . Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the nucleus and the cytoplasm but predominantly found in the nucleus (PubMed:10688363). Its nuclear import may involve the
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 (By similarity). Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length (By similarity). Increases the affinity of poly(A) polymerase for RNA (By similarity). 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. [PubMed: 11371506 Binds to poly(A) and to poly(G) with high affinity (By similarity May protect the poly(A) tail from degradation (By similarity 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]
Protein Sequence MAAAAAAAAAAGAAGGRGSGPGRRRHLVPGAGGEAGEGAPGGAGDYGNGLESEELEPEELLLEPEPEPEPEEEPPRPRAPPGAPGPGPGSGAPGSQEEEEEPGLVEGDPGDGAIEDPELEAIKARVREMEEEAEKLKELQNEVEKQMNMSPPPGNAGPVIMSIEEKMEADARSIYVGNVDYGATAEELEAHFHGCGSVNRVTILCDKFSGHPKGFAYIEFSDKESVRTSLALDESLFRGRQIKVIPKRTNRPGISTTDRGFPRARYRARTTNYNSSRSRFYSGFNSRPRGRVYRGRARATSWYSPY
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		13.0520068231
9UbiquitinationAAAAAAAAAAGAAGG
HHHHHHHHHHHHCCC		7.9732142685
17DimethylationAAGAAGGRGSGPGRR
HHHHCCCCCCCCCCC		34.88-
17MethylationAAGAAGGRGSGPGRR
HHHHCCCCCCCCCCC		34.8830760587
19PhosphorylationGAAGGRGSGPGRRRH
HHCCCCCCCCCCCCC		40.2229255136
22PhosphorylationGGRGSGPGRRRHLVP
CCCCCCCCCCCCCCC		38.9733259812
23DimethylationGRGSGPGRRRHLVPG
CCCCCCCCCCCCCCC		35.28-
23MethylationGRGSGPGRRRHLVPG
CCCCCCCCCCCCCCC		35.2883108811
24MethylationRGSGPGRRRHLVPGA
CCCCCCCCCCCCCCC		35.96115382753
24DimethylationRGSGPGRRRHLVPGA
CCCCCCCCCCCCCCC		35.96-
46PhosphorylationAPGGAGDYGNGLESE
CCCCCCCCCCCCCCC		16.1518669648
52PhosphorylationDYGNGLESEELEPEE
CCCCCCCCCCCCHHH		41.2228464451
79UbiquitinationEEPPRPRAPPGAPGP
CCCCCCCCCCCCCCC		19.8133845483
90PhosphorylationAPGPGPGSGAPGSQE
CCCCCCCCCCCCCCC		34.6124043423
95UbiquitinationPGSGAPGSQEEEEEP
CCCCCCCCCCCCCCC		33.1033845483
95PhosphorylationPGSGAPGSQEEEEEP
CCCCCCCCCCCCCCC		33.1025159151
123 (in isoform 2)Ubiquitination-36.8721890473
123 (in isoform 1)Ubiquitination-36.8721890473
123UbiquitinationDPELEAIKARVREME
CHHHHHHHHHHHHHH		36.8721906983
135AcetylationEMEEEAEKLKELQNE
HHHHHHHHHHHHHHH		72.4226051181
135UbiquitinationEMEEEAEKLKELQNE
HHHHHHHHHHHHHHH		72.4223000965
137AcetylationEEEAEKLKELQNEVE
HHHHHHHHHHHHHHH		68.4026051181
137 (in isoform 2)Ubiquitination-68.4021890473
137UbiquitinationEEEAEKLKELQNEVE
HHHHHHHHHHHHHHH		68.4023000965
137 (in isoform 1)Ubiquitination-68.4021890473
145 (in isoform 1)Ubiquitination-61.0821890473
145UbiquitinationELQNEVEKQMNMSPP
HHHHHHHHHHCCCCC		61.0822817900
145 (in isoform 2)Ubiquitination-61.0821890473
150PhosphorylationVEKQMNMSPPPGNAG
HHHHHCCCCCCCCCC		29.2929255136
162PhosphorylationNAGPVIMSIEEKMEA
CCCCEEEEHHHHHHH		18.7423403867
184PhosphorylationGNVDYGATAEELEAH
EECCCCCCHHHHHHH		30.1821712546
197PhosphorylationAHFHGCGSVNRVTIL
HHHCCCCCCCEEEEE		21.9425159151
207UbiquitinationRVTILCDKFSGHPKG
EEEEEECCCCCCCCE		40.1923000965
207AcetylationRVTILCDKFSGHPKG
EEEEEECCCCCCCCE		40.1923954790
209PhosphorylationTILCDKFSGHPKGFA
EEEECCCCCCCCEEE		41.76-
213UbiquitinationDKFSGHPKGFAYIEF
CCCCCCCCEEEEEEE		62.0723000965
217PhosphorylationGHPKGFAYIEFSDKE
CCCCEEEEEEECCHH		9.95-
223UbiquitinationAYIEFSDKESVRTSL
EEEEECCHHHHHHHH		51.1733845483
227MethylationFSDKESVRTSLALDE
ECCHHHHHHHHHHCH		28.07-
235PhosphorylationTSLALDESLFRGRQI
HHHHHCHHHHCCCEE		32.2624275569
238Asymmetric dimethylarginineALDESLFRGRQIKVI
HHCHHHHCCCEEEEE		44.68-
238MethylationALDESLFRGRQIKVI
HHCHHHHCCCEEEEE		44.6812019537
240MethylationDESLFRGRQIKVIPK
CHHHHCCCEEEEECC		30.6916186511
247UbiquitinationRQIKVIPKRTNRPGI
CEEEEECCCCCCCCC		61.8124816145
256PhosphorylationTNRPGISTTDRGFPR
CCCCCCCCCCCCCCC		30.6928509920
257PhosphorylationNRPGISTTDRGFPRA
CCCCCCCCCCCCCCH		19.5328509920
259MethylationPGISTTDRGFPRARY
CCCCCCCCCCCCHHH		46.7030760599
259Asymmetric dimethylargininePGISTTDRGFPRARY
CCCCCCCCCCCCHHH		46.70-
263MethylationTTDRGFPRARYRART
CCCCCCCCHHHEEEC		29.4524129315
263Asymmetric dimethylarginineTTDRGFPRARYRART
CCCCCCCCHHHEEEC		29.45-
265Asymmetric dimethylarginineDRGFPRARYRARTTN
CCCCCCHHHEEECCC		23.81-
265MethylationDRGFPRARYRARTTN
CCCCCCHHHEEECCC		23.81134971
267Asymmetric dimethylarginineGFPRARYRARTTNYN
CCCCHHHEEECCCCC		16.43-
267MethylationGFPRARYRARTTNYN
CCCCHHHEEECCCCC		16.43134977
269Asymmetric dimethylargininePRARYRARTTNYNSS
CCHHHEEECCCCCCC		32.84-
269MethylationPRARYRARTTNYNSS
CCHHHEEECCCCCCC		32.84134983
277Asymmetric dimethylarginineTTNYNSSRSRFYSGF
CCCCCCCHHHCCCCC		31.50-
277MethylationTTNYNSSRSRFYSGF
CCCCCCCHHHCCCCC		31.5030760581
279MethylationNYNSSRSRFYSGFNS
CCCCCHHHCCCCCCC		33.1518600691
279Asymmetric dimethylarginineNYNSSRSRFYSGFNS
CCCCCHHHCCCCCCC		33.15-
282O-linked_GlycosylationSSRSRFYSGFNSRPR
CCHHHCCCCCCCCCC		33.9130379171
286O-linked_GlycosylationRFYSGFNSRPRGRVY
HCCCCCCCCCCCCEE		41.2130379171
287Asymmetric dimethylarginineFYSGFNSRPRGRVYR
CCCCCCCCCCCCEEC		26.49-
287MethylationFYSGFNSRPRGRVYR
CCCCCCCCCCCCEEC		26.4954557835
289Asymmetric dimethylarginineSGFNSRPRGRVYRGR
CCCCCCCCCCEECCC		44.43-
289MethylationSGFNSRPRGRVYRGR
CCCCCCCCCCEECCC		44.4354557825
291Asymmetric dimethylarginineFNSRPRGRVYRGRAR
CCCCCCCCEECCCCC		24.47-
291MethylationFNSRPRGRVYRGRAR
CCCCCCCCEECCCCC		24.4754557845
294Asymmetric dimethylarginineRPRGRVYRGRARATS
CCCCCEECCCCCCCC		25.84-
294MethylationRPRGRVYRGRARATS
CCCCCEECCCCCCCC		25.84135019
296Asymmetric dimethylarginineRGRVYRGRARATSWY
CCCEECCCCCCCCCC		16.35-
296MethylationRGRVYRGRARATSWY
CCCEECCCCCCCCCC		16.35135025
298Asymmetric dimethylarginineRVYRGRARATSWYSP
CEECCCCCCCCCCCC		36.72-
298MethylationRVYRGRARATSWYSP
CEECCCCCCCCCCCC		36.7224383217
300PhosphorylationYRGRARATSWYSPY-
ECCCCCCCCCCCCC-		17.7828348404
301PhosphorylationRGRARATSWYSPY--
CCCCCCCCCCCCC--		24.0324719451
303PhosphorylationRARATSWYSPY----
CCCCCCCCCCC----		10.2727251275
304PhosphorylationARATSWYSPY-----
CCCCCCCCCC-----		16.0928985074
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PABP2_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 PABP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMCA4_HUMANSMARCA4physical
11371506
DNJB4_HUMANDNAJB4physical
11371506
SNW1_HUMANSNW1physical
11371506
SNW1_HUMANSNW1genetic
11371506
TNPO1_HUMANTNPO1physical
10688363
IL7RA_HUMANIL7Rphysical
23151878
ARI2_HUMANARIH2physical
24486325
IF6_HUMANEIF6physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
164300Oculopharyngeal muscular dystrophy (OPMD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PABP2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-19 AND SER-150, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-19 AND SER-150, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-95 AND SER-150,AND MASS SPECTROMETRY.

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