Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Polyadenylate-binding protein 2  

UniProtKB / Swiss-Prot ID :  PABP2_HUMAN

Gene Name (Synonyms) : 
PABPN1, PAB2, PABP2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (By similarity). Cytoplasm. Note=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 tra 

Protein Function :  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 (By similarity). 

Protein Sequence MAAAAAAAAAAGAAGGRGSGPGRRRHLVPGAGGEAGEGAPGGAGDYGNGLESEELEPEELLLEPEPEPEP...
Predicted Secondary Structure CCCHHHHHHHHCCCCCCCCCCCCEEECCCCCCCCCCCCCCCCCCCCCCCCCHHHCCHHHHCCCCCCCCCC...
Protein Variant
LocationDescription
6A -> AAAA. VAR_018179
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAAAA
---CCCHHH
13.05UniProtKB
Link-
19PhosphoserineGGRGSGPGR
CCCCCCCCC
40.22HPRD
Link-
19PhosphoserineGGRGSGPGR
CCCCCCCCC
40.22Phosphositeplus
Link-
19Phosphoserine.GGRGSGPGR
CCCCCCCCC
40.22UniProtKB
Link-
46PhosphotyrosineGAGDYGNGL
CCCCCCCCC
16.15HPRD
Link-
52PhosphoserineNGLESEELE
CCCCHHHCC
41.22HPRD
Link-
52PhosphoserineNGLESEELE
CCCCHHHCC
41.22Phosphositeplus
Link-
52PhosphoserineNGLESEELE
CCCCHHHCC
41.22SysPTM
Link-
52Phosphoserine.NGLESEELE
CCCCHHHCC
41.22UniProtKB
Link-
90PhosphoserinePGPGSGAPG
CCCCCCCCH
34.61HPRD
Link-
90PhosphoserinePGPGSGAPG
CCCCCCCCH
34.61Phosphositeplus
Link-
90PhosphoserinePGPGSGAPG
CCCCCCCCH
34.61SysPTM
Link-
95PhosphoserineGAPGSQEEE
CCCHHHCCC
33.10HPRD
Link-
95PhosphoserineGAPGSQEEE
CCCHHHCCC
33.10PhosphoELM
Link-
95PhosphoserineGAPGSQEEE
CCCHHHCCC
33.10Phosphositeplus
Link-
95PhosphoserineGAPGSQEEE
CCCHHHCCC
33.10SysPTM
Link-
95Phosphoserine.GAPGSQEEE
CCCHHHCCC
33.10UniProtKB
Link-
111Caspase cleavage aspartic acidGDPGDGAIE
CCCCCCCCC
49.06Phosphositeplus
Link-
123Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LEAIKARVR
CCCCCCCCC
36.87Phosphositeplus
Link-
137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AEKLKELQN
CCCCCCCCC
68.40Phosphositeplus
Link-
145Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NEVEKQMNM
CCCCCCCCC
61.08Phosphositeplus
Link-
150PhosphoserineQMNMSPPPG
CCCCCCCCC
29.29HPRD
Link-
150PhosphoserineQMNMSPPPG
CCCCCCCCC
29.29Phosphositeplus
Link-
150PhosphoserineQMNMSPPPG
CCCCCCCCC
29.29SysPTM
Link-
150Phosphoserine.QMNMSPPPG
CCCCCCCCC
29.29UniProtKB
Link-
207N6-acetyllysineILCDKFSGH
EEECCCCCC
40.19HPRD
Link
207N6-acetyllysineILCDKFSGH
EEECCCCCC
40.19Phosphositeplus
Link
2595-methylarginineSTTDRGFPR
CCHHHCCCC
46.70HPRD
Link-
259N2,N2-dimethylarginineSTTDRGFPR
CCHHHCCCC
46.70Phosphositeplus
Link-
2635-methylarginineRGFPRARYR
HCCCCCCCC
29.45HPRD
Link-
263N2,N2-dimethylarginineRGFPRARYR
HCCCCCCCC
29.45Phosphositeplus
Link-
2655-methylarginineFPRARYRAR
CCCCCCCCC
23.81HPRD
Link-
265N2,N2-dimethylarginineFPRARYRAR
CCCCCCCCC
23.81Phosphositeplus
Link-
2675-methylarginineRARYRARTT
CCCCCCCCC
16.43HPRD
Link-
267N2,N2-dimethylarginineRARYRARTT
CCCCCCCCC
16.43Phosphositeplus
Link-
2695-methylarginineRYRARTTNY
CCCCCCCCC
32.84HPRD
Link-
269N2,N2-dimethylarginineRYRARTTNY
CCCCCCCCC
32.84Phosphositeplus
Link-
2775-methylarginineYNSSRSRFY
CCCCCCCCC
31.50HPRD
Link-
277N2,N2-dimethylarginineYNSSRSRFY
CCCCCCCCC
31.50MeMo
Link-
277N2,N2-dimethylarginineYNSSRSRFY
CCCCCCCCC
31.50Phosphositeplus
Link-
2795-methylarginineSSRSRFYSG
CCCCCCCCC
33.15HPRD
Link-
279N2,N2-dimethylarginineSSRSRFYSG
CCCCCCCCC
33.15MeMo
Link-
279N2,N2-dimethylarginineSSRSRFYSG
CCCCCCCCC
33.15Phosphositeplus
Link-
2875-methylarginineGFNSRPRGR
CCCCCCCCC
26.49HPRD
Link-
287N2,N2-dimethylarginineGFNSRPRGR
CCCCCCCCC
26.49Phosphositeplus
Link-
2895-methylarginineNSRPRGRVY
CCCCCCCCC
44.43HPRD
Link-
289N2,N2-dimethylarginineNSRPRGRVY
CCCCCCCCC
44.43Phosphositeplus
Link-
2915-methylarginineRPRGRVYRG
CCCCCCCCC
24.47HPRD
Link-
291N2,N2-dimethylarginineRPRGRVYRG
CCCCCCCCC
24.47Phosphositeplus
Link-
2945-methylarginineGRVYRGRAR
CCCCCCCCC
25.84HPRD
Link-
294N2,N2-dimethylarginineGRVYRGRAR
CCCCCCCCC
25.84Phosphositeplus
Link-
2965-methylarginineVYRGRARAT
CCCCCCCCC
16.35HPRD
Link-
296N2,N2-dimethylarginineVYRGRARAT
CCCCCCCCC
16.35Phosphositeplus
Link-
2985-methylarginineRGRARATSW
CCCCCCCCC
36.72HPRD
Link-
298N2,N2-dimethylarginineRGRARATSW
CCCCCCCCC
36.72Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
1433Z_HUMANphysical interactionMINT-3297301MINT15161933
STAU1_HUMANin vitroHPRD:03787HPRD15121898
RPAB1_HUMANENSP00000216727STRING
SF3A1_HUMANENSP00000216727STRING
SMD3_HUMANENSP00000216727STRING
NH2L1_HUMANENSP00000216727STRING
RPAB2_HUMANENSP00000216727STRING
PHF5A_HUMANENSP00000216727STRING
PAPOA_HUMANENSP00000216727STRING
SFRS5_HUMANENSP00000216727STRING
CSTF1_HUMANENSP00000216727STRING
RPB3_HUMANENSP00000216727STRING
HNRPL_HUMANENSP00000216727STRING
RU17_HUMANENSP00000216727STRING
SF3A2_HUMANENSP00000216727STRING
RPB9_HUMANENSP00000216727STRING
SFRS9_HUMANENSP00000216727STRING
LSM2_HUMANENSP00000216727STRING
PM14_HUMANENSP00000216727STRING
GRAN_HUMANENSP00000216727STRING
CPSF3_HUMANENSP00000216727STRING
SNRPA_HUMANENSP00000216727STRING
SFRS6_HUMANENSP00000216727STRING
T2FA_HUMANENSP00000216727STRING
RU2B_HUMANENSP00000216727STRING
SF04_HUMANENSP00000216727STRING
FUS_HUMANENSP00000216727STRING
RU2A_HUMANENSP00000216727STRING
SFRS1_HUMANENSP00000216727STRING
U5S1_HUMANENSP00000216727STRING
WDR57_HUMANENSP00000216727STRING
DNJC8_HUMANENSP00000216727STRING
PRP6_HUMANENSP00000216727STRING
RUXF_HUMANENSP00000216727STRING
RUXF_HUMANENSP00000216727STRING
RUXF_HUMANENSP00000216727STRING
PRP16_HUMANENSP00000216727STRING
TXN4A_HUMANENSP00000216727STRING
SF3B4_HUMANENSP00000216727STRING
RUXG_HUMANENSP00000216727STRING
RPB4_HUMANENSP00000216727STRING
REN3B_HUMANENSP00000216727STRING
U2AF1_HUMANENSP00000216727STRING
SFRS2_HUMANENSP00000216727STRING
RPAB3_HUMANENSP00000216727STRING
PCF11_HUMANENSP00000216727STRING
CPSF2_HUMANENSP00000216727STRING
CPSF5_HUMANENSP00000216727STRING
SMD1_HUMANENSP00000216727STRING
RPB7_HUMANENSP00000216727STRING
PRP8_HUMANENSP00000216727STRING
PRP17_HUMANENSP00000216727STRING
HNRPR_HUMANENSP00000216727STRING
CLP1_HUMANENSP00000216727STRING
CD2B2_HUMANENSP00000216727STRING
PCBP1_HUMANENSP00000216727STRING
SF3B3_HUMANENSP00000216727STRING
U2AF2_HUMANENSP00000216727STRING
DDX23_HUMANENSP00000216727STRING
RPB2_HUMANENSP00000216727STRING
HNRPD_HUMANENSP00000216727STRING
RPB1_HUMANENSP00000216727STRING
CSTF3_HUMANENSP00000216727STRING
ROA0_HUMANENSP00000216727STRING
U520_HUMANENSP00000216727STRING
SF3B2_HUMANENSP00000216727STRING
SMC1A_HUMANENSP00000216727STRING
RPAB5_HUMANENSP00000216727STRING
HNRPM_HUMANENSP00000216727STRING
SFRS7_HUMANENSP00000216727STRING
NCBP2_HUMANENSP00000216727STRING
THOC4_HUMANENSP00000216727STRING
SF3B1_HUMANENSP00000216727STRING
HNRPC_HUMANENSP00000216727STRING
CPSF1_HUMANENSP00000216727STRING
ROA1_HUMANENSP00000216727STRING
SMD2_HUMANENSP00000216727STRING
RPAB4_HUMANENSP00000216727STRING
RBM5_HUMANENSP00000216727STRING
CPSF7_HUMANENSP00000216727STRING
HNRPF_HUMANENSP00000216727STRING
T2FB_HUMANENSP00000216727STRING
PCBP2_HUMANENSP00000216727STRING
HNRPK_HUMANENSP00000216727STRING
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Disease Reference
Kegg disease
OMIM disease
164300Oculopharyngeal muscular dystrophy (OPMD)
Drug Reference
There are no disease associations of PTM sites.
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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
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures