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Protein

Polyadenylate-binding protein 2

Gene

Pabpn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 SKIV2L2/MTR4, which links to RNA-binding protein adapters (By similarity).By similarity

GO - Molecular functioni

  • poly(A) binding Source: MGI
  • protein self-association Source: MGI
  • RNA binding Source: MGI
  • RNA polymerase binding Source: UniProtKB

GO - Biological processi

  • cellular response to lipopolysaccharide Source: UniProtKB
  • MAPK cascade Source: UniProtKB
  • mRNA polyadenylation Source: MGI
  • poly(A)+ mRNA export from nucleus Source: MGI
  • positive regulation of polynucleotide adenylyltransferase activity Source: UniProtKB

Keywordsi

Molecular functionRNA-binding
Biological processmRNA processing

Enzyme and pathway databases

ReactomeiR-MMU-109688. Cleavage of Growing Transcript in the Termination Region.
R-MMU-72163. mRNA Splicing - Major Pathway.
R-MMU-72187. mRNA 3'-end processing.
R-MMU-77595. Processing of Intronless Pre-mRNAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyadenylate-binding protein 2
Short name:
PABP-2
Short name:
Poly(A)-binding protein 2
Alternative name(s):
Nuclear poly(A)-binding protein 1
Poly(A)-binding protein II
Short name:
PABII
Polyadenylate-binding nuclear protein 1
Gene namesi
Name:Pabpn1
Synonyms:Pab2, Pabp2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1859158. Pabpn1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000817122 – 302Polyadenylate-binding protein 2Add BLAST301

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei17Omega-N-methylarginineCombined sources1
Modified residuei19PhosphoserineBy similarity1
Modified residuei52PhosphoserineBy similarity1
Modified residuei91PhosphoserineBy similarity1
Modified residuei146PhosphoserineBy similarity1
Modified residuei231PhosphoserineBy similarity1
Modified residuei234Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei234Omega-N-methylarginine; alternateBy similarity1
Modified residuei255Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei255Omega-N-methylarginine; alternateBy similarity1
Modified residuei259Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei259Omega-N-methylarginine; alternateBy similarity1
Modified residuei261Asymmetric dimethylarginineBy similarity1
Modified residuei263Asymmetric dimethylarginineBy similarity1
Modified residuei265Asymmetric dimethylarginineBy similarity1
Modified residuei273Asymmetric dimethylarginineBy similarity1
Modified residuei275Asymmetric dimethylarginineBy similarity1
Modified residuei283Asymmetric dimethylarginineBy similarity1
Modified residuei285Asymmetric dimethylarginineBy similarity1
Modified residuei287Asymmetric dimethylarginineBy similarity1
Modified residuei290Asymmetric dimethylarginineBy similarity1
Modified residuei292Asymmetric dimethylarginineBy similarity1
Modified residuei294Asymmetric dimethylarginineBy similarity1

Post-translational modificationi

Arginine dimethylation is asymmetric and involves PRMT1 and PRMT3. It does not influence the RNA binding properties (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ8CCS6.
PRIDEiQ8CCS6.

PTM databases

iPTMnetiQ8CCS6.
PhosphoSitePlusiQ8CCS6.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSMUSG00000022194.
CleanExiMM_PABPN1.
ExpressionAtlasiQ8CCS6. baseline and differential.
GenevisibleiQ8CCS6. MM.

Interactioni

Subunit structurei

Monomer and homooligomer. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Binds RNA as a monomer and oligomerizes when bound to poly(A). Interacts with PAPOLA, but only in presence of oligo(A) RNA. Interacts with NUDT21/CPSF5 and transportin. Associates in a ternary complex with CPSF4 and NS/NS1 and interaction with NS/NS1, blocks nuclear export of host cell mRNAs. Associates in a single complex with SKIP and MYOD1 and interacts with SKIP in differentiated myocytes. May interact with SETX (By similarity). Interacts (via RRM domain and C-terminal arginine-rich region) with ZFP36 (via hypophosphorylated form); this interaction occurs in the nucleus in a RNA-independent manner, decreases in presence of single-stranded poly(A) RNA-oligomer and in a p38-dependent-manner and may down-regulated RNA poly(A) polymerase activity (PubMed:22844456). Component of the poly(A) tail exosome targeting (PAXT) complex composed of PABPN1, ZFC3H1 and SKIV2L2/MTR. Interacts with ZFC3H1 in a RNase-insensitive manner (By similarity).By similarity1 Publication

GO - Molecular functioni

  • protein self-association Source: MGI
  • RNA polymerase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi207596. 2 interactors.
IntActiQ8CCS6. 2 interactors.
MINTiMINT-1867341.
STRINGi10090.ENSMUSP00000022808.

Structurei

3D structure databases

ProteinModelPortaliQ8CCS6.
SMRiQ8CCS6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini168 – 245RRMPROSITE-ProRule annotationAdd BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 141Interaction with SKIPBy similarityAdd BLAST140
Regioni115 – 143Stimulates PAPOLABy similarityAdd BLAST29
Regioni255 – 302Strong poly(A) affinity and self-associationBy similarityAdd BLAST48
Regioni282 – 302Interaction with PAPOLABy similarityAdd BLAST21

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili111 – 147Sequence analysisAdd BLAST37

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2 – 14Ala-richAdd BLAST13

Domaini

The RRM domain is essential for specific adenine bases recognition in the poly(A) tail but not sufficient for poly(A) binding.By similarity

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4209. Eukaryota.
ENOG4111PFV. LUCA.
GeneTreeiENSGT00390000001517.
HOGENOMiHOG000208465.
HOVERGENiHBG107480.
InParanoidiQ8CCS6.
KOiK14396.
PhylomeDBiQ8CCS6.
TreeFamiTF105907.

Family and domain databases

InterProiView protein in InterPro
IPR034911. PABP2.
IPR035979. RBD_domain_sf.
IPR000504. RRM_dom.
PANTHERiPTHR44316. PTHR44316. 1 hit.
PfamiView protein in Pfam
PF00076. RRM_1. 1 hit.
SMARTiView protein in SMART
SM00360. RRM. 1 hit.
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiView protein in PROSITE
PS50102. RRM. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CCS6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGDP GGAGDYGNGL
60 70 80 90 100
ESEELEPGEL LPEPEPEEEP PRPRAPPGAP GPGPGSGAPG SQEEEEEPGL
110 120 130 140 150
VEADPGDGAI EDPELEAIKA RVREMEEEAE KLKELQNEVE KQMNMSPPPG
160 170 180 190 200
NAGPVIMSLE EKMEADARSI YVGNVDYGAT AEELEAHFHG CGSVNRVTIL
210 220 230 240 250
CDKFSGHPKG FAYIEFSDKE SVRTSLALDE SLFRGRQIKV IPKRTNRPGI
260 270 280 290 300
STTDRGFPRS RYRARTTNYN SSRSRFYSGF NSRPRGRIYR GRARATSWYS

PY
Length:302
Mass (Da):32,297
Last modified:January 23, 2007 - v3
Checksum:i2F0F6F7CC19C1986
GO
Isoform 2 (identifier: Q8CCS6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     291-292: GR → SG
     293-302: Missing.

Note: May be due to a competing donor splice site.
Show »
Length:292
Mass (Da):31,044
Checksum:i0874042BA4A60A2A
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_009849291 – 292GR → SG in isoform 2. 1 Publication2
Alternative sequenceiVSP_009850293 – 302Missing in isoform 2. 1 Publication10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93050 Genomic DNA. Translation: AAC00210.1.
AK032172 mRNA. Translation: BAC27741.1.
BC055866 mRNA. Translation: AAH55866.1.
CCDSiCCDS27104.1. [Q8CCS6-1]
RefSeqiNP_062275.1. NM_019402.2. [Q8CCS6-1]
UniGeneiMm.7723.

Genome annotation databases

EnsembliENSMUST00000022808; ENSMUSP00000022808; ENSMUSG00000022194. [Q8CCS6-1]
ENSMUST00000116476; ENSMUSP00000112177; ENSMUSG00000022194. [Q8CCS6-2]
GeneIDi54196.
KEGGimmu:54196.
UCSCiuc007txg.2. mouse. [Q8CCS6-1]
uc007txi.2. mouse. [Q8CCS6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiPABP2_MOUSE
AccessioniPrimary (citable) accession number: Q8CCS6
Secondary accession number(s): O35935
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 126 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot