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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 (By similarity).By similarity

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) binding Source: MGI
  • poly(A) RNA binding Source: MGI
  • protein self-association 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
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1859158. Pabpn1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Nucleus speckle By similarity

  • 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 transport receptor transportin and a RAN-GTP-sensitive import mechanism. It is exported to the cytoplasm by a carrier-mediated pathway that is independent of mRNA traffic. Nucleus; nuclear speckle (By similarity). Colocalizes with SKIP and poly(A) RNA in nuclear speckles (By similarity).By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • nuclear inclusion body Source: UniProtKB
  • nuclear speck Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
Complete GO annotation...

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).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

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

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

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

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

Cross-referencesi

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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ8CCS6.
PhosphoSitePlusiQ8CCS6.

Proteomic databases

PaxDbiQ8CCS6.
PRIDEiQ8CCS6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi8106.
MGIiMGI:1859158. Pabpn1.

Phylogenomic databases

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

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.

Miscellaneous databases

ChiTaRSiPabpn1. mouse.
PROiQ8CCS6.
SOURCEiSearch...

Gene expression databases

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

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPABP2_MOUSE
AccessioniPrimary (citable) accession number: Q8CCS6
Secondary accession number(s): O35935
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 121 of the entry and version 3 of the sequence. [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
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.