Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Polyadenylate-binding protein 2

Gene

PABPN1

Organism
Bos taurus (Bovine)
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.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 10

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
  • Nucleus speckle 1 Publication

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). 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 (PubMed:10688363). Is exported to the cytoplasm by a carrier-mediated pathway that is independent of mRNA traffic. Nucleus; nuclear speckle. Colocalizes with SKIP and poly(A) RNA in nuclear speckles (By similarity).By similarity1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi119L → A: Strong defects in the stimulation of PAPOLA. 1 Publication1
Mutagenesisi120E → A: No defects in the stimulation of PAPOLA. 1 Publication1
Mutagenesisi122I → Q: Strong defects in the stimulation of PAPOLA. 1 Publication1
Mutagenesisi123K → A: No defects in the stimulation of PAPOLA. 1 Publication1
Mutagenesisi124A → S: Slight defects in the stimulation of PAPOLA. 1 Publication1
Mutagenesisi126V → S: No defects in the stimulation of PAPOLA. 1 Publication1
Mutagenesisi129M → A: Slight defects in the stimulation of PAPOLA. 1 Publication1
Mutagenesisi131E → A: Slight defects in the stimulation of PAPOLA. 1 Publication1
Mutagenesisi133A → S: No defects in the stimulation of PAPOLA. 1 Publication1
Mutagenesisi135K → A: No defects in the stimulation of PAPOLA. 1 Publication1
Mutagenesisi136L → A or S: Inactivates PAPOLA. 1 Publication1
Mutagenesisi143V → A: Slight defects in the stimulation of PAPOLA. 1 Publication1
Mutagenesisi175Y → A: At least 20% decrease in poly(A) binding; no change in nuclear targeting; distributed uniformly in the nucleoplasm; not detected in speckles. Same phenotypic effect; when associated with A-215. 2 Publications1
Mutagenesisi213K → Q: No changes in poly(A) affinity. 1 Publication1
Mutagenesisi215F → A: At least 20% decrease in poly(A); binding; no change in nuclear targeting, distributed uniformly in the nucleoplasm; not detected in speckles. Same phenotypic effect; when associated with A-175. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00000817102 – 306Polyadenylate-binding protein 2Add BLAST305

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Modified residuei17Omega-N-methylarginineBy similarity1
Modified residuei19PhosphoserineBy similarity1
Modified residuei52PhosphoserineBy similarity1
Modified residuei150PhosphoserineBy similarity1
Modified residuei235PhosphoserineBy similarity1
Modified residuei238Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei238Omega-N-methylarginine; alternate1 Publication1
Modified residuei259Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei259Omega-N-methylarginine; alternateBy similarity1
Modified residuei263Asymmetric dimethylarginine; alternate1 Publication1
Modified residuei263Omega-N-methylarginine; alternateBy similarity1
Modified residuei265Asymmetric dimethylarginine1 Publication1
Modified residuei267Asymmetric dimethylarginine1 Publication1
Modified residuei269Asymmetric dimethylarginine1 Publication1
Modified residuei277Asymmetric dimethylarginine1 Publication1
Modified residuei279Asymmetric dimethylarginine1 Publication1
Modified residuei287Asymmetric dimethylarginine1 Publication1
Modified residuei289Asymmetric dimethylarginine1 Publication1
Modified residuei291Asymmetric dimethylarginine1 Publication1
Modified residuei294Asymmetric dimethylarginine1 Publication1
Modified residuei296Asymmetric dimethylarginine1 Publication1
Modified residuei298Asymmetric dimethylarginine1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ28165.
PRIDEiQ28165.

PTM databases

iPTMnetiQ28165.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSBTAG00000006884.
ExpressionAtlasiQ28165. differential.

Interactioni

Subunit structurei

Monomer and homooligomer. Binds RNA as a monomer and oligomerizes when bound to poly(A). 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. Interacts with NUDT21/CPSF5. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PAPOLA, but only in presence of oligo(A) RNA. Interacts with transportin. May interact with SETX. 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 (By similarity).By similarity3 Publications

GO - Molecular functioni

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000021887.

Structurei

3D structure databases

ProteinModelPortaliQ28165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini172 – 249RRMPROSITE-ProRule annotationAdd BLAST78

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 145Interaction with SKIPBy similarityAdd BLAST144
Regioni119 – 147Stimulates PAPOLAAdd BLAST29
Regioni155 – 306Necessary for homooligomerizationBy similarityAdd BLAST152
Regioni286 – 306Interaction with PAPOLA1 PublicationAdd BLAST21

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili115 – 151Sequence 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.

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.
InParanoidiQ28165.
KOiK14396.
OMAiGRTTSWF.
OrthoDBiEOG091G0PAK.
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]

Sequencei

Sequence statusi: Complete.

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

Q28165-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGAP GGAGDYGNGL
60 70 80 90 100
ESEELEPEEL LLEPEPEPEP EEEPPRPRAP PGAPGPGPGS GAPGNQEEEE
110 120 130 140 150
ESGLVEGDPG DGAIEDPELE AIKARVREME EEAEKLKELQ NEVEKQMNMS
160 170 180 190 200
PPPGNAGPVI MSIEEKMEAD ARSIYVGNVD YGATAEELEA HFHGCGSVNR
210 220 230 240 250
VTILCDKFSG HPKGFAYIEF SDKESVRTSL ALDESLFRGR QIKVIPKRTN
260 270 280 290 300
RPGISTTDRG FPRARYRART TNYNSSRSRF YSGFNSRPRG RVYRGRARAT

SWYSPY
Length:306
Mass (Da):32,766
Last modified:January 23, 2007 - v3
Checksum:i11D5E5A555458246
GO

Mass spectrometryi

Molecular mass is 33253±0.5 Da from positions 2 - 306. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89969 mRNA. Translation: CAA62006.1.
BC133558 mRNA. Translation: AAI33559.1.
PIRiS59863.
RefSeqiNP_776994.1. NM_174569.2.
UniGeneiBt.5085.

Genome annotation databases

EnsembliENSBTAT00000021887; ENSBTAP00000021887; ENSBTAG00000006884.
GeneIDi282298.
KEGGibta:282298.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X89969 mRNA. Translation: CAA62006.1.
BC133558 mRNA. Translation: AAI33559.1.
PIRiS59863.
RefSeqiNP_776994.1. NM_174569.2.
UniGeneiBt.5085.

3D structure databases

ProteinModelPortaliQ28165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000021887.

PTM databases

iPTMnetiQ28165.

Proteomic databases

PaxDbiQ28165.
PRIDEiQ28165.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000021887; ENSBTAP00000021887; ENSBTAG00000006884.
GeneIDi282298.
KEGGibta:282298.

Organism-specific databases

CTDi8106.

Phylogenomic databases

eggNOGiKOG4209. Eukaryota.
ENOG4111PFV. LUCA.
GeneTreeiENSGT00390000001517.
HOGENOMiHOG000208465.
HOVERGENiHBG107480.
InParanoidiQ28165.
KOiK14396.
OMAiGRTTSWF.
OrthoDBiEOG091G0PAK.
TreeFamiTF105907.

Gene expression databases

BgeeiENSBTAG00000006884.
ExpressionAtlasiQ28165. differential.

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_BOVIN
AccessioniPrimary (citable) accession number: Q28165
Secondary accession number(s): A3KN38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 125 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, Direct protein sequencing, Reference proteome

Documents

  1. 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.