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Protein

Polyadenylate-binding protein 2

Gene

PABPN1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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 (PubMed:7479061, PubMed:10481015). Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length (PubMed:12637556). Increases the affinity of poly(A) polymerase for RNA (PubMed:12637556, PubMed:12853485). 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 (By similarity). Binds to poly(A) and to poly(G) with high affinity (PubMed:7479061, PubMed:12637556). May protect the poly(A) tail from degradation (PubMed:7479061). 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 (By similarity).By similarity3 Publications

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionRNA-binding
Biological processmRNA processing

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

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

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 baseline

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). Component of the poly(A) tail exosome targeting (PAXT) complex composed of PABPN1, ZFC3H1 and MTREX. Interacts with ZFC3H1 in a RNase-insensitive manner (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
SMRiQ28165
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.

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
InterProiView protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
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

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

Similar proteinsi

Entry informationi

Entry nameiPABP2_BOVIN
AccessioniPrimary (citable) accession number: Q28165
Secondary accession number(s): A3KN38
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 136 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, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health