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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

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: Ensembl
  • protein self-association Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-BTA-109688. Cleavage of Growing Transcript in the Termination Region.
R-BTA-72163. mRNA Splicing - Major Pathway.
R-BTA-72187. mRNA 3'-end processing.
R-BTA-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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 10

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm 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. 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 similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi119 – 1191L → A: Strong defects in the stimulation of PAPOLA. 1 Publication
Mutagenesisi120 – 1201E → A: No defects in the stimulation of PAPOLA. 1 Publication
Mutagenesisi122 – 1221I → Q: Strong defects in the stimulation of PAPOLA. 1 Publication
Mutagenesisi123 – 1231K → A: No defects in the stimulation of PAPOLA. 1 Publication
Mutagenesisi124 – 1241A → S: Slight defects in the stimulation of PAPOLA. 1 Publication
Mutagenesisi126 – 1261V → S: No defects in the stimulation of PAPOLA. 1 Publication
Mutagenesisi129 – 1291M → A: Slight defects in the stimulation of PAPOLA. 1 Publication
Mutagenesisi131 – 1311E → A: Slight defects in the stimulation of PAPOLA. 1 Publication
Mutagenesisi133 – 1331A → S: No defects in the stimulation of PAPOLA. 1 Publication
Mutagenesisi135 – 1351K → A: No defects in the stimulation of PAPOLA. 1 Publication
Mutagenesisi136 – 1361L → A or S: Inactivates PAPOLA. 1 Publication
Mutagenesisi143 – 1431V → A: Slight defects in the stimulation of PAPOLA. 1 Publication
Mutagenesisi175 – 1751Y → 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 Publications
Mutagenesisi213 – 2131K → Q: No changes in poly(A) affinity. 1 Publication
Mutagenesisi215 – 2151F → 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 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 306305Polyadenylate-binding protein 2PRO_0000081710Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei19 – 191PhosphoserineBy similarity
Modified residuei52 – 521PhosphoserineBy similarity
Modified residuei150 – 1501PhosphoserineBy similarity
Modified residuei235 – 2351PhosphoserineBy similarity
Modified residuei238 – 2381Asymmetric dimethylarginine; alternate1 Publication
Modified residuei238 – 2381Omega-N-methylarginine; alternate1 Publication
Modified residuei259 – 2591Asymmetric dimethylarginine1 Publication
Modified residuei263 – 2631Asymmetric dimethylarginine1 Publication
Modified residuei265 – 2651Asymmetric dimethylarginine1 Publication
Modified residuei267 – 2671Asymmetric dimethylarginine1 Publication
Modified residuei269 – 2691Asymmetric dimethylarginine1 Publication
Modified residuei277 – 2771Asymmetric dimethylarginine1 Publication
Modified residuei279 – 2791Asymmetric dimethylarginine1 Publication
Modified residuei287 – 2871Asymmetric dimethylarginine1 Publication
Modified residuei289 – 2891Asymmetric dimethylarginine1 Publication
Modified residuei291 – 2911Asymmetric dimethylarginine1 Publication
Modified residuei294 – 2941Asymmetric dimethylarginine1 Publication
Modified residuei296 – 2961Asymmetric dimethylarginine1 Publication
Modified residuei298 – 2981Asymmetric dimethylarginine1 Publication

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

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.By similarity3 Publications

GO - Molecular functioni

  • protein self-association Source: MGI

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000021887.

Structurei

3D structure databases

ProteinModelPortaliQ28165.
SMRiQ28165. Positions 169-248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini172 – 24978RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 145144Interacts with SKIPBy similarityAdd
BLAST
Regioni119 – 14729Stimulates PAPOLAAdd
BLAST
Regioni155 – 306152Necessary for homooligomerizationBy similarityAdd
BLAST
Regioni286 – 30621Interacts with PAPOLAAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili115 – 15137Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 1413Ala-richAdd
BLAST

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.
OrthoDBiEOG7K9K3Z.
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.
SMRiQ28165. Positions 169-248.
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.
OrthoDBiEOG7K9K3Z.
TreeFamiTF105907.

Enzyme and pathway databases

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

Gene expression databases

ExpressionAtlasiQ28165. baseline.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of genomic and cDNA clones encoding bovine poly(A) binding protein II."
    Nemeth A., Krause S., Blank D., Jenny A., Jenoe P., Lustig A., Wahle E.
    Nucleic Acids Res. 23:4034-4041(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 174-187, RNA-BINDING, FUNCTION IN PRE-MESSENGER POLYADENYLATION, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Aorta, Liver, Muzzle epithelium and Thymus.
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Fetal pons.
  3. "Unusual sites of arginine methylation in poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3."
    Smith J.J., Ruecknagel K.P., Schierhorn A., Tang J., Nemeth A., Linder M., Herschman H.R., Wahle E.
    J. Biol. Chem. 274:13229-13234(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-135; 140-207; 214-243 AND 248-306, MASS SPECTROMETRY, METHYLATION AT ARG-238; ARG-259; ARG-263; ARG-265; ARG-267; ARG-269; ARG-277; ARG-279; ARG-287; ARG-289; ARG-291; ARG-294; ARG-296 AND ARG-298, ACETYLATION AT ALA-2.
  4. "Trinucleotide expansions leading to an extended poly-L-alanine segment in the poly(A) binding protein PABPN1 cause fibril formation."
    Scheuermann T., Schulz B., Blume A., Wahle E., Rudolph R., Schwarz E.
    Protein Sci. 12:2685-2692(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-306, STRUCTURAL ANALYSIS OF POLY-ALA EXTENSION, IDENTIFICATION BY MASS SPECTROMETRY.
  5. "Deciphering the cellular pathway for transport of poly(A)-binding protein II."
    Calado A., Kutay U., Kuehn U., Wahle E., Carmo-Fonseca M.
    RNA 6:245-256(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-175 AND PHE-215, INTERACTION WITH TRANSPORTIN.
  6. "The RNA binding domains of the nuclear poly(A)-binding protein."
    Kuehn U., Nemeth A., Meyer S., Wahle E.
    J. Biol. Chem. 278:16916-16925(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PAPOLA STIMULATION, RNA-BINDING, HOMOOLIGOMERIZATION, MUTAGENESIS OF TYR-175; LYS-213 AND PHE-215.
  7. "Stimulation of poly(A) polymerase through a direct interaction with the nuclear poly(A) binding protein allosterically regulated by RNA."
    Kerwitz Y., Kuehn U., Lilie H., Knoth A., Scheuermann T., Friedrich H., Schwarz E., Wahle E.
    EMBO J. 22:3705-3714(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PAPOLA STIMULATION, MUTAGENESIS OF LEU-119; GLU-120; ILE-122; LYS-123; ALA-124; VAL-126; MET-129; GLU-131; ALA-133; LYS-135; LEU-136 AND VAL-143, INTERACTION WITH PAPOLA.

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: June 8, 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, 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.