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Protein

Polyadenylate-binding protein 2

Gene

PABPN1

Organism
Homo sapiens (Human)
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 (By similarity). Stimulates poly(A) polymerase (PAPOLA) conferring processivity on the poly(A) tail elongation reaction and controls also the poly(A) tail length (By similarity). Increases the affinity of poly(A) polymerase for RNA (By similarity). 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 (PubMed:11371506). Binds to poly(A) and to poly(G) with high affinity (By similarity). May protect the poly(A) tail from degradation (By similarity). 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 (PubMed:27871484).By similarity2 Publications

Miscellaneous

The association of the expanded polyalanine mutations together with the capability to oligomerize may induce intranuclear inclusions and cell death. Expanded polyalanine mutations may either result from unequal crossing over during germ cell homologous recombination or from DNA slippage. The pathogenic mechanisms mediated by polyalanine expansion mutations may be either a general disruption of cellular RNA metabolism due to the trapping by the inclusions of PABPN1, mRNAs and/or nuclear proteins, resulting in the induction of cell death; or may change the normal muscle cell differentiation.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionRNA-binding
Biological processmRNA processing

Enzyme and pathway databases

ReactomeiR-HSA-109688 Cleavage of Growing Transcript in the Termination Region
R-HSA-168315 Inhibition of Host mRNA Processing and RNA Silencing
R-HSA-72163 mRNA Splicing - Major Pathway
R-HSA-72187 mRNA 3'-end processing
R-HSA-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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiHostDB:ENSG00000100836.10
HGNCiHGNC:8565 PABPN1
MIMi602279 gene
neXtProtiNX_Q86U42

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

Involvement in diseasei

Oculopharyngeal muscular dystrophy (OPMD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of late-onset slowly progressive myopathy characterized by eyelid ptosis, dysphagia and, sometimes by other cranial and limb-muscle involvement.
See also OMIM:164300

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi213 – 220Missing : Abolishes self-association, protein aggregation and cell death. 1 Publication8
Mutagenesisi301 – 306Missing : Abolishes self-association, protein aggregation and cell death. 1 Publication6

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi8106
GeneReviewsiPABPN1
MalaCardsiPABPN1
MIMi164300 phenotype
OpenTargetsiENSG00000100836
Orphaneti270 Oculopharyngeal muscular dystrophy
PharmGKBiPA32891

Polymorphism and mutation databases

BioMutaiPABPN1
DMDMi46403176

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000817112 – 306Polyadenylate-binding protein 2Add BLAST305

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei17Omega-N-methylarginineBy similarity1
Modified residuei19PhosphoserineCombined sources1
Modified residuei52PhosphoserineCombined sources1
Modified residuei95PhosphoserineCombined sources1
Modified residuei150PhosphoserineCombined sources1
Modified residuei235PhosphoserineCombined sources1
Modified residuei238Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei238Omega-N-methylarginine; alternateBy similarity1
Modified residuei259Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei259Omega-N-methylarginine; alternateCombined sources1
Modified residuei263Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei263Omega-N-methylarginine; alternateCombined sources1
Modified residuei265Asymmetric dimethylarginineBy similarity1
Modified residuei267Asymmetric dimethylarginineBy similarity1
Modified residuei269Asymmetric dimethylarginineBy similarity1
Modified residuei277Asymmetric dimethylarginineBy similarity1
Modified residuei279Asymmetric dimethylarginineBy similarity1
Modified residuei287Asymmetric dimethylarginineBy similarity1
Modified residuei289Asymmetric dimethylarginineBy similarity1
Modified residuei291Asymmetric dimethylarginineBy similarity1
Modified residuei294Asymmetric dimethylarginineBy similarity1
Modified residuei296Asymmetric dimethylarginineBy similarity1
Modified residuei298Asymmetric dimethylarginineBy similarity1
Isoform 3 (identifier: Q92843-2)
Modified residuei177Phosphoserine1
Modified residuei262Phosphoserine1
Modified residuei286Omega-N-methylarginine1
Modified residuei290Omega-N-methylarginine1

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

EPDiQ86U42
PaxDbiQ86U42
PeptideAtlasiQ86U42
PRIDEiQ86U42
ProteomicsDBi69766
69767 [Q86U42-2]
TopDownProteomicsiQ86U42-1 [Q86U42-1]

PTM databases

iPTMnetiQ86U42
PhosphoSitePlusiQ86U42

Miscellaneous databases

PMAP-CutDBiQ86U42

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000100836
CleanExiHS_PABPN1
ExpressionAtlasiQ86U42 baseline and differential
GenevisibleiQ86U42 HS

Organism-specific databases

HPAiHPA000637

Interactioni

Subunit structurei

May interact with SETX (PubMed:21700224). Monomer and homooligomer. 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 transportin. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Association in a ternary complex with CPSF4 and influenza A virus NS1 blocks pre-mRNAs processing, thereby preventing 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. 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 made of accessory factors, such as PABPN1, ZFC3H1 and MTREX (PubMed:27871484). Interacts with ZFC3H1 in a RNase-insensitive manner (PubMed:27871484).By similarity6 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi113777, 45 interactors
DIPiDIP-37968N
IntActiQ86U42, 37 interactors
MINTiQ86U42
STRINGi9606.ENSP00000216727

Structurei

Secondary structure

1306
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi167 – 171Combined sources5
Beta strandi173 – 178Combined sources6
Helixi185 – 192Combined sources8
Helixi193 – 195Combined sources3
Beta strandi198 – 206Combined sources9
Beta strandi208 – 211Combined sources4
Beta strandi214 – 222Combined sources9
Helixi224 – 229Combined sources6
Helixi230 – 232Combined sources3
Beta strandi243 – 246Combined sources4
Turni247 – 250Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3B4DX-ray2.00A167-254[»]
3B4MX-ray2.82A/B/C/D167-254[»]
3UCGX-ray1.95A167-254[»]
ProteinModelPortaliQ86U42
SMRiQ86U42
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ86U42

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 145Interaction with SKIP1 PublicationAdd BLAST144
Regioni119 – 147Stimulates PAPOLABy similarityAdd BLAST29
Regioni155 – 306Necessary for homooligomerizationAdd BLAST152
Regioni286 – 306Interaction with PAPOLABy similarityAdd 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.By similarity

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4209 Eukaryota
ENOG4111PFV LUCA
GeneTreeiENSGT00390000001517
HOGENOMiHOG000208465
HOVERGENiHBG107480
InParanoidiQ86U42
KOiK14396
OMAiGRTTSWF
OrthoDBiEOG091G0PAK
PhylomeDBiQ86U42
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

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86U42-1) [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 AGGEAGEGAP GGAGDYGNGL
60 70 80 90 100
ESEELEPEEL LLEPEPEPEP EEEPPRPRAP PGAPGPGPGS GAPGSQEEEE
110 120 130 140 150
EPGLVEGDPG 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):32,749
Last modified:January 23, 2007 - v3
Checksum:i2E5B0AEFEA5AFBC3
GO
Isoform 2 (identifier: Q86U42-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     295-296: GR → SG
     297-306: Missing.

Note: May be due to a competing donor splice site.
Show »
Length:296
Mass (Da):31,497
Checksum:iE1AD14BDD69833DD
GO
Isoform 3 (identifier: Q92843-2) [UniParc]FASTAAdd to basket
Also known as: BCL2L2-PABPN1
The sequence of this isoform can be found in the external entry Q92843.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Based on a readthrough transcript which may produce a BCL2L2-PABPN1 fusion protein. No experimental confirmation available.
Length:333
Mass (Da):37,171
GO

Sequence cautioni

The sequence CAD62310 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Polymorphismi

The poly-Ala region of PABPN1 is polymorphic (6-7 repeats) in the population and is expanded to 8-13 repeats in OPMD patients. Compound heterozygotes for (GCG)9 mutation and a (GCG)7 allele result in earlier onset and more severe clinical manifestations of the disease.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0181796A → AAAA. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_009847295 – 296GR → SG in isoform 2. 1 Publication2
Alternative sequenceiVSP_009848297 – 306Missing in isoform 2. 1 Publication10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026029 Genomic DNA Translation: AAC39596.1
BX247976 mRNA Translation: CAD62310.1 Different initiation.
CH471078 Genomic DNA Translation: EAW66167.1
CH471078 Genomic DNA Translation: EAW66168.1
BC010939 mRNA Translation: AAH10939.1
CCDSiCCDS9592.1 [Q86U42-1]
RefSeqiNP_004634.1, NM_004643.3 [Q86U42-1]
UniGeneiHs.707712

Genome annotation databases

EnsembliENST00000216727; ENSP00000216727; ENSG00000100836 [Q86U42-1]
ENST00000397276; ENSP00000380446; ENSG00000100836 [Q86U42-2]
GeneIDi8106
KEGGihsa:8106
UCSCiuc001wjj.4 human [Q86U42-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Triplet repeat expansion

Similar proteinsi

Entry informationi

Entry nameiPABP2_HUMAN
AccessioniPrimary (citable) accession number: Q86U42
Secondary accession number(s): D3DS49, O43484
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 156 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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