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Q86U42 (PABP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PABPN1
Synonyms:PAB2, PABP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length306 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.11

Subunit structure

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. Ref.6 Ref.10 Ref.11 Ref.13 Ref.15

Subcellular location

Nucleus By similarity. Cytoplasm. 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. Ref.8 Ref.9 Ref.12 Ref.15

Tissue specificity

Ubiquitous.

Domain

The RRM domain is essential for specific adenine bases recognition in the poly(A) tail but not sufficient for poly(A) binding By similarity.

Post-translational modification

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

Polymorphism

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.

Involvement in disease

Oculopharyngeal muscular dystrophy (OPMD) [MIM:164300]: A form of late-onset slowly progressive myopathy characterized by eyelid ptosis, dysphagia and, sometimes by other cranial and limb-muscle involvement.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.24

Miscellaneous

Intranuclear filamentous inclusions or "aggregates" are detected in the myocytes of patients; these inclusions contain PABPN1, ubiquitin, subunits of the proteasome and poly(A) RNA. The association of the expanded polyalanine mutations together with the capability to oligomerize may induce these 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.

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Sequence caution

The sequence CAD62310.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
Triplet repeat expansion
   DiseaseDisease mutation
   DomainCoiled coil
   LigandRNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA processing

Traceable author statement Ref.1. Source: ProtInc

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA 3'-end processing

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

modification by virus of host mRNA processing

Traceable author statement. Source: Reactome

modulation by virus of host morphology or physiology

Traceable author statement. Source: Reactome

modulation by virus of host process

Traceable author statement. Source: Reactome

muscle contraction

Traceable author statement Ref.1. Source: ProtInc

poly(A)+ mRNA export from nucleus

Inferred from mutant phenotype PubMed 19364924. Source: UniProtKB

termination of RNA polymerase II transcription

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 19364924. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay Ref.15. Source: UniProtKB

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.13. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SNW1Q135735EBI-1226435,EBI-632715

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86U42-1)

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.
Isoform 2 (identifier: Q86U42-2)

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.
Isoform 3 (identifier: Q92843-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 306305Polyadenylate-binding protein 2
PRO_0000081711

Regions

Domain172 – 24978RRM
Region2 – 145144Interacts with SKIP
Region119 – 14729Stimulates PAPOLA By similarity
Region155 – 306152Necessary for homooligomerization
Region286 – 30621Interacts with PAPOLA By similarity
Coiled coil115 – 15137 Potential
Compositional bias2 – 1413Ala-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.17 Ref.19 Ref.21 Ref.22 Ref.23
Modified residue191Phosphoserine Ref.19 Ref.21
Modified residue951Phosphoserine Ref.16 Ref.19 Ref.21
Modified residue1501Phosphoserine Ref.16 Ref.18 Ref.19 Ref.21
Modified residue2381Asymmetric dimethylarginine; alternate By similarity
Modified residue2381Omega-N-methylarginine; alternate By similarity
Modified residue2591Asymmetric dimethylarginine By similarity
Modified residue2631Asymmetric dimethylarginine By similarity
Modified residue2651Asymmetric dimethylarginine By similarity
Modified residue2671Asymmetric dimethylarginine By similarity
Modified residue2691Asymmetric dimethylarginine By similarity
Modified residue2771Asymmetric dimethylarginine By similarity
Modified residue2791Asymmetric dimethylarginine By similarity
Modified residue2871Asymmetric dimethylarginine By similarity
Modified residue2891Asymmetric dimethylarginine By similarity
Modified residue2911Asymmetric dimethylarginine By similarity
Modified residue2941Asymmetric dimethylarginine By similarity
Modified residue2961Asymmetric dimethylarginine By similarity
Modified residue2981Asymmetric dimethylarginine By similarity

Natural variations

Alternative sequence295 – 2962GR → SG in isoform 2.
VSP_009847
Alternative sequence297 – 30610Missing in isoform 2.
VSP_009848
Natural variant61A → AAAA. Ref.24
VAR_018179

Experimental info

Mutagenesis213 – 2208Missing: Abolishes self-association, protein aggregation and cell death. Ref.10
Mutagenesis301 – 3066Missing: Abolishes self-association, protein aggregation and cell death. Ref.10

Secondary structure

.................... 306
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2E5B0AEFEA5AFBC3

FASTA30632,749
        10         20         30         40         50         60 
MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGAP GGAGDYGNGL ESEELEPEEL 

        70         80         90        100        110        120 
LLEPEPEPEP EEEPPRPRAP PGAPGPGPGS GAPGSQEEEE EPGLVEGDPG DGAIEDPELE 

       130        140        150        160        170        180 
AIKARVREME EEAEKLKELQ NEVEKQMNMS PPPGNAGPVI MSIEEKMEAD ARSIYVGNVD 

       190        200        210        220        230        240 
YGATAEELEA HFHGCGSVNR VTILCDKFSG HPKGFAYIEF SDKESVRTSL ALDESLFRGR 

       250        260        270        280        290        300 
QIKVIPKRTN RPGISTTDRG FPRARYRART TNYNSSRSRF YSGFNSRPRG RVYRGRARAT 


SWYSPY 

« Hide

Isoform 2 [UniParc].

Checksum: E1AD14BDD69833DD
Show »

FASTA29631,497
Isoform 3 (BCL2L2-PABPN1) [UniParc].

See Q92843.

References

« Hide 'large scale' references
[1]"Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy."
Brais B., Bouchard J.-P., Xie Y.-G., Rochefort D.L., Chretien N., Tome F.M.S., Lafreniere R.G., Rommens J.M., Uyama E., Nohira O., Blumen S., Korcyn A.D., Heutink P., Mathieu J., Duranceau A., Codere F., Fardeau M., Rouleau G.A.
Nat. Genet. 18:164-167(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), POLYMORPHISM OF POLY-ALA REGION, DISEASE.
[2]Erratum
Brais B., Bouchard J.-P., Xie Y.-G., Rochefort D.L., Chretien N., Tome F.M.S., Lafreniere R.G., Rommens J.M., Uyama E., Nohira O., Blumen S., Korcyn A.D., Heutink P., Mathieu J., Duranceau A., Codere F., Fardeau M., Rouleau G.A.
Nat. Genet. 19:404-404(1998)
[3]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal brain.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Skin.
[6]"Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery."
Chen Z., Li Y., Krug R.M.
EMBO J. 18:2273-2283(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], ASSOCIATION WITH CPSF AND NS/NS1, INTERACTION WITH NS/NS1.
Tissue: Cervix carcinoma.
[7]Bienvenut W.V.
Submitted (APR-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-17 AND 228-238, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[8]"Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA."
Calado A., Tome F.M.S., Brais B., Rouleau G.A., Kuehn U., Wahle E., Carmo-Fonseca M.
Hum. Mol. Genet. 9:2321-2328(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[9]"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: SUBCELLULAR LOCATION, NUCLEOCYTOPLASMIC SHUTTLING.
[10]"Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death."
Fan X., Dion P., Laganiere J., Brais B., Rouleau G.A.
Hum. Mol. Genet. 10:2341-2351(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL DEATH, HOMOOLIGOMERIZATION, MUTAGENESIS OF 213-LYS--PHE-220 AND 301-SER--TYR-306.
[11]"The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression."
Kim Y.-J., Noguchi S., Hayashi Y.K., Tsukahara T., Shimizu T., Arahata K.
Hum. Mol. Genet. 10:1129-1139(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MYOGENIC DIFFERENTIATION, ASSOCIATION WITH SKIP AND MYOD1, INTERACTION WITH SKIP.
[12]"An aggregate-prone conformational epitope in trinucleotide repeat diseases."
Sugaya K., Matsubara S., Miyamoto K., Kawata A., Hayashi H.
NeuroReport 14:2331-2335(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[13]"Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization."
Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M.
J. Biol. Chem. 279:35788-35797(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NUDT21/CPSF5.
[14]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[16]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-95 AND SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-95 AND SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Oculopharyngeal muscular dystrophy (OPMD) due to a small duplication in the PABPN1 gene."
van der Sluijs B.M., van Engelen B.G.M., Hoefsloot L.H.
Hum. Mutat. 21:553-553(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OPMD ALA-6 INS, DISEASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9592.1. [Q86U42-1]
RefSeqNP_004634.1. NM_004643.3. [Q86U42-1]
UniGeneHs.707712.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3B4DX-ray2.00A167-254[»]
3B4MX-ray2.82A/B/C/D167-254[»]
3UCGX-ray1.95A167-254[»]
ProteinModelPortalQ86U42.
SMRQ86U42. Positions 167-253.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113777. 21 interactions.
DIPDIP-37968N.
IntActQ86U42. 26 interactions.
MINTMINT-89761.
STRING9606.ENSP00000216727.

PTM databases

PhosphoSiteQ86U42.

Polymorphism databases

DMDM46403176.

Proteomic databases

MaxQBQ86U42.
PaxDbQ86U42.
PRIDEQ86U42.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216727; ENSP00000216727; ENSG00000100836. [Q86U42-1]
ENST00000397276; ENSP00000380446; ENSG00000100836. [Q86U42-2]
GeneID8106.
KEGGhsa:8106.
UCSCuc001wjj.3. human. [Q86U42-2]
uc001wjk.3. human. [Q86U42-1]

Organism-specific databases

CTD8106.
GeneCardsGC14P023789.
GeneReviewsPABPN1.
HGNCHGNC:8565. PABPN1.
HPAHPA000637.
MIM164300. phenotype.
602279. gene.
neXtProtNX_Q86U42.
Orphanet270. Oculopharyngeal muscular dystrophy.
PharmGKBPA32891.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG238057.
HOGENOMHOG000208465.
HOVERGENHBG107480.
InParanoidQ86U42.
KOK14396.
OMARGRTTSW.
OrthoDBEOG7K9K3Z.
PhylomeDBQ86U42.
TreeFamTF105907.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpressQ86U42.
BgeeQ86U42.
CleanExHS_PABPN1.
GenevestigatorQ86U42.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ86U42.
GeneWikiPABPN1.
GenomeRNAi8106.
NextBio30755.
PMAP-CutDBQ86U42.
PROQ86U42.
SOURCESearch...

Entry information

Entry namePABP2_HUMAN
AccessionPrimary (citable) accession number: Q86U42
Secondary accession number(s): D3DS49, O43484
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 118 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM