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Q86U42

- PABP2_HUMAN

UniProt

Q86U42 - PABP2_HUMAN

Protein

Polyadenylate-binding protein 2

Gene

PABPN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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 By similarity.By similarity

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. RNA binding Source: ProtInc

    GO - Biological processi

    1. gene expression Source: Reactome
    2. modification by virus of host mRNA processing Source: Reactome
    3. modulation by virus of host morphology or physiology Source: Reactome
    4. modulation by virus of host process Source: Reactome
    5. mRNA 3'-end processing Source: Reactome
    6. mRNA splicing, via spliceosome Source: Reactome
    7. muscle contraction Source: ProtInc
    8. poly(A)+ mRNA export from nucleus Source: UniProtKB
    9. RNA processing Source: ProtInc
    10. RNA splicing Source: Reactome
    11. termination of RNA polymerase II transcription Source: Reactome
    12. transcription from RNA polymerase II promoter Source: Reactome
    13. viral life cycle Source: Reactome

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1096. Processing of Intronless Pre-mRNAs.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_6173. Inhibition of Host mRNA Processing and RNA Silencing.

    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
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:8565. PABPN1.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm 4 Publications
    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

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB
    4. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi213 – 2208Missing: Abolishes self-association, protein aggregation and cell death. 1 Publication
    Mutagenesisi301 – 3066Missing: Abolishes self-association, protein aggregation and cell death. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi164300. phenotype.
    Orphaneti270. Oculopharyngeal muscular dystrophy.
    PharmGKBiPA32891.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed6 Publications
    Chaini2 – 306305Polyadenylate-binding protein 2PRO_0000081711Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine6 Publications
    Modified residuei19 – 191Phosphoserine2 Publications
    Modified residuei95 – 951Phosphoserine3 Publications
    Modified residuei150 – 1501Phosphoserine4 Publications
    Modified residuei238 – 2381Asymmetric dimethylarginine; alternateBy similarity
    Modified residuei238 – 2381Omega-N-methylarginine; alternateBy similarity
    Modified residuei259 – 2591Asymmetric dimethylarginineBy similarity
    Modified residuei263 – 2631Asymmetric dimethylarginineBy similarity
    Modified residuei265 – 2651Asymmetric dimethylarginineBy similarity
    Modified residuei267 – 2671Asymmetric dimethylarginineBy similarity
    Modified residuei269 – 2691Asymmetric dimethylarginineBy similarity
    Modified residuei277 – 2771Asymmetric dimethylarginineBy similarity
    Modified residuei279 – 2791Asymmetric dimethylarginineBy similarity
    Modified residuei287 – 2871Asymmetric dimethylarginineBy similarity
    Modified residuei289 – 2891Asymmetric dimethylarginineBy similarity
    Modified residuei291 – 2911Asymmetric dimethylarginineBy similarity
    Modified residuei294 – 2941Asymmetric dimethylarginineBy similarity
    Modified residuei296 – 2961Asymmetric dimethylarginineBy similarity
    Modified residuei298 – 2981Asymmetric dimethylarginineBy similarity

    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

    MaxQBiQ86U42.
    PaxDbiQ86U42.
    PRIDEiQ86U42.

    PTM databases

    PhosphoSiteiQ86U42.

    Miscellaneous databases

    PMAP-CutDBQ86U42.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiQ86U42.
    BgeeiQ86U42.
    CleanExiHS_PABPN1.
    GenevestigatoriQ86U42.

    Organism-specific databases

    HPAiHPA000637.

    Interactioni

    Subunit structurei

    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/CPSF5.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SNW1Q135735EBI-1226435,EBI-632715

    Protein-protein interaction databases

    BioGridi113777. 22 interactions.
    DIPiDIP-37968N.
    IntActiQ86U42. 26 interactions.
    MINTiMINT-89761.
    STRINGi9606.ENSP00000216727.

    Structurei

    Secondary structure

    1
    306
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi167 – 1715
    Beta strandi173 – 1786
    Helixi185 – 1928
    Helixi193 – 1953
    Beta strandi198 – 2069
    Beta strandi208 – 2114
    Beta strandi214 – 2229
    Helixi224 – 2296
    Helixi230 – 2323
    Beta strandi243 – 2464
    Turni247 – 2504

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3B4DX-ray2.00A167-254[»]
    3B4MX-ray2.82A/B/C/D167-254[»]
    3UCGX-ray1.95A167-254[»]
    ProteinModelPortaliQ86U42.
    SMRiQ86U42. Positions 167-253.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ86U42.

    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 SKIPAdd
    BLAST
    Regioni119 – 14729Stimulates PAPOLABy similarityAdd
    BLAST
    Regioni155 – 306152Necessary for homooligomerizationAdd
    BLAST
    Regioni286 – 30621Interacts with PAPOLABy similarityAdd
    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.By similarity

    Sequence similaritiesi

    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG238057.
    HOGENOMiHOG000208465.
    HOVERGENiHBG107480.
    InParanoidiQ86U42.
    KOiK14396.
    OMAiRGRTTSW.
    OrthoDBiEOG7K9K3Z.
    PhylomeDBiQ86U42.
    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]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    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. Align

    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

    MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGAP GGAGDYGNGL    50
    ESEELEPEEL LLEPEPEPEP EEEPPRPRAP PGAPGPGPGS GAPGSQEEEE 100
    EPGLVEGDPG DGAIEDPELE AIKARVREME EEAEKLKELQ NEVEKQMNMS 150
    PPPGNAGPVI MSIEEKMEAD ARSIYVGNVD YGATAEELEA HFHGCGSVNR 200
    VTILCDKFSG HPKGFAYIEF SDKESVRTSL ALDESLFRGR QIKVIPKRTN 250
    RPGISTTDRG FPRARYRART TNYNSSRSRF YSGFNSRPRG RVYRGRARAT 300
    SWYSPY 306
    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 CAD62310.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti6 – 61A → AAAA.
    VAR_018179

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei295 – 2962GR → SG in isoform 2. 1 PublicationVSP_009847
    Alternative sequencei297 – 30610Missing in isoform 2. 1 PublicationVSP_009848

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.3. human. [Q86U42-2]
    uc001wjk.3. human. [Q86U42-1]

    Polymorphism databases

    DMDMi46403176.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism, Triplet repeat expansion

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS9592.1. [Q86U42-1 ]
    RefSeqi NP_004634.1. NM_004643.3. [Q86U42-1 ]
    UniGenei Hs.707712.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3B4D X-ray 2.00 A 167-254 [» ]
    3B4M X-ray 2.82 A/B/C/D 167-254 [» ]
    3UCG X-ray 1.95 A 167-254 [» ]
    ProteinModelPortali Q86U42.
    SMRi Q86U42. Positions 167-253.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113777. 22 interactions.
    DIPi DIP-37968N.
    IntActi Q86U42. 26 interactions.
    MINTi MINT-89761.
    STRINGi 9606.ENSP00000216727.

    PTM databases

    PhosphoSitei Q86U42.

    Polymorphism databases

    DMDMi 46403176.

    Proteomic databases

    MaxQBi Q86U42.
    PaxDbi Q86U42.
    PRIDEi Q86U42.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216727 ; ENSP00000216727 ; ENSG00000100836 . [Q86U42-1 ]
    ENST00000397276 ; ENSP00000380446 ; ENSG00000100836 . [Q86U42-2 ]
    GeneIDi 8106.
    KEGGi hsa:8106.
    UCSCi uc001wjj.3. human. [Q86U42-2 ]
    uc001wjk.3. human. [Q86U42-1 ]

    Organism-specific databases

    CTDi 8106.
    GeneCardsi GC14P023789.
    GeneReviewsi PABPN1.
    HGNCi HGNC:8565. PABPN1.
    HPAi HPA000637.
    MIMi 164300. phenotype.
    602279. gene.
    neXtProti NX_Q86U42.
    Orphaneti 270. Oculopharyngeal muscular dystrophy.
    PharmGKBi PA32891.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG238057.
    HOGENOMi HOG000208465.
    HOVERGENi HBG107480.
    InParanoidi Q86U42.
    KOi K14396.
    OMAi RGRTTSW.
    OrthoDBi EOG7K9K3Z.
    PhylomeDBi Q86U42.
    TreeFami TF105907.

    Enzyme and pathway databases

    Reactomei REACT_1096. Processing of Intronless Pre-mRNAs.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_6173. Inhibition of Host mRNA Processing and RNA Silencing.

    Miscellaneous databases

    EvolutionaryTracei Q86U42.
    GeneWikii PABPN1.
    GenomeRNAii 8106.
    NextBioi 30755.
    PMAP-CutDB Q86U42.
    PROi Q86U42.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86U42.
    Bgeei Q86U42.
    CleanExi HS_PABPN1.
    Genevestigatori Q86U42.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), POLYMORPHISM OF POLY-ALA REGION, DISEASE.
    2. "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.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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.
    5. "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.
    6. 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.
    7. "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.
    8. "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.
    9. "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.
    10. "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.
    11. "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.
    12. "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.
    13. "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.
    14. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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].
    17. "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.
    18. "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.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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].
    21. "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].
    22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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.

    Entry informationi

    Entry nameiPABP2_HUMAN
    AccessioniPrimary (citable) accession number: Q86U42
    Secondary accession number(s): D3DS49, O43484
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 120 of the entry and version 3 of the sequence. [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

    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.

    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
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3