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P11940

- PABP1_HUMAN

UniProt

P11940 - PABP1_HUMAN

Protein

Polyadenylate-binding protein 1

Gene

PABPC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 186 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Binds the poly(A) tail of mRNA, including that of its own transcript. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed.4 Publications

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. poly(U) RNA binding Source: MGI
    5. protein binding Source: UniProtKB
    6. protein C-terminus binding Source: UniProtKB
    7. translation activator activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. gene silencing by RNA Source: UniProtKB
    4. mRNA metabolic process Source: Reactome
    5. mRNA polyadenylation Source: UniProtKB
    6. mRNA splicing, via spliceosome Source: UniProtKB
    7. mRNA stabilization Source: UniProtKB
    8. negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    9. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
    10. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    11. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
    12. positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
    13. positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: UniProtKB
    14. positive regulation of translation Source: GOC
    15. RNA metabolic process Source: Reactome
    16. translation Source: Reactome
    17. translational initiation Source: Reactome

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Nonsense-mediated mRNA decay

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1979. Translation initiation complex formation.
    REACT_20514. Deadenylation of mRNA.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Polyadenylate-binding protein 1
    Short name:
    PABP-1
    Short name:
    Poly(A)-binding protein 1
    Gene namesi
    Name:PABPC1
    Synonyms:PAB1, PABP1, PABPC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:8554. PABPC1.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the cytoplasm and the nucleus.

    GO - Cellular componenti

    1. catalytic step 2 spliceosome Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    4. cytoplasmic stress granule Source: UniProtKB
    5. cytosol Source: Reactome
    6. membrane Source: UniProtKB
    7. nucleus Source: MGI
    8. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi455 – 4551R → A: Greatly reduces methylation by CARM1 (in vitro); when associated with A-460. 1 Publication
    Mutagenesisi460 – 4601R → A: Greatly reduces methylation by CARM1 (in vitro); when associated with A-455. 1 Publication

    Organism-specific databases

    PharmGKBiPA32880.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 636636Polyadenylate-binding protein 1PRO_0000081698Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei299 – 2991N6-methyllysine1 Publication
    Modified residuei315 – 3151Phosphoserine3 Publications
    Modified residuei455 – 4551Omega-N-methylated arginine; by CARM1; partial1 Publication
    Modified residuei460 – 4601Omega-N-methylated arginine; by CARM1; partial1 Publication
    Modified residuei493 – 4931Dimethylated arginine; alternate2 Publications
    Modified residuei493 – 4931Omega-N-methylarginine; alternate2 Publications
    Modified residuei512 – 5121N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated by MAPKAPK2.3 Publications
    Methylated by CARM1. Arg-493 is dimethylated, probably to asymmetric dimethylarginine.3 Publications

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP11940.
    PaxDbiP11940.
    PRIDEiP11940.

    PTM databases

    PhosphoSiteiP11940.

    Miscellaneous databases

    PMAP-CutDBP11940.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiP11940.
    BgeeiP11940.
    CleanExiHS_PABPC1.
    GenevestigatoriP11940.

    Organism-specific databases

    HPAiCAB011536.
    HPA045423.

    Interactioni

    Subunit structurei

    May form homodimers. Component of a multisubunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. Directly interacts with IGF2BP1. Part of a complex associated with the FOS mCRD domain and consisting of HNRPD, SYNCRIP, PAIP1 and CSDE1/UNR. Interacts with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1 and PAIP2. Interacts with PAIP1 with a 1:1 stoichiometry and with PAIP2 with a 1:2 stoichiometry. The interaction with CSDE1 is direct and RNA-independent. Found in a mRNP complex with YBX2. Interacts with PAPD4/GLD2. Identified in the spliceosome C complex. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with NFX1. Interacts with PIWIL1. Interacts with AGO1, AGO2, GSPT1 and GSPT2. Interacts with human cytomegalovirus/HHV-5 protein UL69. Interacts with LARP1 and LARP4B.21 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN2Q997006EBI-81531,EBI-697691
    DDX3XO0057110EBI-81531,EBI-353779
    EIF4G1Q046372EBI-81531,EBI-73711
    GSPT1P15170-22EBI-81531,EBI-9094806
    GSPT2Q8IYD17EBI-81531,EBI-3869637
    HNRNPDQ14103-42EBI-81531,EBI-432545
    IRS1P355682EBI-81531,EBI-517592
    PAIP1Q9H07410EBI-81531,EBI-81519
    PAIP2Q9BPZ35EBI-81531,EBI-2957445
    PAN3Q58A454EBI-81531,EBI-2513054
    SMG1Q96Q152EBI-81531,EBI-1049832
    TNRC6BQ9UPQ93EBI-81531,EBI-947158
    TNRC6CQ9HCJ017EBI-81531,EBI-6507625
    TOB1P506164EBI-81531,EBI-723281
    TOB2Q141064EBI-81531,EBI-2562000

    Protein-protein interaction databases

    BioGridi117939. 157 interactions.
    DIPiDIP-31613N.
    IntActiP11940. 86 interactions.
    MINTiMINT-96210.
    STRINGi9606.ENSP00000313007.

    Structurei

    Secondary structure

    1
    636
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 176
    Helixi24 – 318
    Helixi32 – 343
    Beta strandi37 – 448
    Turni46 – 483
    Beta strandi51 – 6111
    Helixi62 – 7211
    Beta strandi83 – 864
    Helixi92 – 965
    Beta strandi100 – 1056
    Helixi112 – 1198
    Helixi120 – 1223
    Beta strandi125 – 1339
    Beta strandi136 – 14611
    Helixi148 – 15811
    Beta strandi161 – 1633
    Beta strandi169 – 1746
    Helixi176 – 1838
    Helixi547 – 5515
    Helixi555 – 5573
    Helixi558 – 57316
    Turni575 – 5773
    Helixi578 – 5858
    Helixi590 – 5989
    Helixi600 – 61920
    Turni623 – 6253
    Beta strandi628 – 6303

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CVJX-ray2.60A/B/C/D/E/F/G/H1-190[»]
    1G9LNMR-A498-636[»]
    1JGNNMR-A544-636[»]
    1JH4NMR-A544-636[»]
    2K8GNMR-A90-182[»]
    2RQGNMR-B541-623[»]
    2RQHNMR-B541-623[»]
    2X04X-ray1.49A/B545-619[»]
    3KTPX-ray1.50A544-626[»]
    3KTRX-ray1.70A544-626[»]
    3KUIX-ray2.30A544-626[»]
    3KUJX-ray1.40A544-626[»]
    3KURX-ray2.50A/B/C/D/E/F/G/H544-617[»]
    3KUSX-ray1.40A/B544-626[»]
    3KUTX-ray1.50A/B544-626[»]
    3PKNX-ray1.80A544-626[»]
    3PTHX-ray1.70A543-621[»]
    4F02X-ray2.00A/D1-190[»]
    4F25X-ray1.90A99-199[»]
    4F26X-ray2.00A99-199[»]
    ProteinModelPortaliP11940.
    SMRiP11940. Positions 10-376, 494-636.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP11940.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 8979RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini99 – 17577RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini191 – 26878RRM 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini294 – 37077RRM 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini542 – 61978PABCPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni166 – 289124CSDE1-bindingAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi495 – 5017Poly-Ala

    Domaini

    The RNA-binding domains RRM1 and RRM2 and the C-terminus (last 138 amino acids) regions interact with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.
    The RNA-binding domains RRM2 and RRM3 and the C-terminus (last 138 amino acids) regions interact with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP2, respectively.

    Sequence similaritiesi

    Contains 1 PABC domain.PROSITE-ProRule annotation
    Contains 4 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000217922.
    HOVERGENiHBG002295.
    InParanoidiP11940.
    KOiK13126.
    OMAiXAVDEMN.
    OrthoDBiEOG7RV9FP.
    PhylomeDBiP11940.
    TreeFamiTF300458.

    Family and domain databases

    Gene3Di1.10.1900.10. 1 hit.
    3.30.70.330. 4 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR006515. PABP_1234.
    IPR002004. PABP_HYD.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00658. PABP. 1 hit.
    PF00076. RRM_1. 4 hits.
    [Graphical view]
    SMARTiSM00517. PolyA. 1 hit.
    SM00360. RRM. 4 hits.
    [Graphical view]
    SUPFAMiSSF63570. SSF63570. 1 hit.
    TIGRFAMsiTIGR01628. PABP-1234. 1 hit.
    PROSITEiPS51309. PABC. 1 hit.
    PS50102. RRM. 4 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P11940-1) [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

    MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR    50
    SLGYAYVNFQ QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN 100
    IFIKNLDKSI DNKALYDTFS AFGNILSCKV VCDENGSKGY GFVHFETQEA 150
    AERAIEKMNG MLLNDRKVFV GRFKSRKERE AELGARAKEF TNVYIKNFGE 200
    DMDDERLKDL FGKFGPALSV KVMTDESGKS KGFGFVSFER HEDAQKAVDE 250
    MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN 300
    LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV 350
    TEMNGRIVAT KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY 400
    QPAPPSGYFM AAIPQTQNRA AYYPPSQIAQ LRPSPRWTAQ GARPHPFQNM 450
    PGAIRPAAPR PPFSTMRPAS SQVPRVMSTQ RVANTSTQTM GPRPAAAAAA 500
    ATPAVRTVPQ YKYAAGVRNP QQHLNAQPQV TMQQPAVHVQ GQEPLTASML 550
    ASAPPQEQKQ MLGERLFPLI QAMHPTLAGK ITGMLLEIDN SELLHMLESP 600
    ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV 636
    Length:636
    Mass (Da):70,671
    Last modified:July 15, 1998 - v2
    Checksum:i2EB1B02A346132EE
    GO
    Isoform 2 (identifier: P11940-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         447-535: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:547
    Mass (Da):61,181
    Checksum:i8088B4F7DFABAFB8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti211 – 2133Missing in CAA68428. (PubMed:2885805)Curated
    Sequence conflicti410 – 4101M → I in CAA88401. 1 PublicationCurated
    Sequence conflicti428 – 4281I → V in CAA68428. (PubMed:2885805)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei447 – 53589Missing in isoform 2. 1 PublicationVSP_009846Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00345 mRNA. Translation: CAA68428.1.
    U68104
    , U68093, U68094, U68095, U68097, U68098, U68099, U68100, U68101, U68102, U68103 Genomic DNA. Translation: AAD08718.1.
    AP001205 Genomic DNA. No translation available.
    BC015958 mRNA. Translation: AAH15958.1.
    BC023520 mRNA. Translation: AAH23520.1.
    Z48501 mRNA. Translation: CAA88401.1.
    CCDSiCCDS6289.1. [P11940-1]
    PIRiA93668. DNHUPA.
    S52491.
    RefSeqiNP_002559.2. NM_002568.3. [P11940-1]
    XP_005250918.1. XM_005250861.1. [P11940-1]
    UniGeneiHs.387804.

    Genome annotation databases

    EnsembliENST00000318607; ENSP00000313007; ENSG00000070756. [P11940-1]
    GeneIDi26986.
    KEGGihsa:26986.
    UCSCiuc003yjs.1. human. [P11940-1]

    Polymorphism databases

    DMDMi3183544.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00345 mRNA. Translation: CAA68428.1 .
    U68104
    , U68093 , U68094 , U68095 , U68097 , U68098 , U68099 , U68100 , U68101 , U68102 , U68103 Genomic DNA. Translation: AAD08718.1 .
    AP001205 Genomic DNA. No translation available.
    BC015958 mRNA. Translation: AAH15958.1 .
    BC023520 mRNA. Translation: AAH23520.1 .
    Z48501 mRNA. Translation: CAA88401.1 .
    CCDSi CCDS6289.1. [P11940-1 ]
    PIRi A93668. DNHUPA.
    S52491.
    RefSeqi NP_002559.2. NM_002568.3. [P11940-1 ]
    XP_005250918.1. XM_005250861.1. [P11940-1 ]
    UniGenei Hs.387804.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CVJ X-ray 2.60 A/B/C/D/E/F/G/H 1-190 [» ]
    1G9L NMR - A 498-636 [» ]
    1JGN NMR - A 544-636 [» ]
    1JH4 NMR - A 544-636 [» ]
    2K8G NMR - A 90-182 [» ]
    2RQG NMR - B 541-623 [» ]
    2RQH NMR - B 541-623 [» ]
    2X04 X-ray 1.49 A/B 545-619 [» ]
    3KTP X-ray 1.50 A 544-626 [» ]
    3KTR X-ray 1.70 A 544-626 [» ]
    3KUI X-ray 2.30 A 544-626 [» ]
    3KUJ X-ray 1.40 A 544-626 [» ]
    3KUR X-ray 2.50 A/B/C/D/E/F/G/H 544-617 [» ]
    3KUS X-ray 1.40 A/B 544-626 [» ]
    3KUT X-ray 1.50 A/B 544-626 [» ]
    3PKN X-ray 1.80 A 544-626 [» ]
    3PTH X-ray 1.70 A 543-621 [» ]
    4F02 X-ray 2.00 A/D 1-190 [» ]
    4F25 X-ray 1.90 A 99-199 [» ]
    4F26 X-ray 2.00 A 99-199 [» ]
    ProteinModelPortali P11940.
    SMRi P11940. Positions 10-376, 494-636.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117939. 157 interactions.
    DIPi DIP-31613N.
    IntActi P11940. 86 interactions.
    MINTi MINT-96210.
    STRINGi 9606.ENSP00000313007.

    Chemistry

    BindingDBi P11940.
    ChEMBLi CHEMBL1293286.

    PTM databases

    PhosphoSitei P11940.

    Polymorphism databases

    DMDMi 3183544.

    Proteomic databases

    MaxQBi P11940.
    PaxDbi P11940.
    PRIDEi P11940.

    Protocols and materials databases

    DNASUi 26986.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318607 ; ENSP00000313007 ; ENSG00000070756 . [P11940-1 ]
    GeneIDi 26986.
    KEGGi hsa:26986.
    UCSCi uc003yjs.1. human. [P11940-1 ]

    Organism-specific databases

    CTDi 26986.
    GeneCardsi GC08M101715.
    HGNCi HGNC:8554. PABPC1.
    HPAi CAB011536.
    HPA045423.
    MIMi 604679. gene.
    neXtProti NX_P11940.
    PharmGKBi PA32880.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000217922.
    HOVERGENi HBG002295.
    InParanoidi P11940.
    KOi K13126.
    OMAi XAVDEMN.
    OrthoDBi EOG7RV9FP.
    PhylomeDBi P11940.
    TreeFami TF300458.

    Enzyme and pathway databases

    Reactomei REACT_1979. Translation initiation complex formation.
    REACT_20514. Deadenylation of mRNA.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
    REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
    REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.

    Miscellaneous databases

    ChiTaRSi PABPC1. human.
    EvolutionaryTracei P11940.
    GeneWikii PABPC1.
    GenomeRNAii 26986.
    NextBioi 49454.
    PMAP-CutDB P11940.
    PROi P11940.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P11940.
    Bgeei P11940.
    CleanExi HS_PABPC1.
    Genevestigatori P11940.

    Family and domain databases

    Gene3Di 1.10.1900.10. 1 hit.
    3.30.70.330. 4 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR006515. PABP_1234.
    IPR002004. PABP_HYD.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00658. PABP. 1 hit.
    PF00076. RRM_1. 4 hits.
    [Graphical view ]
    SMARTi SM00517. PolyA. 1 hit.
    SM00360. RRM. 4 hits.
    [Graphical view ]
    SUPFAMi SSF63570. SSF63570. 1 hit.
    TIGRFAMsi TIGR01628. PABP-1234. 1 hit.
    PROSITEi PS51309. PABC. 1 hit.
    PS50102. RRM. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human mRNA polyadenylate binding protein: evolutionary conservation of a nucleic acid binding motif."
      Grange T., de Sa C.M., Oddos J., Pictet R.
      Nucleic Acids Res. 15:4771-4787(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The human poly(A)-binding protein (PABP) gene: structural and functional analysis."
      Hornstein E., Abramzon-Talianker A., Wiesel I., Meyuhas O.
      Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Lung.
    3. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      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: Lung and Muscle.
    5. "Nucleotide sequence of a partial cDNA encoding a novel human polyadenylate-binding protein."
      Murphy E.P., McKenna N.J., Headon D.R.
      Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-636 (ISOFORM 2).
    6. Cited for: PROTEIN SEQUENCE OF 31-41; 51-78; 84-89; 96-104; 158-166; 189-196; 214-221; 232-240; 291-309; 312-324; 357-370; 375-385; 482-506; 566-580 AND 605-620, METHYLATION AT ARG-493, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma and Ovarian carcinoma.
    7. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 31-41; 51-78; 84-89; 96-104; 114-129; 139-153; 158-166; 187-208; 214-221; 232-240; 291-324; 334-348; 357-370; 375-385; 482-506; 519-559; 566-620 AND 626-636, METHYLATION AT LYS-299 AND ARG-493, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Cervix carcinoma.
    8. "The mRNA poly(A)-binding protein: localization, abundance, and RNA-binding specificity."
      Goerlach M., Burd C.G., Dreyfuss G.
      Exp. Cell Res. 211:400-407(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    9. "The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm."
      Afonina E., Stauber R., Pavlakis G.N.
      J. Biol. Chem. 273:13015-13021(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    10. "Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation."
      Craig A.W.B., Haghighat A., Yu A.T.K., Sonenberg N.
      Nature 392:520-523(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAIP1.
    11. "A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex."
      Grosset C., Chen C.-Y.A., Xu N., Sonenberg N., Jacquemin-Sablon H., Shyu A.-B.
      Cell 103:29-40(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSLATIONALLY COUPLED MRNA TURNOVER, IDENTIFICATION IN A COMPLEX WITH HNRPD; SYNCRIP; PAIP1 AND CSDE1.
    12. "Translational repression by a novel partner of human poly(A) binding protein, Paip2."
      Khaleghpour K., Svitkin Y.V., Craig A.W.B., DeMaria C.T., Deo R.C., Burley S.K., Sonenberg N.
      Mol. Cell 7:205-216(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAIP2.
    13. "Dual interactions of the translational repressor Paip2 with poly(A) binding protein."
      Khaleghpour K., Kahvejian A., De Crescenzo G., Roy G., Svitkin Y.V., Imataka H., O'Connor-McCourt M., Sonenberg N.
      Mol. Cell. Biol. 21:5200-5213(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAIP2.
    14. "PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays."
      Lee J., Bedford M.T.
      EMBO Rep. 3:268-273(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-455 AND ARG-460, MUTAGENESIS OF ARG-455 AND ARG-460.
    15. "Paip1 interacts with poly(A) binding protein through two independent binding motifs."
      Roy G., De Crescenzo G., Khaleghpour K., Kahvejian A., O'Connor-McCourt M., Sonenberg N.
      Mol. Cell. Biol. 22:3769-3782(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAIP1.
    16. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
      Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
      RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
    17. "Affinity purification of ARE-binding proteins identifies polyA-binding protein 1 as a potential substrate in MK2-induced mRNA stabilization."
      Bollig F., Winzen R., Gaestel M., Kostka S., Resch K., Holtmann H.
      Biochem. Biophys. Res. Commun. 301:665-670(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY MAPKAPK2.
    18. "UNR, a new partner of poly(A)-binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant."
      Chang T.-C., Yamashita A., Chen C.-Y.A., Yamashita Y., Zhu W., Durdan S., Kahvejian A., Sonenberg N., Shyu A.-B.
      Genes Dev. 18:2010-2023(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSDE1.
    19. "The autoregulatory translational control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex."
      Patel G.P., Ma S., Bag J.
      Nucleic Acids Res. 33:7074-7089(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP1 AND CSDE1.
    20. "IMP1 interacts with poly(A)-binding protein (PABP) and the autoregulatory translational control element of PABP-mRNA through the KH III-IV domain."
      Patel G.P., Bag J.
      FEBS J. 273:5678-5690(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HOMODIMERIZATION, INTERACTION WITH IGF2BP1, RNA-BINDING.
    21. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
      Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
      EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AGO1 AND AGO2.
    22. "NFX1-123 and poly(A) binding proteins synergistically augment activation of telomerase in human papillomavirus type 16 E6-expressing cells."
      Katzenellenbogen R.A., Egelkrout E.M., Vliet-Gregg P., Gewin L.C., Gafken P.R., Galloway D.A.
      J. Virol. 81:3786-3796(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NFX1.
    23. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION.
    24. "Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN."
      Harb M., Becker M.M., Vitour D., Baron C.H., Vende P., Brown S.C., Bolte S., Arold S.T., Poncet D.
      J. Virol. 82:11283-11293(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    25. "A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay."
      Singh G., Rebbapragada I., Lykke-Andersen J.
      PLoS Biol. 6:E111-E111(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, INTERACTION WITH GSPT2.
    26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
      Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
      RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    29. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Poly(A)-binding protein (PABP): a common viral target."
      Smith R.W., Gray N.K.
      Biochem. J. 426:1-12(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    31. Cited for: INTERACTION WITH LARP1.
    32. "Human cytomegalovirus UL69 protein facilitates translation by associating with the mRNA cap-binding complex and excluding 4EBP1."
      Aoyagi M., Gaspar M., Shenk T.E.
      Proc. Natl. Acad. Sci. U.S.A. 107:2640-2645(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-5 PROTEIN UL69.
    33. "A stimulatory role for the La-related protein 4B in translation."
      Schaffler K., Schulz K., Hirmer A., Wiesner J., Grimm M., Sickmann A., Fischer U.
      RNA 16:1488-1499(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PABPC1 AND GNB2L1.
    34. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    36. "Proteomic analysis of cap-dependent translation identifies LARP1 as a key regulator of 5'TOP mRNA translation."
      Tcherkezian J., Cargnello M., Romeo Y., Huttlin E.L., Lavoie G., Gygi S.P., Roux P.P.
      Genes Dev. 28:357-371(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LARP1.
    37. "Recognition of polyadenylate RNA by the poly(A)-binding protein."
      Deo R.C., Bonanno J.B., Sonenberg N., Burley S.K.
      Cell 98:835-845(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-190.
    38. "Structure and function of the C-terminal PABC domain of human poly(A)-binding protein."
      Kozlov G., Trempe J.F., Khaleghpour K., Kahvejian A., Ekiel I., Gehring K.
      Proc. Natl. Acad. Sci. U.S.A. 98:4409-4413(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 498-636, INTERACTION WITH GSPT1; PAIP1 AND PAIP2.
    39. "Eukaryotic translation termination factor Gspt/ERF3 recognizes Pabp with chemical exchange using two overlapping motifs."
      Osawa M., Nakanishi T., Hosoda N., Uchida S., Hoshino T., Katada I., Shimada I.
      Submitted (MAY-2009) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 541-623 IN COMPLEX WITH GSPT1.
    40. "Molecular determinants of PAM2 recognition by the MLLE domain of poly(A)-binding protein."
      Kozlov G., Menade M., Rosenauer A., Nguyen L., Gehring K.
      J. Mol. Biol. 397:397-407(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 544-626 IN COMPLEX WITH PAIP2.

    Entry informationi

    Entry nameiPABP1_HUMAN
    AccessioniPrimary (citable) accession number: P11940
    Secondary accession number(s): Q15097, Q93004
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 186 of the entry and version 2 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

    Many viruses shutoff host mRNA translational machinery by inhibiting cellular PABPC1 activity using different mechanisms. Picornaviruses, caliciviruses or lentiviruses encode proteases that cleave PABPC1 at several defined sites in the proline-rich linker region between RRMs and the C-terminal domain. Rotaviruses, gammherpesviruses and bunyamwera virus relocalize PABPC1 from the cytoplasm to the nucleus thus altering its function. Many of these viruses translate their mRNA in a PABPC1-independent manner and are unaffected by host PABPC1 inhibition.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3