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P29341

- PABP1_MOUSE

UniProt

P29341 - PABP1_MOUSE

Protein

Polyadenylate-binding protein 1

Gene

Pabpc1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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 By similarity.By similarity

    GO - Molecular functioni

    1. mRNA binding Source: Ensembl
    2. nucleotide binding Source: InterPro
    3. poly(A) binding Source: UniProtKB
    4. poly(U) RNA binding Source: MGI
    5. protein binding Source: MGI

    GO - Biological processi

    1. gene silencing by RNA Source: UniProtKB
    2. mRNA processing Source: UniProtKB-KW
    3. negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB-KW
    5. positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
    6. positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: UniProtKB
    7. RNA splicing Source: UniProtKB-KW

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Nonsense-mediated mRNA decay

    Keywords - Ligandi

    RNA-binding

    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:Pabp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:1349722. Pabpc1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. cytoplasmic stress granule Source: UniProtKB
    3. ribonucleoprotein complex Source: UniProtKB
    4. spliceosomal complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Spliceosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 636636Polyadenylate-binding protein 1PRO_0000081699Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei299 – 2991N6-methyllysineBy similarity
    Modified residuei315 – 3151PhosphoserineBy similarity
    Modified residuei455 – 4551Omega-N-methylated arginine; by CARM1By similarity
    Modified residuei460 – 4601Omega-N-methylated arginine; by CARM1By similarity
    Modified residuei493 – 4931Dimethylated arginine; alternateBy similarity
    Modified residuei493 – 4931Omega-N-methylarginine; alternateBy similarity
    Modified residuei512 – 5121N6-acetyllysineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP29341.
    PaxDbiP29341.
    PRIDEiP29341.

    2D gel databases

    REPRODUCTION-2DPAGEP29341.

    PTM databases

    PhosphoSiteiP29341.

    Expressioni

    Gene expression databases

    ArrayExpressiP29341.
    BgeeiP29341.
    CleanExiMM_PABPC1.
    GenevestigatoriP29341.

    Interactioni

    Subunit structurei

    Component of a multi subunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. 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. 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. Identified in the spliceosome C complex. Interacts with NFX1. The interaction with CSDE1 is direct and RNA-independent. Found in a mRNP complex with YBX2. Interacts with PAPD4/GLD2 and PIWIL1. Interacts with AGO1, AGO2, GSPT1 and GSPT2. Interacts with LARP1 and LARP4B.4 Publications

    Protein-protein interaction databases

    BioGridi202010. 15 interactions.
    DIPiDIP-32127N.
    IntActiP29341. 14 interactions.
    MINTiMINT-4123966.

    Structurei

    3D structure databases

    ProteinModelPortaliP29341.
    SMRiP29341. Positions 10-376, 494-636.
    ModBaseiSearch...
    MobiDBiSearch...

    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-bindingBy similarityAdd
    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 respectively with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.By similarity
    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.By similarity

    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.
    GeneTreeiENSGT00640000091232.
    HOGENOMiHOG000217922.
    HOVERGENiHBG002295.
    InParanoidiQ99L36.
    KOiK13126.
    OMAiXAVDEMN.
    OrthoDBiEOG7RV9FP.
    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]

    Sequencei

    Sequence statusi: Complete.

    P29341-1 [UniParc]FASTAAdd to Basket

    « 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
    DMDDERLKEL 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 QAMHPSLAGK ITGMLLEIDN SELLHMLESP 600
    ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV 636
    Length:636
    Mass (Da):70,671
    Last modified:July 27, 2011 - v2
    Checksum:iE5BB6D5BA4F86CB7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti176 – 1761R → Q in CAA46522. (PubMed:1630930)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65553 mRNA. Translation: CAA46522.1.
    AK044829 mRNA. Translation: BAC32110.1.
    AK133196 mRNA. Translation: BAE21553.1.
    AK159703 mRNA. Translation: BAE35302.1.
    AK159733 mRNA. Translation: BAE35327.1.
    AK160968 mRNA. Translation: BAE36120.1.
    AK161123 mRNA. Translation: BAE36203.1.
    AK161671 mRNA. Translation: BAE36522.1.
    AK168466 mRNA. Translation: BAE40360.1.
    CH466541 Genomic DNA. Translation: EDL08818.1.
    BC003870 mRNA. Translation: AAH03870.1.
    BC011207 mRNA. Translation: AAH11207.1.
    BC023145 mRNA. Translation: AAH23145.1.
    BC046233 mRNA. Translation: AAH46233.1.
    CCDSiCCDS27431.1.
    PIRiI48718.
    RefSeqiNP_032800.2. NM_008774.3.
    UniGeneiMm.371570.

    Genome annotation databases

    EnsembliENSMUST00000001809; ENSMUSP00000001809; ENSMUSG00000022283.
    GeneIDi18458.
    KEGGimmu:18458.
    UCSCiuc007vmx.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65553 mRNA. Translation: CAA46522.1 .
    AK044829 mRNA. Translation: BAC32110.1 .
    AK133196 mRNA. Translation: BAE21553.1 .
    AK159703 mRNA. Translation: BAE35302.1 .
    AK159733 mRNA. Translation: BAE35327.1 .
    AK160968 mRNA. Translation: BAE36120.1 .
    AK161123 mRNA. Translation: BAE36203.1 .
    AK161671 mRNA. Translation: BAE36522.1 .
    AK168466 mRNA. Translation: BAE40360.1 .
    CH466541 Genomic DNA. Translation: EDL08818.1 .
    BC003870 mRNA. Translation: AAH03870.1 .
    BC011207 mRNA. Translation: AAH11207.1 .
    BC023145 mRNA. Translation: AAH23145.1 .
    BC046233 mRNA. Translation: AAH46233.1 .
    CCDSi CCDS27431.1.
    PIRi I48718.
    RefSeqi NP_032800.2. NM_008774.3.
    UniGenei Mm.371570.

    3D structure databases

    ProteinModelPortali P29341.
    SMRi P29341. Positions 10-376, 494-636.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202010. 15 interactions.
    DIPi DIP-32127N.
    IntActi P29341. 14 interactions.
    MINTi MINT-4123966.

    PTM databases

    PhosphoSitei P29341.

    2D gel databases

    REPRODUCTION-2DPAGE P29341.

    Proteomic databases

    MaxQBi P29341.
    PaxDbi P29341.
    PRIDEi P29341.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000001809 ; ENSMUSP00000001809 ; ENSMUSG00000022283 .
    GeneIDi 18458.
    KEGGi mmu:18458.
    UCSCi uc007vmx.2. mouse.

    Organism-specific databases

    CTDi 26986.
    MGIi MGI:1349722. Pabpc1.

    Phylogenomic databases

    eggNOGi COG0724.
    GeneTreei ENSGT00640000091232.
    HOGENOMi HOG000217922.
    HOVERGENi HBG002295.
    InParanoidi Q99L36.
    KOi K13126.
    OMAi XAVDEMN.
    OrthoDBi EOG7RV9FP.
    TreeFami TF300458.

    Miscellaneous databases

    ChiTaRSi PABPC1. mouse.
    NextBioi 294152.
    PROi P29341.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29341.
    Bgeei P29341.
    CleanExi MM_PABPC1.
    Genevestigatori P29341.

    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. "Nucleotide sequence of a mouse testis poly(A) binding protein cDNA."
      Wang M.-Y., Cutler M., Karimpour I., Kleene K.C.
      Nucleic Acids Res. 20:3519-3519(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo, Head, Skin and Testis.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      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].
      Strain: C57BL/6 and Czech II.
      Tissue: Mammary tumor.
    5. "The mouse Y-box protein, MSY2, is associated with a kinase on non-polysomal mouse testicular mRNAs."
      Herbert T.P., Hecht N.B.
      Nucleic Acids Res. 27:1747-1753(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH YBX2.
    6. "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.
    7. "Disruption of mouse poly(A) polymerase mGLD-2 does not alter polyadenylation status in oocytes and somatic cells."
      Nakanishi T., Kumagai S., Kimura M., Watanabe H., Sakurai T., Kimura M., Kashiwabara S., Baba T.
      Biochem. Biophys. Res. Commun. 364:14-19(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAPD4.
    8. "Characterization of two cytoplasmic poly(A)-binding proteins, PABPC1 and PABPC2, in mouse spermatogenic cells."
      Kimura M., Ishida K., Kashiwabara S., Baba T.
      Biol. Reprod. 80:545-554(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIWIL1.

    Entry informationi

    Entry nameiPABP1_MOUSE
    AccessioniPrimary (citable) accession number: P29341
    Secondary accession number(s): Q99L36
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3