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Q8CCS6

- PABP2_MOUSE

UniProt

Q8CCS6 - PABP2_MOUSE

Protein

Polyadenylate-binding protein 2

Gene

Pabpn1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 103 (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) binding Source: MGI

    GO - Biological processi

    1. mRNA polyadenylation Source: MGI

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    RNA-binding

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1859158. Pabpn1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    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. It is exported to the cytoplasm by a carrier-mediated pathway that is independent of mRNA traffic. Nucleus; nuclear speckle By similarity. Colocalizes with SKIP and poly(A) RNA in nuclear speckles By similarity.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 302301Polyadenylate-binding protein 2PRO_0000081712Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei19 – 191PhosphoserineBy similarity
    Modified residuei91 – 911PhosphoserineBy similarity
    Modified residuei146 – 1461PhosphoserineBy similarity
    Modified residuei234 – 2341Asymmetric dimethylarginine; alternateBy similarity
    Modified residuei234 – 2341Omega-N-methylarginine; alternateBy similarity
    Modified residuei255 – 2551Asymmetric dimethylarginineBy similarity
    Modified residuei259 – 2591Asymmetric dimethylarginineBy similarity
    Modified residuei261 – 2611Asymmetric dimethylarginineBy similarity
    Modified residuei263 – 2631Asymmetric dimethylarginineBy similarity
    Modified residuei265 – 2651Asymmetric dimethylarginineBy similarity
    Modified residuei273 – 2731Asymmetric dimethylarginineBy similarity
    Modified residuei275 – 2751Asymmetric dimethylarginineBy similarity
    Modified residuei283 – 2831Asymmetric dimethylarginineBy similarity
    Modified residuei285 – 2851Asymmetric dimethylarginineBy similarity
    Modified residuei287 – 2871Asymmetric dimethylarginineBy similarity
    Modified residuei290 – 2901Asymmetric dimethylarginineBy similarity
    Modified residuei292 – 2921Asymmetric dimethylarginineBy similarity
    Modified residuei294 – 2941Asymmetric 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

    MaxQBiQ8CCS6.
    PRIDEiQ8CCS6.

    PTM databases

    PhosphoSiteiQ8CCS6.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiQ8CCS6.
    BgeeiQ8CCS6.
    CleanExiMM_PABPN1.
    GenevestigatoriQ8CCS6.

    Interactioni

    Subunit structurei

    Monomer and homooligomer. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. 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 NUDT21/CPSF5 and transportin. Associates in a ternary complex with CPSF4 and NS/NS1 and interaction with NS/NS1, blocks nuclear export of host cell mRNAs. Associates in a single complex with SKIP and MYOD1 and interacts with SKIP in differentiated myocytes By similarity.By similarity

    Protein-protein interaction databases

    BioGridi207596. 1 interaction.
    IntActiQ8CCS6. 2 interactions.
    MINTiMINT-1867341.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8CCS6.
    SMRiQ8CCS6. Positions 163-249.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini168 – 24578RRMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 141140Interacts with SKIPBy similarityAdd
    BLAST
    Regioni115 – 14329Stimulates PAPOLABy similarityAdd
    BLAST
    Regioni255 – 30248Strong poly(A) affinity and self-associationBy similarityAdd
    BLAST
    Regioni282 – 30221Interacts with PAPOLABy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili111 – 14737Sequence 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

    GeneTreeiENSGT00390000001517.
    HOGENOMiHOG000208465.
    HOVERGENiHBG107480.
    InParanoidiQ8CCS6.
    KOiK14396.
    PhylomeDBiQ8CCS6.
    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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8CCS6-1) [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 AGGEAGEGDP GGAGDYGNGL    50
    ESEELEPGEL LPEPEPEEEP PRPRAPPGAP GPGPGSGAPG SQEEEEEPGL 100
    VEADPGDGAI EDPELEAIKA RVREMEEEAE KLKELQNEVE KQMNMSPPPG 150
    NAGPVIMSLE EKMEADARSI YVGNVDYGAT AEELEAHFHG CGSVNRVTIL 200
    CDKFSGHPKG FAYIEFSDKE SVRTSLALDE SLFRGRQIKV IPKRTNRPGI 250
    STTDRGFPRS RYRARTTNYN SSRSRFYSGF NSRPRGRIYR GRARATSWYS 300
    PY 302
    Length:302
    Mass (Da):32,297
    Last modified:January 23, 2007 - v3
    Checksum:i2F0F6F7CC19C1986
    GO
    Isoform 2 (identifier: Q8CCS6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         291-292: GR → SG
         293-302: Missing.

    Note: May be due to a competing donor splice site.

    Show »
    Length:292
    Mass (Da):31,044
    Checksum:i0874042BA4A60A2A
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei291 – 2922GR → SG in isoform 2. 1 PublicationVSP_009849
    Alternative sequencei293 – 30210Missing in isoform 2. 1 PublicationVSP_009850

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U93050 Genomic DNA. Translation: AAC00210.1.
    AK032172 mRNA. Translation: BAC27741.1.
    BC055866 mRNA. Translation: AAH55866.1.
    CCDSiCCDS27104.1. [Q8CCS6-1]
    RefSeqiNP_062275.1. NM_019402.2. [Q8CCS6-1]
    UniGeneiMm.7723.

    Genome annotation databases

    EnsembliENSMUST00000022808; ENSMUSP00000022808; ENSMUSG00000022194. [Q8CCS6-1]
    ENSMUST00000116476; ENSMUSP00000112177; ENSMUSG00000022194. [Q8CCS6-2]
    GeneIDi54196.
    KEGGimmu:54196.
    UCSCiuc007txg.2. mouse. [Q8CCS6-1]
    uc007txi.2. mouse. [Q8CCS6-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U93050 Genomic DNA. Translation: AAC00210.1 .
    AK032172 mRNA. Translation: BAC27741.1 .
    BC055866 mRNA. Translation: AAH55866.1 .
    CCDSi CCDS27104.1. [Q8CCS6-1 ]
    RefSeqi NP_062275.1. NM_019402.2. [Q8CCS6-1 ]
    UniGenei Mm.7723.

    3D structure databases

    ProteinModelPortali Q8CCS6.
    SMRi Q8CCS6. Positions 163-249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 207596. 1 interaction.
    IntActi Q8CCS6. 2 interactions.
    MINTi MINT-1867341.

    PTM databases

    PhosphoSitei Q8CCS6.

    Proteomic databases

    MaxQBi Q8CCS6.
    PRIDEi Q8CCS6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022808 ; ENSMUSP00000022808 ; ENSMUSG00000022194 . [Q8CCS6-1 ]
    ENSMUST00000116476 ; ENSMUSP00000112177 ; ENSMUSG00000022194 . [Q8CCS6-2 ]
    GeneIDi 54196.
    KEGGi mmu:54196.
    UCSCi uc007txg.2. mouse. [Q8CCS6-1 ]
    uc007txi.2. mouse. [Q8CCS6-2 ]

    Organism-specific databases

    CTDi 8106.
    MGIi MGI:1859158. Pabpn1.

    Phylogenomic databases

    GeneTreei ENSGT00390000001517.
    HOGENOMi HOG000208465.
    HOVERGENi HBG107480.
    InParanoidi Q8CCS6.
    KOi K14396.
    PhylomeDBi Q8CCS6.
    TreeFami TF105907.

    Miscellaneous databases

    ChiTaRSi PABPN1. mouse.
    NextBioi 311042.
    PROi Q8CCS6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8CCS6.
    Bgeei Q8CCS6.
    CleanExi MM_PABPN1.
    Genevestigatori Q8CCS6.

    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. "Genomic structure and expression of murine poly(A) binding protein II gene."
      Lee Y.J., Lee J., Yang I.C., Hahn Y., Lee Y., Chung J.H.
      Biochim. Biophys. Acta 1395:40-46(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Strain: 129.
    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] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Olfactory bulb.
    3. "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).
      Strain: FVB/N.
      Tissue: Colon.

    Entry informationi

    Entry nameiPABP2_MOUSE
    AccessioniPrimary (citable) accession number: Q8CCS6
    Secondary accession number(s): O35935
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 103 of the entry and version 3 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