ID   PABP2_MOUSE             Reviewed;         302 AA.
AC   Q8CCS6; O35935;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Polyadenylate-binding protein 2;
DE            Short=PABP-2;
DE            Short=Poly(A)-binding protein 2;
DE   AltName: Full=Nuclear poly(A)-binding protein 1;
DE   AltName: Full=Poly(A)-binding protein II;
DE            Short=PABII;
DE   AltName: Full=Polyadenylate-binding nuclear protein 1;
GN   Name=Pabpn1; Synonyms=Pab2, Pabp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129;
RX   PubMed=9434149; DOI=10.1016/s0167-4781(97)00147-4;
RA   Lee Y.J., Lee J., Yang I.C., Hahn Y., Lee Y., Chung J.H.;
RT   "Genomic structure and expression of murine poly(A) binding protein II
RT   gene.";
RL   Biochim. Biophys. Acta 1395:40-46(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   INTERACTION WITH ZFP36.
RX   PubMed=22844456; DOI=10.1371/journal.pone.0041313;
RA   Su Y.L., Wang S.C., Chi ang P.Y., Lin N.Y., Shen Y.F., Chang G.D.,
RA   Chang C.J.;
RT   "Tristetraprolin inhibits poly(A)-tail synthesis in nuclear mRNA that
RT   contains AU-rich elements by interacting with poly(A)-binding protein
RT   nuclear 1.";
RL   PLoS ONE 7:E41313-E41313(2012).
RN   [6]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-17, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Involved in the 3'-end formation of mRNA precursors (pre-
CC       mRNA) by the addition of a poly(A) tail of 200-250 nt to the upstream
CC       cleavage product. Stimulates poly(A) polymerase (PAPOLA) conferring
CC       processivity on the poly(A) tail elongation reaction and controls also
CC       the poly(A) tail length. Increases the affinity of poly(A) polymerase
CC       for RNA. Is also present at various stages of mRNA metabolism including
CC       nucleocytoplasmic trafficking and nonsense-mediated decay (NMD) of
CC       mRNA. Cooperates with SKIP to synergistically activate E-box-mediated
CC       transcription through MYOD1 and may regulate the expression of muscle-
CC       specific genes. Binds to poly(A) and to poly(G) with high affinity. May
CC       protect the poly(A) tail from degradation. Subunit of the trimeric
CC       poly(A) tail exosome targeting (PAXT) complex, a complex that directs a
CC       subset of long and polyadenylated poly(A) RNAs for exosomal
CC       degradation. The RNA exosome is fundamental for the degradation of RNA
CC       in eukaryotic nuclei. Substrate targeting is facilitated by its
CC       cofactor MTREX, which links to RNA-binding protein adapters (By
CC       similarity). {ECO:0000250|UniProtKB:Q28165,
CC       ECO:0000250|UniProtKB:Q86U42}.
CC   -!- SUBUNIT: Monomer and homooligomer. Identified in a IGF2BP1-dependent
CC       mRNP granule complex containing untranslated mRNAs. Binds RNA as a
CC       monomer and oligomerizes when bound to poly(A). Interacts with PAPOLA,
CC       but only in presence of oligo(A) RNA. Interacts with NUDT21/CPSF5 and
CC       transportin. Associates in a ternary complex with CPSF4 and NS/NS1 and
CC       interaction with NS/NS1, blocks nuclear export of host cell mRNAs.
CC       Associates in a single complex with SKIP and MYOD1 and interacts with
CC       SKIP in differentiated myocytes. May interact with SETX (By
CC       similarity). Interacts (via RRM domain and C-terminal arginine-rich
CC       region) with ZFP36 (via hypophosphorylated form); this interaction
CC       occurs in the nucleus in a RNA-independent manner, decreases in
CC       presence of single-stranded poly(A) RNA-oligomer and in a p38-
CC       dependent-manner and may down-regulated RNA poly(A) polymerase activity
CC       (PubMed:22844456). Component of the poly(A) tail exosome targeting
CC       (PAXT) complex composed of PABPN1, ZFC3H1 and MTREX. Interacts with
CC       ZFC3H1 in a RNase-insensitive manner (By similarity). Interacts with
CC       FRG1 (By similarity). {ECO:0000250|UniProtKB:Q86U42,
CC       ECO:0000269|PubMed:22844456}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86U42}. Nucleus
CC       {ECO:0000250|UniProtKB:Q86U42}. Nucleus speckle
CC       {ECO:0000250|UniProtKB:Q86U42}. Note=Localized in cytoplasmic mRNP
CC       granules containing untranslated mRNAs. Shuttles between the nucleus
CC       and the cytoplasm but predominantly found in the nucleus. Its nuclear
CC       import may involve the nucleocytoplasmic transport receptor transportin
CC       and a RAN-GTP-sensitive import mechanism. It is exported to the
CC       cytoplasm by a carrier-mediated pathway that is independent of mRNA
CC       traffic. Nucleus; nuclear speckle (By similarity). Colocalizes with
CC       SKIP and poly(A) RNA in nuclear speckles (By similarity).
CC       {ECO:0000250|UniProtKB:Q28165, ECO:0000250|UniProtKB:Q86U42}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CCS6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CCS6-2; Sequence=VSP_009849, VSP_009850;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9434149}.
CC   -!- DOMAIN: The RRM domain is essential for specific adenine bases
CC       recognition in the poly(A) tail but not sufficient for poly(A) binding.
CC       {ECO:0000250}.
CC   -!- PTM: Arginine dimethylation is asymmetric and involves PRMT1 and PRMT3.
CC       It does not influence the RNA binding properties (By similarity).
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing donor splice
CC       site. {ECO:0000305}.
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DR   EMBL; U93050; AAC00210.1; -; Genomic_DNA.
DR   EMBL; AK032172; BAC27741.1; -; mRNA.
DR   EMBL; BC055866; AAH55866.1; -; mRNA.
DR   CCDS; CCDS27104.1; -. [Q8CCS6-1]
DR   RefSeq; NP_062275.1; NM_019402.2. [Q8CCS6-1]
DR   AlphaFoldDB; Q8CCS6; -.
DR   SMR; Q8CCS6; -.
DR   BioGRID; 207596; 25.
DR   IntAct; Q8CCS6; 3.
DR   STRING; 10090.ENSMUSP00000022808; -.
DR   GlyGen; Q8CCS6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8CCS6; -.
DR   PhosphoSitePlus; Q8CCS6; -.
DR   EPD; Q8CCS6; -.
DR   jPOST; Q8CCS6; -.
DR   MaxQB; Q8CCS6; -.
DR   PaxDb; 10090-ENSMUSP00000022808; -.
DR   ProteomicsDB; 287761; -. [Q8CCS6-1]
DR   ProteomicsDB; 287762; -. [Q8CCS6-2]
DR   Pumba; Q8CCS6; -.
DR   DNASU; 54196; -.
DR   Ensembl; ENSMUST00000022808.14; ENSMUSP00000022808.8; ENSMUSG00000022194.16. [Q8CCS6-1]
DR   Ensembl; ENSMUST00000116476.9; ENSMUSP00000112177.3; ENSMUSG00000022194.16. [Q8CCS6-2]
DR   GeneID; 54196; -.
DR   KEGG; mmu:54196; -.
DR   UCSC; uc007txg.2; mouse. [Q8CCS6-1]
DR   UCSC; uc007txi.2; mouse. [Q8CCS6-2]
DR   AGR; MGI:1859158; -.
DR   CTD; 8106; -.
DR   MGI; MGI:1859158; Pabpn1.
DR   VEuPathDB; HostDB:ENSMUSG00000022194; -.
DR   eggNOG; KOG4209; Eukaryota.
DR   GeneTree; ENSGT00940000154606; -.
DR   HOGENOM; CLU_012062_23_1_1; -.
DR   InParanoid; Q8CCS6; -.
DR   OMA; ARFTCHE; -.
DR   OrthoDB; 155884at2759; -.
DR   PhylomeDB; Q8CCS6; -.
DR   TreeFam; TF105907; -.
DR   Reactome; R-MMU-72187; mRNA 3'-end processing.
DR   Reactome; R-MMU-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR   Reactome; R-MMU-73856; RNA Polymerase II Transcription Termination.
DR   Reactome; R-MMU-77595; Processing of Intronless Pre-mRNAs.
DR   BioGRID-ORCS; 54196; 33 hits in 83 CRISPR screens.
DR   ChiTaRS; Pabpn1; mouse.
DR   PRO; PR:Q8CCS6; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q8CCS6; Protein.
DR   Bgee; ENSMUSG00000022194; Expressed in retinal neural layer and 270 other cell types or tissues.
DR   ExpressionAtlas; Q8CCS6; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR   GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR   GO; GO:0043621; F:protein self-association; ISO:MGI.
DR   GO; GO:0070063; F:RNA polymerase binding; IDA:UniProtKB.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
DR   GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; ISO:MGI.
DR   GO; GO:1904247; P:positive regulation of polynucleotide adenylyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0031440; P:regulation of mRNA 3'-end processing; TAS:MGI.
DR   CDD; cd12550; RRM_II_PABPN1; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR23236; EUKARYOTIC TRANSLATION INITIATION FACTOR 4B/4H; 1.
DR   PANTHER; PTHR23236:SF16; POLYADENYLATE-BINDING PROTEIN 2; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   Genevisible; Q8CCS6; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Methylation;
KW   mRNA processing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   CHAIN           2..302
FT                   /note="Polyadenylate-binding protein 2"
FT                   /id="PRO_0000081712"
FT   DOMAIN          168..245
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..141
FT                   /note="Interaction with SKIP"
FT                   /evidence="ECO:0000250"
FT   REGION          115..143
FT                   /note="Stimulates PAPOLA"
FT                   /evidence="ECO:0000250"
FT   REGION          255..302
FT                   /note="Strong poly(A) affinity and self-association"
FT                   /evidence="ECO:0000250"
FT   REGION          282..302
FT                   /note="Interaction with PAPOLA"
FT                   /evidence="ECO:0000250"
FT   COILED          111..147
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        95..111
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         17
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         19
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U42"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U42"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U42"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U42"
FT   MOD_RES         231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U42"
FT   MOD_RES         234
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         234
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         255
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         255
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U42"
FT   MOD_RES         259
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         259
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q86U42"
FT   MOD_RES         261
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         263
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         265
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         273
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         275
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         283
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         285
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         287
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         290
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         292
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   MOD_RES         294
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28165"
FT   VAR_SEQ         291..292
FT                   /note="GR -> SG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_009849"
FT   VAR_SEQ         293..302
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_009850"
SQ   SEQUENCE   302 AA;  32297 MW;  2F0F6F7CC19C1986 CRC64;
     MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGDP GGAGDYGNGL ESEELEPGEL
     LPEPEPEEEP PRPRAPPGAP GPGPGSGAPG SQEEEEEPGL VEADPGDGAI EDPELEAIKA
     RVREMEEEAE KLKELQNEVE KQMNMSPPPG NAGPVIMSLE EKMEADARSI YVGNVDYGAT
     AEELEAHFHG CGSVNRVTIL CDKFSGHPKG FAYIEFSDKE SVRTSLALDE SLFRGRQIKV
     IPKRTNRPGI STTDRGFPRS RYRARTTNYN SSRSRFYSGF NSRPRGRIYR GRARATSWYS
     PY
//