PABP2_MOUSE
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 03-AUG-2022, entry version 149.
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; 23.
DR IntAct; Q8CCS6; 3.
DR STRING; 10090.ENSMUSP00000022808; -.
DR iPTMnet; Q8CCS6; -.
DR PhosphoSitePlus; Q8CCS6; -.
DR EPD; Q8CCS6; -.
DR jPOST; Q8CCS6; -.
DR MaxQB; Q8CCS6; -.
DR PaxDb; Q8CCS6; -.
DR PRIDE; Q8CCS6; -.
DR ProteomicsDB; 287761; -. [Q8CCS6-1]
DR ProteomicsDB; 287762; -. [Q8CCS6-2]
DR DNASU; 54196; -.
DR Ensembl; ENSMUST00000022808; ENSMUSP00000022808; ENSMUSG00000022194. [Q8CCS6-1]
DR Ensembl; ENSMUST00000116476; ENSMUSP00000112177; ENSMUSG00000022194. [Q8CCS6-2]
DR GeneID; 54196; -.
DR KEGG; mmu:54196; -.
DR UCSC; uc007txg.2; mouse. [Q8CCS6-1]
DR UCSC; uc007txi.2; mouse. [Q8CCS6-2]
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; ISAEDQF; -.
DR OrthoDB; 1412946at2759; -.
DR PhylomeDB; Q8CCS6; -.
DR TreeFam; TF105907; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-MMU-72187; mRNA 3'-end processing.
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 78 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 267 other tissues.
DR ExpressionAtlas; Q8CCS6; baseline and differential.
DR Genevisible; Q8CCS6; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; TAS:MGI.
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:0006378; P:mRNA polyadenylation; TAS:MGI.
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 Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034911; PABP2.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23236:SF16; PTHR23236:SF16; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
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
