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Polyadenylate-binding protein 2 (PABP-2) (Poly(A)-binding protein 2) (Nuclear poly(A)-binding protein 1) (Poly(A)-binding protein II) (PABII) (Polyadenylate-binding nuclear protein 1)

 PABP2_MOUSE             Reviewed;         302 AA.
Q8CCS6; O35935;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 126.
RecName: Full=Polyadenylate-binding protein 2;
Short=PABP-2;
Short=Poly(A)-binding protein 2;
AltName: Full=Nuclear poly(A)-binding protein 1;
AltName: Full=Poly(A)-binding protein II;
Short=PABII;
AltName: Full=Polyadenylate-binding nuclear protein 1;
Name=Pabpn1; Synonyms=Pab2, Pabp2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=129;
PubMed=9434149; DOI=10.1016/S0167-4781(97)00147-4;
Lee Y.J., Lee J., Yang I.C., Hahn Y., Lee Y., Chung J.H.;
"Genomic structure and expression of murine poly(A) binding protein II
gene.";
Biochim. Biophys. Acta 1395:40-46(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N; TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
INTERACTION WITH ZFP36.
PubMed=22844456; DOI=10.1371/journal.pone.0041313;
Su Y.L., Wang S.C., Chi ang P.Y., Lin N.Y., Shen Y.F., Chang G.D.,
Chang C.J.;
"Tristetraprolin inhibits poly(A)-tail synthesis in nuclear mRNA that
contains AU-rich elements by interacting with poly(A)-binding protein
nuclear 1.";
PLoS ONE 7:E41313-E41313(2012).
[6]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-17, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: 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. Subunit of the trimeric poly(A)
tail exosome targeting (PAXT) complex, a complex that directs a
subset of long and polyadenylated poly(A) RNAs for exosomal
degradation. The RNA exosome is fundamental for the degradation of
RNA in eukaryotic nuclei. Substrate targeting is facilitated by
its cofactor SKIV2L2/MTR4, which links to RNA-binding protein
adapters (By similarity). {ECO:0000250|UniProtKB:Q28165,
ECO:0000250|UniProtKB:Q86U42}.
-!- SUBUNIT: 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. May interact with SETX (By similarity).
Interacts (via RRM domain and C-terminal arginine-rich region)
with ZFP36 (via hypophosphorylated form); this interaction occurs
in the nucleus in a RNA-independent manner, decreases in presence
of single-stranded poly(A) RNA-oligomer and in a p38-dependent-
manner and may down-regulated RNA poly(A) polymerase activity
(PubMed:22844456). Component of the poly(A) tail exosome targeting
(PAXT) complex composed of PABPN1, ZFC3H1 and SKIV2L2/MTR.
Interacts with ZFC3H1 in a RNase-insensitive manner (By
similarity). {ECO:0000250|UniProtKB:Q86U42,
ECO:0000269|PubMed:22844456}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86U42}.
Nucleus {ECO:0000250|UniProtKB:Q86U42}. Nucleus speckle
{ECO:0000250|UniProtKB:Q86U42}. 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). {ECO:0000250|UniProtKB:Q28165,
ECO:0000250|UniProtKB:Q86U42}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8CCS6-1; Sequence=Displayed;
Name=2;
IsoId=Q8CCS6-2; Sequence=VSP_009849, VSP_009850;
Note=May be due to a competing donor splice site.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9434149}.
-!- DOMAIN: The RRM domain is essential for specific adenine bases
recognition in the poly(A) tail but not sufficient for poly(A)
binding. {ECO:0000250}.
-!- PTM: Arginine dimethylation is asymmetric and involves PRMT1 and
PRMT3. It does not influence the RNA binding properties (By
similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U93050; AAC00210.1; -; Genomic_DNA.
EMBL; AK032172; BAC27741.1; -; mRNA.
EMBL; BC055866; AAH55866.1; -; mRNA.
CCDS; CCDS27104.1; -. [Q8CCS6-1]
RefSeq; NP_062275.1; NM_019402.2. [Q8CCS6-1]
UniGene; Mm.7723; -.
ProteinModelPortal; Q8CCS6; -.
SMR; Q8CCS6; -.
BioGrid; 207596; 2.
IntAct; Q8CCS6; 2.
MINT; MINT-1867341; -.
STRING; 10090.ENSMUSP00000022808; -.
iPTMnet; Q8CCS6; -.
PhosphoSitePlus; Q8CCS6; -.
PaxDb; Q8CCS6; -.
PRIDE; Q8CCS6; -.
Ensembl; ENSMUST00000022808; ENSMUSP00000022808; ENSMUSG00000022194. [Q8CCS6-1]
Ensembl; ENSMUST00000116476; ENSMUSP00000112177; ENSMUSG00000022194. [Q8CCS6-2]
GeneID; 54196; -.
KEGG; mmu:54196; -.
UCSC; uc007txg.2; mouse. [Q8CCS6-1]
UCSC; uc007txi.2; mouse. [Q8CCS6-2]
CTD; 8106; -.
MGI; MGI:1859158; Pabpn1.
eggNOG; KOG4209; Eukaryota.
eggNOG; ENOG4111PFV; LUCA.
GeneTree; ENSGT00390000001517; -.
HOGENOM; HOG000208465; -.
HOVERGEN; HBG107480; -.
InParanoid; Q8CCS6; -.
KO; K14396; -.
PhylomeDB; Q8CCS6; -.
TreeFam; TF105907; -.
Reactome; R-MMU-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
Reactome; R-MMU-72187; mRNA 3'-end processing.
Reactome; R-MMU-77595; Processing of Intronless Pre-mRNAs.
ChiTaRS; Pabpn1; mouse.
PRO; PR:Q8CCS6; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000022194; -.
CleanEx; MM_PABPN1; -.
ExpressionAtlas; Q8CCS6; baseline and differential.
Genevisible; Q8CCS6; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008143; F:poly(A) binding; TAS:MGI.
GO; GO:0043621; F:protein self-association; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0070063; F:RNA polymerase binding; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0006378; P:mRNA polyadenylation; TAS:MGI.
GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; ISO:MGI.
GO; GO:1904247; P:positive regulation of polynucleotide adenylyltransferase activity; IMP:UniProtKB.
InterPro; IPR034911; PABP2.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR44316; PTHR44316; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Coiled coil; Complete proteome;
Cytoplasm; Methylation; mRNA processing; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q28165}.
CHAIN 2 302 Polyadenylate-binding protein 2.
/FTId=PRO_0000081712.
DOMAIN 168 245 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 2 141 Interaction with SKIP. {ECO:0000250}.
REGION 115 143 Stimulates PAPOLA. {ECO:0000250}.
REGION 255 302 Strong poly(A) affinity and self-
association. {ECO:0000250}.
REGION 282 302 Interaction with PAPOLA. {ECO:0000250}.
COILED 111 147 {ECO:0000255}.
COMPBIAS 2 14 Ala-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 17 17 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000250|UniProtKB:Q86U42}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000250|UniProtKB:Q86U42}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000250|UniProtKB:Q86U42}.
MOD_RES 146 146 Phosphoserine.
{ECO:0000250|UniProtKB:Q86U42}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000250|UniProtKB:Q86U42}.
MOD_RES 234 234 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 234 234 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 255 255 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 255 255 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q86U42}.
MOD_RES 259 259 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 259 259 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q86U42}.
MOD_RES 261 261 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 263 263 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 265 265 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 273 273 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 275 275 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 283 283 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 285 285 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 287 287 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 290 290 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 292 292 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 294 294 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
VAR_SEQ 291 292 GR -> SG (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009849.
VAR_SEQ 293 302 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009850.
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


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