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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_BOVIN             Reviewed;         306 AA.
Q28165; A3KN38;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
27-SEP-2017, entry version 132.
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;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 174-187, RNA-BINDING,
FUNCTION IN PRE-MESSENGER POLYADENYLATION, SUBUNIT, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Aorta, Liver, Muzzle epithelium, and Thymus;
PubMed=7479061; DOI=10.1093/nar/23.20.4034;
Nemeth A., Krause S., Blank D., Jenny A., Jenoe P., Lustig A.,
Wahle E.;
"Isolation of genomic and cDNA clones encoding bovine poly(A) binding
protein II.";
Nucleic Acids Res. 23:4034-4041(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Fetal pons;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[3]
PROTEIN SEQUENCE OF 2-135; 140-207; 214-243 AND 248-306, MASS
SPECTROMETRY, METHYLATION AT ARG-238; ARG-259; ARG-263; ARG-265;
ARG-267; ARG-269; ARG-277; ARG-279; ARG-287; ARG-289; ARG-291;
ARG-294; ARG-296 AND ARG-298, AND ACETYLATION AT ALA-2.
PubMed=10224081; DOI=10.1074/jbc.274.19.13229;
Smith J.J., Ruecknagel K.P., Schierhorn A., Tang J., Nemeth A.,
Linder M., Herschman H.R., Wahle E.;
"Unusual sites of arginine methylation in poly(A)-binding protein II
and in vitro methylation by protein arginine methyltransferases PRMT1
and PRMT3.";
J. Biol. Chem. 274:13229-13234(1999).
[4]
PROTEIN SEQUENCE OF 2-306, STRUCTURAL ANALYSIS OF POLY-ALA EXTENSION,
AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=14627730; DOI=10.1110/ps.03214703;
Scheuermann T., Schulz B., Blume A., Wahle E., Rudolph R., Schwarz E.;
"Trinucleotide expansions leading to an extended poly-L-alanine
segment in the poly(A) binding protein PABPN1 cause fibril
formation.";
Protein Sci. 12:2685-2692(2003).
[5]
FUNCTION.
PubMed=10481015; DOI=10.1093/nar/27.19.3771;
Benoit B., Nemeth A., Aulner N., Kuhn U., Simonelig M., Wahle E.,
Bourbon H.-M.;
"The Drosophila poly(A)-binding protein II is ubiquitous throughout
Drosophila development and has the same function in mRNA
polyadenylation as its bovine homolog in vitro.";
Nucleic Acids Res. 27:3771-3778(1999).
[6]
MUTAGENESIS OF TYR-175 AND PHE-215, INTERACTION WITH TRANSPORTIN, AND
SUBCELLULAR LOCATION.
PubMed=10688363; DOI=10.1017/S1355838200991908;
Calado A., Kutay U., Kuehn U., Wahle E., Carmo-Fonseca M.;
"Deciphering the cellular pathway for transport of poly(A)-binding
protein II.";
RNA 6:245-256(2000).
[7]
FUNCTION IN PAPOLA STIMULATION, RNA-BINDING, HOMOOLIGOMERIZATION, AND
MUTAGENESIS OF TYR-175; LYS-213 AND PHE-215.
PubMed=12637556; DOI=10.1074/jbc.M209886200;
Kuehn U., Nemeth A., Meyer S., Wahle E.;
"The RNA binding domains of the nuclear poly(A)-binding protein.";
J. Biol. Chem. 278:16916-16925(2003).
[8]
FUNCTION IN PAPOLA STIMULATION, MUTAGENESIS OF LEU-119; GLU-120;
ILE-122; LYS-123; ALA-124; VAL-126; MET-129; GLU-131; ALA-133;
LYS-135; LEU-136 AND VAL-143, AND INTERACTION WITH PAPOLA.
PubMed=12853485; DOI=10.1093/emboj/cdg347;
Kerwitz Y., Kuehn U., Lilie H., Knoth A., Scheuermann T.,
Friedrich H., Schwarz E., Wahle E.;
"Stimulation of poly(A) polymerase through a direct interaction with
the nuclear poly(A) binding protein allosterically regulated by RNA.";
EMBO J. 22:3705-3714(2003).
-!- 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 (PubMed:7479061, PubMed:10481015).
Stimulates poly(A) polymerase (PAPOLA) conferring processivity on
the poly(A) tail elongation reaction and controls also the poly(A)
tail length (PubMed:12637556). Increases the affinity of poly(A)
polymerase for RNA (PubMed:12637556, PubMed:12853485). 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 (By similarity). Binds to
poly(A) and to poly(G) with high affinity (PubMed:7479061,
PubMed:12637556). May protect the poly(A) tail from degradation
(PubMed:7479061). {ECO:0000250|UniProtKB:Q86U42,
ECO:0000269|PubMed:12637556, ECO:0000269|PubMed:12853485,
ECO:0000269|PubMed:7479061}.
-!- SUBUNIT: Monomer and homooligomer. Binds RNA as a monomer and
oligomerizes when bound to poly(A). 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. Interacts with NUDT21/CPSF5. Identified in a IGF2BP1-
dependent mRNP granule complex containing untranslated mRNAs.
Interacts with PAPOLA, but only in presence of oligo(A) RNA.
Interacts with transportin. May interact with SETX. 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 (By
similarity). {ECO:0000250|UniProtKB:Q86U42,
ECO:0000250|UniProtKB:Q8CCS6, ECO:0000269|PubMed:10688363,
ECO:0000269|PubMed:12853485, ECO:0000269|PubMed:7479061}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10688363}.
Cytoplasm {ECO:0000269|PubMed:10688363}. Nucleus speckle
{ECO:0000269|PubMed:10688363}. Note=Localized in cytoplasmic mRNP
granules containing untranslated mRNAs (By similarity). 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 (PubMed:10688363). Is exported to the cytoplasm by a
carrier-mediated pathway that is independent of mRNA traffic.
Nucleus; nuclear speckle. Colocalizes with SKIP and poly(A) RNA in
nuclear speckles (By similarity). {ECO:0000250|UniProtKB:Q86U42,
ECO:0000269|PubMed:10688363}.
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DOMAIN: The RRM domain is essential for specific adenine bases
recognition in the poly(A) tail but not sufficient for poly(A)
binding.
-!- PTM: Arginine dimethylation is asymmetric and involves PRMT1 and
PRMT3. It does not influence the RNA binding properties.
-!- MASS SPECTROMETRY: Mass=33253; Mass_error=0.5; Method=MALDI;
Range=2-306; Evidence={ECO:0000269|PubMed:10224081};
-----------------------------------------------------------------------
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EMBL; X89969; CAA62006.1; -; mRNA.
EMBL; BC133558; AAI33559.1; -; mRNA.
PIR; S59863; S59863.
RefSeq; NP_776994.1; NM_174569.2.
UniGene; Bt.5085; -.
ProteinModelPortal; Q28165; -.
SMR; Q28165; -.
STRING; 9913.ENSBTAP00000021887; -.
iPTMnet; Q28165; -.
PaxDb; Q28165; -.
PRIDE; Q28165; -.
Ensembl; ENSBTAT00000021887; ENSBTAP00000021887; ENSBTAG00000006884.
GeneID; 282298; -.
KEGG; bta:282298; -.
CTD; 8106; -.
eggNOG; KOG4209; Eukaryota.
eggNOG; ENOG4111PFV; LUCA.
GeneTree; ENSGT00390000001517; -.
HOGENOM; HOG000208465; -.
HOVERGEN; HBG107480; -.
InParanoid; Q28165; -.
KO; K14396; -.
OMA; RTTSWYS; -.
OrthoDB; EOG091G0PAK; -.
TreeFam; TF105907; -.
Reactome; R-BTA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-BTA-72163; mRNA Splicing - Major Pathway.
Reactome; R-BTA-72187; mRNA 3'-end processing.
Reactome; R-BTA-77595; Processing of Intronless Pre-mRNAs.
Proteomes; UP000009136; Chromosome 10.
Bgee; ENSBTAG00000006884; -.
ExpressionAtlas; Q28165; baseline.
GO; GO:0097136; C:Bcl-2 family protein complex; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; ISS:UniProtKB.
GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0043621; F:protein self-association; IDA:MGI.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0070063; F:RNA polymerase binding; ISS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:1904247; P:positive regulation of polynucleotide adenylyltransferase activity; ISS:UniProtKB.
InterPro; IPR034911; PABP2.
InterPro; IPR000504; RRM_dom.
PANTHER; PTHR24012:SF667; PTHR24012:SF667; 1.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; Methylation; mRNA processing; Nucleus;
Phosphoprotein; Reference proteome; RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10224081,
ECO:0000269|PubMed:14627730}.
CHAIN 2 306 Polyadenylate-binding protein 2.
/FTId=PRO_0000081710.
DOMAIN 172 249 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 2 145 Interaction with SKIP. {ECO:0000250}.
REGION 119 147 Stimulates PAPOLA.
REGION 155 306 Necessary for homooligomerization.
{ECO:0000250}.
REGION 286 306 Interaction with PAPOLA.
{ECO:0000269|PubMed:12853485}.
COILED 115 151 {ECO:0000255}.
COMPBIAS 2 14 Ala-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:10224081}.
MOD_RES 17 17 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q8CCS6}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000250|UniProtKB:Q86U42}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000250|UniProtKB:Q86U42}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000250|UniProtKB:Q86U42}.
MOD_RES 235 235 Phosphoserine.
{ECO:0000250|UniProtKB:Q86U42}.
MOD_RES 238 238 Asymmetric dimethylarginine; alternate.
{ECO:0000269|PubMed:10224081}.
MOD_RES 238 238 Omega-N-methylarginine; alternate.
{ECO:0000269|PubMed:10224081}.
MOD_RES 259 259 Asymmetric dimethylarginine; alternate.
{ECO:0000269|PubMed:10224081}.
MOD_RES 259 259 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q86U42}.
MOD_RES 263 263 Asymmetric dimethylarginine; alternate.
{ECO:0000269|PubMed:10224081}.
MOD_RES 263 263 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q86U42}.
MOD_RES 265 265 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:10224081}.
MOD_RES 267 267 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:10224081}.
MOD_RES 269 269 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:10224081}.
MOD_RES 277 277 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:10224081}.
MOD_RES 279 279 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:10224081}.
MOD_RES 287 287 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:10224081}.
MOD_RES 289 289 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:10224081}.
MOD_RES 291 291 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:10224081}.
MOD_RES 294 294 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:10224081}.
MOD_RES 296 296 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:10224081}.
MOD_RES 298 298 Asymmetric dimethylarginine.
{ECO:0000269|PubMed:10224081}.
MUTAGEN 119 119 L->A: Strong defects in the stimulation
of PAPOLA. {ECO:0000269|PubMed:12853485}.
MUTAGEN 120 120 E->A: No defects in the stimulation of
PAPOLA. {ECO:0000269|PubMed:12853485}.
MUTAGEN 122 122 I->Q: Strong defects in the stimulation
of PAPOLA. {ECO:0000269|PubMed:12853485}.
MUTAGEN 123 123 K->A: No defects in the stimulation of
PAPOLA. {ECO:0000269|PubMed:12853485}.
MUTAGEN 124 124 A->S: Slight defects in the stimulation
of PAPOLA. {ECO:0000269|PubMed:12853485}.
MUTAGEN 126 126 V->S: No defects in the stimulation of
PAPOLA. {ECO:0000269|PubMed:12853485}.
MUTAGEN 129 129 M->A: Slight defects in the stimulation
of PAPOLA. {ECO:0000269|PubMed:12853485}.
MUTAGEN 131 131 E->A: Slight defects in the stimulation
of PAPOLA. {ECO:0000269|PubMed:12853485}.
MUTAGEN 133 133 A->S: No defects in the stimulation of
PAPOLA. {ECO:0000269|PubMed:12853485}.
MUTAGEN 135 135 K->A: No defects in the stimulation of
PAPOLA. {ECO:0000269|PubMed:12853485}.
MUTAGEN 136 136 L->A,S: Inactivates PAPOLA.
{ECO:0000269|PubMed:12853485}.
MUTAGEN 143 143 V->A: Slight defects in the stimulation
of PAPOLA. {ECO:0000269|PubMed:12853485}.
MUTAGEN 175 175 Y->A: At least 20% decrease in poly(A)
binding; no change in nuclear targeting;
distributed uniformly in the nucleoplasm;
not detected in speckles. Same phenotypic
effect; when associated with A-215.
{ECO:0000269|PubMed:10688363,
ECO:0000269|PubMed:12637556}.
MUTAGEN 213 213 K->Q: No changes in poly(A) affinity.
{ECO:0000269|PubMed:12637556}.
MUTAGEN 215 215 F->A: At least 20% decrease in poly(A);
binding; no change in nuclear targeting,
distributed uniformly in the nucleoplasm;
not detected in speckles. Same phenotypic
effect; when associated with A-175.
{ECO:0000269|PubMed:10688363,
ECO:0000269|PubMed:12637556}.
SEQUENCE 306 AA; 32766 MW; 11D5E5A555458246 CRC64;
MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGAP GGAGDYGNGL ESEELEPEEL
LLEPEPEPEP EEEPPRPRAP PGAPGPGPGS GAPGNQEEEE ESGLVEGDPG DGAIEDPELE
AIKARVREME EEAEKLKELQ NEVEKQMNMS PPPGNAGPVI MSIEEKMEAD ARSIYVGNVD
YGATAEELEA HFHGCGSVNR VTILCDKFSG HPKGFAYIEF SDKESVRTSL ALDESLFRGR
QIKVIPKRTN RPGISTTDRG FPRARYRART TNYNSSRSRF YSGFNSRPRG RVYRGRARAT
SWYSPY


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