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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_HUMAN             Reviewed;         306 AA.
Q86U42; D3DS49; O43484;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 151.
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;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), POLYMORPHISM OF
POLY-ALA REGION, AND DISEASE.
PubMed=9462747; DOI=10.1038/ng0298-164;
Brais B., Bouchard J.-P., Xie Y.-G., Rochefort D.L., Chretien N.,
Tome F.M.S., Lafreniere R.G., Rommens J.M., Uyama E., Nohira O.,
Blumen S., Korcyn A.D., Heutink P., Mathieu J., Duranceau A.,
Codere F., Fardeau M., Rouleau G.A.;
"Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular
dystrophy.";
Nat. Genet. 18:164-167(1998).
[2]
ERRATUM.
Brais B., Bouchard J.-P., Xie Y.-G., Rochefort D.L., Chretien N.,
Tome F.M.S., Lafreniere R.G., Rommens J.M., Uyama E., Nohira O.,
Blumen S., Korcyn A.D., Heutink P., Mathieu J., Duranceau A.,
Codere F., Fardeau M., Rouleau G.A.;
Nat. Genet. 19:404-404(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Fetal brain;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
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).
[6]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA], ASSOCIATION WITH CPSF AND NS/NS1,
AND INTERACTION WITH NS/NS1.
TISSUE=Cervix carcinoma;
PubMed=10205180; DOI=10.1093/emboj/18.8.2273;
Chen Z., Li Y., Krug R.M.;
"Influenza A virus NS1 protein targets poly(A)-binding protein II of
the cellular 3'-end processing machinery.";
EMBO J. 18:2273-2283(1999).
[7]
PROTEIN SEQUENCE OF 2-17 AND 228-238, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (APR-2005) to UniProtKB.
[8]
SUBCELLULAR LOCATION.
PubMed=11001936; DOI=10.1093/oxfordjournals.hmg.a018924;
Calado A., Tome F.M.S., Brais B., Rouleau G.A., Kuehn U., Wahle E.,
Carmo-Fonseca M.;
"Nuclear inclusions in oculopharyngeal muscular dystrophy consist of
poly(A) binding protein 2 aggregates which sequester poly(A) RNA.";
Hum. Mol. Genet. 9:2321-2328(2000).
[9]
SUBCELLULAR LOCATION, AND NUCLEOCYTOPLASMIC SHUTTLING.
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).
[10]
FUNCTION IN CELL DEATH, HOMOOLIGOMERIZATION, AND MUTAGENESIS OF
213-LYS--PHE-220 AND 301-SER--TYR-306.
PubMed=11689481; DOI=10.1093/hmg/10.21.2341;
Fan X., Dion P., Laganiere J., Brais B., Rouleau G.A.;
"Oligomerization of polyalanine expanded PABPN1 facilitates nuclear
protein aggregation that is associated with cell death.";
Hum. Mol. Genet. 10:2341-2351(2001).
[11]
FUNCTION IN MYOGENIC DIFFERENTIATION, ASSOCIATION WITH SKIP AND MYOD1,
INTERACTION WITH SKIP, AND SUBCELLULAR LOCATION.
PubMed=11371506; DOI=10.1093/hmg/10.11.1129;
Kim Y.-J., Noguchi S., Hayashi Y.K., Tsukahara T., Shimizu T.,
Arahata K.;
"The product of an oculopharyngeal muscular dystrophy gene, poly(A)-
binding protein 2, interacts with SKIP and stimulates muscle-specific
gene expression.";
Hum. Mol. Genet. 10:1129-1139(2001).
[12]
SUBCELLULAR LOCATION.
PubMed=14663186; DOI=10.1097/00001756-200312190-00009;
Sugaya K., Matsubara S., Miyamoto K., Kawata A., Hayashi H.;
"An aggregate-prone conformational epitope in trinucleotide repeat
diseases.";
NeuroReport 14:2331-2335(2003).
[13]
INTERACTION WITH NUDT21/CPSF5.
PubMed=15169763; DOI=10.1074/jbc.M403927200;
Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M.;
"Distinct sequence motifs within the 68-kDa subunit of cleavage factor
Im mediate RNA binding, protein-protein interactions, and subcellular
localization.";
J. Biol. Chem. 279:35788-35797(2004).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS
SPECTROMETRY, AND SUBCELLULAR LOCATION.
PubMed=17289661; DOI=10.1074/mcp.M600346-MCP200;
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
Johnsen A.H., Christiansen J., Nielsen F.C.;
"Molecular composition of IMP1 ribonucleoprotein granules.";
Mol. Cell. Proteomics 6:798-811(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-95 AND SER-150,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-19; SER-95 AND SER-150, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
INTERACTION WITH SETX.
PubMed=21700224; DOI=10.1016/j.molcel.2011.04.026;
Skourti-Stathaki K., Proudfoot N.J., Gromak N.;
"Human senataxin resolves RNA/DNA hybrids formed at transcriptional
pause sites to promote Xrn2-dependent termination.";
Mol. Cell 42:794-805(2011).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-19 AND SER-95, CLEAVAGE OF INITIATOR METHIONINE
[LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-150, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-259 AND ARG-263, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
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).
[28]
FUNCTION, SUBUNIT, AND INTERACTION WITH ZFC3H1.
PubMed=27871484; DOI=10.1016/j.molcel.2016.09.025;
Meola N., Domanski M., Karadoulama E., Chen Y., Gentil C., Pultz D.,
Vitting-Seerup K., Lykke-Andersen S., Andersen J.S., Sandelin A.,
Jensen T.H.;
"Identification of a nuclear exosome decay pathway for processed
transcripts.";
Mol. Cell 64:520-533(2016).
[29]
SUBCELLULAR LOCATION.
PubMed=27209344; DOI=10.1016/j.nmd.2016.05.001;
Matsubara S., Shimizu T., Komori T., Mori-Yoshimura M., Minami N.,
Hayashi Y.K.;
"Nuclear inclusions mimicking poly(A)-binding protein nuclear 1
inclusions in a case of inclusion body myopathy associated with Paget
disease of bone and frontotemporal dementia with a novel mutation in
the valosin-containing protein gene.";
Neuromuscul. Disord. 26:436-440(2016).
[30]
VARIANT OPMD ALA-6 INS, AND DISEASE.
PubMed=12673802; DOI=10.1002/humu.9138;
van der Sluijs B.M., van Engelen B.G.M., Hoefsloot L.H.;
"Oculopharyngeal muscular dystrophy (OPMD) due to a small duplication
in the PABPN1 gene.";
Hum. Mutat. 21:553-553(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 (By similarity). Stimulates poly(A)
polymerase (PAPOLA) conferring processivity on the poly(A) tail
elongation reaction and controls also the poly(A) tail length (By
similarity). Increases the affinity of poly(A) polymerase for RNA
(By similarity). 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
(PubMed:11371506). Binds to poly(A) and to poly(G) with high
affinity (By similarity). May protect the poly(A) tail from
degradation (By similarity). 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
(PubMed:27871484). {ECO:0000250|UniProtKB:Q28165,
ECO:0000269|PubMed:11371506, ECO:0000269|PubMed:27871484}.
-!- SUBUNIT: May interact with SETX (PubMed:21700224). Monomer and
homooligomer. 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 transportin. Identified in a IGF2BP1-
dependent mRNP granule complex containing untranslated mRNAs.
Association in a ternary complex with CPSF4 and influenza A virus
NS1 blocks pre-mRNAs processing, thereby preventing 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. 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). Component of the
poly(A) tail exosome targeting (PAXT) complex made of accessory
factors, such as PABPN1, ZFC3H1 and SKIV2L2/MTR4
(PubMed:27871484). Interacts with ZFC3H1 in a RNase-insensitive
manner (PubMed:27871484). {ECO:0000250|UniProtKB:Q8CCS6,
ECO:0000269|PubMed:10205180, ECO:0000269|PubMed:11371506,
ECO:0000269|PubMed:15169763, ECO:0000269|PubMed:17289661,
ECO:0000269|PubMed:21700224, ECO:0000269|PubMed:27871484}.
-!- INTERACTION:
P11940:PABPC1; NbExp=2; IntAct=EBI-1226435, EBI-81531;
Q13573:SNW1; NbExp=5; IntAct=EBI-1226435, EBI-632715;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10688363,
ECO:0000269|PubMed:11001936, ECO:0000269|PubMed:14663186,
ECO:0000269|PubMed:27209344}. Cytoplasm
{ECO:0000269|PubMed:10688363, ECO:0000269|PubMed:11001936,
ECO:0000269|PubMed:14663186, ECO:0000269|PubMed:17289661}. Nucleus
speckle {ECO:0000269|PubMed:10688363,
ECO:0000269|PubMed:11371506}. Note=Localized in cytoplasmic mRNP
granules containing untranslated mRNAs. Shuttles between the
nucleus and the cytoplasm but predominantly found in the nucleus
(PubMed:10688363). Its nuclear import may involve the
nucleocytoplasmic transport receptor transportin and a RAN-GTP-
sensitive import mechanism (By similarity). Is exported to the
cytoplasm by a carrier-mediated pathway that is independent of
mRNA traffic. Colocalizes with SKIP and poly(A) RNA in nuclear
speckles (By similarity). Intranuclear filamentous inclusions or
"aggregates" are detected in the myocytes of patients; these
inclusions contain PABPN1, ubiquitin, subunits of the proteasome
and poly(A) RNA. {ECO:0000250|UniProtKB:Q28165,
ECO:0000269|PubMed:10688363, ECO:0000269|PubMed:11001936,
ECO:0000269|PubMed:11371506, ECO:0000269|PubMed:14663186,
ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:27209344}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q86U42-1; Sequence=Displayed;
Name=2;
IsoId=Q86U42-2; Sequence=VSP_009847, VSP_009848;
Note=May be due to a competing donor splice site.;
Name=3; Synonyms=BCL2L2-PABPN1;
IsoId=Q92843-2; Sequence=External;
Note=Based on a readthrough transcript which may produce a
BCL2L2-PABPN1 fusion protein. No experimental confirmation
available. Contains a phosphoserine at position 177. Contains a
phosphoserine at position 262. Contains a omega-N-methylarginine
at position 286. Contains a omega-N-methylarginine at position
290. {ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24129315, ECO:0000244|PubMed:24275569};
-!- 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. {ECO:0000250}.
-!- PTM: Arginine dimethylation is asymmetric and involves PRMT1 and
PRMT3. It does not influence the RNA binding properties (By
similarity). {ECO:0000250}.
-!- POLYMORPHISM: The poly-Ala region of PABPN1 is polymorphic (6-7
repeats) in the population and is expanded to 8-13 repeats in OPMD
patients. Compound heterozygotes for (GCG)9 mutation and a (GCG)7
allele result in earlier onset and more severe clinical
manifestations of the disease.
-!- DISEASE: Oculopharyngeal muscular dystrophy (OPMD) [MIM:164300]: A
form of late-onset slowly progressive myopathy characterized by
eyelid ptosis, dysphagia and, sometimes by other cranial and limb-
muscle involvement. {ECO:0000269|PubMed:12673802}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: The association of the expanded polyalanine
mutations together with the capability to oligomerize may induce
intranuclear inclusions and cell death. Expanded polyalanine
mutations may either result from unequal crossing over during germ
cell homologous recombination or from DNA slippage. The pathogenic
mechanisms mediated by polyalanine expansion mutations may be
either a general disruption of cellular RNA metabolism due to the
trapping by the inclusions of PABPN1, mRNAs and/or nuclear
proteins, resulting in the induction of cell death; or may change
the normal muscle cell differentiation.
{ECO:0000269|PubMed:11689481}.
-!- SEQUENCE CAUTION:
Sequence=CAD62310.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AF026029; AAC39596.1; -; Genomic_DNA.
EMBL; BX247976; CAD62310.1; ALT_INIT; mRNA.
EMBL; CH471078; EAW66167.1; -; Genomic_DNA.
EMBL; CH471078; EAW66168.1; -; Genomic_DNA.
EMBL; BC010939; AAH10939.1; -; mRNA.
CCDS; CCDS9592.1; -. [Q86U42-1]
RefSeq; NP_004634.1; NM_004643.3. [Q86U42-1]
UniGene; Hs.707712; -.
PDB; 3B4D; X-ray; 2.00 A; A=167-254.
PDB; 3B4M; X-ray; 2.82 A; A/B/C/D=167-254.
PDB; 3UCG; X-ray; 1.95 A; A=167-254.
PDBsum; 3B4D; -.
PDBsum; 3B4M; -.
PDBsum; 3UCG; -.
ProteinModelPortal; Q86U42; -.
SMR; Q86U42; -.
BioGrid; 113777; 43.
DIP; DIP-37968N; -.
IntAct; Q86U42; 35.
MINT; MINT-89761; -.
STRING; 9606.ENSP00000216727; -.
iPTMnet; Q86U42; -.
PhosphoSitePlus; Q86U42; -.
BioMuta; PABPN1; -.
DMDM; 46403176; -.
EPD; Q86U42; -.
PaxDb; Q86U42; -.
PeptideAtlas; Q86U42; -.
PRIDE; Q86U42; -.
TopDownProteomics; Q86U42-1; -. [Q86U42-1]
Ensembl; ENST00000216727; ENSP00000216727; ENSG00000100836. [Q86U42-1]
Ensembl; ENST00000397276; ENSP00000380446; ENSG00000100836. [Q86U42-2]
GeneID; 8106; -.
KEGG; hsa:8106; -.
UCSC; uc001wjj.4; human. [Q86U42-1]
CTD; 8106; -.
DisGeNET; 8106; -.
EuPathDB; HostDB:ENSG00000100836.10; -.
GeneCards; PABPN1; -.
GeneReviews; PABPN1; -.
HGNC; HGNC:8565; PABPN1.
HPA; HPA000637; -.
MalaCards; PABPN1; -.
MIM; 164300; phenotype.
MIM; 602279; gene.
neXtProt; NX_Q86U42; -.
OpenTargets; ENSG00000100836; -.
Orphanet; 270; Oculopharyngeal muscular dystrophy.
PharmGKB; PA32891; -.
eggNOG; KOG4209; Eukaryota.
eggNOG; ENOG4111PFV; LUCA.
GeneTree; ENSGT00390000001517; -.
HOGENOM; HOG000208465; -.
HOVERGEN; HBG107480; -.
InParanoid; Q86U42; -.
KO; K14396; -.
OMA; RTTSWYS; -.
OrthoDB; EOG091G0PAK; -.
PhylomeDB; Q86U42; -.
TreeFam; TF105907; -.
Reactome; R-HSA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-HSA-168315; Inhibition of Host mRNA Processing and RNA Silencing.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72187; mRNA 3'-end processing.
Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
EvolutionaryTrace; Q86U42; -.
GeneWiki; PABPN1; -.
GenomeRNAi; 8106; -.
PMAP-CutDB; Q86U42; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100836; -.
CleanEx; HS_PABPN1; -.
ExpressionAtlas; Q86U42; baseline and differential.
Genevisible; Q86U42; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
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:0046778; P:modification by virus of host mRNA processing; TAS:Reactome.
GO; GO:0031124; P:mRNA 3'-end processing; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:UniProtKB.
GO; GO:1904247; P:positive regulation of polynucleotide adenylyltransferase activity; ISS:UniProtKB.
GO; GO:0006396; P:RNA processing; TAS:ProtInc.
GO; GO:0006369; P:termination of RNA polymerase II transcription; TAS:Reactome.
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;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Methylation; mRNA processing; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; RNA-binding;
Triplet repeat expansion.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.7}.
CHAIN 2 306 Polyadenylate-binding protein 2.
/FTId=PRO_0000081711.
DOMAIN 172 249 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 2 145 Interaction with SKIP.
{ECO:0000269|PubMed:11371506}.
REGION 119 147 Stimulates PAPOLA. {ECO:0000250}.
REGION 155 306 Necessary for homooligomerization.
REGION 286 306 Interaction with PAPOLA. {ECO:0000250}.
COILED 115 151 {ECO:0000255}.
COMPBIAS 2 14 Ala-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.7}.
MOD_RES 17 17 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q8CCS6}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 235 235 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 238 238 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 238 238 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 259 259 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 259 259 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 263 263 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 263 263 Omega-N-methylarginine; alternate.
{ECO:0000244|PubMed:24129315}.
MOD_RES 265 265 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 267 267 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 269 269 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 277 277 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 279 279 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 287 287 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 289 289 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 291 291 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 294 294 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 296 296 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
MOD_RES 298 298 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q28165}.
VAR_SEQ 295 296 GR -> SG (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_009847.
VAR_SEQ 297 306 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_009848.
VARIANT 6 6 A -> AAAA.
/FTId=VAR_018179.
MUTAGEN 213 220 Missing: Abolishes self-association,
protein aggregation and cell death.
{ECO:0000269|PubMed:11689481}.
MUTAGEN 301 306 Missing: Abolishes self-association,
protein aggregation and cell death.
{ECO:0000269|PubMed:11689481}.
HELIX 167 171 {ECO:0000244|PDB:3UCG}.
STRAND 173 178 {ECO:0000244|PDB:3UCG}.
HELIX 185 192 {ECO:0000244|PDB:3UCG}.
HELIX 193 195 {ECO:0000244|PDB:3UCG}.
STRAND 198 206 {ECO:0000244|PDB:3UCG}.
STRAND 208 211 {ECO:0000244|PDB:3UCG}.
STRAND 214 222 {ECO:0000244|PDB:3UCG}.
HELIX 224 229 {ECO:0000244|PDB:3UCG}.
HELIX 230 232 {ECO:0000244|PDB:3UCG}.
STRAND 243 246 {ECO:0000244|PDB:3UCG}.
TURN 247 250 {ECO:0000244|PDB:3UCG}.
SEQUENCE 306 AA; 32749 MW; 2E5B0AEFEA5AFBC3 CRC64;
MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGAP GGAGDYGNGL ESEELEPEEL
LLEPEPEPEP EEEPPRPRAP PGAPGPGPGS GAPGSQEEEE EPGLVEGDPG DGAIEDPELE
AIKARVREME EEAEKLKELQ NEVEKQMNMS PPPGNAGPVI MSIEEKMEAD ARSIYVGNVD
YGATAEELEA HFHGCGSVNR VTILCDKFSG HPKGFAYIEF SDKESVRTSL ALDESLFRGR
QIKVIPKRTN RPGISTTDRG FPRARYRART TNYNSSRSRF YSGFNSRPRG RVYRGRARAT
SWYSPY


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