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Q86U42

- PABP2_HUMAN

UniProt

Q86U42 - PABP2_HUMAN

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Protein

Polyadenylate-binding protein 2

Gene

PABPN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA binding Source: ProtInc

GO - Biological processi

  1. gene expression Source: Reactome
  2. modification by virus of host mRNA processing Source: Reactome
  3. modulation by virus of host morphology or physiology Source: Reactome
  4. modulation by virus of host process Source: Reactome
  5. mRNA 3'-end processing Source: Reactome
  6. mRNA splicing, via spliceosome Source: Reactome
  7. muscle contraction Source: ProtInc
  8. poly(A)+ mRNA export from nucleus Source: UniProtKB
  9. RNA processing Source: ProtInc
  10. RNA splicing Source: Reactome
  11. termination of RNA polymerase II transcription Source: Reactome
  12. transcription from RNA polymerase II promoter Source: Reactome
  13. viral life cycle Source: Reactome
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_1096. Processing of Intronless Pre-mRNAs.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.
REACT_6173. Inhibition of Host mRNA Processing and RNA Silencing.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyadenylate-binding protein 2
Short name:
PABP-2
Short name:
Poly(A)-binding protein 2
Alternative name(s):
Nuclear poly(A)-binding protein 1
Poly(A)-binding protein II
Short name:
PABII
Polyadenylate-binding nuclear protein 1
Gene namesi
Name:PABPN1
Synonyms:PAB2, PABP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:8565. PABPN1.

Subcellular locationi

Nucleus By similarity. Cytoplasm 4 Publications
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. 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).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
  4. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi213 – 2208Missing: Abolishes self-association, protein aggregation and cell death. 1 Publication
Mutagenesisi301 – 3066Missing: Abolishes self-association, protein aggregation and cell death. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi164300. phenotype.
Orphaneti270. Oculopharyngeal muscular dystrophy.
PharmGKBiPA32891.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed6 Publications
Chaini2 – 306305Polyadenylate-binding protein 2PRO_0000081711Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine6 Publications
Modified residuei19 – 191Phosphoserine2 Publications
Modified residuei95 – 951Phosphoserine3 Publications
Modified residuei150 – 1501Phosphoserine4 Publications
Modified residuei238 – 2381Asymmetric dimethylarginine; alternateBy similarity
Modified residuei238 – 2381Omega-N-methylarginine; alternateBy similarity
Modified residuei259 – 2591Asymmetric dimethylarginineBy similarity
Modified residuei263 – 2631Asymmetric dimethylarginineBy similarity
Modified residuei265 – 2651Asymmetric dimethylarginineBy similarity
Modified residuei267 – 2671Asymmetric dimethylarginineBy similarity
Modified residuei269 – 2691Asymmetric dimethylarginineBy similarity
Modified residuei277 – 2771Asymmetric dimethylarginineBy similarity
Modified residuei279 – 2791Asymmetric dimethylarginineBy similarity
Modified residuei287 – 2871Asymmetric dimethylarginineBy similarity
Modified residuei289 – 2891Asymmetric dimethylarginineBy similarity
Modified residuei291 – 2911Asymmetric dimethylarginineBy similarity
Modified residuei294 – 2941Asymmetric dimethylarginineBy similarity
Modified residuei296 – 2961Asymmetric dimethylarginineBy similarity
Modified residuei298 – 2981Asymmetric dimethylarginineBy similarity

Post-translational modificationi

Arginine dimethylation is asymmetric and involves PRMT1 and PRMT3. It does not influence the RNA binding properties (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ86U42.
PaxDbiQ86U42.
PRIDEiQ86U42.

PTM databases

PhosphoSiteiQ86U42.

Miscellaneous databases

PMAP-CutDBQ86U42.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiQ86U42.
CleanExiHS_PABPN1.
ExpressionAtlasiQ86U42. baseline and differential.
GenevestigatoriQ86U42.

Organism-specific databases

HPAiHPA000637.

Interactioni

Subunit structurei

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/CPSF5.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SNW1Q135735EBI-1226435,EBI-632715

Protein-protein interaction databases

BioGridi113777. 23 interactions.
DIPiDIP-37968N.
IntActiQ86U42. 26 interactions.
MINTiMINT-89761.
STRINGi9606.ENSP00000216727.

Structurei

Secondary structure

1
306
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi167 – 1715Combined sources
Beta strandi173 – 1786Combined sources
Helixi185 – 1928Combined sources
Helixi193 – 1953Combined sources
Beta strandi198 – 2069Combined sources
Beta strandi208 – 2114Combined sources
Beta strandi214 – 2229Combined sources
Helixi224 – 2296Combined sources
Helixi230 – 2323Combined sources
Beta strandi243 – 2464Combined sources
Turni247 – 2504Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B4DX-ray2.00A167-254[»]
3B4MX-ray2.82A/B/C/D167-254[»]
3UCGX-ray1.95A167-254[»]
ProteinModelPortaliQ86U42.
SMRiQ86U42. Positions 118-253.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ86U42.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini172 – 24978RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 145144Interacts with SKIPAdd
BLAST
Regioni119 – 14729Stimulates PAPOLABy similarityAdd
BLAST
Regioni155 – 306152Necessary for homooligomerizationAdd
BLAST
Regioni286 – 30621Interacts with PAPOLABy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili115 – 15137Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 1413Ala-richAdd
BLAST

Domaini

The RRM domain is essential for specific adenine bases recognition in the poly(A) tail but not sufficient for poly(A) binding.By similarity

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG238057.
GeneTreeiENSGT00390000001517.
HOGENOMiHOG000208465.
HOVERGENiHBG107480.
InParanoidiQ86U42.
KOiK14396.
OMAiRGRTTSW.
OrthoDBiEOG7K9K3Z.
PhylomeDBiQ86U42.
TreeFamiTF105907.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q86U42-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGAP GGAGDYGNGL
60 70 80 90 100
ESEELEPEEL LLEPEPEPEP EEEPPRPRAP PGAPGPGPGS GAPGSQEEEE
110 120 130 140 150
EPGLVEGDPG DGAIEDPELE AIKARVREME EEAEKLKELQ NEVEKQMNMS
160 170 180 190 200
PPPGNAGPVI MSIEEKMEAD ARSIYVGNVD YGATAEELEA HFHGCGSVNR
210 220 230 240 250
VTILCDKFSG HPKGFAYIEF SDKESVRTSL ALDESLFRGR QIKVIPKRTN
260 270 280 290 300
RPGISTTDRG FPRARYRART TNYNSSRSRF YSGFNSRPRG RVYRGRARAT

SWYSPY
Length:306
Mass (Da):32,749
Last modified:January 23, 2007 - v3
Checksum:i2E5B0AEFEA5AFBC3
GO
Isoform 2 (identifier: Q86U42-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     295-296: GR → SG
     297-306: Missing.

Note: May be due to a competing donor splice site.

Show »
Length:296
Mass (Da):31,497
Checksum:iE1AD14BDD69833DD
GO
Isoform 3 (identifier: Q92843-2) [UniParc]FASTAAdd to Basket

Also known as: BCL2L2-PABPN1

The sequence of this isoform can be found in the external entry Q92843.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Based on a readthrough transcript which may produce a BCL2L2-PABPN1 fusion protein. No experimental confirmation available.

Length:333
Mass (Da):37,171
GO

Sequence cautioni

The sequence CAD62310.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti6 – 61A → AAAA.
VAR_018179

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei295 – 2962GR → SG in isoform 2. 1 PublicationVSP_009847
Alternative sequencei297 – 30610Missing in isoform 2. 1 PublicationVSP_009848

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026029 Genomic DNA. Translation: AAC39596.1.
BX247976 mRNA. Translation: CAD62310.1. Different initiation.
CH471078 Genomic DNA. Translation: EAW66167.1.
CH471078 Genomic DNA. Translation: EAW66168.1.
BC010939 mRNA. Translation: AAH10939.1.
CCDSiCCDS9592.1. [Q86U42-1]
RefSeqiNP_004634.1. NM_004643.3. [Q86U42-1]
UniGeneiHs.707712.

Genome annotation databases

EnsembliENST00000216727; ENSP00000216727; ENSG00000100836. [Q86U42-1]
ENST00000397276; ENSP00000380446; ENSG00000100836. [Q86U42-2]
GeneIDi8106.
KEGGihsa:8106.
UCSCiuc001wjj.3. human. [Q86U42-2]
uc001wjk.3. human. [Q86U42-1]

Polymorphism databases

DMDMi46403176.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism, Triplet repeat expansion

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF026029 Genomic DNA. Translation: AAC39596.1 .
BX247976 mRNA. Translation: CAD62310.1 . Different initiation.
CH471078 Genomic DNA. Translation: EAW66167.1 .
CH471078 Genomic DNA. Translation: EAW66168.1 .
BC010939 mRNA. Translation: AAH10939.1 .
CCDSi CCDS9592.1. [Q86U42-1 ]
RefSeqi NP_004634.1. NM_004643.3. [Q86U42-1 ]
UniGenei Hs.707712.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3B4D X-ray 2.00 A 167-254 [» ]
3B4M X-ray 2.82 A/B/C/D 167-254 [» ]
3UCG X-ray 1.95 A 167-254 [» ]
ProteinModelPortali Q86U42.
SMRi Q86U42. Positions 118-253.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113777. 23 interactions.
DIPi DIP-37968N.
IntActi Q86U42. 26 interactions.
MINTi MINT-89761.
STRINGi 9606.ENSP00000216727.

PTM databases

PhosphoSitei Q86U42.

Polymorphism databases

DMDMi 46403176.

Proteomic databases

MaxQBi Q86U42.
PaxDbi Q86U42.
PRIDEi Q86U42.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000216727 ; ENSP00000216727 ; ENSG00000100836 . [Q86U42-1 ]
ENST00000397276 ; ENSP00000380446 ; ENSG00000100836 . [Q86U42-2 ]
GeneIDi 8106.
KEGGi hsa:8106.
UCSCi uc001wjj.3. human. [Q86U42-2 ]
uc001wjk.3. human. [Q86U42-1 ]

Organism-specific databases

CTDi 8106.
GeneCardsi GC14P023789.
GeneReviewsi PABPN1.
HGNCi HGNC:8565. PABPN1.
HPAi HPA000637.
MIMi 164300. phenotype.
602279. gene.
neXtProti NX_Q86U42.
Orphaneti 270. Oculopharyngeal muscular dystrophy.
PharmGKBi PA32891.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG238057.
GeneTreei ENSGT00390000001517.
HOGENOMi HOG000208465.
HOVERGENi HBG107480.
InParanoidi Q86U42.
KOi K14396.
OMAi RGRTTSW.
OrthoDBi EOG7K9K3Z.
PhylomeDBi Q86U42.
TreeFami TF105907.

Enzyme and pathway databases

Reactomei REACT_1096. Processing of Intronless Pre-mRNAs.
REACT_1849. mRNA 3'-end processing.
REACT_467. mRNA Splicing - Major Pathway.
REACT_6173. Inhibition of Host mRNA Processing and RNA Silencing.

Miscellaneous databases

EvolutionaryTracei Q86U42.
GeneWikii PABPN1.
GenomeRNAii 8106.
NextBioi 30755.
PMAP-CutDB Q86U42.
PROi Q86U42.
SOURCEi Search...

Gene expression databases

Bgeei Q86U42.
CleanExi HS_PABPN1.
ExpressionAtlasi Q86U42. baseline and differential.
Genevestigatori Q86U42.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), POLYMORPHISM OF POLY-ALA REGION, DISEASE.
  2. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Fetal brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skin.
  5. "Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery."
    Chen Z., Li Y., Krug R.M.
    EMBO J. 18:2273-2283(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA], ASSOCIATION WITH CPSF AND NS/NS1, INTERACTION WITH NS/NS1.
    Tissue: Cervix carcinoma.
  6. Bienvenut W.V.
    Submitted (APR-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17 AND 228-238, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  7. "Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA."
    Calado A., Tome F.M.S., Brais B., Rouleau G.A., Kuehn U., Wahle E., Carmo-Fonseca M.
    Hum. Mol. Genet. 9:2321-2328(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Deciphering the cellular pathway for transport of poly(A)-binding protein II."
    Calado A., Kutay U., Kuehn U., Wahle E., Carmo-Fonseca M.
    RNA 6:245-256(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, NUCLEOCYTOPLASMIC SHUTTLING.
  9. "Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death."
    Fan X., Dion P., Laganiere J., Brais B., Rouleau G.A.
    Hum. Mol. Genet. 10:2341-2351(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL DEATH, HOMOOLIGOMERIZATION, MUTAGENESIS OF 213-LYS--PHE-220 AND 301-SER--TYR-306.
  10. "The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding protein 2, interacts with SKIP and stimulates muscle-specific gene expression."
    Kim Y.-J., Noguchi S., Hayashi Y.K., Tsukahara T., Shimizu T., Arahata K.
    Hum. Mol. Genet. 10:1129-1139(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN MYOGENIC DIFFERENTIATION, ASSOCIATION WITH SKIP AND MYOD1, INTERACTION WITH SKIP.
  11. "An aggregate-prone conformational epitope in trinucleotide repeat diseases."
    Sugaya K., Matsubara S., Miyamoto K., Kawata A., Hayashi H.
    NeuroReport 14:2331-2335(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. "Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization."
    Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M.
    J. Biol. Chem. 279:35788-35797(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NUDT21/CPSF5.
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-95 AND SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-95 AND SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Oculopharyngeal muscular dystrophy (OPMD) due to a small duplication in the PABPN1 gene."
    van der Sluijs B.M., van Engelen B.G.M., Hoefsloot L.H.
    Hum. Mutat. 21:553-553(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT OPMD ALA-6 INS, DISEASE.

Entry informationi

Entry nameiPABP2_HUMAN
AccessioniPrimary (citable) accession number: Q86U42
Secondary accession number(s): D3DS49, O43484
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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. The association of the expanded polyalanine mutations together with the capability to oligomerize may induce these 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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3