Q86U42 (PABP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PABPN1
Synonyms:	PAB2, PABP2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	306 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 By similarity. Ref.10 Ref.11
Subunit structure	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 By similarity. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and 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. Ref.6 Ref.10 Ref.11 Ref.13 Ref.15
Subcellular location	Nucleus By similarity. Cytoplasm. 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. Ref.8 Ref.9 Ref.12 Ref.15
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 By similarity.
Post-translational modification	Arginine dimethylation is asymmetric and involves PRMT1 and PRMT3. It does not influence the RNA binding properties By similarity.
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.
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.21
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.
Sequence similarities	Contains 1 RRM (RNA recognition motif) domain.
Sequence caution	The sequence CAD62310.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism Triplet repeat expansion
Disease	Disease mutation
Domain	Coiled coil
Ligand	RNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA 3'-end processing Traceable author statement. Source: Reactome mRNA splicing, via spliceosome Traceable author statement. Source: Reactome modification by virus of host mRNA processing Traceable author statement. Source: Reactome muscle contraction Traceable author statement Ref.1. Source: ProtInc poly(A)+ mRNA export from nucleus Inferred from mutant phenotype PubMed 19364924. Source: UniProtKB termination of RNA polymerase II transcription Traceable author statement. Source: Reactome viral infectious cycle Traceable author statement. Source: Reactome
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome ribonucleoprotein complex Inferred from direct assay Ref.15. Source: UniProtKB
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SNW1	Q13573	4	EBI-1226435,EBI-632715

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q86U42-1)

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.

Isoform 2 (identifier: Q86U42-2)

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.

Isoform 3 (identifier: Q92843-2)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 306

305

Polyadenylate-binding protein 2

PRO_0000081711

Regions

Domain

172 – 249

78

RRM

Region

2 – 145

144

Interacts with SKIP

Region

119 – 147

29

Stimulates PAPOLA By similarity

Region

155 – 306

152

Necessary for homooligomerization

Region

286 – 306

21

Interacts with PAPOLA By similarity

Coiled coil

115 – 151

37

Potential

Compositional bias

2 – 14

13

Ala-rich

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7 Ref.18 Ref.20

Modified residue

19

1

Phosphoserine Ref.18 Ref.20

Modified residue

95

1

Phosphoserine Ref.16 Ref.18 Ref.20

Modified residue

150

1

Phosphoserine Ref.16 Ref.17 Ref.18 Ref.20

Modified residue

238

1

Asymmetric dimethylarginine; alternate By similarity

Modified residue

238

1

Omega-N-methylarginine; alternate By similarity

Modified residue

259

1

Asymmetric dimethylarginine By similarity

Modified residue

263

1

Asymmetric dimethylarginine By similarity

Modified residue

265

1

Asymmetric dimethylarginine By similarity

Modified residue

267

1

Asymmetric dimethylarginine By similarity

Modified residue

269

1

Asymmetric dimethylarginine By similarity

Modified residue

277

1

Asymmetric dimethylarginine By similarity

Modified residue

279

1

Asymmetric dimethylarginine By similarity

Modified residue

287

1

Asymmetric dimethylarginine By similarity

Modified residue

289

1

Asymmetric dimethylarginine By similarity

Modified residue

291

1

Asymmetric dimethylarginine By similarity

Modified residue

294

1

Asymmetric dimethylarginine By similarity

Modified residue

296

1

Asymmetric dimethylarginine By similarity

Modified residue

298

1

Asymmetric dimethylarginine By similarity

Natural variations

Alternative sequence

295 – 296

2

GR → SG in isoform 2.

VSP_009847

Alternative sequence

297 – 306

10

Missing in isoform 2.

VSP_009848

Natural variant

6

1

A → AAAA. Ref.21

VAR_018179

Experimental info

Mutagenesis

213 – 220

8

Missing: Abolishes self-association, protein aggregation and cell death. Ref.10

Mutagenesis

301 – 306

6

Missing: Abolishes self-association, protein aggregation and cell death. Ref.10

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

306

Helix Strand Turn

Details...

Helix

167 – 171

5

Beta strand

173 – 178

6

Helix

185 – 192

8

Helix

193 – 195

3

Beta strand

198 – 206

9

Beta strand

208 – 211

4

Beta strand

214 – 222

9

Helix

224 – 229

6

Helix

230 – 232

3

Beta strand

243 – 246

4

Turn

247 – 250

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 2E5B0AEFEA5AFBC3	FASTA	306	32,749
	10 20 30 40 50 60 MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGAP GGAGDYGNGL ESEELEPEEL 70 80 90 100 110 120 LLEPEPEPEP EEEPPRPRAP PGAPGPGPGS GAPGSQEEEE EPGLVEGDPG DGAIEDPELE 130 140 150 160 170 180 AIKARVREME EEAEKLKELQ NEVEKQMNMS PPPGNAGPVI MSIEEKMEAD ARSIYVGNVD 190 200 210 220 230 240 YGATAEELEA HFHGCGSVNR VTILCDKFSG HPKGFAYIEF SDKESVRTSL ALDESLFRGR 250 260 270 280 290 300 QIKVIPKRTN RPGISTTDRG FPRARYRART TNYNSSRSRF YSGFNSRPRG RVYRGRARAT SWYSPY
	Isoform 2 [UniParc]. Checksum: E1AD14BDD69833DD	FASTA	296	31,497
	10 20 30 40 50 60 MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGAP GGAGDYGNGL ESEELEPEEL 70 80 90 100 110 120 LLEPEPEPEP EEEPPRPRAP PGAPGPGPGS GAPGSQEEEE EPGLVEGDPG DGAIEDPELE 130 140 150 160 170 180 AIKARVREME EEAEKLKELQ NEVEKQMNMS PPPGNAGPVI MSIEEKMEAD ARSIYVGNVD 190 200 210 220 230 240 YGATAEELEA HFHGCGSVNR VTILCDKFSG HPKGFAYIEF SDKESVRTSL ALDESLFRGR 250 260 270 280 290 QIKVIPKRTN RPGISTTDRG FPRARYRART TNYNSSRSRF YSGFNSRPRG RVYRSG
	Isoform 3 (BCL2L2-PABPN1) [UniParc]. See Q92843.		–	–

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Short GCG expansions in the PABP2 gene cause oculopharyngeal muscular dystrophy." 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. 18:164-167(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), POLYMORPHISM OF POLY-ALA REGION, DISEASE.
[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]	"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.
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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.
[6]	"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.
[7]	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, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"Molecular composition of IMP1 ribonucleoprotein granules." Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C. Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95 AND SER-150, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
[21]	"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.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00005792.
IPI00414963.

RefSeq

NP_004634.1. NM_004643.3.

UniGene

Hs.707712.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q86U42.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q86U42. 14 interactions.

MINT

MINT-89761.

STRING

9606.ENSP00000216727.

PTM databases

PhosphoSite

Q86U42.

Polymorphism databases

DMDM

46403176.

Proteomic databases

PaxDb

Q86U42.

PRIDE

Q86U42.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216727; ENSP00000216727; ENSG00000100836.
ENST00000397276; ENSP00000380446; ENSG00000100836.

GeneID

8106.

KEGG

hsa:8106.

UCSC

uc001wjh.4. human.
uc001wjj.3. human.

Organism-specific databases

CTD

8106.

GeneCards

GC14P023789.

HGNC

HGNC:8565. PABPN1.

HPA

HPA000637.

MIM

164300. phenotype.
602279. gene.

neXtProt

NX_Q86U42.

Orphanet

270. Oculopharyngeal muscular dystrophy.

PharmGKB

PA32891.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG238057.

HOGENOM

HOG000208465.

HOVERGEN

HBG107480.

InParanoid

Q86U42.

KO

K14396.

OMA

RTTSWYS.

OrthoDB

EOG4N04GD.

PhylomeDB

Q86U42.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_71. Gene Expression.
REACT_78. Post-Elongation Processing of the Transcript.

Gene expression databases

ArrayExpress

Q86U42.

Bgee

Q86U42.

CleanEx

HS_PABPN1.

Genevestigator

Q86U42.

GermOnline

ENSG00000100836. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q86U42.

GenomeRNAi

8106.

NextBio

30755.

PMAP-CutDB

Q86U42.

SOURCE

Search...

Entry information

Entry name

PABP2_HUMAN

Accession

Primary (citable) accession number: Q86U42
Secondary accession number(s): D3DS49, O43484

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 106 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.