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Q8CCS6 (PABP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length302 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.

Subunit structure

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 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. 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.

Tissue specificity

Ubiquitous. Ref.1

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.

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandRNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA polyadenylation

Traceable author statement PubMed 10862355. Source: MGI

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

ribonucleoprotein complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionnucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) binding

Traceable author statement PubMed 10862355. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8CCS6-1)

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: Q8CCS6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     291-292: GR → SG
     293-302: Missing.
Note: May be due to a competing donor splice site.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 302301Polyadenylate-binding protein 2
PRO_0000081712

Regions

Domain168 – 24578RRM
Region2 – 141140Interacts with SKIP By similarity
Region115 – 14329Stimulates PAPOLA By similarity
Region255 – 30248Strong poly(A) affinity and self-association By similarity
Region282 – 30221Interacts with PAPOLA By similarity
Coiled coil111 – 14737 Potential
Compositional bias2 – 1413Ala-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue191Phosphoserine By similarity
Modified residue911Phosphoserine By similarity
Modified residue1461Phosphoserine By similarity
Modified residue2341Asymmetric dimethylarginine; alternate By similarity
Modified residue2341Omega-N-methylarginine; alternate By similarity
Modified residue2551Asymmetric dimethylarginine By similarity
Modified residue2591Asymmetric dimethylarginine By similarity
Modified residue2611Asymmetric dimethylarginine By similarity
Modified residue2631Asymmetric dimethylarginine By similarity
Modified residue2651Asymmetric dimethylarginine By similarity
Modified residue2731Asymmetric dimethylarginine By similarity
Modified residue2751Asymmetric dimethylarginine By similarity
Modified residue2831Asymmetric dimethylarginine By similarity
Modified residue2851Asymmetric dimethylarginine By similarity
Modified residue2871Asymmetric dimethylarginine By similarity
Modified residue2901Asymmetric dimethylarginine By similarity
Modified residue2921Asymmetric dimethylarginine By similarity
Modified residue2941Asymmetric dimethylarginine By similarity

Natural variations

Alternative sequence291 – 2922GR → SG in isoform 2.
VSP_009849
Alternative sequence293 – 30210Missing in isoform 2.
VSP_009850

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 2F0F6F7CC19C1986

FASTA30232,297
        10         20         30         40         50         60 
MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGDP GGAGDYGNGL ESEELEPGEL 

        70         80         90        100        110        120 
LPEPEPEEEP PRPRAPPGAP GPGPGSGAPG SQEEEEEPGL VEADPGDGAI EDPELEAIKA 

       130        140        150        160        170        180 
RVREMEEEAE KLKELQNEVE KQMNMSPPPG NAGPVIMSLE EKMEADARSI YVGNVDYGAT 

       190        200        210        220        230        240 
AEELEAHFHG CGSVNRVTIL CDKFSGHPKG FAYIEFSDKE SVRTSLALDE SLFRGRQIKV 

       250        260        270        280        290        300 
IPKRTNRPGI STTDRGFPRS RYRARTTNYN SSRSRFYSGF NSRPRGRIYR GRARATSWYS 


PY 

« Hide

Isoform 2 [UniParc].

Checksum: 0874042BA4A60A2A
Show »

FASTA29231,044

References

« Hide 'large scale' references
[1]"Genomic structure and expression of murine poly(A) binding protein II gene."
Lee Y.J., Lee J., Yang I.C., Hahn Y., Lee Y., Chung J.H.
Biochim. Biophys. Acta 1395:40-46(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: 129.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Olfactory bulb.
[3]"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).
Strain: FVB/N.
Tissue: Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U93050 Genomic DNA. Translation: AAC00210.1.
AK032172 mRNA. Translation: BAC27741.1.
BC055866 mRNA. Translation: AAH55866.1.
CCDSCCDS27104.1. [Q8CCS6-1]
RefSeqNP_062275.1. NM_019402.2. [Q8CCS6-1]
UniGeneMm.7723.

3D structure databases

ProteinModelPortalQ8CCS6.
SMRQ8CCS6. Positions 163-249.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207596. 1 interaction.
IntActQ8CCS6. 2 interactions.
MINTMINT-1867341.

PTM databases

PhosphoSiteQ8CCS6.

Proteomic databases

MaxQBQ8CCS6.
PRIDEQ8CCS6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022808; ENSMUSP00000022808; ENSMUSG00000022194. [Q8CCS6-1]
ENSMUST00000116476; ENSMUSP00000112177; ENSMUSG00000022194. [Q8CCS6-2]
GeneID54196.
KEGGmmu:54196.
UCSCuc007txg.2. mouse. [Q8CCS6-1]
uc007txi.2. mouse. [Q8CCS6-2]

Organism-specific databases

CTD8106.
MGIMGI:1859158. Pabpn1.

Phylogenomic databases

GeneTreeENSGT00390000001517.
HOGENOMHOG000208465.
HOVERGENHBG107480.
InParanoidQ8CCS6.
KOK14396.
PhylomeDBQ8CCS6.
TreeFamTF105907.

Gene expression databases

ArrayExpressQ8CCS6.
BgeeQ8CCS6.
CleanExMM_PABPN1.
GenevestigatorQ8CCS6.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPABPN1. mouse.
NextBio311042.
PROQ8CCS6.
SOURCESearch...

Entry information

Entry namePABP2_MOUSE
AccessionPrimary (citable) accession number: Q8CCS6
Secondary accession number(s): O35935
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot