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Protein

Polyadenylate-binding protein 2

Gene

Pabpn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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) binding Source: MGI
  3. poly(A) RNA binding Source: MGI
  4. protein self-association Source: MGI

GO - Biological processi

  1. mRNA polyadenylation Source: MGI
  2. poly(A)+ mRNA export from nucleus Source: MGI
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_291263. mRNA 3'-end processing.
REACT_305017. Processing of Intronless Pre-mRNAs.
REACT_307866. mRNA Splicing - Major Pathway.
REACT_351784. Cleavage of Growing Transcript in the Termination Region.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1859158. Pabpn1.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: MGI
  3. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 302301Polyadenylate-binding protein 2PRO_0000081712Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei19 – 191PhosphoserineBy similarity
Modified residuei52 – 521PhosphoserineBy similarity
Modified residuei91 – 911PhosphoserineBy similarity
Modified residuei146 – 1461PhosphoserineBy similarity
Modified residuei231 – 2311PhosphoserineBy similarity
Modified residuei234 – 2341Asymmetric dimethylarginine; alternateBy similarity
Modified residuei234 – 2341Omega-N-methylarginine; alternateBy similarity
Modified residuei255 – 2551Asymmetric dimethylarginineBy similarity
Modified residuei259 – 2591Asymmetric dimethylarginineBy similarity
Modified residuei261 – 2611Asymmetric dimethylarginineBy similarity
Modified residuei263 – 2631Asymmetric dimethylarginineBy similarity
Modified residuei265 – 2651Asymmetric dimethylarginineBy similarity
Modified residuei273 – 2731Asymmetric dimethylarginineBy similarity
Modified residuei275 – 2751Asymmetric dimethylarginineBy similarity
Modified residuei283 – 2831Asymmetric dimethylarginineBy similarity
Modified residuei285 – 2851Asymmetric dimethylarginineBy similarity
Modified residuei287 – 2871Asymmetric dimethylarginineBy similarity
Modified residuei290 – 2901Asymmetric dimethylarginineBy similarity
Modified residuei292 – 2921Asymmetric dimethylarginineBy similarity
Modified residuei294 – 2941Asymmetric 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

MaxQBiQ8CCS6.
PRIDEiQ8CCS6.

PTM databases

PhosphoSiteiQ8CCS6.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ8CCS6.
CleanExiMM_PABPN1.
ExpressionAtlasiQ8CCS6. baseline and differential.
GenevestigatoriQ8CCS6.

Interactioni

Subunit structurei

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. May interact with SETX (By similarity).By similarity

Protein-protein interaction databases

BioGridi207596. 1 interaction.
IntActiQ8CCS6. 2 interactions.
MINTiMINT-1867341.

Structurei

3D structure databases

ProteinModelPortaliQ8CCS6.
SMRiQ8CCS6. Positions 114-249.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 24578RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 141140Interacts with SKIPBy similarityAdd
BLAST
Regioni115 – 14329Stimulates PAPOLABy similarityAdd
BLAST
Regioni255 – 30248Strong poly(A) affinity and self-associationBy similarityAdd
BLAST
Regioni282 – 30221Interacts with PAPOLABy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili111 – 14737Sequence 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

GeneTreeiENSGT00390000001517.
HOGENOMiHOG000208465.
HOVERGENiHBG107480.
InParanoidiQ8CCS6.
KOiK14396.
PhylomeDBiQ8CCS6.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8CCS6-1) [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 AGGEAGEGDP GGAGDYGNGL
60 70 80 90 100
ESEELEPGEL LPEPEPEEEP PRPRAPPGAP GPGPGSGAPG SQEEEEEPGL
110 120 130 140 150
VEADPGDGAI EDPELEAIKA RVREMEEEAE KLKELQNEVE KQMNMSPPPG
160 170 180 190 200
NAGPVIMSLE EKMEADARSI YVGNVDYGAT AEELEAHFHG CGSVNRVTIL
210 220 230 240 250
CDKFSGHPKG FAYIEFSDKE SVRTSLALDE SLFRGRQIKV IPKRTNRPGI
260 270 280 290 300
STTDRGFPRS RYRARTTNYN SSRSRFYSGF NSRPRGRIYR GRARATSWYS

PY
Length:302
Mass (Da):32,297
Last modified:January 22, 2007 - v3
Checksum:i2F0F6F7CC19C1986
GO
Isoform 2 (identifier: Q8CCS6-2) [UniParc]FASTAAdd to basket

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.

Show »
Length:292
Mass (Da):31,044
Checksum:i0874042BA4A60A2A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei291 – 2922GR → SG in isoform 2. 1 PublicationVSP_009849
Alternative sequencei293 – 30210Missing in isoform 2. 1 PublicationVSP_009850

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93050 Genomic DNA. Translation: AAC00210.1.
AK032172 mRNA. Translation: BAC27741.1.
BC055866 mRNA. Translation: AAH55866.1.
CCDSiCCDS27104.1. [Q8CCS6-1]
RefSeqiNP_062275.1. NM_019402.2. [Q8CCS6-1]
UniGeneiMm.7723.

Genome annotation databases

EnsembliENSMUST00000022808; ENSMUSP00000022808; ENSMUSG00000022194. [Q8CCS6-1]
ENSMUST00000116476; ENSMUSP00000112177; ENSMUSG00000022194. [Q8CCS6-2]
GeneIDi54196.
KEGGimmu:54196.
UCSCiuc007txg.2. mouse. [Q8CCS6-1]
uc007txi.2. mouse. [Q8CCS6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93050 Genomic DNA. Translation: AAC00210.1.
AK032172 mRNA. Translation: BAC27741.1.
BC055866 mRNA. Translation: AAH55866.1.
CCDSiCCDS27104.1. [Q8CCS6-1]
RefSeqiNP_062275.1. NM_019402.2. [Q8CCS6-1]
UniGeneiMm.7723.

3D structure databases

ProteinModelPortaliQ8CCS6.
SMRiQ8CCS6. Positions 114-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207596. 1 interaction.
IntActiQ8CCS6. 2 interactions.
MINTiMINT-1867341.

PTM databases

PhosphoSiteiQ8CCS6.

Proteomic databases

MaxQBiQ8CCS6.
PRIDEiQ8CCS6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022808; ENSMUSP00000022808; ENSMUSG00000022194. [Q8CCS6-1]
ENSMUST00000116476; ENSMUSP00000112177; ENSMUSG00000022194. [Q8CCS6-2]
GeneIDi54196.
KEGGimmu:54196.
UCSCiuc007txg.2. mouse. [Q8CCS6-1]
uc007txi.2. mouse. [Q8CCS6-2]

Organism-specific databases

CTDi8106.
MGIiMGI:1859158. Pabpn1.

Phylogenomic databases

GeneTreeiENSGT00390000001517.
HOGENOMiHOG000208465.
HOVERGENiHBG107480.
InParanoidiQ8CCS6.
KOiK14396.
PhylomeDBiQ8CCS6.
TreeFamiTF105907.

Enzyme and pathway databases

ReactomeiREACT_291263. mRNA 3'-end processing.
REACT_305017. Processing of Intronless Pre-mRNAs.
REACT_307866. mRNA Splicing - Major Pathway.
REACT_351784. Cleavage of Growing Transcript in the Termination Region.

Miscellaneous databases

ChiTaRSiPabpn1. mouse.
NextBioi311042.
PROiQ8CCS6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CCS6.
CleanExiMM_PABPN1.
ExpressionAtlasiQ8CCS6. baseline and differential.
GenevestigatoriQ8CCS6.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1997) [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.
    , 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(2004) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Colon.

Entry informationi

Entry nameiPABP2_MOUSE
AccessioniPrimary (citable) accession number: Q8CCS6
Secondary accession number(s): O35935
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2004
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 109 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.