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Q8CCS6

- PABP2_MOUSE

UniProt

Q8CCS6 - PABP2_MOUSE

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Protein
Polyadenylate-binding protein 2
Gene
Pabpn1, Pab2, Pabp2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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.

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) binding Source: MGI

GO - Biological processi

  1. mRNA polyadenylation Source: MGI
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

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: 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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
  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 – 11Removed By similarity
Chaini2 – 302301Polyadenylate-binding protein 2
PRO_0000081712Add
BLAST

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ8CCS6.
PRIDEiQ8CCS6.

PTM databases

PhosphoSiteiQ8CCS6.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

ArrayExpressiQ8CCS6.
BgeeiQ8CCS6.
CleanExiMM_PABPN1.
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 By similarity.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ8CCS6.
SMRiQ8CCS6. Positions 163-249.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 24578RRM
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 141140Interacts with SKIP By similarity
Add
BLAST
Regioni115 – 14329Stimulates PAPOLA By similarity
Add
BLAST
Regioni255 – 30248Strong poly(A) affinity and self-association By similarity
Add
BLAST
Regioni282 – 30221Interacts with PAPOLA By similarity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili111 – 14737 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 1413Ala-rich
Add
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

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. Align

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

MAAAAAAAAA AGAAGGRGSG PGRRRHLVPG AGGEAGEGDP GGAGDYGNGL    50
ESEELEPGEL LPEPEPEEEP PRPRAPPGAP GPGPGSGAPG SQEEEEEPGL 100
VEADPGDGAI EDPELEAIKA RVREMEEEAE KLKELQNEVE KQMNMSPPPG 150
NAGPVIMSLE EKMEADARSI YVGNVDYGAT AEELEAHFHG CGSVNRVTIL 200
CDKFSGHPKG FAYIEFSDKE SVRTSLALDE SLFRGRQIKV IPKRTNRPGI 250
STTDRGFPRS RYRARTTNYN SSRSRFYSGF NSRPRGRIYR GRARATSWYS 300
PY 302
Length:302
Mass (Da):32,297
Last modified:January 23, 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.
VSP_009849
Alternative sequencei293 – 30210Missing in isoform 2.
VSP_009850

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
U93050 Genomic DNA. Translation: AAC00210.1 .
AK032172 mRNA. Translation: BAC27741.1 .
BC055866 mRNA. Translation: AAH55866.1 .
CCDSi CCDS27104.1. [Q8CCS6-1 ]
RefSeqi NP_062275.1. NM_019402.2. [Q8CCS6-1 ]
UniGenei Mm.7723.

3D structure databases

ProteinModelPortali Q8CCS6.
SMRi Q8CCS6. Positions 163-249.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 207596. 1 interaction.
IntActi Q8CCS6. 2 interactions.
MINTi MINT-1867341.

PTM databases

PhosphoSitei Q8CCS6.

Proteomic databases

MaxQBi Q8CCS6.
PRIDEi Q8CCS6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022808 ; ENSMUSP00000022808 ; ENSMUSG00000022194 . [Q8CCS6-1 ]
ENSMUST00000116476 ; ENSMUSP00000112177 ; ENSMUSG00000022194 . [Q8CCS6-2 ]
GeneIDi 54196.
KEGGi mmu:54196.
UCSCi uc007txg.2. mouse. [Q8CCS6-1 ]
uc007txi.2. mouse. [Q8CCS6-2 ]

Organism-specific databases

CTDi 8106.
MGIi MGI:1859158. Pabpn1.

Phylogenomic databases

GeneTreei ENSGT00390000001517.
HOGENOMi HOG000208465.
HOVERGENi HBG107480.
InParanoidi Q8CCS6.
KOi K14396.
PhylomeDBi Q8CCS6.
TreeFami TF105907.

Miscellaneous databases

ChiTaRSi PABPN1. mouse.
NextBioi 311042.
PROi Q8CCS6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8CCS6.
Bgeei Q8CCS6.
CleanExi MM_PABPN1.
Genevestigatori Q8CCS6.

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. "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.
    , 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.

Entry informationi

Entry nameiPABP2_MOUSE
AccessioniPrimary (citable) accession number: Q8CCS6
Secondary accession number(s): O35935
Entry historyi
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 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

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