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P29341 (PABP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polyadenylate-binding protein 1

Short name=PABP-1
Short name=Poly(A)-binding protein 1
Gene names
Name:Pabpc1
Synonyms:Pabp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length636 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds the poly(A) tail of mRNA, including that of its own transcript. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed By similarity.

Subunit structure

Component of a multi subunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1. Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Directly interacts with IGF2BP1. Part of a complex associated with the FOS mCRD domain and consisting of HNRPD, SYNCRIP, PAIP1 and CSDE1/UNR. Interacts with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1 and PAIP2. Interacts with PAIP1 with a 1:1 stoichiometry and with PAIP2 with a 1:2 stoichiometry. Identified in the spliceosome C complex. Interacts with NFX1. The interaction with CSDE1 is direct and RNA-independent. Found in a mRNP complex with YBX2. Interacts with PAPD4/GLD2 and PIWIL1. Interacts with AGO1, AGO2, GSPT1 and GSPT2. Interacts with LARP1 and LARP4B. Ref.5 Ref.6 Ref.7 Ref.8

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between the cytoplasm and the nucleus By similarity.

Domain

The RNA-binding domains RRM1 and RRM2 and the C-terminus (last 138 amino acids) regions interact respectively with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively By similarity.

The RNA-binding domains RRM2 and RRM3 and the C-terminus (last 138 amino acids) regions interact with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP2, respectively By similarity.

Post-translational modification

Phosphorylated by MAPKAPK2 By similarity.

Methylated by CARM1. Arg-493 is dimethylated, probably to asymmetric dimethylarginine By similarity.

Sequence similarities

Belongs to the polyadenylate-binding protein type-1 family.

Contains 1 PABC domain.

Contains 4 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
Nonsense-mediated mRNA decay
   Cellular componentCytoplasm
Nucleus
Spliceosome
   DomainRepeat
   LigandRNA-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

gene silencing by RNA

Inferred from mutant phenotype PubMed 19716330. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Inferred from mutant phenotype PubMed 19716330. Source: UniProtKB

positive regulation of nuclear-transcribed mRNA poly(A) tail shortening

Inferred from mutant phenotype PubMed 19716330. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 18625844. Source: MGI

cytoplasmic stress granule

Inferred from sequence or structural similarity. Source: UniProtKB

ribonucleoprotein complex

Inferred from sequence or structural similarity. Source: UniProtKB

spliceosomal complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionmRNA binding

Inferred from electronic annotation. Source: Ensembl

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) binding

Inferred from sequence or structural similarity. Source: UniProtKB

poly(U) RNA binding

Inferred from sequence orthology PubMed 21984414. Source: MGI

protein binding

Inferred from physical interaction Ref.7PubMed 18625844. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 636636Polyadenylate-binding protein 1
PRO_0000081699

Regions

Domain11 – 8979RRM 1
Domain99 – 17577RRM 2
Domain191 – 26878RRM 3
Domain294 – 37077RRM 4
Domain542 – 61978PABC
Region166 – 289124CSDE1-binding By similarity
Compositional bias495 – 5017Poly-Ala

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue2991N6-methyllysine By similarity
Modified residue3151Phosphoserine By similarity
Modified residue4551Omega-N-methylated arginine; by CARM1 By similarity
Modified residue4601Omega-N-methylated arginine; by CARM1 By similarity
Modified residue4931Dimethylated arginine; alternate By similarity
Modified residue4931Omega-N-methylarginine; alternate By similarity
Modified residue5121N6-acetyllysine By similarity

Experimental info

Sequence conflict1761R → Q in CAA46522. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29341 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: E5BB6D5BA4F86CB7

FASTA63670,671
        10         20         30         40         50         60 
MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR SLGYAYVNFQ 

        70         80         90        100        110        120 
QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN IFIKNLDKSI DNKALYDTFS 

       130        140        150        160        170        180 
AFGNILSCKV VCDENGSKGY GFVHFETQEA AERAIEKMNG MLLNDRKVFV GRFKSRKERE 

       190        200        210        220        230        240 
AELGARAKEF TNVYIKNFGE DMDDERLKEL FGKFGPALSV KVMTDESGKS KGFGFVSFER 

       250        260        270        280        290        300 
HEDAQKAVDE MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN 

       310        320        330        340        350        360 
LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT 

       370        380        390        400        410        420 
KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY QPAPPSGYFM AAIPQTQNRA 

       430        440        450        460        470        480 
AYYPPSQIAQ LRPSPRWTAQ GARPHPFQNM PGAIRPAAPR PPFSTMRPAS SQVPRVMSTQ 

       490        500        510        520        530        540 
RVANTSTQTM GPRPAAAAAA ATPAVRTVPQ YKYAAGVRNP QQHLNAQPQV TMQQPAVHVQ 

       550        560        570        580        590        600 
GQEPLTASML ASAPPQEQKQ MLGERLFPLI QAMHPSLAGK ITGMLLEIDN SELLHMLESP 

       610        620        630 
ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of a mouse testis poly(A) binding protein cDNA."
Wang M.-Y., Cutler M., Karimpour I., Kleene K.C.
Nucleic Acids Res. 20:3519-3519(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[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].
Strain: C57BL/6J.
Tissue: Embryo, Head, Skin and Testis.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
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].
Strain: C57BL/6 and Czech II.
Tissue: Mammary tumor.
[5]"The mouse Y-box protein, MSY2, is associated with a kinase on non-polysomal mouse testicular mRNAs."
Herbert T.P., Hecht N.B.
Nucleic Acids Res. 27:1747-1753(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP COMPLEX WITH YBX2.
[6]"UNR, a new partner of poly(A)-binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant."
Chang T.-C., Yamashita A., Chen C.-Y.A., Yamashita Y., Zhu W., Durdan S., Kahvejian A., Sonenberg N., Shyu A.-B.
Genes Dev. 18:2010-2023(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CSDE1.
[7]"Disruption of mouse poly(A) polymerase mGLD-2 does not alter polyadenylation status in oocytes and somatic cells."
Nakanishi T., Kumagai S., Kimura M., Watanabe H., Sakurai T., Kimura M., Kashiwabara S., Baba T.
Biochem. Biophys. Res. Commun. 364:14-19(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PAPD4.
[8]"Characterization of two cytoplasmic poly(A)-binding proteins, PABPC1 and PABPC2, in mouse spermatogenic cells."
Kimura M., Ishida K., Kashiwabara S., Baba T.
Biol. Reprod. 80:545-554(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIWIL1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X65553 mRNA. Translation: CAA46522.1.
AK044829 mRNA. Translation: BAC32110.1.
AK133196 mRNA. Translation: BAE21553.1.
AK159703 mRNA. Translation: BAE35302.1.
AK159733 mRNA. Translation: BAE35327.1.
AK160968 mRNA. Translation: BAE36120.1.
AK161123 mRNA. Translation: BAE36203.1.
AK161671 mRNA. Translation: BAE36522.1.
AK168466 mRNA. Translation: BAE40360.1.
CH466541 Genomic DNA. Translation: EDL08818.1.
BC003870 mRNA. Translation: AAH03870.1.
BC011207 mRNA. Translation: AAH11207.1.
BC023145 mRNA. Translation: AAH23145.1.
BC046233 mRNA. Translation: AAH46233.1.
CCDSCCDS27431.1.
PIRI48718.
RefSeqNP_032800.2. NM_008774.3.
UniGeneMm.371570.

3D structure databases

ProteinModelPortalP29341.
SMRP29341. Positions 10-376, 494-636.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202010. 15 interactions.
DIPDIP-32127N.
IntActP29341. 14 interactions.
MINTMINT-4123966.

PTM databases

PhosphoSiteP29341.

2D gel databases

REPRODUCTION-2DPAGEP29341.

Proteomic databases

MaxQBP29341.
PaxDbP29341.
PRIDEP29341.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000001809; ENSMUSP00000001809; ENSMUSG00000022283.
GeneID18458.
KEGGmmu:18458.
UCSCuc007vmx.2. mouse.

Organism-specific databases

CTD26986.
MGIMGI:1349722. Pabpc1.

Phylogenomic databases

eggNOGCOG0724.
GeneTreeENSGT00640000091232.
HOGENOMHOG000217922.
HOVERGENHBG002295.
InParanoidQ99L36.
KOK13126.
OMAXAVDEMN.
OrthoDBEOG7RV9FP.
TreeFamTF300458.

Gene expression databases

ArrayExpressP29341.
BgeeP29341.
CleanExMM_PABPC1.
GenevestigatorP29341.

Family and domain databases

Gene3D1.10.1900.10. 1 hit.
3.30.70.330. 4 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view]
SMARTSM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view]
SUPFAMSSF63570. SSF63570. 1 hit.
TIGRFAMsTIGR01628. PABP-1234. 1 hit.
PROSITEPS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPABPC1. mouse.
NextBio294152.
PROP29341.
SOURCESearch...

Entry information

Entry namePABP1_MOUSE
AccessionPrimary (citable) accession number: P29341
Secondary accession number(s): Q99L36
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 143 of the entry and version 2 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