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Protein

Polyadenylate-binding protein 2

Gene

Pabp2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. Binds to poly(A) and to poly(G) with high affinity. May protect the poly(A) tail from degradation.1 Publication

GO - Molecular functioni

  • mRNA binding Source: FlyBase
  • nucleotide binding Source: InterPro
  • poly(A) binding Source: UniProtKB
  • RNA binding Source: UniProtKB

GO - Biological processi

  • mRNA polyadenylation Source: UniProtKB
  • mRNA splicing, via spliceosome Source: FlyBase
  • neurogenesis Source: FlyBase
  • nuclear-transcribed mRNA poly(A) tail shortening Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-DME-109688. Cleavage of Growing Transcript in the Termination Region.
R-DME-72163. mRNA Splicing - Major Pathway.
R-DME-72187. mRNA 3'-end processing.
R-DME-77595. Processing of Intronless Pre-mRNAs.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyadenylate-binding protein 2
Short name:
PABP-2
Short name:
Poly(A)-binding protein 2
Short name:
dPABP2
Alternative name(s):
Nuclear poly(A)-binding protein 1
Poly(A)-binding protein II
Short name:
PABII
Polyadenylate-binding nuclear protein 1
Protein rox2
Gene namesi
Name:Pabp2Imported
Synonyms:rox22 Publications
ORF Names:CG2163
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0005648. Pabp2.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

  • Note: Shuttles between the nucleus and the cytoplasm but predominantly found in the nucleus. Mostly found in the nucleus in the germarium. From egg chamber formation onwards, expressed in both the nuclei and cytoplasm of nurse cells and the oocyte. At stage 10, abundant in the nuclei of nurse cells, oocyte and follicle cells and in the cytoplasm of nurse cells. Uniformly distributed in the cytoplasm of early embryos then progressively localizes to nuclei during the pre-blastoderm and syncytial blastoderm stages. After cellularization, localizes mainly to the nucleus and remains nuclear in later embryonic and larval stages. During mitosis, expression levels are reduced in prophase nuclei and expression is localized to the cytoplasm during metaphase. Localizes to nuclear speckles.

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: FlyBase
  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • precatalytic spliceosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 224224Polyadenylate-binding protein 2PRO_0000252085Add
BLAST

Proteomic databases

PaxDbiQ7KNF2.
PRIDEiQ7KNF2.

Expressioni

Tissue specificityi

Expressed ubiquitously in all transcriptionally active cells.1 Publication

Developmental stagei

Expressed both maternally and zygotically. Expressed in all developmental stages; egg, embryo, larva, pupa and in both adult males and females.1 Publication

Gene expression databases

BgeeiQ7KNF2.
ExpressionAtlasiQ7KNF2. differential.
GenevisibleiQ7KNF2. DM.

Interactioni

Subunit structurei

Interacts with ZC3H3.1 Publication

Protein-protein interaction databases

BioGridi61644. 6 interactions.
IntActiQ7KNF2. 1 interaction.
STRINGi7227.FBpp0087863.

Structurei

3D structure databases

ProteinModelPortaliQ7KNF2.
SMRiQ7KNF2. Positions 64-183.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini96 – 17378RRMPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili9 – 7466Sequence analysisAdd
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

eggNOGiKOG4209. Eukaryota.
ENOG4111PFV. LUCA.
GeneTreeiENSGT00390000001517.
InParanoidiQ7KNF2.
KOiK14396.
OMAiEGSMQID.
OrthoDBiEOG7K9K3Z.
PhylomeDBiQ7KNF2.

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]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7KNF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEDITLNE DQLLESLEET NGEQETEIAT EVEEEGSMQI DPELEAIKAR
60 70 80 90 100
VKEMEEEAEK IKQMQSEVDK QMAGGSTTGL ATVPLSLEEK QEIDTRSVYV
110 120 130 140 150
GNVDYGASAE ELEAHFHGCG TINRVTILCN KADGHPKGFA YIEFGSKEFV
160 170 180 190 200
ETALAMNETL FRGRQIKVMS KRTNRPGLST TNRFARGSFR GRGARVSRAC
210 220
CHSTFRGARR AMGYRGRANY YAPY
Length:224
Mass (Da):24,978
Last modified:July 5, 2004 - v1
Checksum:iFD2B99E62DD633A5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731A → R in AAA73522 (PubMed:7890163).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23873 mRNA. Translation: AAA28862.1.
L34934 mRNA. Translation: AAA73522.1.
AF116341 Genomic DNA. Translation: AAF00976.1.
AE013599 Genomic DNA. Translation: AAF59127.1.
AY070631 mRNA. Translation: AAL48102.1.
AY075519 mRNA. Translation: AAL68327.1.
RefSeqiNP_476902.1. NM_057554.4.
NP_724648.1. NM_165589.3.
UniGeneiDm.521.

Genome annotation databases

EnsemblMetazoaiFBtr0088785; FBpp0087863; FBgn0005648.
FBtr0088786; FBpp0087864; FBgn0005648.
GeneIDi35788.
KEGGidme:Dmel_CG2163.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L23873 mRNA. Translation: AAA28862.1.
L34934 mRNA. Translation: AAA73522.1.
AF116341 Genomic DNA. Translation: AAF00976.1.
AE013599 Genomic DNA. Translation: AAF59127.1.
AY070631 mRNA. Translation: AAL48102.1.
AY075519 mRNA. Translation: AAL68327.1.
RefSeqiNP_476902.1. NM_057554.4.
NP_724648.1. NM_165589.3.
UniGeneiDm.521.

3D structure databases

ProteinModelPortaliQ7KNF2.
SMRiQ7KNF2. Positions 64-183.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61644. 6 interactions.
IntActiQ7KNF2. 1 interaction.
STRINGi7227.FBpp0087863.

Proteomic databases

PaxDbiQ7KNF2.
PRIDEiQ7KNF2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088785; FBpp0087863; FBgn0005648.
FBtr0088786; FBpp0087864; FBgn0005648.
GeneIDi35788.
KEGGidme:Dmel_CG2163.

Organism-specific databases

CTDi35788.
FlyBaseiFBgn0005648. Pabp2.

Phylogenomic databases

eggNOGiKOG4209. Eukaryota.
ENOG4111PFV. LUCA.
GeneTreeiENSGT00390000001517.
InParanoidiQ7KNF2.
KOiK14396.
OMAiEGSMQID.
OrthoDBiEOG7K9K3Z.
PhylomeDBiQ7KNF2.

Enzyme and pathway databases

ReactomeiR-DME-109688. Cleavage of Growing Transcript in the Termination Region.
R-DME-72163. mRNA Splicing - Major Pathway.
R-DME-72187. mRNA 3'-end processing.
R-DME-77595. Processing of Intronless Pre-mRNAs.

Miscellaneous databases

ChiTaRSiPabp2. fly.
GenomeRNAii35788.
NextBioi795217.
PROiQ7KNF2.

Gene expression databases

BgeeiQ7KNF2.
ExpressionAtlasiQ7KNF2. differential.
GenevisibleiQ7KNF2. DM.

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]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Novel Drosophila melanogaster genes encoding RRM-type RNA-binding proteins identified by a degenerate PCR strategy."
    Brand S.F., Pichoff S., Noselli S., Bourbon H.-M.
    Gene 154:187-192(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo1 Publication.
  2. "The Drosophila poly(A)-binding protein II is ubiquitous throughout Drosophila development and has the same function in mRNA polyadenylation as its bovine homolog in vitro."
    Benoit B., Nemeth A., Aulner N., Kuhn U., Simonelig M., Wahle E., Bourbon H.-M.
    Nucleic Acids Res. 27:3771-3778(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Oregon-RImported.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BerkeleyImported.
    Tissue: Embryo1 Publication.
  6. "A conserved CCCH-type zinc finger protein regulates mRNA nuclear adenylation and export."
    Hurt J.A., Obar R.A., Zhai B., Farny N.G., Gygi S.P., Silver P.A.
    J. Cell Biol. 185:265-277(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZC3H3.

Entry informationi

Entry nameiPABP2_DROME
AccessioniPrimary (citable) accession number: Q7KNF2
Secondary accession number(s): A1Z7B1, Q27926, Q7JQ60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: July 5, 2004
Last modified: May 11, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.