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Protein

Polyadenylate-binding protein

Gene

pAbp

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds the poly(A) tail of mRNA.1 Publication

GO - Molecular functioni

  • mRNA 3'-UTR binding Source: FlyBase
  • mRNA binding Source: FlyBase
  • nucleotide binding Source: InterPro
  • poly(A) binding Source: FlyBase

GO - Biological processi

  • dorsal/ventral pattern formation Source: FlyBase
  • male meiosis Source: FlyBase
  • male meiosis cytokinesis Source: FlyBase
  • mRNA splicing, via spliceosome Source: FlyBase
  • negative regulation of neuron death Source: FlyBase
  • neurogenesis Source: FlyBase
  • oocyte development Source: FlyBase
  • oogenesis Source: FlyBase
  • positive regulation of translation Source: FlyBase
  • regulation of compound eye photoreceptor development Source: FlyBase
  • spermatid nucleus differentiation Source: FlyBase
  • spermatogenesis Source: FlyBase
  • synaptic transmission Source: FlyBase
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Polyadenylate-binding protein
Short name:
PABP
Short name:
Poly(A)-binding protein
Gene namesi
Name:pAbp
ORF Names:CG5119
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0265297. pAbp.

Subcellular locationi

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: FlyBase
  • cytoplasm Source: FlyBase
  • cytosol Source: FlyBase
  • intracellular ribonucleoprotein complex Source: FlyBase
  • lipid particle Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • nucleus Source: FlyBase
  • precatalytic spliceosome Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 634634Polyadenylate-binding proteinPRO_0000081713Add
BLAST

Proteomic databases

PaxDbiP21187.
PRIDEiP21187.

Expressioni

Developmental stagei

Expressed both maternally and zygotically throughout development.1 Publication

Gene expression databases

BgeeiP21187.
GenevisibleiP21187. DM.

Interactioni

Subunit structurei

Interacts with gw; this interaction interferes with the binding of pAbp to eIF4G and is required for miRNA-mediated silencing. Interacts with larp.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
gwQ8SY3311EBI-103658,EBI-160693
TNRC6BQ9UPQ96EBI-103658,EBI-947158From a different organism.
TNRC6CQ9HCJ05EBI-103658,EBI-6507625From a different organism.

Protein-protein interaction databases

BioGridi62753. 31 interactions.
DIPiDIP-52140N.
IntActiP21187. 16 interactions.
MINTiMINT-280350.
STRINGi7227.FBpp0085915.

Structurei

3D structure databases

ProteinModelPortaliP21187.
SMRiP21187. Positions 1-374, 510-633.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8079RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini90 – 16778RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini181 – 25979RRM 3PROSITE-ProRule annotationAdd
BLAST
Domaini285 – 36278RRM 4PROSITE-ProRule annotationAdd
BLAST
Domaini552 – 62978PABCPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PABC domain.PROSITE-ProRule annotation
Contains 4 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0123. Eukaryota.
ENOG410XR5X. LUCA.
GeneTreeiENSGT00760000118913.
InParanoidiP21187.
KOiK13126.
OMAiGMAQVQF.
PhylomeDBiP21187.

Family and domain databases

Gene3Di1.10.1900.10. 1 hit.
3.30.70.330. 4 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view]
SMARTiSM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
SSF63570. SSF63570. 1 hit.
TIGRFAMsiTIGR01628. PABP-1234. 1 hit.
PROSITEiPS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21187-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLYVGDLP QDVNESGLFD KFSSAGPVLS IRVCRDVITR RSLGYAYVNF
60 70 80 90 100
QQPADAERAL DTMNFDLVRN KPIRIMWSQR DPSLRRSGVG NVFIKNLDRA
110 120 130 140 150
IDNKAIYDTF SAFGNILSCK VATDEKGNSK GYGFVHFETE EAANTSIDKV
160 170 180 190 200
NGMLLNGKKV YVGKFIPRKE REKELGEKAK LFTNVYVKNF TEDFDDEKLK
210 220 230 240 250
EFFEPYGKIT SYKVMSKEDG KSKGFGFVAF ETTEAAEAAV QALNGKDMGE
260 270 280 290 300
GKSLYVARAQ KKAERQQELK RKFEELKQKR HESVFGVNLY VKNLDDTIDD
310 320 330 340 350
DRLRIAFSPY GNITSAKVMT DEEGRSKGFG FVCFNAASEA TCAVTELNGR
360 370 380 390 400
VVGSKPLYVA LAQRKEERKA HLASQYMRHM TGMRMQQLGQ IYQPNAASGF
410 420 430 440 450
FVPTLPSNQR FFGSQVATQM RNTPRWVPQV RPPAAIQGVQ AGAAAAGGFQ
460 470 480 490 500
GTAGAVPTQF RSAAAGARGA QPQVQGTHAA AAAANNMRNT GARAITGQQT
510 520 530 540 550
AAPNMQIPGA QIAGGAQQRT SNYKYTSNMR NPPVPQLHQT QPIPQQLQGK
560 570 580 590 600
NSEKLIASLL ANAKPQEQKQ ILGERLYPMI EHMHANLAGK ITGMLLEIEN
610 620 630
SELLHMIEDQ EALKAKVEEA VAVLQVHRVT EPAN
Length:634
Mass (Da):69,925
Last modified:September 27, 2005 - v3
Checksum:iA76B204ED206392E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti171 – 1733REK → Q in AAA70421 (PubMed:2125288).Curated
Sequence conflicti336 – 3372AA → PE in AAA70421 (PubMed:2125288).Curated
Sequence conflicti371 – 3711H → D in AAA70421 (PubMed:2125288).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05109 mRNA. Translation: AAA70421.1.
AE013599 Genomic DNA. Translation: AAF57746.1.
AE013599 Genomic DNA. Translation: AAM68175.1.
AY118528 mRNA. Translation: AAM49897.1.
PIRiS30887.
RefSeqiNP_476667.1. NM_057319.5.
NP_725749.1. NM_166264.4.
NP_725750.1. NM_166265.2.
UniGeneiDm.7069.

Genome annotation databases

EnsemblMetazoaiFBtr0086736; FBpp0085915; FBgn0265297.
FBtr0086738; FBpp0085917; FBgn0265297.
FBtr0086740; FBpp0085919; FBgn0265297.
GeneIDi37070.
KEGGidme:Dmel_CG5119.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05109 mRNA. Translation: AAA70421.1.
AE013599 Genomic DNA. Translation: AAF57746.1.
AE013599 Genomic DNA. Translation: AAM68175.1.
AY118528 mRNA. Translation: AAM49897.1.
PIRiS30887.
RefSeqiNP_476667.1. NM_057319.5.
NP_725749.1. NM_166264.4.
NP_725750.1. NM_166265.2.
UniGeneiDm.7069.

3D structure databases

ProteinModelPortaliP21187.
SMRiP21187. Positions 1-374, 510-633.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62753. 31 interactions.
DIPiDIP-52140N.
IntActiP21187. 16 interactions.
MINTiMINT-280350.
STRINGi7227.FBpp0085915.

Proteomic databases

PaxDbiP21187.
PRIDEiP21187.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086736; FBpp0085915; FBgn0265297.
FBtr0086738; FBpp0085917; FBgn0265297.
FBtr0086740; FBpp0085919; FBgn0265297.
GeneIDi37070.
KEGGidme:Dmel_CG5119.

Organism-specific databases

CTDi37070.
FlyBaseiFBgn0265297. pAbp.

Phylogenomic databases

eggNOGiKOG0123. Eukaryota.
ENOG410XR5X. LUCA.
GeneTreeiENSGT00760000118913.
InParanoidiP21187.
KOiK13126.
OMAiGMAQVQF.
PhylomeDBiP21187.

Miscellaneous databases

ChiTaRSipAbp. fly.
GenomeRNAii37070.
PROiP21187.

Gene expression databases

BgeeiP21187.
GenevisibleiP21187. DM.

Family and domain databases

Gene3Di1.10.1900.10. 1 hit.
3.30.70.330. 4 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view]
SMARTiSM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
SSF63570. SSF63570. 1 hit.
TIGRFAMsiTIGR01628. PABP-1234. 1 hit.
PROSITEiPS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Drosophila melanogaster poly(A)-binding protein: cDNA cloning reveals an unusually long 3'-untranslated region of the mRNA, also present in other eukaryotic species."
    Lefrere V., Vincent A., Amalric F.
    Gene 96:219-225(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  2. "Drosophila melanogaster poly(A)-binding protein: cDNA cloning reveals an unusually long 3'-untranslated region of the mRNA, also present in other eukaryotic species."
    Lefrere V., Vincent A., Amalric F.
    Gene 126:295-296(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  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: Berkeley.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. "The silencing domain of GW182 interacts with PABPC1 to promote translational repression and degradation of microRNA targets and is required for target release."
    Zekri L., Huntzinger E., Heimstadt S., Izaurralde E.
    Mol. Cell. Biol. 29:6220-6231(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GW.
  7. "Drosophila Larp associates with poly(A)-binding protein and is required for male fertility and syncytial embryo development."
    Blagden S.P., Gatt M.K., Archambault V., Lada K., Ichihara K., Lilley K.S., Inoue Y.H., Glover D.M.
    Dev. Biol. 334:186-197(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LARP.

Entry informationi

Entry nameiPABP_DROME
AccessioniPrimary (citable) accession number: P21187
Secondary accession number(s): A4UZM5, Q0E932, Q9V8C3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: September 27, 2005
Last modified: June 8, 2016
This is version 157 of the entry and version 3 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.