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Protein

Partner of Y14 and mago

Gene

Pym

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

Functioni

Regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs and serves as a positional landmarks for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. Acts as a EJC disassembly factor by disrupting mature EJC from spliced mRNAs. Required for normal localization of osk mRNA to the posterior pole of the developing oocyte. Does not interact with the small ribosomal unit or components of the translation initiation complex. May not function in cap-dependent translation regulation.1 Publication

GO - Molecular functioni

  • exon-exon junction complex binding Source: FlyBase
  • RNA binding Source: FlyBase

GO - Biological processi

  • exon-exon junction complex disassembly Source: FlyBase
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Partner of Y14 and magoImported
Short name:
DmPYM
Alternative name(s):
Protein within the bgcn gene intron
Gene namesi
Name:PymImported
Synonyms:wibgImported
ORF Names:CG30176Imported
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0034918. Pym.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • exon-exon junction complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Viable and fertile. No visible phenotype.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 207207Partner of Y14 and magoPRO_0000065972Add
BLAST

Proteomic databases

PaxDbiP82804.
PRIDEiP82804.

Expressioni

Tissue specificityi

Expression detected in the ovary. In the oocyte expressed in the germarium, nurse cell and follicle cell.1 Publication

Gene expression databases

BgeeiP82804.
GenevisibleiP82804. DM.

Interactioni

Subunit structurei

Interacts (via N-terminus) with mago and tsu/RBM8A; the interaction is direct.3 Publications

GO - Molecular functioni

  • exon-exon junction complex binding Source: FlyBase

Protein-protein interaction databases

BioGridi63373. 2 interactions.
IntActiP82804. 3 interactions.
STRINGi7227.FBpp0072142.

Structurei

Secondary structure

1
207
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 73Combined sources
Beta strandi10 – 134Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RK8X-ray1.90C1-58[»]
ProteinModelPortaliP82804.
SMRiP82804. Positions 3-35.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP82804.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili64 – 9128Sequence analysisAdd
BLAST
Coiled coili152 – 18433Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the pym family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4325. Eukaryota.
ENOG4111KHQ. LUCA.
GeneTreeiENSGT00730000111107.
InParanoidiP82804.
KOiK14294.
OMAiECIEKKI.
OrthoDBiEOG7NSB3W.
PhylomeDBiP82804.

Family and domain databases

InterProiIPR015362. WIBG_fam.
[Graphical view]
PfamiPF09282. Mago-bind. 1 hit.
[Graphical view]
SMARTiSM01273. Mago-bind. 1 hit.
[Graphical view]
SUPFAMiSSF101931. SSF101931. 1 hit.

Sequencei

Sequence statusi: Complete.

P82804-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTYLQSSEG KFIPATKRPD GTWRKARRVK DGYVPQEEVP LYESKGKQFV
60 70 80 90 100
AQRQAGVPPG MCPLLAAESK KEREKQERTR AKKQEKESGR QPKAPAPGVL
110 120 130 140 150
VMPPSTCPPP KVSQQQQQQQ QQPSGSRDIN SISKTLEDTL KLDAAQEVVD
160 170 180 190 200
PAKQLKKLRK KIREIEQIES RIQAGEQKKL DKDQLDKVKK KSEILRQIKD

LESTPRS
Length:207
Mass (Da):23,450
Last modified:March 1, 2001 - v1
Checksum:iF7E6B7C98A2961DE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293388 mRNA. Translation: AAG00610.1.
AJ459405 mRNA. Translation: CAD30676.1.
AE013599 Genomic DNA. Translation: AAM68273.1.
AY070957 mRNA. Translation: AAL48579.1.
AY071704 mRNA. Translation: AAL49326.1.
RefSeqiNP_726372.1. NM_166627.3.
UniGeneiDm.12746.

Genome annotation databases

EnsemblMetazoaiFBtr0072233; FBpp0072142; FBgn0034918.
GeneIDi37780.
KEGGidme:Dmel_CG30176.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293388 mRNA. Translation: AAG00610.1.
AJ459405 mRNA. Translation: CAD30676.1.
AE013599 Genomic DNA. Translation: AAM68273.1.
AY070957 mRNA. Translation: AAL48579.1.
AY071704 mRNA. Translation: AAL49326.1.
RefSeqiNP_726372.1. NM_166627.3.
UniGeneiDm.12746.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RK8X-ray1.90C1-58[»]
ProteinModelPortaliP82804.
SMRiP82804. Positions 3-35.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63373. 2 interactions.
IntActiP82804. 3 interactions.
STRINGi7227.FBpp0072142.

Proteomic databases

PaxDbiP82804.
PRIDEiP82804.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0072233; FBpp0072142; FBgn0034918.
GeneIDi37780.
KEGGidme:Dmel_CG30176.

Organism-specific databases

CTDi37780.
FlyBaseiFBgn0034918. Pym.

Phylogenomic databases

eggNOGiKOG4325. Eukaryota.
ENOG4111KHQ. LUCA.
GeneTreeiENSGT00730000111107.
InParanoidiP82804.
KOiK14294.
OMAiECIEKKI.
OrthoDBiEOG7NSB3W.
PhylomeDBiP82804.

Miscellaneous databases

EvolutionaryTraceiP82804.
GenomeRNAii37780.
PROiP82804.

Gene expression databases

BgeeiP82804.
GenevisibleiP82804. DM.

Family and domain databases

InterProiIPR015362. WIBG_fam.
[Graphical view]
PfamiPF09282. Mago-bind. 1 hit.
[Graphical view]
SMARTiSM01273. Mago-bind. 1 hit.
[Graphical view]
SUPFAMiSSF101931. SSF101931. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila cystoblast differentiation factor, benign gonial cell neoplasm, is related to DExH-box proteins and interacts genetically with bag-of-marbles."
    Ohlstein B., Lavoie C.A., Vef O., Gateff E., McKearin D.M.
    Genetics 155:1809-1819(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  2. "An efficient protein complex purification method for functional proteomics in higher eukaryotes."
    Forler D., Kocher T., Rode M., Gentzel M., Izaurralde E., Wilm M.
    Nat. Biotechnol. 21:89-92(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MAGO AND TSU.
  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 EJC binding and dissociating activity of PYM is regulated in Drosophila."
    Ghosh S., Obrdlik A., Marchand V., Ephrussi A.
    PLoS Genet. 10:E1004455-E1004455(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, INTERACTION WITH MAGO AND TSU.
  7. "Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex."
    Bono F., Ebert J., Unterholzner L., Guettler T., Izaurralde E., Conti E.
    EMBO Rep. 5:304-310(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-58 IN COMPLEX WITH MAGO AND TSU, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPYM_DROME
AccessioniPrimary (citable) accession number: P82804
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.