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Protein

60S ribosomal protein L32

Gene

RpL32

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L32
Alternative name(s):
Ribosomal protein 49
Gene namesi
Name:RpL32
Synonyms:M(3)99D, rp49
ORF Names:CG7939
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0002626. RpL32.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • cytosolic large ribosomal subunit Source: GO_Central
  • nuclear chromosome Source: FlyBase
  • nucleolus Source: FlyBase
  • ribosome Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13413460S ribosomal protein L32PRO_0000131128Add
BLAST

Proteomic databases

PaxDbiP04359.

Expressioni

Gene expression databases

BgeeiP04359.
ExpressionAtlasiP04359. differential.
GenevisibleiP04359. DM.

Interactioni

Protein-protein interaction databases

BioGridi68429. 5 interactions.
IntActiP04359. 12 interactions.
MINTiMINT-815292.
STRINGi7227.FBpp0084959.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00Ce1-134[»]
ProteinModelPortaliP04359.
SMRiP04359. Positions 18-124.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L32e family.Curated

Phylogenomic databases

eggNOGiKOG0878. Eukaryota.
COG1717. LUCA.
GeneTreeiENSGT00390000014729.
InParanoidiP04359.
KOiK02912.
OrthoDBiEOG779P0S.
PhylomeDBiP04359.

Family and domain databases

InterProiIPR001515. Ribosomal_L32e.
IPR018263. Ribosomal_L32e_CS.
[Graphical view]
PfamiPF01655. Ribosomal_L32e. 1 hit.
[Graphical view]
ProDomiPD003823. Ribosomal_L32e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01393. Ribosomal_L32e. 1 hit.
[Graphical view]
SUPFAMiSSF52042. SSF52042. 1 hit.
PROSITEiPS00580. RIBOSOMAL_L32E. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform AImported (identifier: P04359-1) [UniParc]FASTAAdd to basket

Also known as: B, DImported

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

        10         20         30         40         50
MTIRPAYRPK IVKKRTKHFI RHQSDRYAKL SHKWRKPKGI DNRVRRRFKG
60 70 80 90 100
QYLMPNIGYG SNKRTRHMLP TGFKKFLVHN VRELEVLLMQ NRVYCGEIAH
110 120 130
GVSSKKRKEI VERAKQLSVR LTNPNGRLRS QENE
Length:134
Mass (Da):16,020
Last modified:July 15, 1998 - v3
Checksum:iAC00FA7EEEE46D9A
GO
Isoform CImported (identifier: P04359-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDTAQEASPTCFKM

Show »
Length:147
Mass (Da):17,430
Checksum:iF0F52B64DBF25BB8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181H → D in CAA25404 (PubMed:6087289).Curated
Sequence conflicti45 – 451R → G in CAA25404 (PubMed:6087289).Curated
Sequence conflicti92 – 10716RVYCG…SSKKR → PRLLREMPTASPPRS in CAA25404 (PubMed:6087289).CuratedAdd
BLAST
Sequence conflicti111 – 1111V → I in CAA25404 (PubMed:6087289).Curated
Sequence conflicti119 – 13416VRLTN…SQENE → LRSPTPTVACVSRRTR in CAA25404 (PubMed:6087289).CuratedAdd
BLAST

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MDTAQEASPTCFKM in isoform C. CuratedVSP_058151

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00848 Genomic DNA. Translation: CAA25404.1.
U92431 mRNA. Translation: AAB51389.1.
Y13939 Genomic DNA. Translation: CAA74278.1.
AE014297 Genomic DNA. Translation: AAF57001.1.
AE014297 Genomic DNA. Translation: AAN14210.1.
AE014297 Genomic DNA. Translation: AAN14211.1.
AE014297 Genomic DNA. Translation: ACL83583.1.
AY070656 mRNA. Translation: AAL48127.1.
BT011442 mRNA. Translation: AAR99100.1.
PIRiA02830. R5FF49.
RefSeqiNP_001138127.1. NM_001144655.3. [P04359-1]
NP_524582.1. NM_079843.4. [P04359-1]
NP_733339.1. NM_170460.2. [P04359-2]
NP_733340.1. NM_170461.3. [P04359-1]
UniGeneiDm.7621.

Genome annotation databases

EnsemblMetazoaiFBtr0085592; FBpp0084958; FBgn0002626. [P04359-1]
FBtr0085594; FBpp0084960; FBgn0002626. [P04359-1]
FBtr0114555; FBpp0113047; FBgn0002626. [P04359-1]
GeneIDi43573.
KEGGidme:Dmel_CG7939.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00848 Genomic DNA. Translation: CAA25404.1.
U92431 mRNA. Translation: AAB51389.1.
Y13939 Genomic DNA. Translation: CAA74278.1.
AE014297 Genomic DNA. Translation: AAF57001.1.
AE014297 Genomic DNA. Translation: AAN14210.1.
AE014297 Genomic DNA. Translation: AAN14211.1.
AE014297 Genomic DNA. Translation: ACL83583.1.
AY070656 mRNA. Translation: AAL48127.1.
BT011442 mRNA. Translation: AAR99100.1.
PIRiA02830. R5FF49.
RefSeqiNP_001138127.1. NM_001144655.3. [P04359-1]
NP_524582.1. NM_079843.4. [P04359-1]
NP_733339.1. NM_170460.2. [P04359-2]
NP_733340.1. NM_170461.3. [P04359-1]
UniGeneiDm.7621.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00Ce1-134[»]
ProteinModelPortaliP04359.
SMRiP04359. Positions 18-124.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68429. 5 interactions.
IntActiP04359. 12 interactions.
MINTiMINT-815292.
STRINGi7227.FBpp0084959.

Proteomic databases

PaxDbiP04359.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085592; FBpp0084958; FBgn0002626. [P04359-1]
FBtr0085594; FBpp0084960; FBgn0002626. [P04359-1]
FBtr0114555; FBpp0113047; FBgn0002626. [P04359-1]
GeneIDi43573.
KEGGidme:Dmel_CG7939.

Organism-specific databases

CTDi6161.
FlyBaseiFBgn0002626. RpL32.

Phylogenomic databases

eggNOGiKOG0878. Eukaryota.
COG1717. LUCA.
GeneTreeiENSGT00390000014729.
InParanoidiP04359.
KOiK02912.
OrthoDBiEOG779P0S.
PhylomeDBiP04359.

Enzyme and pathway databases

ReactomeiR-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-DME-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSiRpL32. fly.
GenomeRNAii43573.
PROiP04359.

Gene expression databases

BgeeiP04359.
ExpressionAtlasiP04359. differential.
GenevisibleiP04359. DM.

Family and domain databases

InterProiIPR001515. Ribosomal_L32e.
IPR018263. Ribosomal_L32e_CS.
[Graphical view]
PfamiPF01655. Ribosomal_L32e. 1 hit.
[Graphical view]
ProDomiPD003823. Ribosomal_L32e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01393. Ribosomal_L32e. 1 hit.
[Graphical view]
SUPFAMiSSF52042. SSF52042. 1 hit.
PROSITEiPS00580. RIBOSOMAL_L32E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence, structure, and codon preference of the Drosophila ribosomal protein 49 gene."
    O'Connell P., Rosbash M.
    Nucleic Acids Res. 12:5495-5513(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. McMahill M.S., Danielson P.D., Fogleman J.C.
    Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
    Strain: Canton-S.
  3. "Molecular and chromosomal phylogeny in the obscura group of Drosophila inferred from sequences of the rp49 gene region."
    Ramos-Onsins S., Segarra C., Rozas J., Aguade M.
    Mol. Phylogenet. Evol. 9:33-41(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: M66.
  4. "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.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Head.
  7. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
    Strain: Berkeley.
    Tissue: Embryo.
  8. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRL32_DROME
AccessioniPrimary (citable) accession number: P04359
Secondary accession number(s): A4V3M7
, B7Z0S1, O01386, Q8IMJ6, Q9VAB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: July 15, 1998
Last modified: July 6, 2016
This is version 132 of the entry and version 3 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. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. 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.