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Protein

60S ribosomal protein L22

Gene

RpL22

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • structural constituent of ribosome Source: FlyBase

GO - Biological processi

  • cytoplasmic translation Source: GO_Central
  • mitotic spindle elongation Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • positive regulation of multicellular organism growth Source: FlyBase
  • translation Source: FlyBase
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 L22
Gene namesi
Name:RpL22
ORF Names:CG7434
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0015288. RpL22.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: GO_Central
  • ribosome Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 29929960S ribosomal protein L22PRO_0000215509Add
BLAST

Proteomic databases

PaxDbiP50887.
PRIDEiP50887.

Expressioni

Gene expression databases

BgeeiP50887.
GenevisibleiP50887. DM.

Interactioni

Protein-protein interaction databases

BioGridi57590. 39 interactions.
DIPiDIP-19124N.
IntActiP50887. 4 interactions.
MINTiMINT-313603.
STRINGi7227.FBpp0070143.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CU1-299[»]
ProteinModelPortaliP50887.
SMRiP50887. Positions 184-299.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi24 – 318Poly-Ala
Compositional biasi46 – 505Poly-Ala
Compositional biasi65 – 706Poly-Ala
Compositional biasi93 – 986Poly-Ala
Compositional biasi103 – 11210Poly-Ala
Compositional biasi136 – 15217Poly-AlaAdd
BLAST
Compositional biasi185 – 1884Poly-Lys
Compositional biasi292 – 2998Asp/Glu-rich (highly acidic)

Sequence similaritiesi

Belongs to the ribosomal protein L22e family.Curated

Phylogenomic databases

eggNOGiKOG3434. Eukaryota.
ENOG4111UVJ. LUCA.
GeneTreeiENSGT00390000003719.
InParanoidiP50887.
KOiK02891.
OMAiTIDCTNI.
OrthoDBiEOG72VH8D.
PhylomeDBiP50887.

Family and domain databases

InterProiIPR002671. Ribosomal_L22e.
[Graphical view]
PfamiPF01776. Ribosomal_L22e. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50887-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPTAKTNKG DTKTAAAKPA EKKAAPAAAA AKGKVEKPKA EAAKPAAAAA
60 70 80 90 100
KNVKKASEAA KDVKAAAAAA KPAAAKPAAA KPAAASKDAG KKAPAAAAPK
110 120 130 140 150
KDAKAAAAPA PAKAAPAKKA ASTPAAAPPA KKAAPAKAAA PAAAAPAPAA
160 170 180 190 200
AAPAVAKPAP KPKAKAAPAP SKVVKKNVLR GKGQKKKKVS LRFTIDCTNI
210 220 230 240 250
AEDSIMDVAD FEKYIKARLK VNGKVNNLGN NVTFERSKLK LIVSSDVHFS
260 270 280 290
KAYLKYLTKK YLKKNSLRDW IRVVANEKDS YELRYFRISS NDDEDDDAE
Length:299
Mass (Da):30,611
Last modified:November 1, 1997 - v2
Checksum:i46A99005610E4EB0
GO

Sequence cautioni

The sequence AAD19341.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti242 – 2421I → T in AAD19341 (PubMed:9931508).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U42587 mRNA. Translation: AAB17433.1.
AF080131 mRNA. Translation: AAD19341.1. Different initiation.
AE014298 Genomic DNA. Translation: AAF45546.1.
AL132792 Genomic DNA. Translation: CAB60023.1.
AY118961 mRNA. Translation: AAM50821.1.
BT025837 mRNA. Translation: ABF85737.1.
RefSeqiNP_477134.1. NM_057786.5.
UniGeneiDm.6921.

Genome annotation databases

EnsemblMetazoaiFBtr0070148; FBpp0070143; FBgn0015288.
GeneIDi31022.
KEGGidme:Dmel_CG7434.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U42587 mRNA. Translation: AAB17433.1.
AF080131 mRNA. Translation: AAD19341.1. Different initiation.
AE014298 Genomic DNA. Translation: AAF45546.1.
AL132792 Genomic DNA. Translation: CAB60023.1.
AY118961 mRNA. Translation: AAM50821.1.
BT025837 mRNA. Translation: ABF85737.1.
RefSeqiNP_477134.1. NM_057786.5.
UniGeneiDm.6921.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00CU1-299[»]
ProteinModelPortaliP50887.
SMRiP50887. Positions 184-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57590. 39 interactions.
DIPiDIP-19124N.
IntActiP50887. 4 interactions.
MINTiMINT-313603.
STRINGi7227.FBpp0070143.

Proteomic databases

PaxDbiP50887.
PRIDEiP50887.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070148; FBpp0070143; FBgn0015288.
GeneIDi31022.
KEGGidme:Dmel_CG7434.

Organism-specific databases

CTDi6146.
FlyBaseiFBgn0015288. RpL22.

Phylogenomic databases

eggNOGiKOG3434. Eukaryota.
ENOG4111UVJ. LUCA.
GeneTreeiENSGT00390000003719.
InParanoidiP50887.
KOiK02891.
OMAiTIDCTNI.
OrthoDBiEOG72VH8D.
PhylomeDBiP50887.

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

ChiTaRSiRpL22. fly.
GenomeRNAii31022.
PROiP50887.

Gene expression databases

BgeeiP50887.
GenevisibleiP50887. DM.

Family and domain databases

InterProiIPR002671. Ribosomal_L22e.
[Graphical view]
PfamiPF01776. Ribosomal_L22e. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Glover C.V.C., Bidwai A.P., Zhao W.F.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Poly(ADP-ribose) polymerase interacts with novel Drosophila ribosomal proteins, L22 and L23a, with unique histone-like amino-terminal extensions."
    Koyama Y., Katagiri S., Hanai S., Uchida K., Miwa M.
    Gene 226:339-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Oregon-R.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  7. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
  8. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRL22_DROME
AccessioniPrimary (citable) accession number: P50887
Secondary accession number(s): Q1EC97, Q9UAN1, Q9V3X9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: July 6, 2016
This is version 114 of the entry and version 2 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.