Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ubiquitin-40S ribosomal protein S27a

Gene

RpS27A

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

Functioni

Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).By similarity
Ribosomal protein S27a is a component of the 40S subunit of the ribosome.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541Activating enzyme
Sitei68 – 681Essential for function
Binding sitei72 – 721Activating enzyme

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri121 – 14424C4-typeAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-110312. Translesion synthesis by REV1.
R-DME-110320. Translesion Synthesis by POLH.
R-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-1227986. Signaling by ERBB2.
R-DME-1295596. Spry regulation of FGF signaling.
R-DME-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-DME-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-DME-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-DME-174154. APC/C:Cdc20 mediated degradation of Securin.
R-DME-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-DME-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-DME-179409. APC-Cdc20 mediated degradation of Nek2A.
R-DME-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-DME-182971. EGFR downregulation.
R-DME-195253. Degradation of beta-catenin by the destruction complex.
R-DME-201681. TCF dependent signaling in response to WNT.
R-DME-202424. Downstream TCR signaling.
R-DME-209560. NF-kB is activated and signals survival.
R-DME-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-DME-2173788. Downregulation of TGF-beta receptor signaling.
R-DME-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-DME-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-DME-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-DME-2467813. Separation of Sister Chromatids.
R-DME-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
R-DME-3769402. Deactivation of the beta-catenin transactivating complex.
R-DME-446652. Interleukin-1 signaling.
R-DME-450302. activated TAK1 mediates p38 MAPK activation.
R-DME-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-DME-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-DME-4608870. Asymmetric localization of PCP proteins.
R-DME-4641257. Degradation of AXIN.
R-DME-4641258. Degradation of DVL.
R-DME-5205685. Pink/Parkin Mediated Mitophagy.
R-DME-5358346. Hedgehog ligand biogenesis.
R-DME-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-DME-5607764. CLEC7A (Dectin-1) signaling.
R-DME-5610780. Degradation of GLI1 by the proteasome.
R-DME-5610785. GLI3 is processed to GLI3R by the proteasome.
R-DME-5632684. Hedgehog 'on' state.
R-DME-5654726. Negative regulation of FGFR1 signaling.
R-DME-5654727. Negative regulation of FGFR2 signaling.
R-DME-5654732. Negative regulation of FGFR3 signaling.
R-DME-5654733. Negative regulation of FGFR4 signaling.
R-DME-5655862. Translesion synthesis by POLK.
R-DME-5656121. Translesion synthesis by POLI.
R-DME-5656169. Termination of translesion DNA synthesis.
R-DME-5668541. TNFR2 non-canonical NF-kB pathway.
R-DME-5675221. Negative regulation of MAPK pathway.
R-DME-5675482. Regulation of necroptotic cell death.
R-DME-5676590. NIK-->noncanonical NF-kB signaling.
R-DME-5696395. Formation of Incision Complex in GG-NER.
R-DME-6781823. Formation of TC-NER Pre-Incision Complex.
R-DME-6782135. Dual incision in TC-NER.
R-DME-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-DME-6791226. Major pathway of rRNA processing in the nucleolus.
R-DME-68949. Orc1 removal from chromatin.
R-DME-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-DME-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-DME-69231. Cyclin D associated events in G1.
R-DME-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-DME-72649. Translation initiation complex formation.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-8849469. PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
R-DME-912631. Regulation of signaling by CBL.
R-DME-917729. Endosomal Sorting Complex Required For Transport (ESCRT).
R-DME-937039. IRAK1 recruits IKK complex.
R-DME-937042. IRAK2 mediated activation of TAK1 complex.
R-DME-937072. TRAF6 mediated induction of TAK1 complex.
R-DME-975110. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
R-DME-975144. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
R-DME-975163. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
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).
R-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-40S ribosomal protein S27a
Cleaved into the following 2 chains:
Gene namesi
Name:RpS27A
Synonyms:UB3-D, UBI-F80, Ubi-m
ORF Names:CG5271
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0003942. RpS27A.

Subcellular locationi

Ubiquitin :

GO - Cellular componenti

  • cytosol Source: Reactome
  • microtubule associated complex Source: FlyBase
  • nucleus Source: UniProtKB-SubCell
  • ribosome Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676UbiquitinPRO_0000396482Add
BLAST
Chaini77 – 1568040S ribosomal protein S27aPRO_0000396483Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki48 – 48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki76 – 76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiP15357.
PRIDEiP15357.

Expressioni

Gene expression databases

BgeeiP15357.
ExpressionAtlasiP15357. differential.
GenevisibleiP15357. DM.

Interactioni

Subunit structurei

Ribosomal protein S27a is part of the 40S ribosomal subunit.By similarity

Protein-protein interaction databases

BioGridi60502. 89 interactions.
IntActiP15357. 7 interactions.
MINTiMINT-1554051.
STRINGi7227.FBpp0079606.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00Af77-156[»]
ProteinModelPortaliP15357.
SMRiP15357. Positions 1-76, 78-148.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi78 – 10730Lys-richAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the ubiquitin family.Curated
In the C-terminal section; belongs to the ribosomal protein S27Ae family.Curated
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri121 – 14424C4-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0004. Eukaryota.
COG5272. LUCA.
InParanoidiP15357.
KOiK02977.
OMAiMSILKYY.
OrthoDBiEOG7JDR1W.
PhylomeDBiP15357.

Family and domain databases

InterProiIPR002906. Ribosomal_S27a.
IPR011332. Ribosomal_zn-bd.
IPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF01599. Ribosomal_S27. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM01402. Ribosomal_S27. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF57829. SSF57829. 1 hit.
PROSITEiPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15357-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGAKKR KKKNYSTPKK IKHKRKKVKL
110 120 130 140 150
AVLKYYKVDE NGKIHRLRRE CPGENCGAGV FMAAHEDRHY CGKCNLTFVF

SKPEEK
Length:156
Mass (Da):17,940
Last modified:August 10, 2010 - v2
Checksum:i4FB9AC25B8E86EF5
GO

Sequence cautioni

The sequence CAA48871.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22536 mRNA. Translation: AAA28998.1.
X69119 Genomic DNA. Translation: CAA48871.1. Sequence problems.
AE014134 Genomic DNA. Translation: AAF52941.1.
RefSeqiNP_476778.1. NM_057430.4.
UniGeneiDm.36737.
Dm.4835.

Genome annotation databases

EnsemblMetazoaiFBtr0080016; FBpp0079606; FBgn0003942.
GeneIDi34420.
KEGGidme:Dmel_CG5271.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22536 mRNA. Translation: AAA28998.1.
X69119 Genomic DNA. Translation: CAA48871.1. Sequence problems.
AE014134 Genomic DNA. Translation: AAF52941.1.
RefSeqiNP_476778.1. NM_057430.4.
UniGeneiDm.36737.
Dm.4835.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00Af77-156[»]
ProteinModelPortaliP15357.
SMRiP15357. Positions 1-76, 78-148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi60502. 89 interactions.
IntActiP15357. 7 interactions.
MINTiMINT-1554051.
STRINGi7227.FBpp0079606.

Proteomic databases

PaxDbiP15357.
PRIDEiP15357.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0080016; FBpp0079606; FBgn0003942.
GeneIDi34420.
KEGGidme:Dmel_CG5271.

Organism-specific databases

CTDi6233.
FlyBaseiFBgn0003942. RpS27A.

Phylogenomic databases

eggNOGiKOG0004. Eukaryota.
COG5272. LUCA.
InParanoidiP15357.
KOiK02977.
OMAiMSILKYY.
OrthoDBiEOG7JDR1W.
PhylomeDBiP15357.

Enzyme and pathway databases

ReactomeiR-DME-110312. Translesion synthesis by REV1.
R-DME-110320. Translesion Synthesis by POLH.
R-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-1227986. Signaling by ERBB2.
R-DME-1295596. Spry regulation of FGF signaling.
R-DME-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-DME-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-DME-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-DME-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-DME-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-DME-174154. APC/C:Cdc20 mediated degradation of Securin.
R-DME-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-DME-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-DME-179409. APC-Cdc20 mediated degradation of Nek2A.
R-DME-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-DME-182971. EGFR downregulation.
R-DME-195253. Degradation of beta-catenin by the destruction complex.
R-DME-201681. TCF dependent signaling in response to WNT.
R-DME-202424. Downstream TCR signaling.
R-DME-209560. NF-kB is activated and signals survival.
R-DME-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-DME-2173788. Downregulation of TGF-beta receptor signaling.
R-DME-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-DME-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-DME-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-DME-2467813. Separation of Sister Chromatids.
R-DME-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
R-DME-3769402. Deactivation of the beta-catenin transactivating complex.
R-DME-446652. Interleukin-1 signaling.
R-DME-450302. activated TAK1 mediates p38 MAPK activation.
R-DME-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-DME-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-DME-4608870. Asymmetric localization of PCP proteins.
R-DME-4641257. Degradation of AXIN.
R-DME-4641258. Degradation of DVL.
R-DME-5205685. Pink/Parkin Mediated Mitophagy.
R-DME-5358346. Hedgehog ligand biogenesis.
R-DME-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-DME-5607764. CLEC7A (Dectin-1) signaling.
R-DME-5610780. Degradation of GLI1 by the proteasome.
R-DME-5610785. GLI3 is processed to GLI3R by the proteasome.
R-DME-5632684. Hedgehog 'on' state.
R-DME-5654726. Negative regulation of FGFR1 signaling.
R-DME-5654727. Negative regulation of FGFR2 signaling.
R-DME-5654732. Negative regulation of FGFR3 signaling.
R-DME-5654733. Negative regulation of FGFR4 signaling.
R-DME-5655862. Translesion synthesis by POLK.
R-DME-5656121. Translesion synthesis by POLI.
R-DME-5656169. Termination of translesion DNA synthesis.
R-DME-5668541. TNFR2 non-canonical NF-kB pathway.
R-DME-5675221. Negative regulation of MAPK pathway.
R-DME-5675482. Regulation of necroptotic cell death.
R-DME-5676590. NIK-->noncanonical NF-kB signaling.
R-DME-5696395. Formation of Incision Complex in GG-NER.
R-DME-6781823. Formation of TC-NER Pre-Incision Complex.
R-DME-6782135. Dual incision in TC-NER.
R-DME-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-DME-6791226. Major pathway of rRNA processing in the nucleolus.
R-DME-68949. Orc1 removal from chromatin.
R-DME-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-DME-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-DME-69231. Cyclin D associated events in G1.
R-DME-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-DME-72649. Translation initiation complex formation.
R-DME-72689. Formation of a pool of free 40S subunits.
R-DME-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-DME-72702. Ribosomal scanning and start codon recognition.
R-DME-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-DME-8849469. PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
R-DME-912631. Regulation of signaling by CBL.
R-DME-917729. Endosomal Sorting Complex Required For Transport (ESCRT).
R-DME-937039. IRAK1 recruits IKK complex.
R-DME-937042. IRAK2 mediated activation of TAK1 complex.
R-DME-937072. TRAF6 mediated induction of TAK1 complex.
R-DME-975110. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
R-DME-975144. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
R-DME-975163. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
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).
R-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

GenomeRNAii34420.
PROiP15357.

Gene expression databases

BgeeiP15357.
ExpressionAtlasiP15357. differential.
GenevisibleiP15357. DM.

Family and domain databases

InterProiIPR002906. Ribosomal_S27a.
IPR011332. Ribosomal_zn-bd.
IPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF01599. Ribosomal_S27. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM01402. Ribosomal_S27. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF57829. SSF57829. 1 hit.
PROSITEiPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of ubiquitin genes of Drosophila melanogaster."
    Lee H., Simon J.A., Lis J.T.
    Mol. Cell. Biol. 8:4727-4735(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Structure and expression of the Drosophila ubiquitin-80-amino-acid fusion-protein gene."
    Barrio R., del Arco A., Cabrera H., Arribas C.
    Biochem. J. 302:237-244(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-S.
  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: STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.

Entry informationi

Entry nameiRS27A_DROME
AccessioniPrimary (citable) accession number: P15357
Secondary accession number(s): P68198
, Q0E8I1, Q9VKW6, Q9VQX7, Q9VZL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: August 10, 2010
Last modified: June 8, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

In Drosophila ubiquitin is encoded by 3 different genes. RpL40 and RpS27A genes code for a single copy of ubiquitin fused to the ribosomal proteins L40 and S27a, respectively. Ubi-p63E gene codes for a polyubiquitin precursor with exact head to tail repeats.
For a better understanding, features related to ubiquitin are only indicated for the first chain.

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.