FlyBase Gene Report: Dmel\RpS27A

General Information

Symbol

Dmel\RpS27A

Species

D. melanogaster

Name

Ribosomal protein S27A

Annotation Symbol

CG5271

Feature Type

protein_coding_gene

FlyBase ID

FBgn0003942

Gene Model Status

Current

Stock Availability

15 publicly available

Gene Summary

Contribute a Gene Snapshot for this gene.

All Summaries

Alliance
Auto summary
Gene Group
Red Book
Interactive Fly

Also Known As

DUb80, l(2)04820, mfs48, Ubi-m, UB3-D

Key Links

Genomic Location

Cytogenetic map

31E1-31E1

Sequence location

2L:10,408,352..10,410,456 [+]

Recombination map

2-42

RefSeq locus

NT_033779 REGION:10408352..10410456

Sequence

Get Decorated FASTA

Genomic Maps

JBrowse

Other Genome Views

The following external sites may use different assemblies or annotations than FlyBase.

Function

Gene Ontology (GO) Annotations (14 terms)

Molecular Function (3 terms)

Terms Based on Experimental Evidence (1 term)

CV Term

Evidence

References

enables structural constituent of ribosome

inferred from direct assay

(Anger et al., 2013)

Terms Based on Predictions or Assertions (3 terms)

CV Term

Evidence

References

enables protein tag activity

inferred from sequence or structural similarity with SGD:S000003962

(Gene Ontology Curators, 2002-)

inferred from biological aspect of ancestor with PANTHER:PTN000071508

(GO Reference Genome Project, 2011-)

enables structural constituent of ribosome

inferred from electronic annotation with InterPro:IPR002906

(InterPro Project Members, 2004-)

traceable author statement

(Marygold et al., 2007)

enables ubiquitin protein ligase binding

inferred from biological aspect of ancestor with PANTHER:PTN000071508

(GO Reference Genome Project, 2011-)

Biological Process (5 terms)

Terms Based on Experimental Evidence (0 terms)

Terms Based on Predictions or Assertions (5 terms)

CV Term

Evidence

References

involved_in cytoplasmic translation

traceable author statement

(Marygold et al., 2007)

inferred by curator from GO:0022626

(Anger et al., 2013)

involved_in modification-dependent protein catabolic process

inferred from biological aspect of ancestor with PANTHER:PTN000071508

(GO Reference Genome Project, 2011-)

involved_in protein ubiquitination

inferred from sequence or structural similarity with SGD:S000003962

(Gene Ontology Curators, 2002-)

inferred from biological aspect of ancestor with PANTHER:PTN000071508

(GO Reference Genome Project, 2011-)

involved_in ribosomal small subunit biogenesis

inferred from sequence or structural similarity with UniProtKB:P62979-PRO_0000396478

(Gene Ontology Curators, 2002-)

involved_in translation

inferred from electronic annotation with InterPro:IPR002906, InterPro:IPR011332

(InterPro Project Members, 2004-)

Cellular Component (6 terms)

Terms Based on Experimental Evidence (1 term)

CV Term

Evidence

References

located_in cytosolic ribosome

inferred from direct assay

(Anger et al., 2013)

Terms Based on Predictions or Assertions (5 terms)

CV Term

Evidence

References

is_active_in cytoplasm

inferred from biological aspect of ancestor with PANTHER:PTN000071508

(GO Reference Genome Project, 2011-)

part_of cytosolic small ribosomal subunit

traceable author statement

(Marygold et al., 2007)

is_active_in nucleus

inferred from biological aspect of ancestor with PANTHER:PTN000071508

(GO Reference Genome Project, 2011-)

located_in ribosome

inferred from electronic annotation with InterPro:IPR002906

(InterPro Project Members, 2004-)

part_of small-subunit processome

inferred from sequence or structural similarity with UniProtKB:P62979

(Gene Ontology Curators, 2002-)

Gene Group (FlyBase)

CYTOPLASMIC SMALL RIBOSOMAL PROTEINS

UBIQUITIN

Protein Family (UniProt)

Protein Signatures (InterPro)

Summaries

Gene Group (FlyBase)

CYTOPLASMIC SMALL RIBOSOMAL PROTEINS -: Cytoplasmic ribosomes are found on the endoplasmic reticulum and in the cytoplasm. They translate all mRNAs produced from nuclear genes and perform the majority of cellular protein synthesis. Ribosomes are formed by two ribonucleoprotein subunits, large and small. The principle function of the small subunit is to bind mRNA. (Adapted from FBrf0205398)
UBIQUITIN -: Ubiquitin is a small (76 amino acid), highly conserved protein found in all eukaryotes. Through its covalent attachment to other proteins, ubiquitin can modify protein activity in numerous ways. The most well known is the targeting of proteins for proteasomal degradation. Ubiquitin is often expressed as a fusion protein, either as polyubiquitin or fused with the ribosomal proteins L40 and S27a. Ubiquitin monomers are generated by post-translational cleavage. (Adapted from PMID:12729753 and PMID:27012465)

Phenotypic Description (Red Book; Lindsley and Zimm 1992)

mfs(2)31: male-female-sterile (2) in region 31

Homozygotes have short thin bristles; relative viability 25% at 25; hemizygotes lethal. Both males and females sterile at 25 but some fertility observed in flies raised at 23. Males raised at 28.5 have no motile sperm and some spermatids have micronuclei, and occasionally two basal bodies and axonemes are observed.

Ubi-m: Ubiquitin-monomeric

Structural gene for ubiquitin (Lee et al., 1988). Ubi-m codes for a fusion protein whose single ubiquitin sequence is attached to a tail polypeptide with 65% identity to the yeast ubiquitin tail protein and 82% identity to the human ubiquitin tail protein. Ubiquitin-monomeric is not inducible by heat shock.

Gene Model and Products

Number of Transcripts

Number of Unique Polypeptides

Please see the JBrowse view of Dmel\RpS27A for information on other features

To submit a correction to a gene model please use the Contact FlyBase form

Protein Domains (via Pfam)

Isoform displayed:

Pfam protein domains

InterPro name

classification

start

end

Protein Domains (via SMART)

Isoform displayed:

SMART protein domains

InterPro name

classification

start

end

Structure

Protein 3D structure (Predicted by AlphaFold) (AlphaFold entry P15357)

If you don't see a structure in the viewer, refresh your browser.

Model Confidence:

Very high (pLDDT > 90)
Confident (90 > pLDDT > 70)
Low (70 > pLDDT > 50)
Very low (pLDDT < 50)

AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.

Experimentally Determined Structures

Crossreferences

PDB - An information portal to biological macromolecular structures

Comments on Gene Model

Shares 5' UTR with upstream gene.

Gene model reviewed during 5.45

Transcript Data

Annotated Transcripts

Name

FlyBase ID

RefSeq ID

Length (nt)

Assoc. CDS (aa)

RpS27A-RA

FBtr0080016

NM_057430

592

156

Additional Transcript Data and Comments

Reported size (kB)

0.9 (northern blot)

(Barrio et al., 1994, Lee et al., 1988)

Comments

External Data

Crossreferences

Polypeptide Data

Annotated Polypeptides

Name

FlyBase ID

Predicted MW (kDa)

Length (aa)

Theoretical pI

UniProt

RefSeq ID

GenBank

RpS27A-PA

FBpp0079606

17.9

156

10.44

P15357

NP_476778

AAF52941

Polypeptides with Identical Sequences

There is only one protein coding transcript and one polypeptide associated with this gene

Additional Polypeptide Data and Comments

Reported size (kDa)

156 (aa)

(Lee et al., 1988)

Comments

External Data

Crossreferences

InterPro - A database of protein families, domains and functional sites

PDB - An information portal to biological macromolecular structures

Linkouts

Sequences Consistent with the Gene Model

Nucleotide / Polypeptide Records

UniProt

P15357

Mapped Features

Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\RpS27A using the Feature Mapper tool.

External Data

Crossreferences

Linkouts

Expression Data

Testis-specificity index

The testis specificity index was calculated from modENCODE tissue expression data by Vedelek et al., 2018 to indicate the degree of testis enrichment compared to other tissues. Scores range from -2.52 (underrepresented) to 5.2 (very high testis bias).

-1.20

Transcript Expression

in situ

Stage

Tissue/Position (including subcellular localization)

Reference

adult stage | male & spermatogenesis

germinal proliferation center

(Lu et al., 2013)

northern blot

Stage

Tissue/Position (including subcellular localization)

Reference

embryonic stage -- adult stage

(Barrio et al., 1994)

third instar larval stage

embryonic/larval fat body

(Barrio et al., 1994)

embryonic/larval salivary gland

(Barrio et al., 1994)

imaginal disc

(Barrio et al., 1994)

Malpighian tubule

(Barrio et al., 1994)

adult stage

ovary

(Barrio et al., 1994)

Additional Descriptive Data

RpS27A transcript is expressed at the apical end of the testis.

(Lu et al., 2013)

RpS27A transcripts are detected in all stages and in all tissues tested. Tissues include larval third instar Malpighian tubules, imaginal discs, fat body, and salivary gland and adult ovary.

(Barrio et al., 1994)

Marker for

Subcellular Localization

CV Term

Polypeptide Expression

Additional Descriptive Data

Marker for

Subcellular Localization

CV Term

Evidence

References

located_in cytosolic ribosome

inferred from direct assay

(Anger et al., 2013)

Expression Deduced from Reporters

High-Throughput Expression Data

Associated Tools

JBrowse - Visual display of RNA-Seq signals

View Dmel\RpS27A in JBrowse

RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region

View exonic expression by developmental stage for Dmel\RpS27A

View exonic expression by tissue for Dmel\RpS27A

Bulk Downloads

RNA-Seq RPKM values for all genes

Reference

See Gelbart and Emmert, 2013 for analysis details and data files for all genes.

Developmental Proteome: Life Cycle

Developmental Proteome: Embryogenesis

External Data and Images

Linkouts

DRscDB - A single-cell RNA-seq resource for data mining and data comparison across species

34420/tissue=All

EMBL-EBI Single Cell Expression Atlas - Single cell expression across species

FBgn0003942

FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array

FBgn0003942

FlyAtlas2 - A Drosophila melanogaster expression atlas with RNA-Seq, miRNA-Seq and sex-specific data

FBgn0003942

Flygut - An atlas of the Drosophila adult midgut

FBgn0003942

Images

FlyBase Wiki

Image Based Resources

Alleles, Insertions, Transgenic Constructs, and Aberrations

Classical and Insertion Alleles ( 7 )

For All Classical and Insertion Alleles Show

Other relevant insertions

Transgenic Constructs ( 8 )

For All Alleles Carried on Transgenic Constructs Show

Transgenic constructs containing/affecting coding region of RpS27A

Transgenic constructs containing regulatory region of RpS27A

Aberrations (Deficiencies and Duplications) ( 19 )

Inferred from experimentation ( 19 )

Gene disrupted in

Df(2L)BSC144

(Marygold et al., 2007)

Df(2L)BSC209

(Bloomington Drosophila Stock Center, 2014.8.18, Marygold et al., 2007, Christensen and Cook, 2006.8.30)

Df(2L)BSC342

(Christensen and Cook, 2007.10.29)

Df(2L)BSC453

(Christensen et al., 2008.4.15)

Df(2L)ED13205

(Marygold et al., 2007)

Df(2L)G2

(Clegg et al., 1993)

Df(2L)J2

(Spradling et al., 1999, BDGP Project Members, 1994-1999, Clegg et al., 1993, Sinclair et al., 1992)

Df(2L)J3

(Clegg et al., 1993)

Df(2L)J4

(Marygold et al., 2007)

Df(2L)J16

(Clegg et al., 1993)

Df(2L)J27

(Clegg et al., 1993, Sinclair et al., 1992)

Df(2L)J39

(Marygold et al., 2007, Clegg et al., 1993, Sinclair et al., 1992)

Df(2L)J77

(Mottus et al., 1997, Clegg et al., 1993, Salas and Lengyel, 1984)

Df(2L)J106

(Marygold et al., 2007, Clegg et al., 1993, Sinclair et al., 1992, Salas and Lengyel, 1984)

Df(2L)J233

(Sinclair et al., 1992, Salas and Lengyel, 1984)

In(2L)EIN52^LEIN53^R

(Marygold et al., 2007)

Gene not disrupted in

Df(2L)J1

(Clegg et al., 1993)

Df(2L)J17

(Clegg et al., 1993)

T(Y;2)J^rv99

(Salas and Lengyel, 1984)

Inferred from location ( 8 )

Variants

Variant Molecular Consequences

Alleles Representing Disease-Implicated Variants

Phenotypes

For more details about a specific phenotype click on the relevant allele symbol.

Lethality

Allele

lethal, with Scer\GAL4^pnr-MD237

RpS27A^GD10725

lethal | recessive

lethal - all die during larval stage, with Scer\GAL4^Mef2.PR

RpS27A^GD10725

partially lethal

RpS27A^mfs31

Sterility

Allele

female sterile | heat sensitive

RpS27A^mfs31

male sterile | heat sensitive

RpS27A^mfs31

Phenotype manifest in

Allele

macrochaeta

RpS27A^mfs31

spermatid

RpS27A^mfs31

Orthologs

Downloads

Download All DIOPT Orthologs

Human Orthologs (via DIOPT v9.1)

Species\Gene Symbol

Score

Best Score

Best Reverse Score

Source

Alignment

Complementation?

Transgene?

Homo sapiens (Human) (23)

Hsap\RPS27A

13 of 14

Yes

Hsap\RPS27AP5

10 of 14

Yes

5 of 14

3 of 14

3 of 14

3 of 14

2 of 14

2 of 14

2 of 14

2 of 14

2 of 14

1 of 14

Yes

Hsap\NEDD8-MDP1

1 of 14

Yes

Hsap\OASL

1 of 14

Yes

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

Model Organism Orthologs (via DIOPT v9.1)

Species\Gene Symbol

Score

Best Score

Best Reverse Score

Source

Alignment

Complementation?

Transgene?

Rattus norvegicus (Norway rat) (38)

Rnor\Rps27a

13 of 14

Yes

Rnor\Rps27a-ps1

10 of 14

Yes

Rnor\Ubbp4

10 of 14

Yes

Rnor\Rps27a-ps6

8 of 14

Yes

Rnor\Rps27a-ps5

7 of 14

Yes

3 of 14

3 of 14

3 of 14

2 of 14

2 of 14

2 of 14

2 of 14

2 of 14

1 of 14

Yes

Rnor\LOC679594

1 of 14

Yes

Rnor\LOC687780

1 of 14

Rnor\LOC100360645

1 of 14

Yes

Rnor\LOC100363494

1 of 14

Yes

Rnor\LOC100910768

1 of 14

Yes

Rnor\Oas1a

1 of 14

Yes

Rnor\Oas1b

1 of 14

Yes

Rnor\Oas1d

1 of 14

Yes

Rnor\Oas1e

1 of 14

Yes

Rnor\Oas1i

1 of 14

Yes

Rnor\Oasl2

1 of 14

Yes

Rnor\Oasl

1 of 14

Yes

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

Mus musculus (laboratory mouse) (34)

Mmus\Rps27a

13 of 14

Yes

Mmus\Gm8797

4 of 14

Yes

4 of 14

3 of 14

3 of 14

2 of 14

2 of 14

2 of 14

2 of 14

2 of 14

2 of 14

2 of 14

1 of 14

Yes

Mmus\Gm44504

1 of 14

Mmus\Isg15

1 of 14

Yes

Mmus\Oas1a

1 of 14

Yes

Mmus\Oas1c

1 of 14

Yes

Mmus\Oas1d

1 of 14

Yes

Mmus\Oas1e

1 of 14

Yes

Mmus\Oas1f

1 of 14

Yes

Mmus\Oas1g

1 of 14

Yes

Mmus\Oas1h

1 of 14

Yes

Mmus\Oasl1

1 of 14

Yes

Mmus\Oasl2

1 of 14

Yes

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

Xenopus tropicalis (Western clawed frog) (14)

Xtro\rps27a

8 of 13

Yes

7 of 13

6 of 13

2 of 13

2 of 13

2 of 13

2 of 13

2 of 13

1 of 13

Yes

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

Danio rerio (Zebrafish) (22)

Drer\rps27a

13 of 14

Yes

3 of 14

3 of 14

3 of 14

3 of 14

2 of 14

2 of 14

2 of 14

Drer\si:ch211-202a12.4

2 of 14

2 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

1 of 14

Caenorhabditis elegans (Nematode, roundworm) (18)

Cele\ubl-1

11 of 14

Yes

Cele\F34H10.1

3 of 14

Yes

Cele\K08C9.7

3 of 14

Yes

3 of 14

3 of 14

3 of 14

2 of 14

2 of 14

1 of 14

1 of 14

Yes

Cele\C16C8.11

1 of 14

Cele\C16C8.13

1 of 14

Yes

Cele\C16C8.14

1 of 14

Yes

1 of 14

1 of 14

1 of 14

1 of 14

Yes

Cele\rad-23

1 of 14

Anopheles gambiae (African malaria mosquito) (13)

Agam\AgaP_AGAP001969

4 of 12

Yes

Agam\AgaP_AGAP001970

4 of 12

Yes

Agam\AgaP_AGAP001971

4 of 12

Yes

Agam\AgaP_AGAP002599

4 of 12

Yes

3 of 12

3 of 12

2 of 12

2 of 12

1 of 12

1 of 12

1 of 12

1 of 12

1 of 12

Arabidopsis thaliana (thale-cress) (54)

Atha\AT1G23410

12 of 13

Yes

Atha\UBQ5

12 of 13

Yes

Atha\UBQ6

12 of 13

Yes

4 of 13

4 of 13

4 of 13

4 of 13

4 of 13

4 of 13

4 of 13

4 of 13

4 of 13

4 of 13

3 of 13

Yes

3 of 13

3 of 13

3 of 13

3 of 13

2 of 13

Yes

Atha\AT2G17190

2 of 13

Atha\AT4G03360

2 of 13

Atha\AT5G09340

2 of 13

Yes

2 of 13

2 of 13

2 of 13

2 of 13

2 of 13

2 of 13

1 of 13

1 of 13

1 of 13

Yes

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

Yes

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

Saccharomyces cerevisiae (Brewer's yeast) (10)

Scer\RPS31

13 of 13

Yes

3 of 13

3 of 13

3 of 13

2 of 13

2 of 13

1 of 13

1 of 13

1 of 13

1 of 13

Schizosaccharomyces pombe (Fission yeast) (12)

Spom\SPAC589.10c

12 of 12

Yes

Spom\ubi3

12 of 12

Yes

3 of 12

3 of 12

3 of 12

2 of 12

2 of 12

1 of 12

1 of 12

1 of 12

1 of 12

1 of 12

Escherichia coli (enterobacterium) (0)

Other Organism Orthologs (via OrthoDB)

Data provided directly from OrthoDB:RpS27A. Refer to their site for version information.

Paralogs

Downloads

Download All DIOPT Paralogs

Paralogs (via DIOPT v9.1)

Gene Symbol

Score

Source

Alignment

Drosophila melanogaster (Fruit fly) (13)

6 of 13

5 of 13

5 of 13

5 of 13

5 of 13

2 of 13

2 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

1 of 13

Human Disease Associations

FlyBase Human Disease Model Reports

Disease Ontology (DO) Annotations

Models Based on Experimental Evidence ( 0 )

Allele

Disease

Evidence

References

Potential Models Based on Orthology ( 0 )

Human Ortholog

Disease

Evidence

References

Modifiers Based on Experimental Evidence ( 1 )

Allele

Disease

Interaction

References

RpS27A^NIG.5271R

exacerbates frontotemporal dementia and/or amyotrophic lateral sclerosis 1

modeled by Zzzz\poly-GR^PO-36.UAS

(Park et al., 2021)

Disease Associations of Human Orthologs (via DIOPT v9.1 and OMIM)

Note that ortholog calls supported by only 1 or 2 algorithms (DIOPT score < 3) are not shown.

Homo sapiens (Human)

Gene name

Score

OMIM

OMIM Phenotype

DO term

Complementation?

Transgene?

RPS27A; ribosomal protein S27a

13 of 14

191343

RPS27AP5; ribosomal protein S27a pseudogene 5

10 of 14

UBB; ubiquitin B

5 of 14

191339

NEDD8; NEDD8 ubiquitin like modifier

3 of 14

603171

UBA52; ubiquitin A-52 residue ribosomal protein fusion product 1

3 of 14

191321

UBC; ubiquitin C

3 of 14

191340

Functional Complementation Data

Functional complementation data is computed by FlyBase using a combination of the orthology data obtained from DIOPT and OrthoDB and the allele-level genetic interaction data curated from the literature.

Interactions

Summary of Physical Interactions

esyN Network Diagram

Show neighbor-neighbor interactions:

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(data from AllianceMine provided by esyN)

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Force Directed

Circle

Concentric

Legend:

Protein

RNA

Selected Interactor(s)

Other Interaction Browsers

View in FlyBase Interactions Browser View in MIST tool (external link)

Please see the Physical Interaction reports below for full details

protein-protein

Physical Interaction

Assay

References

RpS27A - Nrd1

anti tag coimmunoprecipitation, Identification by mass spectrometry

(Yoon et al., 2017)

RpS27A - Rack1

cosedimentation, electron microscopy

(Anger et al., 2013)

RpS27A - Raf

anti tag coimmunoprecipitation, peptide massfingerprinting

(Friedman et al., 2011)

RpS27A - RpL10

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL10Ab

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL11

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL12

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL13

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL13A

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL14

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL15

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL17

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL18

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL18A

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL19

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL21

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL22

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL23

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL23A

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL24

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL26

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL27

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL27A

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL28

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL29

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL3

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL30

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL31

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL32

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL34a

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL35

cosedimentation, electron microscopy

(Anger et al., 2013)

RpS27A - RpL35A

cosedimentation, electron microscopy

(Anger et al., 2013)

RpS27A - RpL36

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL36A

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL37-1

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL37A

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL38

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL39

cosedimentation, electron microscopy

(Anger et al., 2013)

RpS27A - RpL4

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL40

cosedimentation, electron microscopy

(Anger et al., 2013)

RpS27A - RpL41

cosedimentation, electron microscopy

(Anger et al., 2013)

RpS27A - RpL5

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL6

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL7

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL7A

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL8

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpL9

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpLP0

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpLP1

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpLP2

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS10a

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS11

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS12

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS13

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS14a

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS14b

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS15

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS15Aa

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS16

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS17

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS18

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS19a

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS2

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS20

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS21

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS23

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS24

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS25

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS26

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS27

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS28b

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS29

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS3

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS30

cosedimentation, electron microscopy

(Anger et al., 2013)

RpS27A - RpS3A

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS4

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS5a

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS6

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS7

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS8

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - RpS9

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - bbx

anti tag coimmunoprecipitation, peptide massfingerprinting, experimental knowledge based

(Rhee et al., 2014)

RpS27A - eEF2

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - gig

anti tag coimmunoprecipitation, Identification by mass spectrometry

(Vinayagam et al., 2016)

RpS27A - her

anti tag coimmunoprecipitation, peptide massfingerprinting, experimental knowledge based

(Rhee et al., 2014)

RpS27A - slim

anti tag coimmunoprecipitation, peptide massfingerprinting, experimental knowledge based

(Rhee et al., 2014)

RpS27A - sta

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RpS27A - vig2

cosedimentation, Identification by mass spectrometry, electron microscopy

(Anger et al., 2013)

RNA-protein

Physical Interaction

Assay

References

RpS27A - 18SrRNA

cosedimentation, electron microscopy

(Anger et al., 2013)

RpS27A - 28SrRNA

cosedimentation, electron microscopy

(Anger et al., 2013)

RpS27A - 2SrRNA

cosedimentation, electron microscopy

(Anger et al., 2013)

RpS27A - 5.8SrRNA

cosedimentation, electron microscopy

(Anger et al., 2013)

RpS27A - 5SrRNA

cosedimentation, electron microscopy

(Anger et al., 2013)

Summary of Genetic Interactions

esyN Network Diagram

Other Interaction Browsers

Starting gene(s)

Interaction type

Interacting gene(s)

Reference

Starting gene(s)

Interaction type

Interacting gene(s)

Reference

External Data

Linkouts

BioGRID - A database of protein and genetic interactions.

60502

DroID - A comprehensive database of gene and protein interactions.

FBgn0003942

MIST (protein-protein) - An integrated Molecular Interaction Database

34420

Pathways

Signaling Pathways (FlyBase)

Metabolic Pathways

FlyBase

External Links

Reactome Metabolic Pathways - An open-source, open access, manually curated and peer-reviewed metabolic pathway database.

Regulation of pyruvate metabolism

External Data

Linkouts

KEGG Pathways - A collection of manually drawn pathway maps representing knowledge of molecular interaction, reaction and relation networks.

Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.

Class of Gene

nuclear_gene

protein_coding_gene

Genomic Location and Detailed Mapping Data

Chromosome (arm)

Recombination map

2-42

Cytogenetic map

31E1-31E1

Sequence location

2L:10,408,352..10,410,456 [+]

FlyBase Computed Cytological Location

Cytogenetic map

Evidence for location

31E1-31E1

Limits computationally determined from genome sequence between P{lacW}RnrL^k06709 and P{lacW}KdelR^k00311

Experimentally Determined Cytological Location

Cytogenetic map

Notes

References

31E-31E

(Barrio, 1992.11.5)

31E3-31E5

(determined by in situ hybridisation)

(Spradling et al., 1999)

31E-31E

(determined by in situ hybridisation)

(Ranz et al., 1997, Izquierdo, 1994)

31E3-31E5

(BDGP Project Members, 1994-1999)

Experimentally Determined Recombination Data

Location

2-42

(FlyBase, 2016)

2-35.5

(Comeron et al., 2012)

(Barrio, 1992.11.5)

2-41.35

Left of (cM)

Right of (cM)

Notes

Based on 23 recombinants between J and RpS27A with da as a middle marker.

Stocks and Reagents

Stocks (15)

Genomic Clones (28)

Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete

cDNA Clones (300)

Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see JBrowse for alignment of the cDNAs and ESTs to the gene model.

cDNA clones, fully sequenced

BDGP DGC clones

SD13292

Other clones

Drosophila Genomics Resource Center cDNA clones

For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.

FBgn0003942

cDNA Clones, End Sequenced (ESTs)

BDGP DGC clones

Other clones

RNAi and Array Information

Linkouts

DRSC - Results frm RNAi screens

FBgn0003942

Antibody Information

Laboratory Generated Antibodies

Commercially Available Antibodies

Cell Line Information

Publicly Available Cell Lines

Other Stable Cell Lines

Other Comments

Likely Minute gene.

(Marygold et al., 2007)

Deletions removing RpS27A but no other cytoplasmic ribosomal protein-encoding genes show Minute phenotypes.

(Marygold et al., 2007)

RpS27A and Ip259 share a 5' untranslated exon, however, alternative splicing produces two structurally unrelated proteins which do not share any common sequences.

(Mottus et al., 1997)

The genomic organisation of the RpS27A locus has been characterised.

(Barrio et al., 1994)

Antibody staining of polytene chromosomes shows that ubiquitin is mainly associated with the compact and stabilized structure that forms the bands rather than with the more decondensed and destabilized protein-DNA structure that forms interbands and puffs.

(Izquierdo, 1994)

Four (unnamed) recessive lethal alleles have been isolated during a cytogenetic analysis of chromosomal region 31.

(Clegg et al., 1993)

RpS27A expression has been studied in heat shocked aging flies.

(Niedzwiecki and Fleming, 1993)

Recessive alleles suppress position-effect variegation of In(1)w^m4 when homozygous. The suppressor phenotypes are sexually dimorphic.

(Sinclair et al., 1992)

Structural gene for ubiquitin (Lee et al., 1988). Ubi-f80 codes for a fusion protein whose single ubiquitin sequence is attached to a tail polypeptide with 65% identity to the yeast ubiquitin tail protein and 82% identity to the human ubiquitin tail protein. Ubiquitin-monomeric is not inducible by heat shock.

Relationship to Other Genes

Source for database merge of

Source for merge of: RpS27A l(2)04820

(Spradling et al., 1999)

Additional comments

"RpS27A" likely corresponds to "M(2)31E".

(Marygold et al., 2007)

One or more of the processed transcripts for this gene share(s) untranslated sequences with a transcript of an adjacent gene, but encode(s) a single open reading frame (ORF). The non-overlapping ORFs that share untranslated sequences are represented by RpS27A and Ip259.

(FlyBase Genome Annotators, 2002-2003)

Nomenclature History

Source for database identify of

Nomenclature comments

Etymology

Synonyms and Secondary IDs (21)

Reported As

Symbol Synonym

CG5271

(National Institute of Genetics Fly Stocks, 2022-, Kolkhof et al., 2017, Neuert et al., 2017, Caizzi et al., 2016, Ristic et al., 2016, Lu et al., 2014, Sing et al., 2014, Schertel et al., 2013, Ni et al., 2011.7.19, Keleman et al., 2009.8.5, Hughes et al., 2008, Goldman and Arbeitman, 2007, Marygold et al., 2007, Quinones-Coello, 2007)

DUb80

(Mottus et al., 1997, Barrio et al., 1994, Barrio, 1992.11.5)

Dub80

RpS27

(Lu et al., 2013)

S31e

(Anger et al., 2013)

UB3-D

(Niedzwiecki and Fleming, 1993)

Ubi-f80

Ubi-m

(Lindsley and Zimm, 1992)

Ubiq

(Wesley and Mok, 2003)

l(2)04820

(Mesilaty-Gross et al., 1999, Meister and Braun, 1995.10, BDGP Project Members, 1994-1999)

l(2)31Ei

mfs(2)31

mfs(2)48

mfs48

(Cummings and Cronmiller, 1994, Salas and Lengyel, 1984)

Name Synonyms

CG5271

(Goldman and Arbeitman, 2007)

Ribosomal protein S27A

Ubiquitin

(Herz et al., 2006, Wesley and Mok, 2003)

Ubiquitin fusion 80

Ubiquitin-monomeric

(Lindsley and Zimm, 1992)

male female sterile 31

ubiquitin

(Murphey and Godenschwege, 2002)

Secondary FlyBase IDs

FBgn0002728
FBgn0010585
FBgn0064114

Datasets (0)

Study focus (0)

Experimental Role

Project

Project Type

Title

Study result (0)

Result

Result Type

Title

External Crossreferences and Linkouts ( 158 )

Sequence Crossreferences

NCBI Gene - Gene integrates information from a wide range of species. A record may include nomenclature, Reference Sequences (RefSeqs), maps, pathways, variations, phenotypes, and links to genome-, phenotype-, and locus-specific resources worldwide.

34420

GenBank Nucleotide - A collection of sequences from several sources, including GenBank, RefSeq, TPA, and PDB.

GenBank Protein - A collection of sequences from several sources, including translations from annotated coding regions in GenBank, RefSeq and TPA, as well as records from SwissProt, PIR, PRF, and PDB.

RefSeq - A comprehensive, integrated, non-redundant, well-annotated set of reference sequences including genomic, transcript, and protein.

UniProt/GCRP - The gene-centric reference proteome (GCRP) provides a 1:1 mapping between genes and UniProt accessions in which a single 'canonical' isoform represents the product(s) of each protein-coding gene.

P15357

UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information

P15357

Other crossreferences

AlphaFold DB - AlphaFold provides open access to protein structure predictions for the human proteome and other key proteins of interest, to accelerate scientific research.

P15357

DRscDB - A single-cell RNA-seq resource for data mining and data comparison across species

34420/tissue=All

EMBL-EBI Single Cell Expression Atlas - Single cell expression across species

FBgn0003942

FlyAtlas2 - A Drosophila melanogaster expression atlas with RNA-Seq, miRNA-Seq and sex-specific data

FBgn0003942

FlyMine - An integrated database for Drosophila genomics

FBgn0003942

InterPro - A database of protein families, domains and functional sites

KEGG Genes - Molecular building blocks of life in the genomic space.

dme:Dmel_CG5271

MARRVEL_MODEL - MARRVEL (model organism gene)

34420

PDB - An information portal to biological macromolecular structures

Linkouts

BioGRID - A database of protein and genetic interactions.

60502

Drosophila Genomics Resource Center - Drosophila Genomics Resource Center (DGRC) cDNA clones

FBgn0003942

DroID - A comprehensive database of gene and protein interactions.

FBgn0003942

DRSC - Results frm RNAi screens

FBgn0003942

FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array

FBgn0003942

FlyCyc Genes - Genes from a BioCyc PGDB for Dmel

FBGN0003942

Flygut - An atlas of the Drosophila adult midgut

FBgn0003942

iBeetle-Base - RNAi phenotypes in the red flour beetle (Tribolium castaneum)

TC007754

KEGG Pathways - A collection of manually drawn pathway maps representing knowledge of molecular interaction, reaction and relation networks.

MIST (protein-protein) - An integrated Molecular Interaction Database

34420

Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.

Reactome Metabolic Pathways - An open-source, open access, manually curated and peer-reviewed metabolic pathway database.

Regulation of pyruvate metabolism

References (108)

The following external sites may use different assemblies or annotations than FlyBase.

-1.20

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