Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P05759 (RS27A_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-40S ribosomal protein S31

Cleaved into the following 2 chains:

  1. Ubiquitin
  2. 40S ribosomal protein S31
    Alternative name(s):
    CEP76
    S37
    YS24
Gene names
Name:RPS31
Synonyms:RPS37, UBI3
Ordered Locus Names:YLR167W
ORF Names:L9470.14
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. 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.

40S ribosomal protein S31 is a component of the 40S subunit of the ribosome By similarity.

Subunit structure

Ribosomal protein S31 is part of the 40S ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains 32 different proteins (encoded by 56 genes) and 1 molecule of RNA (18S). The 60S subunit contains 46 different proteins (encoded by 81 genes) and 3 molecules of RNA (25S, 5.8S and 5S). Ref.8

Subcellular location

Ubiquitin: Cytoplasm By similarity. Nucleus By similarity.

40S ribosomal protein S31: Cytoplasm By similarity.

Miscellaneous

Ubiquitin is encoded by several different genes. UBI1 and UBI2 genes code for a single copy of ubiquitin fused to the ribosomal proteins L40. UBI3 is a polyprotein with one copy of ubiquitin fused to ribosomal protein S37. UBI4 is a polyprotein containing 5 exact head to tail repeats of ubiquitin.

Sequence similarities

In the N-terminal section; belongs to the ubiquitin family.

In the C-terminal section; belongs to the ribosomal protein S27Ae family.

Contains 1 ubiquitin-like domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7676Ubiquitin
PRO_0000396487
Chain77 – 1527640S ribosomal protein S31
PRO_0000137688

Regions

Domain1 – 7676Ubiquitin-like
Zinc finger121 – 14424C4-type
Compositional bias77 – 9923Lys-rich (highly basic)

Amino acid modifications

Modified residue1221Phosphoserine Ref.11 Ref.13
Cross-link6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9 Ref.10
Cross-link27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Cross-link48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9 Ref.10
Cross-link63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9 Ref.10
Cross-link76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Experimental info

Mutagenesis291K → R: Deficiency in ubiquitin-protein conjugate formation. Ref.6 Ref.7
Mutagenesis481K → R: Deficiency in ubiquitin-protein conjugate formation. Ref.6 Ref.7
Mutagenesis631K → R: Deficiency in ubiquitin-protein conjugate formation. Loss of DNA repair function. Ref.6 Ref.7

Secondary structure

............. 152
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05759 [UniParc].

Last modified August 10, 2010. Version 3.
Checksum: 53BF38E2E2F8B38E

FASTA15217,216
        10         20         30         40         50         60 
MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 

        70         80         90        100        110        120 
IQKESTLHLV LRLRGGGKKR KKKVYTTPKK IKHKHKKVKL AVLSYYKVDA EGKVTKLRRE 

       130        140        150 
CSNPTCGAGV FLANHKDRLY CGKCHSVYKV NA 

« Hide

References

« Hide 'large scale' references
[1]"The yeast ubiquitin genes: a family of natural gene fusions."
Oezkaynak E., Finley D., Solomon M.J., Varshavsky A.
EMBO J. 6:1429-1439(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. expand/collapse author list , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence characterization of twenty-four proteins from cytoplasmic ribosomes."
Otaka E., Higo K., Itoh T.
Mol. Gen. Genet. 195:544-546(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE OF 77-95.
[5]"The tails of ubiquitin precursors are ribosomal proteins whose fusion to ubiquitin facilitates ribosome biogenesis."
Finley D., Bartel B., Varshavsky A.
Nature 338:394-401(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF PROTEIN (S31).
[6]"A proteolytic pathway that recognizes ubiquitin as a degradation signal."
Johnson E.S., Ma P.C.M., Ota I.M., Varshavsky A.
J. Biol. Chem. 270:17442-17456(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-29; LYS-48 AND LYS-63.
[7]"A ubiquitin mutant with specific defects in DNA repair and multiubiquitination."
Spence J., Sadis S., Haas A.L., Finley D.
Mol. Cell. Biol. 15:1265-1273(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYSINE RESIDUES IN UBIQUITIN.
[8]"The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae."
Planta R.J., Mager W.H.
Yeast 14:471-477(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE, SUBUNIT (S31).
[9]"A proteomics approach to understanding protein ubiquitination."
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P.
Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-11; LYS-27; LYS-29; LYS-33; LYS-48 AND LYS-63.
Strain: SUB592.
[10]"A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery."
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-11; LYS-48 AND LYS-63.
[11]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05730 Genomic DNA. Translation: CAA29197.1.
U17246 Genomic DNA. Translation: AAB67466.1.
BK006945 Genomic DNA. Translation: DAA09489.1.
PIRUQBYR7. C29456.
RefSeqNP_013268.1. NM_001182054.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3U5CX-ray3.00f1-152[»]
3U5GX-ray3.00f1-152[»]
4BYLelectron microscopy4.3051-152[»]
4BYTelectron microscopy6.6051-152[»]
ProteinModelPortalP05759.
SMRP05759. Positions 1-74, 83-151.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31440. 35 interactions.
DIPDIP-6389N.
IntActP05759. 16 interactions.
MINTMINT-8285344.
STRING4932.YLR167W.

2D gel databases

SWISS-2DPAGEP61864.

Proteomic databases

MaxQBP05759.
PaxDbP05759.
PRIDEP05759.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYLR167W; YLR167W; YLR167W.
GeneID850864.
KEGGsce:YLR167W.

Organism-specific databases

SGDS000004157. RPS31.

Phylogenomic databases

eggNOGCOG5272.
GeneTreeENSGT00550000074763.
HOGENOMHOG000224977.
KOK02977.
OMAMSILKYY.
OrthoDBEOG7D5B06.

Enzyme and pathway databases

BioCycYEAST:G3O-32297-MONOMER.

Gene expression databases

GenevestigatorP61864.

Family and domain databases

InterProIPR002906. Ribosomal_S27a.
IPR011332. Ribosomal_zn-bd.
IPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamPF01599. Ribosomal_S27. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
PRINTSPR00348. UBIQUITIN.
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
SSF57829. SSF57829. 1 hit.
PROSITEPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio967191.
PROP05759.

Entry information

Entry nameRS27A_YEAST
AccessionPrimary (citable) accession number: P05759
Secondary accession number(s): D6VYH3 expand/collapse secondary AC list , P04838, P14800, P61864, Q6LA96
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: August 10, 2010
Last modified: July 9, 2014
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XII

Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references