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P05759

- RS27A_YEAST

UniProt

P05759 - RS27A_YEAST

Protein

Ubiquitin-40S ribosomal protein S31

Gene

RPS31

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 3 (10 Aug 2010)
      Previous versions | rss
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    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-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.By similarity
    40S ribosomal protein S31 is a component of the 40S subunit of the ribosome.By similarity

    Regions

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

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein tag Source: SGD
    3. structural constituent of ribosome Source: SGD

    GO - Biological processi

    1. cytoplasmic translation Source: SGD
    2. maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, LSU-rRNA,5S) Source: SGD
    3. ribosomal small subunit assembly Source: SGD
    4. ribosome biogenesis Source: SGD

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32297-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-40S ribosomal protein S31
    Cleaved into the following 2 chains:
    Alternative name(s):
    CEP76
    S37
    YS24
    Gene namesi
    Name:RPS31
    Synonyms:RPS37, UBI3
    Ordered Locus Names:YLR167W
    ORF Names:L9470.14
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    SGDiS000004157. RPS31.

    Subcellular locationi

    Chain Ubiquitin : Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytosolic small ribosomal subunit Source: SGD
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 291K → R: Deficiency in ubiquitin-protein conjugate formation. 2 Publications
    Mutagenesisi48 – 481K → R: Deficiency in ubiquitin-protein conjugate formation. 2 Publications
    Mutagenesisi63 – 631K → R: Deficiency in ubiquitin-protein conjugate formation. Loss of DNA repair function. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 7676UbiquitinPRO_0000396487Add
    BLAST
    Chaini77 – 1527640S ribosomal protein S31PRO_0000137688Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki6 – 6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Cross-linki27 – 27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki29 – 29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki33 – 33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki48 – 48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Cross-linki63 – 63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
    Cross-linki76 – 76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
    Modified residuei122 – 1221Phosphoserine2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP05759.
    PaxDbiP05759.
    PRIDEiP05759.

    2D gel databases

    SWISS-2DPAGEP61864.

    Expressioni

    Gene expression databases

    GenevestigatoriP61864.

    Interactioni

    Subunit structurei

    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).1 Publication

    Protein-protein interaction databases

    BioGridi31440. 35 interactions.
    DIPiDIP-6389N.
    IntActiP05759. 16 interactions.
    MINTiMINT-8285344.
    STRINGi4932.YLR167W.

    Structurei

    Secondary structure

    1
    152
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi79 – 813
    Beta strandi106 – 1083
    Beta strandi110 – 1123
    Turni124 – 1263
    Beta strandi128 – 1347
    Beta strandi139 – 1468

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VW9electron microscopy6.10g1-152[»]
    1VWVelectron microscopy6.10g1-152[»]
    3U5CX-ray3.00f1-152[»]
    3U5GX-ray3.00f1-152[»]
    4BYLelectron microscopy4.3051-152[»]
    4BYTelectron microscopy6.6051-152[»]
    4CUYelectron microscopy3.70f101-152[»]
    ProteinModelPortaliP05759.
    SMRiP05759. Positions 1-74, 83-151.
    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 biasi77 – 9923Lys-rich (highly basic)Add
    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

    eggNOGiCOG5272.
    GeneTreeiENSGT00550000074763.
    HOGENOMiHOG000224977.
    KOiK02977.
    OMAiMSILKYY.
    OrthoDBiEOG7D5B06.

    Family and domain databases

    InterProiIPR002906. Ribosomal_S27a.
    IPR011332. Ribosomal_zn-bd.
    IPR019956. Ubiquitin.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR019954. Ubiquitin_CS.
    [Graphical view]
    PfamiPF01599. Ribosomal_S27. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view]
    PRINTSiPR00348. UBIQUITIN.
    SMARTiSM00213. 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.

    P05759-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL    50
    EDGRTLSDYN IQKESTLHLV LRLRGGGKKR KKKVYTTPKK IKHKHKKVKL 100
    AVLSYYKVDA EGKVTKLRRE CSNPTCGAGV FLANHKDRLY CGKCHSVYKV 150
    NA 152
    Length:152
    Mass (Da):17,216
    Last modified:August 10, 2010 - v3
    Checksum:i53BF38E2E2F8B38E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05730 Genomic DNA. Translation: CAA29197.1.
    U17246 Genomic DNA. Translation: AAB67466.1.
    BK006945 Genomic DNA. Translation: DAA09489.1.
    PIRiC29456. UQBYR7.
    RefSeqiNP_013268.1. NM_001182054.1.

    Genome annotation databases

    EnsemblFungiiYLR167W; YLR167W; YLR167W.
    GeneIDi850864.
    KEGGisce:YLR167W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05730 Genomic DNA. Translation: CAA29197.1 .
    U17246 Genomic DNA. Translation: AAB67466.1 .
    BK006945 Genomic DNA. Translation: DAA09489.1 .
    PIRi C29456. UQBYR7.
    RefSeqi NP_013268.1. NM_001182054.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VW9 electron microscopy 6.10 g 1-152 [» ]
    1VWV electron microscopy 6.10 g 1-152 [» ]
    3U5C X-ray 3.00 f 1-152 [» ]
    3U5G X-ray 3.00 f 1-152 [» ]
    4BYL electron microscopy 4.30 5 1-152 [» ]
    4BYT electron microscopy 6.60 5 1-152 [» ]
    4CUY electron microscopy 3.70 f 101-152 [» ]
    ProteinModelPortali P05759.
    SMRi P05759. Positions 1-74, 83-151.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31440. 35 interactions.
    DIPi DIP-6389N.
    IntActi P05759. 16 interactions.
    MINTi MINT-8285344.
    STRINGi 4932.YLR167W.

    2D gel databases

    SWISS-2DPAGE P61864.

    Proteomic databases

    MaxQBi P05759.
    PaxDbi P05759.
    PRIDEi P05759.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR167W ; YLR167W ; YLR167W .
    GeneIDi 850864.
    KEGGi sce:YLR167W.

    Organism-specific databases

    SGDi S000004157. RPS31.

    Phylogenomic databases

    eggNOGi COG5272.
    GeneTreei ENSGT00550000074763.
    HOGENOMi HOG000224977.
    KOi K02977.
    OMAi MSILKYY.
    OrthoDBi EOG7D5B06.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32297-MONOMER.

    Miscellaneous databases

    NextBioi 967191.
    PROi P05759.

    Gene expression databases

    Genevestigatori P61864.

    Family and domain databases

    InterProi IPR002906. Ribosomal_S27a.
    IPR011332. Ribosomal_zn-bd.
    IPR019956. Ubiquitin.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR019954. Ubiquitin_CS.
    [Graphical view ]
    Pfami PF01599. Ribosomal_S27. 1 hit.
    PF00240. ubiquitin. 1 hit.
    [Graphical view ]
    PRINTSi PR00348. UBIQUITIN.
    SMARTi SM00213. UBQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    SSF57829. SSF57829. 1 hit.
    PROSITEi PS00299. UBIQUITIN_1. 1 hit.
    PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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].

    Entry informationi

    Entry nameiRS27A_YEAST
    AccessioniPrimary (citable) accession number: P05759
    Secondary accession number(s): D6VYH3
    , P04838, P14800, P61864, Q6LA96
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: August 10, 2010
    Last modified: October 1, 2014
    This is version 136 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Ribosomal proteins
      Ribosomal proteins families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3