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Protein

Ubiquitin-40S ribosomal protein S31

Gene

RPS31

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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-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

  • metal ion binding Source: UniProtKB-KW
  • protein tag Source: SGD
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, LSU-rRNA,5S) Source: SGD
  • ribosomal small subunit assembly Source: SGD
  • ribosome biogenesis Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-32297-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_291351. Orc1 removal from chromatin.
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_303262. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_305425. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_316133. Translesion synthesis by REV1.
REACT_326247. Translesion Synthesis by POLH.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_335938. Ribosomal scanning and start codon recognition.
REACT_343353. Peptide chain elongation.
REACT_343770. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_346191. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_347103. ER-Phagosome pathway.
REACT_351622. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_354180. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_357098. Termination of translesion DNA synthesis.
REACT_357697. Translesion synthesis by POLI.
REACT_359959. Translesion synthesis by POLK.

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 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR167W.
SGDiS000004157. RPS31.

Subcellular locationi

Ubiquitin :

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: SGD
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi29 – 291K → R: Deficiency in ubiquitin-protein conjugate formation. 1 Publication
Mutagenesisi48 – 481K → R: Deficiency in ubiquitin-protein conjugate formation. 1 Publication
Mutagenesisi63 – 631K → R: Deficiency in ubiquitin-protein conjugate formation. Loss of DNA repair function. 1 Publication

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.

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. 36 interactions.
DIPiDIP-6389N.
IntActiP05759. 18 interactions.
MINTiMINT-8285344.

Structurei

Secondary structure

1
152
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi79 – 813Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi110 – 1123Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi120 – 1234Combined sources
Turni124 – 1263Combined sources
Beta strandi128 – 1347Combined sources
Beta strandi139 – 1468Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10311-152[»]
3J6Yelectron microscopy6.10311-152[»]
3J77electron microscopy6.20311-152[»]
3J78electron microscopy6.30311-152[»]
3V88X-ray3.00f1-152[»]
4U3MX-ray3.00E177-152[»]
e178-152[»]
4U3NX-ray3.20E177-152[»]
e178-152[»]
4U3UX-ray2.90E177-152[»]
e178-152[»]
4U4NX-ray3.10E1/e177-152[»]
4U4OX-ray3.60E178-152[»]
e177-152[»]
4U4QX-ray3.00E1/e177-152[»]
4U4RX-ray2.80E1/e177-152[»]
4U4UX-ray3.00E1/e177-152[»]
4U4YX-ray3.20E1/e177-152[»]
4U4ZX-ray3.10E1/e177-152[»]
4U50X-ray3.20E1/e178-152[»]
4U51X-ray3.20E1/e177-152[»]
4U52X-ray3.00E1/e177-152[»]
4U53X-ray3.30E1/e177-152[»]
4U55X-ray3.20E1/e177-152[»]
4U56X-ray3.45E1/e177-152[»]
4U6FX-ray3.10E1/e177-152[»]
4V88X-ray3.00Af/Cf1-152[»]
4V8Yelectron microscopy4.30A51-152[»]
4V8Zelectron microscopy6.60A51-152[»]
4V92electron microscopy3.70f101-152[»]
ProteinModelPortaliP05759.
SMRiP05759. Positions 1-76, 82-148.
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 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.
InParanoidiP05759.
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

        10         20         30         40         50
MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGGKKR KKKVYTTPKK IKHKHKKVKL
110 120 130 140 150
AVLSYYKVDA EGKVTKLRRE CSNPTCGAGV FLANHKDRLY CGKCHSVYKV

NA
Length:152
Mass (Da):17,216
Last modified:August 10, 2010 - v3
Checksum:i53BF38E2E2F8B38E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10311-152[»]
3J6Yelectron microscopy6.10311-152[»]
3J77electron microscopy6.20311-152[»]
3J78electron microscopy6.30311-152[»]
3V88X-ray3.00f1-152[»]
4U3MX-ray3.00E177-152[»]
e178-152[»]
4U3NX-ray3.20E177-152[»]
e178-152[»]
4U3UX-ray2.90E177-152[»]
e178-152[»]
4U4NX-ray3.10E1/e177-152[»]
4U4OX-ray3.60E178-152[»]
e177-152[»]
4U4QX-ray3.00E1/e177-152[»]
4U4RX-ray2.80E1/e177-152[»]
4U4UX-ray3.00E1/e177-152[»]
4U4YX-ray3.20E1/e177-152[»]
4U4ZX-ray3.10E1/e177-152[»]
4U50X-ray3.20E1/e178-152[»]
4U51X-ray3.20E1/e177-152[»]
4U52X-ray3.00E1/e177-152[»]
4U53X-ray3.30E1/e177-152[»]
4U55X-ray3.20E1/e177-152[»]
4U56X-ray3.45E1/e177-152[»]
4U6FX-ray3.10E1/e177-152[»]
4V88X-ray3.00Af/Cf1-152[»]
4V8Yelectron microscopy4.30A51-152[»]
4V8Zelectron microscopy6.60A51-152[»]
4V92electron microscopy3.70f101-152[»]
ProteinModelPortaliP05759.
SMRiP05759. Positions 1-76, 82-148.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31440. 36 interactions.
DIPiDIP-6389N.
IntActiP05759. 18 interactions.
MINTiMINT-8285344.

2D gel databases

SWISS-2DPAGEP61864.

Proteomic databases

MaxQBiP05759.
PaxDbiP05759.
PRIDEiP05759.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YLR167W.
SGDiS000004157. RPS31.

Phylogenomic databases

eggNOGiCOG5272.
GeneTreeiENSGT00550000074763.
HOGENOMiHOG000224977.
InParanoidiP05759.
KOiK02977.
OMAiMSILKYY.
OrthoDBiEOG7D5B06.

Enzyme and pathway databases

BioCyciYEAST:G3O-32297-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_291351. Orc1 removal from chromatin.
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_303262. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_305425. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_316133. Translesion synthesis by REV1.
REACT_326247. Translesion Synthesis by POLH.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_335938. Ribosomal scanning and start codon recognition.
REACT_343353. Peptide chain elongation.
REACT_343770. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_346191. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_347103. ER-Phagosome pathway.
REACT_351622. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_354180. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_357098. Termination of translesion DNA synthesis.
REACT_357697. Translesion synthesis by POLI.
REACT_359959. Translesion synthesis by POLK.

Miscellaneous databases

NextBioi967191.
PROiP05759.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: July 22, 2015
This is version 146 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

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 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.