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Protein

60S ribosomal protein L28

Gene

RPL28

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. RNA binding Source: SGD
  2. structural constituent of ribosome Source: SGD

GO - Biological processi

  1. cytoplasmic translation Source: SGD
  2. response to antibiotic Source: UniProtKB-KW
  3. response to cycloheximide Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Antibiotic resistance, Cycloheximide resistance

Enzyme and pathway databases

BioCyciYEAST:G3O-30602-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L28
Alternative name(s):
L27a
L29
RP44
RP62
YL24
Gene namesi
Name:RPL28
Synonyms:CYH2
Ordered Locus Names:YGL103W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome VII

Organism-specific databases

SGDiS000003071. RPL28.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 14914860S ribosomal protein L28PRO_0000104904Add
BLAST

Proteomic databases

MaxQBiP02406.
PaxDbiP02406.
PeptideAtlasiP02406.

Expressioni

Gene expression databases

GenevestigatoriP02406.

Interactioni

Subunit structurei

Component of the large 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

BioGridi33147. 121 interactions.
IntActiP02406. 32 interactions.
MINTiMINT-1324980.
STRINGi4932.YGL103W.

Structurei

Secondary structure

1
149
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Helixi7 – 115Combined sources
Beta strandi14 – 163Combined sources
Helixi17 – 193Combined sources
Beta strandi21 – 233Combined sources
Turni33 – 419Combined sources
Helixi42 – 454Combined sources
Turni46 – 483Combined sources
Turni65 – 684Combined sources
Beta strandi72 – 743Combined sources
Turni75 – 784Combined sources
Helixi79 – 813Combined sources
Helixi84 – 918Combined sources
Beta strandi96 – 983Combined sources
Beta strandi101 – 1033Combined sources
Turni104 – 1085Combined sources
Beta strandi110 – 1134Combined sources
Beta strandi124 – 1307Combined sources
Helixi132 – 1409Combined sources
Beta strandi144 – 1474Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-V6-148[»]
3J6Xelectron microscopy6.10681-149[»]
3J6Yelectron microscopy6.10681-149[»]
3J77electron microscopy6.20781-149[»]
3J78electron microscopy6.30781-149[»]
4U3MX-ray3.00N8/n82-149[»]
4U3NX-ray3.20N8/n82-149[»]
4U3UX-ray2.90N8/n82-149[»]
4U4NX-ray3.10N8/n82-149[»]
4U4OX-ray3.60N8/n82-149[»]
4U4QX-ray3.00N8/n82-149[»]
4U4RX-ray2.80N8/n82-149[»]
4U4UX-ray3.00N8/n82-149[»]
4U4YX-ray3.20N8/n82-149[»]
4U4ZX-ray3.10N8/n82-149[»]
4U50X-ray3.20N8/n82-149[»]
4U51X-ray3.20N8/n82-149[»]
4U52X-ray3.00N8/n82-149[»]
4U53X-ray3.30N8/n82-149[»]
4U55X-ray3.20N8/n82-149[»]
4U56X-ray3.45N8/n82-149[»]
4U6FX-ray3.10N8/n82-149[»]
4V4Belectron microscopy11.70BV2-149[»]
4V6Ielectron microscopy8.80BO1-149[»]
4V7Felectron microscopy8.70N1-149[»]
4V7RX-ray4.00BY/DY1-149[»]
4V88X-ray3.00Ba/Da1-149[»]
4V8Telectron microscopy8.10a1-149[»]
4V8Yelectron microscopy4.30Ba2-149[»]
4V8Zelectron microscopy6.60Ba2-149[»]
4V91electron microscopy3.70a1-149[»]
ProteinModelPortaliP02406.
SMRiP02406. Positions 2-149.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02406.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi7 – 137Nuclear localization signal1 Publication
Motifi24 – 307Nuclear localization signal1 Publication

Sequence similaritiesi

Belongs to the ribosomal protein L15P family.Curated

Phylogenomic databases

eggNOGiCOG0200.
GeneTreeiENSGT00390000005534.
HOGENOMiHOG000231263.
InParanoidiP02406.
KOiK02900.
OMAiVCPTINI.
OrthoDBiEOG7C5MN5.

Family and domain databases

HAMAPiMF_01341. Ribosomal_L15.
InterProiIPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02406-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSRFTKTRK HRGHVSAGKG RIGKHRKHPG GRGMAGGQHH HRINMDKYHP
60 70 80 90 100
GYFGKVGMRY FHKQQAHFWK PVLNLDKLWT LIPEDKRDQY LKSASKETAP
110 120 130 140
VIDTLAAGYG KILGKGRIPN VPVIVKARFV SKLAEEKIRA AGGVVELIA
Length:149
Mass (Da):16,722
Last modified:October 4, 2010 - v3
Checksum:iB34C325C01E14ACB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381Q → E Confers resistance to cycloheximide, an inhibitor of polypeptide elongation. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01573 Genomic DNA. Translation: CAA25729.1.
Z72625 Genomic DNA. Translation: CAA96808.1.
M19490 Genomic DNA. Translation: AAA35002.1.
BK006941 Genomic DNA. Translation: DAA08004.1.
PIRiA02782. R6BY29.
RefSeqiNP_011412.1. NM_001180968.1.

Genome annotation databases

EnsemblFungiiYGL103W; YGL103W; YGL103W.
GeneIDi852775.
KEGGisce:YGL103W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01573 Genomic DNA. Translation: CAA25729.1.
Z72625 Genomic DNA. Translation: CAA96808.1.
M19490 Genomic DNA. Translation: AAA35002.1.
BK006941 Genomic DNA. Translation: DAA08004.1.
PIRiA02782. R6BY29.
RefSeqiNP_011412.1. NM_001180968.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-V6-148[»]
3J6Xelectron microscopy6.10681-149[»]
3J6Yelectron microscopy6.10681-149[»]
3J77electron microscopy6.20781-149[»]
3J78electron microscopy6.30781-149[»]
4U3MX-ray3.00N8/n82-149[»]
4U3NX-ray3.20N8/n82-149[»]
4U3UX-ray2.90N8/n82-149[»]
4U4NX-ray3.10N8/n82-149[»]
4U4OX-ray3.60N8/n82-149[»]
4U4QX-ray3.00N8/n82-149[»]
4U4RX-ray2.80N8/n82-149[»]
4U4UX-ray3.00N8/n82-149[»]
4U4YX-ray3.20N8/n82-149[»]
4U4ZX-ray3.10N8/n82-149[»]
4U50X-ray3.20N8/n82-149[»]
4U51X-ray3.20N8/n82-149[»]
4U52X-ray3.00N8/n82-149[»]
4U53X-ray3.30N8/n82-149[»]
4U55X-ray3.20N8/n82-149[»]
4U56X-ray3.45N8/n82-149[»]
4U6FX-ray3.10N8/n82-149[»]
4V4Belectron microscopy11.70BV2-149[»]
4V6Ielectron microscopy8.80BO1-149[»]
4V7Felectron microscopy8.70N1-149[»]
4V7RX-ray4.00BY/DY1-149[»]
4V88X-ray3.00Ba/Da1-149[»]
4V8Telectron microscopy8.10a1-149[»]
4V8Yelectron microscopy4.30Ba2-149[»]
4V8Zelectron microscopy6.60Ba2-149[»]
4V91electron microscopy3.70a1-149[»]
ProteinModelPortaliP02406.
SMRiP02406. Positions 2-149.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33147. 121 interactions.
IntActiP02406. 32 interactions.
MINTiMINT-1324980.
STRINGi4932.YGL103W.

Proteomic databases

MaxQBiP02406.
PaxDbiP02406.
PeptideAtlasiP02406.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL103W; YGL103W; YGL103W.
GeneIDi852775.
KEGGisce:YGL103W.

Organism-specific databases

SGDiS000003071. RPL28.

Phylogenomic databases

eggNOGiCOG0200.
GeneTreeiENSGT00390000005534.
HOGENOMiHOG000231263.
InParanoidiP02406.
KOiK02900.
OMAiVCPTINI.
OrthoDBiEOG7C5MN5.

Enzyme and pathway databases

BioCyciYEAST:G3O-30602-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

EvolutionaryTraceiP02406.
NextBioi972248.
PROiP02406.

Gene expression databases

GenevestigatoriP02406.

Family and domain databases

HAMAPiMF_01341. Ribosomal_L15.
InterProiIPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
[Graphical view]
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiPS00475. RIBOSOMAL_L15. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cycloheximide resistance in yeast: the gene and its protein."
    Kaufer N.F., Fried H.M., Schwindinger W.F., Jasin M., Warner J.R.
    Nucleic Acids Res. 11:3123-3135(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLU-38.
  2. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
    Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
    Yeast 13:1077-1090(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Transcriptional elements of the yeast ribosomal protein gene CYH2."
    Schwindinger W.F., Warner J.R.
    J. Biol. Chem. 262:5690-5695(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
  6. "Characterization of nuclear localizing sequences derived from yeast ribosomal protein L29."
    Underwood M.R., Fried H.M.
    EMBO J. 9:91-99(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEAR LOCALIZATION SIGNAL.
  7. "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae."
    Planta R.J., Mager W.H.
    Yeast 14:471-477(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE, SUBUNIT.
  8. "The action of N-terminal acetyltransferases on yeast ribosomal proteins."
    Arnold R.J., Polevoda B., Reilly J.P., Sherman F.
    J. Biol. Chem. 274:37035-37040(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF INITIATOR METHIONINE.
  9. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-ribosome and subunit-subunit interactions."
    Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., Frank J.
    Cell 107:373-386(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 6-148, ELECTRON MICROSCOPY.
  11. "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation."
    Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.
    EMBO J. 23:1008-1019(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING, ELECTRON MICROSCOPY.
  12. "Crystal structure of the eukaryotic ribosome."
    Ben-Shem A., Jenner L., Yusupova G., Yusupov M.
    Science 330:1203-1209(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 80S RIBOSOME.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRL28_YEAST
AccessioniPrimary (citable) accession number: P02406
Secondary accession number(s): D6VU43
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: October 4, 2010
Last modified: March 31, 2015
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.