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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: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.1 Publication

GO - Molecular functioni

  • RNA binding Source: SGD
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • response to antibiotic Source: UniProtKB-KW
  • response to cycloheximide Source: UniProtKB-KW

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein
Biological processAntibiotic resistance, Cycloheximide resistance

Enzyme and pathway databases

BioCyciYEAST:G3O-30602-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L281 Publication
Alternative name(s):
L27a
L29
Large ribosomal subunit protein uL151 Publication
RP44
RP62
YL24
Gene namesi
Name:RPL281 Publication
Synonyms:CYH2
Ordered Locus Names:YGL103W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL103W.
SGDiS000003071. RPL28.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD
  • nucleus Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001049042 – 14960S ribosomal protein L28Add BLAST148

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP02406.
PRIDEiP02406.

Interactioni

Subunit structurei

Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).1 Publication1 Publication

Protein-protein interaction databases

BioGridi33147. 266 interactors.
IntActiP02406. 32 interactors.
MINTiMINT-1324980.

Structurei

Secondary structure

1149
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Helixi7 – 11Combined sources5
Beta strandi14 – 16Combined sources3
Helixi17 – 19Combined sources3
Beta strandi21 – 23Combined sources3
Turni33 – 41Combined sources9
Helixi42 – 45Combined sources4
Turni46 – 48Combined sources3
Turni65 – 68Combined sources4
Beta strandi72 – 74Combined sources3
Turni75 – 78Combined sources4
Helixi79 – 81Combined sources3
Helixi84 – 91Combined sources8
Beta strandi96 – 98Combined sources3
Beta strandi101 – 103Combined sources3
Turni104 – 108Combined sources5
Beta strandi110 – 113Combined sources4
Beta strandi124 – 130Combined sources7
Helixi132 – 140Combined sources9
Beta strandi144 – 147Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-V6-148[»]
3J6Xelectron microscopy6.10681-149[»]
3J6Yelectron microscopy6.10681-149[»]
3J77electron microscopy6.20781-149[»]
3J78electron microscopy6.30781-149[»]
3JCTelectron microscopy3.08a1-149[»]
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[»]
5APNelectron microscopy3.91a1-149[»]
5APOelectron microscopy3.41a1-149[»]
5DATX-ray3.15N8/n82-149[»]
5DC3X-ray3.25N8/n82-149[»]
5DGEX-ray3.45N8/n82-149[»]
5DGFX-ray3.30N8/n82-149[»]
5DGVX-ray3.10N8/n82-149[»]
5FCIX-ray3.40N8/n82-149[»]
5FCJX-ray3.10N8/n82-149[»]
5FL8electron microscopy9.50a1-149[»]
5GAKelectron microscopy3.88c1-149[»]
5H4Pelectron microscopy3.07a1-149[»]
5I4LX-ray3.10N8/n82-149[»]
5JCSelectron microscopy9.50a1-149[»]
5JUOelectron microscopy4.00FA1-149[»]
5JUPelectron microscopy3.50FA1-149[»]
5JUSelectron microscopy4.20FA1-149[»]
5JUTelectron microscopy4.00FA1-149[»]
5JUUelectron microscopy4.00FA1-149[»]
5LYBX-ray3.25N8/n82-149[»]
5M1Jelectron microscopy3.30a52-149[»]
5MC6electron microscopy3.80AR1-149[»]
5T62electron microscopy3.30n1-149[»]
5T6Relectron microscopy4.50n1-149[»]
5TGAX-ray3.30N8/n82-149[»]
5TGMX-ray3.50N8/n82-149[»]
ProteinModelPortaliP02406.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02406.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi7 – 13Nuclear localization signal1 Publication7
Motifi24 – 30Nuclear localization signal1 Publication7

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000005534.
HOGENOMiHOG000231263.
InParanoidiP02406.
KOiK02900.
OMAiKKDTVPV.
OrthoDBiEOG092C5786.

Family and domain databases

Gene3Di4.10.990.10. 1 hit.
HAMAPiMF_01341. Ribosomal_L15. 1 hit.
InterProiView protein in InterPro
IPR027386. 50S_Rbsml_prot_L15P_N.
IPR030878. Ribosomal_L15.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
PfamiView protein in Pfam
PF00828. Ribosomal_L27A. 1 hit.
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiView protein in PROSITE
PS00475. RIBOSOMAL_L15. 1 hit.

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 5, 2010 - v3
Checksum:iB34C325C01E14ACB
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti38Q → E Confers resistance to cycloheximide, an inhibitor of polypeptide elongation. 1 Publication1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-V6-148[»]
3J6Xelectron microscopy6.10681-149[»]
3J6Yelectron microscopy6.10681-149[»]
3J77electron microscopy6.20781-149[»]
3J78electron microscopy6.30781-149[»]
3JCTelectron microscopy3.08a1-149[»]
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[»]
5APNelectron microscopy3.91a1-149[»]
5APOelectron microscopy3.41a1-149[»]
5DATX-ray3.15N8/n82-149[»]
5DC3X-ray3.25N8/n82-149[»]
5DGEX-ray3.45N8/n82-149[»]
5DGFX-ray3.30N8/n82-149[»]
5DGVX-ray3.10N8/n82-149[»]
5FCIX-ray3.40N8/n82-149[»]
5FCJX-ray3.10N8/n82-149[»]
5FL8electron microscopy9.50a1-149[»]
5GAKelectron microscopy3.88c1-149[»]
5H4Pelectron microscopy3.07a1-149[»]
5I4LX-ray3.10N8/n82-149[»]
5JCSelectron microscopy9.50a1-149[»]
5JUOelectron microscopy4.00FA1-149[»]
5JUPelectron microscopy3.50FA1-149[»]
5JUSelectron microscopy4.20FA1-149[»]
5JUTelectron microscopy4.00FA1-149[»]
5JUUelectron microscopy4.00FA1-149[»]
5LYBX-ray3.25N8/n82-149[»]
5M1Jelectron microscopy3.30a52-149[»]
5MC6electron microscopy3.80AR1-149[»]
5T62electron microscopy3.30n1-149[»]
5T6Relectron microscopy4.50n1-149[»]
5TGAX-ray3.30N8/n82-149[»]
5TGMX-ray3.50N8/n82-149[»]
ProteinModelPortaliP02406.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33147. 266 interactors.
IntActiP02406. 32 interactors.
MINTiMINT-1324980.

Proteomic databases

MaxQBiP02406.
PRIDEiP02406.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YGL103W.
SGDiS000003071. RPL28.

Phylogenomic databases

GeneTreeiENSGT00390000005534.
HOGENOMiHOG000231263.
InParanoidiP02406.
KOiK02900.
OMAiKKDTVPV.
OrthoDBiEOG092C5786.

Enzyme and pathway databases

BioCyciYEAST:G3O-30602-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

EvolutionaryTraceiP02406.
PROiPR:P02406.

Family and domain databases

Gene3Di4.10.990.10. 1 hit.
HAMAPiMF_01341. Ribosomal_L15. 1 hit.
InterProiView protein in InterPro
IPR027386. 50S_Rbsml_prot_L15P_N.
IPR030878. Ribosomal_L15.
IPR001196. Ribosomal_L15_CS.
IPR021131. Ribosomal_L18e/L15P.
PfamiView protein in Pfam
PF00828. Ribosomal_L27A. 1 hit.
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiView protein in PROSITE
PS00475. RIBOSOMAL_L15. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL28_YEAST
AccessioniPrimary (citable) accession number: P02406
Secondary accession number(s): D6VU43
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: October 5, 2010
Last modified: April 12, 2017
This is version 152 of the entry and version 3 of the sequence. See 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

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 one 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.