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Protein

60S ribosomal protein L11-B

Gene

RPL11B

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

Binds to 5S ribosomal RNA.

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-KW
  2. structural constituent of ribosome Source: SGD

GO - Biological processi

  1. cytoplasmic translation Source: SGD
  2. ribosomal large subunit assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30797-MONOMER.
ReactomeiREACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257951. Peptide chain elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L11-B
Alternative name(s):
L16
RP39
YL22
Gene namesi
Name:RPL11B
Synonyms:RP39B, RPL16B
Ordered Locus Names:YGR085C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

SGDiS000003317. RPL11B.

Subcellular locationi

Cytoplasm. Nucleus
Note: The SYO1/RPL11/RPL5 complex is transported into the nucleus by KAP104.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 17417360S ribosomal protein L11-BPRO_0000125105Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei75 – 751N6,N6,N6-trimethyllysine1 Publication

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.1 Publication

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

MaxQBiQ3E757.
PaxDbiQ3E757.
PRIDEiQ3E757.

Expressioni

Gene expression databases

GenevestigatoriQ3E757.

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). Forms a heterotrimeric complex with RPL5 and SYO1. Interaction of this complex with KAP104 allows the nuclear import of the heterotrimer.1 Publication

Protein-protein interaction databases

BioGridi33327. 141 interactions.
DIPiDIP-29386N.
IntActiQ3E757. 18 interactions.
MINTiMINT-564941.

Structurei

Secondary structure

1
174
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 218Combined sources
Beta strandi25 – 273Combined sources
Helixi28 – 4114Combined sources
Beta strandi46 – 483Combined sources
Beta strandi55 – 573Combined sources
Beta strandi66 – 716Combined sources
Helixi74 – 8613Combined sources
Turni87 – 893Combined sources
Beta strandi90 – 923Combined sources
Beta strandi93 – 964Combined sources
Beta strandi102 – 1076Combined sources
Helixi109 – 1113Combined sources
Turni118 – 1203Combined sources
Beta strandi125 – 1317Combined sources
Turni134 – 1363Combined sources
Helixi137 – 1404Combined sources
Beta strandi141 – 1444Combined sources
Helixi150 – 1523Combined sources
Helixi156 – 1649Combined sources
Turni165 – 1673Combined sources
Beta strandi170 – 1723Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NOQelectron microscopy7.30H7-171[»]
3J0Qelectron microscopy10.60k7-171[»]
4U3MX-ray3.00M1/m12-174[»]
4U3NX-ray3.20M1/m12-174[»]
4U3UX-ray2.90M1/m12-174[»]
4U4NX-ray3.10M1/m12-174[»]
4U4OX-ray3.60M1/m12-174[»]
4U4QX-ray3.00M1/m12-174[»]
4U4RX-ray2.80M1/m12-174[»]
4U4UX-ray3.00M1/m12-174[»]
4U4YX-ray3.20M1/m12-174[»]
4U4ZX-ray3.10M1/m12-174[»]
4U50X-ray3.20M1/m12-174[»]
4U51X-ray3.20M1/m12-174[»]
4U52X-ray3.00M1/m12-174[»]
4U53X-ray3.30M1/m12-174[»]
4U55X-ray3.20M1/m12-174[»]
4U56X-ray3.45M1/m12-174[»]
4U6FX-ray3.10M1/m12-174[»]
4V8Telectron microscopy8.10J1-174[»]
ProteinModelPortaliQ3E757.
SMRiQ3E757. Positions 6-174.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ3E757.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L5P family.Curated

Phylogenomic databases

eggNOGiCOG0094.
GeneTreeiENSGT00390000013411.
HOGENOMiHOG000231312.
InParanoidiQ3E757.
KOiK02868.
OMAiNICVGEN.
OrthoDBiEOG7GBG86.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERiPTHR11994. PTHR11994. 1 hit.
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q3E757-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTKAQNPMR DLKIEKLVLN ISVGESGDRL TRASKVLEQL SGQTPVQSKA
60 70 80 90 100
RYTVRTFGIR RNEKIAVHVT VRGPKAEEIL ERGLKVKEYQ LRDRNFSATG
110 120 130 140 150
NFGFGIDEHI DLGIKYDPSI GIFGMDFYVV MNRPGARVTR RKRCKGTVGN
160 170
SHKTTKEDTV SWFKQKYDAD VLDK
Length:174
Mass (Da):19,750
Last modified:January 23, 2007 - v3
Checksum:i04F6CD88FEBD63E4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti138 – 1381V → A (PubMed:6390341).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72870 Genomic DNA. Translation: CAA97087.1.
M12933 Genomic DNA. Translation: AAA34990.1.
BK006941 Genomic DNA. Translation: DAA08178.1.
PIRiA02764. R5BY16.
RefSeqiNP_011599.1. NM_001181214.1.

Genome annotation databases

EnsemblFungiiYGR085C; YGR085C; YGR085C.
GeneIDi852976.
KEGGisce:YGR085C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z72870 Genomic DNA. Translation: CAA97087.1.
M12933 Genomic DNA. Translation: AAA34990.1.
BK006941 Genomic DNA. Translation: DAA08178.1.
PIRiA02764. R5BY16.
RefSeqiNP_011599.1. NM_001181214.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NOQelectron microscopy7.30H7-171[»]
3J0Qelectron microscopy10.60k7-171[»]
4U3MX-ray3.00M1/m12-174[»]
4U3NX-ray3.20M1/m12-174[»]
4U3UX-ray2.90M1/m12-174[»]
4U4NX-ray3.10M1/m12-174[»]
4U4OX-ray3.60M1/m12-174[»]
4U4QX-ray3.00M1/m12-174[»]
4U4RX-ray2.80M1/m12-174[»]
4U4UX-ray3.00M1/m12-174[»]
4U4YX-ray3.20M1/m12-174[»]
4U4ZX-ray3.10M1/m12-174[»]
4U50X-ray3.20M1/m12-174[»]
4U51X-ray3.20M1/m12-174[»]
4U52X-ray3.00M1/m12-174[»]
4U53X-ray3.30M1/m12-174[»]
4U55X-ray3.20M1/m12-174[»]
4U56X-ray3.45M1/m12-174[»]
4U6FX-ray3.10M1/m12-174[»]
4V8Telectron microscopy8.10J1-174[»]
ProteinModelPortaliQ3E757.
SMRiQ3E757. Positions 6-174.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33327. 141 interactions.
DIPiDIP-29386N.
IntActiQ3E757. 18 interactions.
MINTiMINT-564941.

Proteomic databases

MaxQBiQ3E757.
PaxDbiQ3E757.
PRIDEiQ3E757.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGR085C; YGR085C; YGR085C.
GeneIDi852976.
KEGGisce:YGR085C.

Organism-specific databases

SGDiS000003317. RPL11B.

Phylogenomic databases

eggNOGiCOG0094.
GeneTreeiENSGT00390000013411.
HOGENOMiHOG000231312.
InParanoidiQ3E757.
KOiK02868.
OMAiNICVGEN.
OrthoDBiEOG7GBG86.

Enzyme and pathway databases

BioCyciYEAST:G3O-30797-MONOMER.
ReactomeiREACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.
REACT_232946. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_252688. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_257951. Peptide chain elongation.

Miscellaneous databases

EvolutionaryTraceiQ3E757.
NextBioi972774.

Gene expression databases

GenevestigatoriQ3E757.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERiPTHR11994. PTHR11994. 1 hit.
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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(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. "Tripartite upstream promoter element essential for expression of Saccharomyces cerevisiae ribosomal protein genes."
    Rotenberg M.O., Woolford J.L. Jr.
    Mol. Cell. Biol. 6:674-687(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
  5. "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.
  6. "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(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2 BY NATA.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases."
    Couttas T.A., Raftery M.J., Padula M.P., Herbert B.R., Wilkins M.R.
    Proteomics 12:960-972(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-75.
  11. Cited for: INTERACTION WITH RPL5 AND SYO1, SUBCELLULAR LOCATION.
  12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (7.3 ANGSTROMS) OF 7-171.

Entry informationi

Entry nameiRL11B_YEAST
AccessioniPrimary (citable) accession number: Q3E757
Secondary accession number(s): D6VUL7, P06380
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 90 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 21200 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for L11 in yeast.

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.