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Protein

60S ribosomal protein L16-B

Gene

RPL16B

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
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-33099-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 L16-B
Alternative name(s):
L21
RP23
YL15
Gene namesi
Name:RPL16B
Synonyms:RP23, RPL21B
Ordered Locus Names:YNL069C
ORF Names:N2377
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

SGDiS000005013. RPL16B.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 19819760S ribosomal protein L16-BPRO_0000133792Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine; partial2 Publications
Modified residuei43 – 431Phosphoserine1 Publication
Modified residuei181 – 1811Phosphoserine1 Publication
Modified residuei185 – 1851Phosphoserine2 Publications
Modified residuei187 – 1871Phosphoserine3 Publications

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP26785.
PaxDbiP26785.
PeptideAtlasiP26785.

Expressioni

Gene expression databases

GenevestigatoriP26785.

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

BioGridi35754. 138 interactions.
IntActiP26785. 25 interactions.
MINTiMINT-8285422.
STRINGi4932.YNL069C.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V88X-ray3.00BO/DO68-198[»]
SMRiP26785. Positions 3-198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L13P family.Curated

Phylogenomic databases

eggNOGiCOG0102.
GeneTreeiENSGT00390000010799.
HOGENOMiHOG000225289.
InParanoidiP26785.
KOiK02872.
OMAiFEGIPAP.
OrthoDBiEOG70W3RX.

Family and domain databases

Gene3Di3.90.1180.10. 1 hit.
HAMAPiMF_01366. Ribosomal_L13.
InterProiIPR005822. Ribosomal_L13.
IPR023563. Ribosomal_L13_CS.
IPR023564. Ribosomal_L13_dom.
IPR005755. Ribosomal_L13_euk/arc.
[Graphical view]
PANTHERiPTHR11545. PTHR11545. 1 hit.
PTHR11545:SF3. PTHR11545:SF3. 1 hit.
PfamiPF00572. Ribosomal_L13. 1 hit.
[Graphical view]
SUPFAMiSSF52161. SSF52161. 1 hit.
TIGRFAMsiTIGR01077. L13_A_E. 1 hit.
PROSITEiPS00783. RIBOSOMAL_L13. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P26785-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQPVVVIDA KDHLLGRLAS TIAKQVLNGQ KIVVVRAEAL NISGEFFRNK
60 70 80 90 100
LKYHDFLRKA TAFNKTRGPF HFRAPSRILY KAIRGMVSHK TARGKAALER
110 120 130 140 150
LKIFEGIPPP YDKKKRVVVP QALRVLRLKP GRKYTTLGKL STSVGWKYED
160 170 180 190
VVAKLEDKRK VRSAEYYAKK RAFTKKVSSA SAAASESDVA KQLASFGY
Length:198
Mass (Da):22,249
Last modified:January 22, 2007 - v3
Checksum:i959CFEC64DAF2F83
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141L → H AA sequence (PubMed:1544921).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86470 Genomic DNA. Translation: CAA60191.1.
X86470 Genomic DNA. Translation: CAA60192.1.
Z71345 Genomic DNA. Translation: CAA95943.1.
BK006947 Genomic DNA. Translation: DAA10476.1.
PIRiS53911.
RefSeqiNP_014330.1. NM_001182907.1.

Genome annotation databases

EnsemblFungiiYNL069C; YNL069C; YNL069C.
GeneIDi855655.
KEGGisce:YNL069C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X86470 Genomic DNA. Translation: CAA60191.1.
X86470 Genomic DNA. Translation: CAA60192.1.
Z71345 Genomic DNA. Translation: CAA95943.1.
BK006947 Genomic DNA. Translation: DAA10476.1.
PIRiS53911.
RefSeqiNP_014330.1. NM_001182907.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V88X-ray3.00BO/DO68-198[»]
SMRiP26785. Positions 3-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35754. 138 interactions.
IntActiP26785. 25 interactions.
MINTiMINT-8285422.
STRINGi4932.YNL069C.

Proteomic databases

MaxQBiP26785.
PaxDbiP26785.
PeptideAtlasiP26785.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL069C; YNL069C; YNL069C.
GeneIDi855655.
KEGGisce:YNL069C.

Organism-specific databases

SGDiS000005013. RPL16B.

Phylogenomic databases

eggNOGiCOG0102.
GeneTreeiENSGT00390000010799.
HOGENOMiHOG000225289.
InParanoidiP26785.
KOiK02872.
OMAiFEGIPAP.
OrthoDBiEOG70W3RX.

Enzyme and pathway databases

BioCyciYEAST:G3O-33099-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

NextBioi979911.

Gene expression databases

GenevestigatoriP26785.

Family and domain databases

Gene3Di3.90.1180.10. 1 hit.
HAMAPiMF_01366. Ribosomal_L13.
InterProiIPR005822. Ribosomal_L13.
IPR023563. Ribosomal_L13_CS.
IPR023564. Ribosomal_L13_dom.
IPR005755. Ribosomal_L13_euk/arc.
[Graphical view]
PANTHERiPTHR11545. PTHR11545. 1 hit.
PTHR11545:SF3. PTHR11545:SF3. 1 hit.
PfamiPF00572. Ribosomal_L13. 1 hit.
[Graphical view]
SUPFAMiSSF52161. SSF52161. 1 hit.
TIGRFAMsiTIGR01077. L13_A_E. 1 hit.
PROSITEiPS00783. RIBOSOMAL_L13. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV reveals 12 new open reading frames (ORFs) and an ancient duplication of six ORFs."
    Poehlmann R., Philippsen P.
    Yeast 12:391-402(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1996) [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. "NH2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae."
    Takakura H., Tsunasawa S., Miyagi M., Warner J.R.
    J. Biol. Chem. 267:5442-5445(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-26, ACETYLATION AT SER-2 BY NATA.
  5. "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.
  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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2 BY NATA.
  7. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  8. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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].
  13. "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.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRL16B_YEAST
AccessioniPrimary (citable) accession number: P26785
Secondary accession number(s): D6W1B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1992
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 134 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 2 genes for L16 in yeast.

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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.