Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P26785 (RL16B_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L16-B
Alternative name(s):
L21
RP23
YL15
Gene names
Name:RPL16B
Synonyms:RP23, RPL21B
Ordered Locus Names:YNL069C
ORF Names:N2377
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

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). Ref.5

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01366.

Post-translational modification

N-terminally acetylated by acetyltransferase NatA. Ref.4 Ref.6

Miscellaneous

There are 2 genes for L16 in yeast.

Sequence similarities

Belongs to the ribosomal protein L13P family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.6
Chain2 – 19819760S ribosomal protein L16-B HAMAP-Rule MF_01366
PRO_0000133792

Amino acid modifications

Modified residue21N-acetylserine; partial Ref.4 Ref.6
Modified residue431Phosphoserine Ref.8
Modified residue1811Phosphoserine Ref.9
Modified residue1851Phosphoserine Ref.7 Ref.10
Modified residue1871Phosphoserine Ref.7 Ref.9 Ref.10

Experimental info

Sequence conflict141L → H AA sequence Ref.4

Sequences

Sequence LengthMass (Da)Tools
P26785 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 959CFEC64DAF2F83

FASTA19822,249
        10         20         30         40         50         60 
MSQPVVVIDA KDHLLGRLAS TIAKQVLNGQ KIVVVRAEAL NISGEFFRNK LKYHDFLRKA 

        70         80         90        100        110        120 
TAFNKTRGPF HFRAPSRILY KAIRGMVSHK TARGKAALER LKIFEGIPPP YDKKKRVVVP 

       130        140        150        160        170        180 
QALRVLRLKP GRKYTTLGKL STSVGWKYED VVAKLEDKRK VRSAEYYAKK RAFTKKVSSA 

       190 
SAAASESDVA KQLASFGY 

« Hide

References

« Hide 'large scale' references
[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(1996) [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. expand/collapse author list , 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(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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(1992) [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(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]"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(2007) [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(2007) [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(2008) [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(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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(2012) [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(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 80S RIBOSOME.
[14]"The structure of the eukaryotic ribosome at 3.0 A resolution."
Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G., Yusupov M.
Science 334:1524-1529(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X86470 Genomic DNA. Translation: CAA60191.1.
X86470 Genomic DNA. Translation: CAA60192.1.
Z71345 Genomic DNA. Translation: CAA95943.1.
BK006947 Genomic DNA. Translation: DAA10476.1.
PIRS53911.
RefSeqNP_014330.1. NM_001182907.1.

3D structure databases

ProteinModelPortalP26785.
SMRP26785. Positions 3-198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid35754. 135 interactions.
IntActP26785. 25 interactions.
MINTMINT-8285422.
STRING4932.YNL069C.

Proteomic databases

MaxQBP26785.
PaxDbP26785.
PeptideAtlasP26785.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYNL069C; YNL069C; YNL069C.
GeneID855655.
KEGGsce:YNL069C.

Organism-specific databases

SGDS000005013. RPL16B.

Phylogenomic databases

eggNOGCOG0102.
GeneTreeENSGT00390000010799.
HOGENOMHOG000225289.
KOK02872.
OMAFEGIPAP.
OrthoDBEOG70W3RX.

Enzyme and pathway databases

BioCycYEAST:G3O-33099-MONOMER.

Gene expression databases

GenevestigatorP26785.

Family and domain databases

Gene3D3.90.1180.10. 1 hit.
HAMAPMF_01366. Ribosomal_L13.
InterProIPR005822. Ribosomal_L13.
IPR023563. Ribosomal_L13_CS.
IPR023564. Ribosomal_L13_dom.
IPR005755. Ribosomal_L13_euk/arc.
[Graphical view]
PANTHERPTHR11545. PTHR11545. 1 hit.
PTHR11545:SF3. PTHR11545:SF3. 1 hit.
PfamPF00572. Ribosomal_L13. 1 hit.
[Graphical view]
PIRSFPIRSF002181. Ribosomal_L13. 1 hit.
SUPFAMSSF52161. SSF52161. 1 hit.
TIGRFAMsTIGR01077. L13_A_E. 1 hit.
PROSITEPS00783. RIBOSOMAL_L13. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio979911.

Entry information

Entry nameRL16B_YEAST
AccessionPrimary (citable) accession number: P26785
Secondary accession number(s): D6W1B0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries