Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

60S ribosomal protein L17-A

Gene

RPL17A

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. 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-31946-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 L17-A
Alternative name(s):
L20A
YL17
Gene namesi
Name:RPL17A
Synonyms:RPL17, RPL20A
Ordered Locus Names:YKL180W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XI

Organism-specific databases

SGDiS000001663. RPL17A.

Subcellular locationi

Cytoplasm 1 Publication

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 – 18418360S ribosomal protein L17-APRO_0000125347Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei70 – 701Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PeptideAtlasiP05740.

Expressioni

Gene expression databases

GenevestigatoriP05740.

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

BioGridi33959. 132 interactions.
DIPiDIP-5529N.
IntActiP05740. 54 interactions.
MINTiMINT-8285293.
STRINGi4932.YKL180W.

Structurei

Secondary structure

1
184
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 133Combined sources
Beta strandi14 – 229Combined sources
Helixi26 – 349Combined sources
Turni35 – 384Combined sources
Helixi41 – 5212Combined sources
Beta strandi54 – 563Combined sources
Beta strandi61 – 633Combined sources
Helixi71 – 766Combined sources
Beta strandi79 – 824Combined sources
Helixi85 – 10521Combined sources
Beta strandi111 – 12111Combined sources
Beta strandi125 – 1317Combined sources
Helixi132 – 1343Combined sources
Beta strandi135 – 1417Combined sources
Beta strandi144 – 1529Combined sources
Helixi170 – 18213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-N6-152[»]
2WW9electron microscopy8.60I1-184[»]
2WWAelectron microscopy8.90I1-184[»]
2WWBelectron microscopy6.48I1-184[»]
3J6Xelectron microscopy6.10571-184[»]
3J6Yelectron microscopy6.10571-184[»]
3J77electron microscopy6.20671-184[»]
3J78electron microscopy6.30671-184[»]
4U3MX-ray3.00M7/m72-184[»]
4U3NX-ray3.20M7/m72-184[»]
4U3UX-ray2.90M7/m72-184[»]
4U4NX-ray3.10M7/m72-184[»]
4U4OX-ray3.60M7/m72-184[»]
4U4QX-ray3.00M7/m72-184[»]
4U4RX-ray2.80M7/m72-184[»]
4U4UX-ray3.00M7/m72-184[»]
4U4YX-ray3.20M7/m72-184[»]
4U4ZX-ray3.10M7/m72-184[»]
4U50X-ray3.20M7/m72-184[»]
4U51X-ray3.20M7/m72-184[»]
4U52X-ray3.00M7/m72-184[»]
4U53X-ray3.30M7/m72-184[»]
4U55X-ray3.20M7/m72-184[»]
4U56X-ray3.45M7/m72-184[»]
4U6FX-ray3.10M7/m72-184[»]
4V4Belectron microscopy11.70BN2-184[»]
4V6Ielectron microscopy8.80BV1-170[»]
4V7Felectron microscopy8.70U1-184[»]
4V7RX-ray4.00BQ/DQ1-184[»]
4V88X-ray3.00BP/DP1-184[»]
4V8Telectron microscopy8.10P1-184[»]
4V8Yelectron microscopy4.30BP2-184[»]
4V8Zelectron microscopy6.60BP2-184[»]
4V91electron microscopy3.70P1-184[»]
ProteinModelPortaliP05740.
SMRiP05740. Positions 2-184.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05740.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L22P family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000014873.
HOGENOMiHOG000205045.
InParanoidiP05740.
KOiK02880.
OMAiMHIRKAN.
OrthoDBiEOG7P02WD.

Family and domain databases

Gene3Di3.90.470.10. 1 hit.
InterProiIPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005721. Ribosomal_L22/L17_euk/arc.
[Graphical view]
PANTHERiPTHR11593. PTHR11593. 1 hit.
PfamiPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMiSSF54843. SSF54843. 1 hit.
TIGRFAMsiTIGR01038. L22_arch. 1 hit.
PROSITEiPS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P05740-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARYGATSTN PAKSASARGS YLRVSFKNTR ETAQAINGWE LTKAQKYLEQ
60 70 80 90 100
VLDHQRAIPF RRFNSSIGRT AQGKEFGVTK ARWPAKSVKF VQGLLQNAAA
110 120 130 140 150
NAEAKGLDAT KLYVSHIQVN QAPKQRRRTY RAHGRINKYE SSPSHIELVV
160 170 180
TEKEEAVAKA AEKKVVRLTS RQRGRIAAQK RIAA
Length:184
Mass (Da):20,549
Last modified:January 23, 2007 - v4
Checksum:iB8902DD90714671D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 11411AKGLDATKLYV → VCQEYYMFSTR in CAA52258 (PubMed:8154185).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28180 Genomic DNA. Translation: CAA82023.1.
Z28179 Genomic DNA. Translation: CAA82022.1.
X74151 Genomic DNA. Translation: CAA52258.1.
BK006944 Genomic DNA. Translation: DAA08987.1.
PIRiS38012.
RefSeqiNP_012741.1. NM_001179746.1.

Genome annotation databases

EnsemblFungiiYKL180W; YKL180W; YKL180W.
GeneIDi853674.
KEGGisce:YKL180W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28180 Genomic DNA. Translation: CAA82023.1.
Z28179 Genomic DNA. Translation: CAA82022.1.
X74151 Genomic DNA. Translation: CAA52258.1.
BK006944 Genomic DNA. Translation: DAA08987.1.
PIRiS38012.
RefSeqiNP_012741.1. NM_001179746.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-N6-152[»]
2WW9electron microscopy8.60I1-184[»]
2WWAelectron microscopy8.90I1-184[»]
2WWBelectron microscopy6.48I1-184[»]
3J6Xelectron microscopy6.10571-184[»]
3J6Yelectron microscopy6.10571-184[»]
3J77electron microscopy6.20671-184[»]
3J78electron microscopy6.30671-184[»]
4U3MX-ray3.00M7/m72-184[»]
4U3NX-ray3.20M7/m72-184[»]
4U3UX-ray2.90M7/m72-184[»]
4U4NX-ray3.10M7/m72-184[»]
4U4OX-ray3.60M7/m72-184[»]
4U4QX-ray3.00M7/m72-184[»]
4U4RX-ray2.80M7/m72-184[»]
4U4UX-ray3.00M7/m72-184[»]
4U4YX-ray3.20M7/m72-184[»]
4U4ZX-ray3.10M7/m72-184[»]
4U50X-ray3.20M7/m72-184[»]
4U51X-ray3.20M7/m72-184[»]
4U52X-ray3.00M7/m72-184[»]
4U53X-ray3.30M7/m72-184[»]
4U55X-ray3.20M7/m72-184[»]
4U56X-ray3.45M7/m72-184[»]
4U6FX-ray3.10M7/m72-184[»]
4V4Belectron microscopy11.70BN2-184[»]
4V6Ielectron microscopy8.80BV1-170[»]
4V7Felectron microscopy8.70U1-184[»]
4V7RX-ray4.00BQ/DQ1-184[»]
4V88X-ray3.00BP/DP1-184[»]
4V8Telectron microscopy8.10P1-184[»]
4V8Yelectron microscopy4.30BP2-184[»]
4V8Zelectron microscopy6.60BP2-184[»]
4V91electron microscopy3.70P1-184[»]
ProteinModelPortaliP05740.
SMRiP05740. Positions 2-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33959. 132 interactions.
DIPiDIP-5529N.
IntActiP05740. 54 interactions.
MINTiMINT-8285293.
STRINGi4932.YKL180W.

Proteomic databases

PeptideAtlasiP05740.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL180W; YKL180W; YKL180W.
GeneIDi853674.
KEGGisce:YKL180W.

Organism-specific databases

SGDiS000001663. RPL17A.

Phylogenomic databases

GeneTreeiENSGT00390000014873.
HOGENOMiHOG000205045.
InParanoidiP05740.
KOiK02880.
OMAiMHIRKAN.
OrthoDBiEOG7P02WD.

Enzyme and pathway databases

BioCyciYEAST:G3O-31946-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

EvolutionaryTraceiP05740.
NextBioi974625.
PROiP05740.

Gene expression databases

GenevestigatoriP05740.

Family and domain databases

Gene3Di3.90.470.10. 1 hit.
InterProiIPR001063. Ribosomal_L22.
IPR018260. Ribosomal_L22/L17_CS.
IPR005721. Ribosomal_L22/L17_euk/arc.
[Graphical view]
PANTHERiPTHR11593. PTHR11593. 1 hit.
PfamiPF00237. Ribosomal_L22. 1 hit.
[Graphical view]
SUPFAMiSSF54843. SSF54843. 1 hit.
TIGRFAMsiTIGR01038. L22_arch. 1 hit.
PROSITEiPS00464. RIBOSOMAL_L22. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI from Saccharomyces cerevisiae reveals 23 open reading frames including the FAS1 gene."
    Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J., Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.
    Yeast 9:1343-1348(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
  4. "Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence characterization of twenty-four proteins from cytoplasmic ribosomes."
    Otaka E., Higo K., Itoh T.
    Mol. Gen. Genet. 195:544-546(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE OF 2-41, CLEAVAGE OF INITIATOR METHIONINE.
  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.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  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 THR-70, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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 6-152, 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 nameiRL17A_YEAST
AccessioniPrimary (citable) accession number: P05740
Secondary accession number(s): D6VX21
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 2 genes for L17 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: 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.