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 L8-A

Gene

RPL8A

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

Miscellaneous

Present with 238000 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eL8 in yeast.Curated

GO - Molecular functioni

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

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • maturation of LSU-rRNA Source: SGD
  • translation Source: GO_Central

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-31052-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 L8-A1 Publication
Alternative name(s):
L4
L4-2
L7a-1
Large ribosomal subunit protein eL8-A1 Publication
Maintenance of killer protein 7
RP6
YL5
Gene namesi
Name:RPL8A1 Publication
Synonyms:MAK7, RPL4A
Ordered Locus Names:YHL033C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHL033C.
SGDiS000001025. RPL8A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001367602 – 25660S ribosomal protein L8-AAdd BLAST255

Proteomic databases

MaxQBiP17076.
PRIDEiP17076.

PTM databases

iPTMnetiP17076.

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

BioGridi36389. 355 interactors.
DIPiDIP-5102N.
IntActiP17076. 38 interactors.
MINTiMINT-483885.

Structurei

Secondary structure

1256
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 39Combined sources5
Helixi47 – 49Combined sources3
Helixi54 – 68Combined sources15
Beta strandi69 – 71Combined sources3
Helixi73 – 76Combined sources4
Turni77 – 79Combined sources3
Helixi84 – 94Combined sources11
Helixi95 – 97Combined sources3
Helixi102 – 119Combined sources18
Beta strandi121 – 123Combined sources3
Beta strandi133 – 135Combined sources3
Helixi136 – 144Combined sources9
Beta strandi149 – 155Combined sources7
Helixi161 – 164Combined sources4
Helixi166 – 172Combined sources7
Beta strandi177 – 181Combined sources5
Helixi183 – 188Combined sources6
Turni189 – 191Combined sources3
Beta strandi196 – 201Combined sources6
Helixi205 – 221Combined sources17
Turni222 – 225Combined sources4
Helixi226 – 229Combined sources4
Helixi240 – 252Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-G102-220[»]
3J6Xelectron microscopy6.10L81-256[»]
3J6Yelectron microscopy6.10L81-256[»]
3J77electron microscopy6.20L81-256[»]
3J78electron microscopy6.30L81-256[»]
3JCTelectron microscopy3.08G1-256[»]
4U3MX-ray3.00L8/l82-256[»]
4U3NX-ray3.20L8/l82-256[»]
4U3UX-ray2.90L8/l82-256[»]
4U4NX-ray3.10L8/l82-256[»]
4U4OX-ray3.60L8/l82-256[»]
4U4QX-ray3.00L8/l82-256[»]
4U4RX-ray2.80L8/l82-256[»]
4U4UX-ray3.00L8/l82-256[»]
4U4YX-ray3.20L8/l82-256[»]
4U4ZX-ray3.10L8/l82-256[»]
4U50X-ray3.20L8/l82-256[»]
4U51X-ray3.20L8/l82-256[»]
4U52X-ray3.00L8/l82-256[»]
4U53X-ray3.30L8/l82-256[»]
4U55X-ray3.20L8/l82-256[»]
4U56X-ray3.45L8/l82-256[»]
4U6FX-ray3.10L8/l82-256[»]
4V4Belectron microscopy11.70BG102-220[»]
4V6Ielectron microscopy8.80BH1-256[»]
4V7Felectron microscopy8.70H1-256[»]
4V7RX-ray4.00BH/DH1-256[»]
4V88X-ray3.00BG/DG1-256[»]
4V8Telectron microscopy8.10G1-256[»]
4V8Yelectron microscopy4.30BG2-256[»]
4V8Zelectron microscopy6.60BG2-256[»]
4V91electron microscopy3.70G1-256[»]
5APNelectron microscopy3.91G1-256[»]
5APOelectron microscopy3.41G1-256[»]
5DATX-ray3.15L8/l82-256[»]
5DC3X-ray3.25L8/l82-256[»]
5DGEX-ray3.45L8/l82-256[»]
5DGFX-ray3.30L8/l82-256[»]
5FCIX-ray3.40L8/l82-256[»]
5FCJX-ray3.10L8/l82-256[»]
5FL8electron microscopy9.50G1-256[»]
5GAKelectron microscopy3.88K1-256[»]
5H4Pelectron microscopy3.07G1-256[»]
5I4LX-ray3.10L824-256[»]
l824-254[»]
5JCSelectron microscopy9.50G1-256[»]
5JUOelectron microscopy4.00L1-256[»]
5JUPelectron microscopy3.50L1-256[»]
5JUSelectron microscopy4.20L1-256[»]
5JUTelectron microscopy4.00L1-256[»]
5JUUelectron microscopy4.00L1-256[»]
5LYBX-ray3.25L824-256[»]
l824-248[»]
5M1Jelectron microscopy3.30G524-256[»]
5MC6electron microscopy3.80AA1-256[»]
5T62electron microscopy3.30J1-256[»]
5T6Relectron microscopy4.50J1-256[»]
5TGAX-ray3.30L8/l824-256[»]
5TGMX-ray3.50L824-256[»]
l824-248[»]
ProteinModelPortaliP17076.
SMRiP17076.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17076.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000004753.
HOGENOMiHOG000216644.
InParanoidiP17076.
KOiK02936.
OMAiRNPLTHS.
OrthoDBiEOG092C4PDY.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiView protein in InterPro
IPR029064. L30e-like.
IPR001921. Ribosomal_L7A/L8.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR018492. Ribosomal_L7Ae/L8/Nhp2.
IPR004037. Ribosomal_L7Ae_CS.
PfamiView protein in Pfam
PF01248. Ribosomal_L7Ae. 1 hit.
PRINTSiPR00881. L7ARS6FAMILY.
PR00882. RIBOSOMALL7A.
SUPFAMiSSF55315. SSF55315. 1 hit.
PROSITEiView protein in PROSITE
PS01082. RIBOSOMAL_L7AE. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P17076-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPGKKVAPA PFGAKSTKSN KTRNPLTHST PKNFGIGQAV QPKRNLSRYV
60 70 80 90 100
KWPEYVRVQR QKKILSIRLK VPPTIAQFQY TLDRNTAAET FKLFNKYRPE
110 120 130 140 150
TAAEKKERLT KEAAAVAEGK SKQDASPKPY AVKYGLNHVV ALIENKKAKL
160 170 180 190 200
VLIANDVDPI ELVVFLPALC KKMGVPYAIV KGKARLGTLV NQKTSAVAAL
210 220 230 240 250
TEVRAEDEAA LAKLVSTIDA NFADKYDEVK KHWGGGILGN KAQAKMDKRA

KNSDSA
Length:256
Mass (Da):28,125
Last modified:January 23, 2007 - v4
Checksum:iE3C8537D8683C905
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti113A → R in CAA35073 (PubMed:2183194).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17204 Genomic DNA. Translation: CAA35073.1.
X56836 Genomic DNA. Translation: CAA40166.1.
U17361 Genomic DNA. Translation: AAA64574.1.
U11583 Genomic DNA. Translation: AAB65045.1.
BK006934 Genomic DNA. Translation: DAA06652.1.
PIRiS16811. R5BY7A.
RefSeqiNP_011830.1. NM_001179113.1.

Genome annotation databases

EnsemblFungiiYHL033C; YHL033C; YHL033C.
GeneIDi856352.
KEGGisce:YHL033C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X17204 Genomic DNA. Translation: CAA35073.1.
X56836 Genomic DNA. Translation: CAA40166.1.
U17361 Genomic DNA. Translation: AAA64574.1.
U11583 Genomic DNA. Translation: AAB65045.1.
BK006934 Genomic DNA. Translation: DAA06652.1.
PIRiS16811. R5BY7A.
RefSeqiNP_011830.1. NM_001179113.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-G102-220[»]
3J6Xelectron microscopy6.10L81-256[»]
3J6Yelectron microscopy6.10L81-256[»]
3J77electron microscopy6.20L81-256[»]
3J78electron microscopy6.30L81-256[»]
3JCTelectron microscopy3.08G1-256[»]
4U3MX-ray3.00L8/l82-256[»]
4U3NX-ray3.20L8/l82-256[»]
4U3UX-ray2.90L8/l82-256[»]
4U4NX-ray3.10L8/l82-256[»]
4U4OX-ray3.60L8/l82-256[»]
4U4QX-ray3.00L8/l82-256[»]
4U4RX-ray2.80L8/l82-256[»]
4U4UX-ray3.00L8/l82-256[»]
4U4YX-ray3.20L8/l82-256[»]
4U4ZX-ray3.10L8/l82-256[»]
4U50X-ray3.20L8/l82-256[»]
4U51X-ray3.20L8/l82-256[»]
4U52X-ray3.00L8/l82-256[»]
4U53X-ray3.30L8/l82-256[»]
4U55X-ray3.20L8/l82-256[»]
4U56X-ray3.45L8/l82-256[»]
4U6FX-ray3.10L8/l82-256[»]
4V4Belectron microscopy11.70BG102-220[»]
4V6Ielectron microscopy8.80BH1-256[»]
4V7Felectron microscopy8.70H1-256[»]
4V7RX-ray4.00BH/DH1-256[»]
4V88X-ray3.00BG/DG1-256[»]
4V8Telectron microscopy8.10G1-256[»]
4V8Yelectron microscopy4.30BG2-256[»]
4V8Zelectron microscopy6.60BG2-256[»]
4V91electron microscopy3.70G1-256[»]
5APNelectron microscopy3.91G1-256[»]
5APOelectron microscopy3.41G1-256[»]
5DATX-ray3.15L8/l82-256[»]
5DC3X-ray3.25L8/l82-256[»]
5DGEX-ray3.45L8/l82-256[»]
5DGFX-ray3.30L8/l82-256[»]
5FCIX-ray3.40L8/l82-256[»]
5FCJX-ray3.10L8/l82-256[»]
5FL8electron microscopy9.50G1-256[»]
5GAKelectron microscopy3.88K1-256[»]
5H4Pelectron microscopy3.07G1-256[»]
5I4LX-ray3.10L824-256[»]
l824-254[»]
5JCSelectron microscopy9.50G1-256[»]
5JUOelectron microscopy4.00L1-256[»]
5JUPelectron microscopy3.50L1-256[»]
5JUSelectron microscopy4.20L1-256[»]
5JUTelectron microscopy4.00L1-256[»]
5JUUelectron microscopy4.00L1-256[»]
5LYBX-ray3.25L824-256[»]
l824-248[»]
5M1Jelectron microscopy3.30G524-256[»]
5MC6electron microscopy3.80AA1-256[»]
5T62electron microscopy3.30J1-256[»]
5T6Relectron microscopy4.50J1-256[»]
5TGAX-ray3.30L8/l824-256[»]
5TGMX-ray3.50L824-256[»]
l824-248[»]
ProteinModelPortaliP17076.
SMRiP17076.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36389. 355 interactors.
DIPiDIP-5102N.
IntActiP17076. 38 interactors.
MINTiMINT-483885.

PTM databases

iPTMnetiP17076.

Proteomic databases

MaxQBiP17076.
PRIDEiP17076.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHL033C; YHL033C; YHL033C.
GeneIDi856352.
KEGGisce:YHL033C.

Organism-specific databases

EuPathDBiFungiDB:YHL033C.
SGDiS000001025. RPL8A.

Phylogenomic databases

GeneTreeiENSGT00390000004753.
HOGENOMiHOG000216644.
InParanoidiP17076.
KOiK02936.
OMAiRNPLTHS.
OrthoDBiEOG092C4PDY.

Enzyme and pathway databases

BioCyciYEAST:G3O-31052-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

EvolutionaryTraceiP17076.
PROiPR:P17076.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiView protein in InterPro
IPR029064. L30e-like.
IPR001921. Ribosomal_L7A/L8.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
IPR018492. Ribosomal_L7Ae/L8/Nhp2.
IPR004037. Ribosomal_L7Ae_CS.
PfamiView protein in Pfam
PF01248. Ribosomal_L7Ae. 1 hit.
PRINTSiPR00881. L7ARS6FAMILY.
PR00882. RIBOSOMALL7A.
SUPFAMiSSF55315. SSF55315. 1 hit.
PROSITEiView protein in PROSITE
PS01082. RIBOSOMAL_L7AE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL8A_YEAST
AccessioniPrimary (citable) accession number: P17076
Secondary accession number(s): D3DKT5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: January 23, 2007
Last modified: April 12, 2017
This is version 172 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 VIII
    Yeast (Saccharomyces cerevisiae) chromosome VIII: 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.