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Protein

60S ribosomal protein L8-A

Gene

RPL8A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP17076
PRIDEiP17076

PTM databases

CarbonylDBiP17076
iPTMnetiP17076

Interactioni

Subunit structurei

Component of the large ribosomal subunit (LSU). 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, 369 interactors
DIPiDIP-5102N
IntActiP17076, 39 interactors
MINTiP17076
STRINGi4932.YHL033C

Structurei

Secondary structure

1256
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni73 – 76Combined sources4
Beta strandi77 – 80Combined sources4
Helixi84 – 94Combined sources11
Helixi102 – 116Combined sources15
Helixi136 – 142Combined sources7
Turni143 – 146Combined sources4
Beta strandi149 – 155Combined sources7
Helixi160 – 162Combined sources3
Turni163 – 165Combined sources3
Helixi166 – 173Combined sources8
Beta strandi177 – 181Combined sources5
Helixi184 – 188Combined sources5
Turni189 – 191Combined sources3
Beta strandi196 – 200Combined sources5
Helixi205 – 207Combined sources3
Helixi208 – 221Combined sources14
Turni222 – 226Combined sources5
Helixi227 – 230Combined sources4

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[»]
5MEIX-ray3.50CJ/p24-256[»]
5NDGX-ray3.70L8/l824-256[»]
5NDVX-ray3.30L8/l824-254[»]
5NDWX-ray3.70L8/l824-256[»]
5OBMX-ray3.40L8/l824-256[»]
5ON6X-ray3.10CJ/p24-256[»]
5T62electron microscopy3.30J1-256[»]
5T6Relectron microscopy4.50J1-256[»]
5TBWX-ray3.00CJ/p24-256[»]
5TGAX-ray3.30L8/l824-256[»]
5TGMX-ray3.50L824-256[»]
l824-248[»]
5Z3Gelectron microscopy3.65K1-256[»]
6C0Felectron microscopy3.70G1-256[»]
6CB1electron microscopy4.60G1-256[»]
6ELZelectron microscopy3.30G1-256[»]
6EM1electron microscopy3.60G1-256[»]
6EM3electron microscopy3.20G1-256[»]
6EM4electron microscopy4.10G1-256[»]
6EM5electron microscopy4.30G1-256[»]
6FT6electron microscopy3.90G1-256[»]
ProteinModelPortaliP17076
SMRiP17076
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17076

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000004753
HOGENOMiHOG000216644
InParanoidiP17076
KOiK02936
OMAiKNLATSM
OrthoDBiEOG092C4PDY

Family and domain databases

Gene3Di3.30.1330.210, 1 hit
InterProiView protein in InterPro
IPR029064 L30e-like
IPR001921 Ribosomal_L7A/L8
IPR038524 Ribosomal_L7A/L8_sf
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

Similar proteinsi

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: June 20, 2018
This is version 185 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

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