UniProtKB - P05748 (RL15A_YEAST)
60S ribosomal protein L15-A
RPL15A
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 PublicationMiscellaneous
GO - Molecular functioni
- RNA binding Source: SGD
- structural constituent of ribosome Source: SGD
GO - Biological processi
- cytoplasmic translation Source: SGD
Keywordsi
Molecular function | Ribonucleoprotein, Ribosomal protein |
Enzyme and pathway databases
Reactomei | R-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 L15-A1 PublicationAlternative name(s): L13 Large ribosomal subunit protein eL15-A1 Publication RP15R YL10 YP18 |
Gene namesi | Ordered Locus Names:YLR029C |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000004019, RPL15A |
VEuPathDBi | FungiDB:YLR029C |
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Cytosol
- cytosol Source: Reactome
- cytosolic large ribosomal subunit Source: SGD
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed2 Publications | |||
ChainiPRO_0000127566 | 2 – 204 | 60S ribosomal protein L15-AAdd BLAST | 203 |
Proteomic databases
MaxQBi | P05748 |
PaxDbi | P05748 |
PRIDEi | P05748 |
PTM databases
iPTMneti | P05748 |
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 PublicationProtein-protein interaction databases
BioGRIDi | 31303, 279 interactors |
IntActi | P05748, 27 interactors |
MINTi | P05748 |
STRINGi | 4932.YLR029C |
Miscellaneous databases
RNActi | P05748, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P05748 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P05748 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 164 – 185 | DisorderedSequence analysisAdd BLAST | 22 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG1678, Eukaryota |
GeneTreei | ENSGT00910000144184 |
HOGENOMi | CLU_080796_0_0_1 |
InParanoidi | P05748 |
OMAi | KYMQELY |
Family and domain databases
Gene3Di | 3.40.1120.10, 1 hit |
InterProi | View protein in InterPro IPR024794, Rbsml_L15e_core_dom_sf IPR000439, Ribosomal_L15e IPR020925, Ribosomal_L15e_CS IPR012678, Ribosomal_L23/L15e_core_dom_sf |
PANTHERi | PTHR11847, PTHR11847, 1 hit |
Pfami | View protein in Pfam PF00827, Ribosomal_L15e, 1 hit |
SMARTi | View protein in SMART SM01384, Ribosomal_L15e, 1 hit |
SUPFAMi | SSF54189, SSF54189, 1 hit |
PROSITEi | View protein in PROSITE PS01194, RIBOSOMAL_L15E, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MGAYKYLEEL QRKKQSDVLR FLQRVRVWEY RQKNVIHRAA RPTRPDKARR
60 70 80 90 100
LGYKAKQGFV IYRVRVRRGN RKRPVPKGAT YGKPTNQGVN ELKYQRSLRA
110 120 130 140 150
TAEERVGRRA ANLRVLNSYW VNQDSTYKYF EVILVDPQHK AIRRDARYNW
160 170 180 190 200
ICDPVHKHRE ARGLTATGKK SRGINKGHKF NNTKAGRRKT WKRQNTLSLW
RYRK
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 28 | W → G AA sequence (PubMed:6814480).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D14675 Genomic DNA Translation: BAA03506.1 Z73201 Genomic DNA Translation: CAA97553.1 BK006945 Genomic DNA Translation: DAA09347.1 |
PIRi | S48502 |
RefSeqi | NP_013129.1, NM_001181916.1 |
Genome annotation databases
EnsemblFungii | YLR029C_mRNA; YLR029C; YLR029C |
GeneIDi | 850716 |
KEGGi | sce:YLR029C |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D14675 Genomic DNA Translation: BAA03506.1 Z73201 Genomic DNA Translation: CAA97553.1 BK006945 Genomic DNA Translation: DAA09347.1 |
PIRi | S48502 |
RefSeqi | NP_013129.1, NM_001181916.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3J6X | electron microscopy | 6.10 | 55 | 1-204 | [»] | |
3J6Y | electron microscopy | 6.10 | 55 | 1-204 | [»] | |
3J77 | electron microscopy | 6.20 | 65 | 1-204 | [»] | |
3J78 | electron microscopy | 6.30 | 65 | 1-204 | [»] | |
3JCT | electron microscopy | 3.08 | N | 1-204 | [»] | |
4U3M | X-ray | 3.00 | M5/m5 | 2-204 | [»] | |
4U3N | X-ray | 3.20 | M5/m5 | 2-204 | [»] | |
4U3U | X-ray | 2.90 | M5/m5 | 2-204 | [»] | |
4U4N | X-ray | 3.10 | M5/m5 | 2-204 | [»] | |
4U4O | X-ray | 3.60 | M5/m5 | 2-204 | [»] | |
4U4Q | X-ray | 3.00 | M5/m5 | 2-204 | [»] | |
4U4R | X-ray | 2.80 | M5/m5 | 2-204 | [»] | |
4U4U | X-ray | 3.00 | M5/m5 | 2-204 | [»] | |
4U4Y | X-ray | 3.20 | M5/m5 | 2-204 | [»] | |
4U4Z | X-ray | 3.10 | M5/m5 | 2-204 | [»] | |
4U50 | X-ray | 3.20 | M5/m5 | 2-204 | [»] | |
4U51 | X-ray | 3.20 | M5/m5 | 2-204 | [»] | |
4U52 | X-ray | 3.00 | M5/m5 | 2-204 | [»] | |
4U53 | X-ray | 3.30 | M5/m5 | 2-204 | [»] | |
4U55 | X-ray | 3.20 | M5/m5 | 2-204 | [»] | |
4U56 | X-ray | 3.45 | M5/m5 | 2-204 | [»] | |
4U6F | X-ray | 3.10 | M5/m5 | 2-204 | [»] | |
4V4B | electron microscopy | 11.70 | BL | 2-204 | [»] | |
4V6I | electron microscopy | 8.80 | BP | 1-204 | [»] | |
4V7F | electron microscopy | 8.70 | O | 1-204 | [»] | |
4V7R | X-ray | 4.00 | BO/DO | 1-204 | [»] | |
4V88 | X-ray | 3.00 | BN/DN | 1-204 | [»] | |
4V8T | electron microscopy | 8.10 | N | 1-204 | [»] | |
4V8Y | electron microscopy | 4.30 | BN | 2-204 | [»] | |
4V8Z | electron microscopy | 6.60 | BN | 2-204 | [»] | |
4V91 | electron microscopy | 3.70 | N | 1-204 | [»] | |
5APN | electron microscopy | 3.91 | N | 1-204 | [»] | |
5APO | electron microscopy | 3.41 | N | 1-204 | [»] | |
5DAT | X-ray | 3.15 | M5 | 2-204 | [»] | |
m5 | 2-204 | [»] | ||||
5DC3 | X-ray | 3.25 | M5/m5 | 2-204 | [»] | |
5DGE | X-ray | 3.45 | M5/m5 | 2-204 | [»] | |
5DGF | X-ray | 3.30 | M5/m5 | 2-204 | [»] | |
5DGV | X-ray | 3.10 | M5/m5 | 2-204 | [»] | |
5FCI | X-ray | 3.40 | M5/m5 | 2-204 | [»] | |
5FCJ | X-ray | 3.10 | M5/m5 | 2-204 | [»] | |
5FL8 | electron microscopy | 9.50 | N | 1-204 | [»] | |
5GAK | electron microscopy | 3.88 | P | 1-204 | [»] | |
5H4P | electron microscopy | 3.07 | N | 1-204 | [»] | |
5I4L | X-ray | 3.10 | M5/m5 | 2-204 | [»] | |
5JCS | electron microscopy | 9.50 | N | 1-204 | [»] | |
5JUO | electron microscopy | 4.00 | S | 1-204 | [»] | |
5JUP | electron microscopy | 3.50 | S | 1-204 | [»] | |
5JUS | electron microscopy | 4.20 | S | 1-204 | [»] | |
5JUT | electron microscopy | 4.00 | S | 1-204 | [»] | |
5JUU | electron microscopy | 4.00 | S | 1-204 | [»] | |
5LYB | X-ray | 3.25 | M5/m5 | 2-204 | [»] | |
5M1J | electron microscopy | 3.30 | N5 | 2-204 | [»] | |
5MC6 | electron microscopy | 3.80 | AQ | 1-204 | [»] | |
5MEI | X-ray | 3.50 | CP/v | 2-204 | [»] | |
5NDG | X-ray | 3.70 | M5/m5 | 2-204 | [»] | |
5NDV | X-ray | 3.30 | M5/m5 | 2-204 | [»] | |
5NDW | X-ray | 3.70 | M5/m5 | 2-204 | [»] | |
5OBM | X-ray | 3.40 | M5/m5 | 2-204 | [»] | |
5ON6 | X-ray | 3.10 | CP/v | 2-204 | [»] | |
5T62 | electron microscopy | 3.30 | a | 1-204 | [»] | |
5T6R | electron microscopy | 4.50 | a | 1-204 | [»] | |
5TBW | X-ray | 3.00 | CP/v | 2-204 | [»] | |
5TGA | X-ray | 3.30 | M5/m5 | 2-204 | [»] | |
5TGM | X-ray | 3.50 | M5/m5 | 2-204 | [»] | |
5Z3G | electron microscopy | 3.65 | R | 1-204 | [»] | |
6C0F | electron microscopy | 3.70 | N | 1-204 | [»] | |
6CB1 | electron microscopy | 4.60 | N | 1-204 | [»] | |
6ELZ | electron microscopy | 3.30 | N | 1-204 | [»] | |
6EM1 | electron microscopy | 3.60 | N | 1-204 | [»] | |
6EM3 | electron microscopy | 3.20 | N | 1-204 | [»] | |
6EM4 | electron microscopy | 4.10 | N | 1-204 | [»] | |
6EM5 | electron microscopy | 4.30 | N | 1-204 | [»] | |
6FT6 | electron microscopy | 3.90 | N | 1-204 | [»] | |
6GQ1 | electron microscopy | 4.40 | N | 2-204 | [»] | |
6GQB | electron microscopy | 3.90 | N | 2-204 | [»] | |
6GQV | electron microscopy | 4.00 | N | 2-204 | [»] | |
6HD7 | electron microscopy | 3.40 | P | 1-204 | [»] | |
6HHQ | X-ray | 3.10 | CP/v | 1-204 | [»] | |
6I7O | electron microscopy | 5.30 | AQ/XQ | 2-204 | [»] | |
6M62 | electron microscopy | 3.20 | N | 1-204 | [»] | |
6N8J | electron microscopy | 3.50 | N | 1-204 | [»] | |
6N8K | electron microscopy | 3.60 | N | 1-204 | [»] | |
6N8L | electron microscopy | 3.60 | N | 1-204 | [»] | |
6N8M | electron microscopy | 3.50 | a | 1-204 | [»] | |
6N8N | electron microscopy | 3.80 | a | 1-204 | [»] | |
6N8O | electron microscopy | 3.50 | a | 1-204 | [»] | |
6OIG | electron microscopy | 3.80 | N | 2-204 | [»] | |
6Q8Y | electron microscopy | 3.10 | AQ | 2-204 | [»] | |
6QIK | electron microscopy | 3.10 | O | 1-204 | [»] | |
6QT0 | electron microscopy | 3.40 | O | 1-204 | [»] | |
6QTZ | electron microscopy | 3.50 | O | 1-204 | [»] | |
6R84 | electron microscopy | 3.60 | p | 2-204 | [»] | |
6R86 | electron microscopy | 3.40 | p | 2-204 | [»] | |
6R87 | electron microscopy | 3.40 | p | 2-204 | [»] | |
6RI5 | electron microscopy | 3.30 | O | 1-204 | [»] | |
6RZZ | electron microscopy | 3.20 | O | 1-204 | [»] | |
6S05 | electron microscopy | 3.90 | O | 1-204 | [»] | |
6S47 | electron microscopy | 3.28 | AP | 2-204 | [»] | |
6SNT | electron microscopy | 2.80 | t | 1-204 | [»] | |
6SV4 | electron microscopy | 3.30 | AQ/XQ/zQ | 1-204 | [»] | |
6T4Q | electron microscopy | 2.60 | LN | 2-204 | [»] | |
6T7I | electron microscopy | 3.20 | LN | 1-204 | [»] | |
6T7T | electron microscopy | 3.10 | LN | 1-204 | [»] | |
6T83 | electron microscopy | 4.00 | Ny/Pa | 1-204 | [»] | |
6TB3 | electron microscopy | 2.80 | AQ | 2-204 | [»] | |
6TNU | electron microscopy | 3.10 | AQ | 2-204 | [»] | |
6WOO | electron microscopy | 2.90 | N | 2-203 | [»] | |
6XIQ | electron microscopy | 4.20 | N | 1-204 | [»] | |
6XIR | electron microscopy | 3.20 | N | 1-204 | [»] | |
6YLG | electron microscopy | 3.00 | N | 1-204 | [»] | |
6YLH | electron microscopy | 3.10 | N | 1-204 | [»] | |
6YLX | electron microscopy | 3.90 | N | 1-204 | [»] | |
6YLY | electron microscopy | 3.80 | N | 1-204 | [»] | |
6Z6J | electron microscopy | 3.40 | LN | 1-204 | [»] | |
6Z6K | electron microscopy | 3.40 | LN | 1-204 | [»] | |
7AZY | electron microscopy | 2.88 | R | 1-204 | [»] | |
7B7D | electron microscopy | 3.30 | LP | 2-204 | [»] | |
7BT6 | electron microscopy | 3.12 | N | 1-204 | [»] | |
7BTB | electron microscopy | 3.22 | N | 1-204 | [»] | |
7NRC | electron microscopy | 3.90 | LP | 2-204 | [»] | |
7NRD | electron microscopy | 4.36 | LP | 2-204 | [»] | |
SMRi | P05748 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 31303, 279 interactors |
IntActi | P05748, 27 interactors |
MINTi | P05748 |
STRINGi | 4932.YLR029C |
PTM databases
iPTMneti | P05748 |
Proteomic databases
MaxQBi | P05748 |
PaxDbi | P05748 |
PRIDEi | P05748 |
Genome annotation databases
EnsemblFungii | YLR029C_mRNA; YLR029C; YLR029C |
GeneIDi | 850716 |
KEGGi | sce:YLR029C |
Organism-specific databases
SGDi | S000004019, RPL15A |
VEuPathDBi | FungiDB:YLR029C |
Phylogenomic databases
eggNOGi | KOG1678, Eukaryota |
GeneTreei | ENSGT00910000144184 |
HOGENOMi | CLU_080796_0_0_1 |
InParanoidi | P05748 |
OMAi | KYMQELY |
Enzyme and pathway databases
Reactomei | R-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
EvolutionaryTracei | P05748 |
PROi | PR:P05748 |
RNActi | P05748, protein |
Family and domain databases
Gene3Di | 3.40.1120.10, 1 hit |
InterProi | View protein in InterPro IPR024794, Rbsml_L15e_core_dom_sf IPR000439, Ribosomal_L15e IPR020925, Ribosomal_L15e_CS IPR012678, Ribosomal_L23/L15e_core_dom_sf |
PANTHERi | PTHR11847, PTHR11847, 1 hit |
Pfami | View protein in Pfam PF00827, Ribosomal_L15e, 1 hit |
SMARTi | View protein in SMART SM01384, Ribosomal_L15e, 1 hit |
SUPFAMi | SSF54189, SSF54189, 1 hit |
PROSITEi | View protein in PROSITE PS01194, RIBOSOMAL_L15E, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | RL15A_YEAST | |
Accessioni | P05748Primary (citable) accession number: P05748 Secondary accession number(s): D6VY31 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1988 |
Last sequence update: | January 23, 2007 | |
Last modified: | February 23, 2022 | |
This is version 189 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome XII
Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names - Ribosomal proteins
Ribosomal proteins families and list of entries - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families