UniProtKB - P0ADY3 (RL14_ECOLI)
Protein
50S ribosomal protein L14
Gene
rplN
Organism
Escherichia coli (strain K12)
Status
Functioni
This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits (PubMed:12809609). Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8 (PubMed:16272117).3 Publications
Can also interact with RsfS, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation.1 Publication
GO - Molecular functioni
- large ribosomal subunit rRNA binding Source: EcoCyc
- structural constituent of ribosome Source: GO_Central
GO - Biological processi
- translation Source: UniProtKB-UniRule
Keywordsi
Molecular function | Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10875-MONOMER MetaCyc:EG10875-MONOMER |
Protein family/group databases
MoonProti | P0ADY3 |
Names & Taxonomyi
Protein namesi | Recommended name: 50S ribosomal protein L14UniRule annotationAlternative name(s): Large ribosomal subunit protein uL141 Publication |
Gene namesi | Name:rplNUniRule annotation Ordered Locus Names:b3310, JW3272 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
GO - Cellular componenti
- cytosol Source: EcoCyc
- cytosolic large ribosomal subunit Source: EcoCyc
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 97 | T → A: Reduced RsfS binding. 1 Publication | 1 | |
Mutagenesisi | 98 | R → A: Reduced RsfS binding. 1 Publication | 1 | |
Mutagenesisi | 114 | K → A: Reduced RsfS binding. 1 Publication | 1 | |
Mutagenesisi | 117 | S → A: No change in RsfS binding. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000128540 | 1 – 123 | 50S ribosomal protein L14Add BLAST | 123 |
Proteomic databases
jPOSTi | P0ADY3 |
PaxDbi | P0ADY3 |
PRIDEi | P0ADY3 |
Interactioni
Subunit structurei
Part of the 50S ribosomal subunit (PubMed:352727, PubMed:7556101, PubMed:2665813, PubMed:10094780, PubMed:10756104, PubMed:12809609, PubMed:16272117, PubMed:25310980, PubMed:24844575, PubMed:27934701, PubMed:27906160, PubMed:27906161). Contacts L19 (PubMed:2665813, PubMed:16272117). Forms two bridges to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Can also contact RsfS, which then probably inhibits ribosomal subunit association.
12 PublicationsProtein-protein interaction databases
BioGRIDi | 852121, 1 interactor |
ComplexPortali | CPX-3807, 50S large ribosomal subunit |
DIPi | DIP-35798N |
IntActi | P0ADY3, 53 interactors |
STRINGi | 511145.b3310 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P0ADY3 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P0ADY3 |
Family & Domainsi
Sequence similaritiesi
Belongs to the universal ribosomal protein uL14 family.UniRule annotation
Phylogenomic databases
eggNOGi | COG0093, Bacteria |
HOGENOMi | CLU_095071_2_1_6 |
InParanoidi | P0ADY3 |
PhylomeDBi | P0ADY3 |
Family and domain databases
Gene3Di | 2.40.150.20, 1 hit |
HAMAPi | MF_01367, Ribosomal_L14, 1 hit |
InterProi | View protein in InterPro IPR036853, Ribosomal_L14_sf IPR000218, Ribosomal_L14P IPR005745, Ribosomal_L14P_bac-type IPR019972, Ribosomal_L14P_CS |
PANTHERi | PTHR11761, PTHR11761, 1 hit |
Pfami | View protein in Pfam PF00238, Ribosomal_L14, 1 hit |
SMARTi | View protein in SMART SM01374, Ribosomal_L14, 1 hit |
SUPFAMi | SSF50193, SSF50193, 1 hit |
TIGRFAMsi | TIGR01067, rplN_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00049, RIBOSOMAL_L14, 1 hit |
i Sequence
Sequence statusi: Complete.
P0ADY3-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MIQEQTMLNV ADNSGARRVM CIKVLGGSHR RYAGVGDIIK ITIKEAIPRG
60 70 80 90 100
KVKKGDVLKA VVVRTKKGVR RPDGSVIRFD GNACVLLNNN SEQPIGTRIF
110 120
GPVTRELRSE KFMKIISLAP EVL
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 63 | Missing AA sequence (PubMed:352727).Curated | 1 | |
Sequence conflicti | 84 | C → S AA sequence (PubMed:352727).Curated | 1 | |
Sequence conflicti | 90 – 91 | NS → TD AA sequence (PubMed:352727).Curated | 2 | |
Sequence conflicti | 97 | Missing AA sequence (PubMed:352727).Curated | 1 | |
Sequence conflicti | 115 | I → L AA sequence (PubMed:352727).Curated | 1 | |
Sequence conflicti | 123 | Missing AA sequence (PubMed:352727).Curated | 1 |
Mass spectrometryi
Molecular mass is 13540.2 Da. Determined by MALDI. 1 Publication
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X01563 Genomic DNA Translation: CAA25715.1 U18997 Genomic DNA Translation: AAA58107.1 U00096 Genomic DNA Translation: AAC76335.1 AP009048 Genomic DNA Translation: BAE77981.1 V00357 Genomic DNA Translation: CAA23653.1 |
PIRi | A65124, R5EC14 |
RefSeqi | NP_417769.1, NC_000913.3 WP_000613955.1, NZ_STEB01000038.1 |
Genome annotation databases
EnsemblBacteriai | AAC76335; AAC76335; b3310 BAE77981; BAE77981; BAE77981 |
GeneIDi | 52075115 947809 |
KEGGi | ecj:JW3272 eco:b3310 |
PATRICi | fig|1411691.4.peg.3421 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X01563 Genomic DNA Translation: CAA25715.1 U18997 Genomic DNA Translation: AAA58107.1 U00096 Genomic DNA Translation: AAC76335.1 AP009048 Genomic DNA Translation: BAE77981.1 V00357 Genomic DNA Translation: CAA23653.1 |
PIRi | A65124, R5EC14 |
RefSeqi | NP_417769.1, NC_000913.3 WP_000613955.1, NZ_STEB01000038.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1ML5 | electron microscopy | 14.00 | n | 1-122 | [»] | |
2J28 | electron microscopy | 8.00 | K | 2-122 | [»] | |
2RDO | electron microscopy | 9.10 | K | 1-123 | [»] | |
3BBX | electron microscopy | 10.00 | K | 1-123 | [»] | |
3IY9 | electron microscopy | 14.10 | K | 2-122 | [»] | |
3IZZ | electron microscopy | 10.80 | G | 2-122 | [»] | |
3J5L | electron microscopy | 6.60 | K | 1-122 | [»] | |
3J7Z | electron microscopy | 3.90 | K | 1-123 | [»] | |
3J8G | electron microscopy | 5.00 | K | 1-123 | [»] | |
3J9Y | electron microscopy | 3.90 | K | 1-123 | [»] | |
3J9Z | electron microscopy | 3.60 | LG | 1-123 | [»] | |
3JA1 | electron microscopy | 3.60 | LM | 1-123 | [»] | |
3JBU | electron microscopy | 3.64 | k | 1-123 | [»] | |
3JBV | electron microscopy | 3.32 | k | 1-123 | [»] | |
3JCD | electron microscopy | 3.70 | K | 1-123 | [»] | |
3JCE | electron microscopy | 3.20 | K | 1-123 | [»] | |
3JCJ | electron microscopy | 3.70 | J | 1-123 | [»] | |
3JCN | electron microscopy | 4.60 | K | 1-123 | [»] | |
487D | electron microscopy | 7.50 | M | 1-122 | [»] | |
4CSU | electron microscopy | 5.50 | K | 1-123 | [»] | |
4U1U | X-ray | 2.95 | BK/DK | 1-122 | [»] | |
4U1V | X-ray | 3.00 | BK/DK | 1-122 | [»] | |
4U20 | X-ray | 2.90 | BK/DK | 1-122 | [»] | |
4U24 | X-ray | 2.90 | BK/DK | 1-122 | [»] | |
4U25 | X-ray | 2.90 | BK/DK | 1-122 | [»] | |
4U26 | X-ray | 2.80 | BK/DK | 1-122 | [»] | |
4U27 | X-ray | 2.80 | BK/DK | 1-122 | [»] | |
4UY8 | electron microscopy | 3.80 | K | 1-122 | [»] | |
4V47 | electron microscopy | 12.30 | AI | 1-123 | [»] | |
4V48 | electron microscopy | 11.50 | AI | 1-123 | [»] | |
4V4H | X-ray | 3.46 | BK/DK | 1-123 | [»] | |
4V4Q | X-ray | 3.46 | BK/DK | 1-123 | [»] | |
4V4V | electron microscopy | 15.00 | BI | 2-123 | [»] | |
4V4W | electron microscopy | 15.00 | BI | 2-123 | [»] | |
4V50 | X-ray | 3.22 | BK/DK | 1-123 | [»] | |
4V52 | X-ray | 3.21 | BK/DK | 1-123 | [»] | |
4V53 | X-ray | 3.54 | BK/DK | 1-123 | [»] | |
4V54 | X-ray | 3.30 | BK/DK | 1-123 | [»] | |
4V55 | X-ray | 4.00 | BK/DK | 1-123 | [»] | |
4V56 | X-ray | 3.93 | BK/DK | 1-123 | [»] | |
4V57 | X-ray | 3.50 | BK/DK | 1-123 | [»] | |
4V5B | X-ray | 3.74 | AK/CK | 1-123 | [»] | |
4V5H | electron microscopy | 5.80 | BK | 1-121 | [»] | |
4V5Y | X-ray | 4.45 | BK/DK | 1-123 | [»] | |
4V64 | X-ray | 3.50 | BK/DK | 1-123 | [»] | |
4V65 | electron microscopy | 9.00 | BD | 1-123 | [»] | |
4V66 | electron microscopy | 9.00 | BD | 1-123 | [»] | |
4V69 | electron microscopy | 6.70 | BK | 2-122 | [»] | |
4V6C | X-ray | 3.19 | BK/DK | 1-123 | [»] | |
4V6D | X-ray | 3.81 | BK/DK | 1-123 | [»] | |
4V6E | X-ray | 3.71 | BK/DK | 1-123 | [»] | |
4V6K | electron microscopy | 8.25 | AL | 1-123 | [»] | |
4V6L | electron microscopy | 13.20 | BL | 1-123 | [»] | |
4V6M | electron microscopy | 7.10 | BK | 1-123 | [»] | |
4V6N | electron microscopy | 12.10 | AM | 1-123 | [»] | |
4V6O | electron microscopy | 14.70 | BM | 1-123 | [»] | |
4V6P | electron microscopy | 13.50 | BM | 1-123 | [»] | |
4V6Q | electron microscopy | 11.50 | BM | 1-123 | [»] | |
4V6R | electron microscopy | 11.50 | BM | 1-123 | [»] | |
4V6S | electron microscopy | 13.10 | AM | 1-123 | [»] | |
4V6T | electron microscopy | 8.30 | BK | 1-122 | [»] | |
4V6V | electron microscopy | 9.80 | BO | 1-123 | [»] | |
4V6Y | electron microscopy | 12.00 | BK | 1-122 | [»] | |
4V6Z | electron microscopy | 12.00 | BK | 1-122 | [»] | |
4V70 | electron microscopy | 17.00 | BK | 1-122 | [»] | |
4V71 | electron microscopy | 20.00 | BK | 1-122 | [»] | |
4V72 | electron microscopy | 13.00 | BK | 1-122 | [»] | |
4V73 | electron microscopy | 15.00 | BK | 1-122 | [»] | |
4V74 | electron microscopy | 17.00 | BK | 1-122 | [»] | |
4V75 | electron microscopy | 12.00 | BK | 1-122 | [»] | |
4V76 | electron microscopy | 17.00 | BK | 1-122 | [»] | |
4V77 | electron microscopy | 17.00 | BK | 1-122 | [»] | |
4V78 | electron microscopy | 20.00 | BK | 1-122 | [»] | |
4V79 | electron microscopy | 15.00 | BK | 1-122 | [»] | |
4V7A | electron microscopy | 9.00 | BK | 1-122 | [»] | |
4V7B | electron microscopy | 6.80 | BK | 1-123 | [»] | |
4V7C | electron microscopy | 7.60 | BM | 1-123 | [»] | |
4V7D | electron microscopy | 7.60 | AN | 1-123 | [»] | |
4V7I | electron microscopy | 9.60 | AK | 1-123 | [»] | |
4V7S | X-ray | 3.25 | BK/DK | 1-122 | [»] | |
4V7T | X-ray | 3.19 | BK/DK | 1-122 | [»] | |
4V7U | X-ray | 3.10 | BK/DK | 1-122 | [»] | |
4V7V | X-ray | 3.29 | BK/DK | 1-122 | [»] | |
4V85 | X-ray | 3.20 | BO | 1-123 | [»] | |
4V89 | X-ray | 3.70 | BO | 1-123 | [»] | |
4V9C | X-ray | 3.30 | BK/DK | 1-123 | [»] | |
4V9D | X-ray | 3.00 | CK/DK | 1-122 | [»] | |
4V9O | X-ray | 2.90 | AK/CK/EK/GK | 1-123 | [»] | |
4V9P | X-ray | 2.90 | AK/CK/EK/GK | 1-123 | [»] | |
4WF1 | X-ray | 3.09 | BK/DK | 1-122 | [»] | |
4WOI | X-ray | 3.00 | BK/CK | 1-123 | [»] | |
4WWW | X-ray | 3.10 | RK/YK | 1-122 | [»] | |
4YBB | X-ray | 2.10 | CL/DL | 1-123 | [»] | |
5ADY | electron microscopy | 4.50 | K | 1-123 | [»] | |
5AFI | electron microscopy | 2.90 | K | 1-123 | [»] | |
5AKA | electron microscopy | 5.70 | K | 1-123 | [»] | |
5GAD | electron microscopy | 3.70 | L | 1-123 | [»] | |
5GAE | electron microscopy | 3.33 | L | 1-123 | [»] | |
5GAF | electron microscopy | 4.30 | L | 1-123 | [»] | |
5GAG | electron microscopy | 3.80 | L | 1-123 | [»] | |
5GAH | electron microscopy | 3.80 | L | 1-123 | [»] | |
5H5U | electron microscopy | 3.00 | L | 1-123 | [»] | |
5IQR | electron microscopy | 3.00 | K | 1-123 | [»] | |
5IT8 | X-ray | 3.12 | CL/DL | 1-123 | [»] | |
5J5B | X-ray | 2.80 | CL/DL | 1-123 | [»] | |
5J7L | X-ray | 3.00 | CL/DL | 1-123 | [»] | |
5J88 | X-ray | 3.32 | CL/DL | 1-123 | [»] | |
5J8A | X-ray | 3.10 | CL/DL | 1-123 | [»] | |
5J91 | X-ray | 2.96 | CL/DL | 1-123 | [»] | |
5JC9 | X-ray | 3.03 | CL/DL | 1-123 | [»] | |
5JTE | electron microscopy | 3.60 | BK | 1-123 | [»] | |
5JU8 | electron microscopy | 3.60 | BK | 1-123 | [»] | |
5KCR | electron microscopy | 3.60 | 1O | 1-123 | [»] | |
5KCS | electron microscopy | 3.90 | 1O | 1-123 | [»] | |
5KPS | electron microscopy | 3.90 | K | 1-123 | [»] | |
5KPV | electron microscopy | 4.10 | J | 1-123 | [»] | |
5KPW | electron microscopy | 3.90 | J | 1-123 | [»] | |
5KPX | electron microscopy | 3.90 | J | 1-123 | [»] | |
5L3P | electron microscopy | 3.70 | O | 1-123 | [»] | |
5LZA | electron microscopy | 3.60 | K | 1-122 | [»] | |
5LZB | electron microscopy | 5.30 | K | 1-122 | [»] | |
5LZC | electron microscopy | 4.80 | K | 1-122 | [»] | |
5LZD | electron microscopy | 3.40 | K | 1-122 | [»] | |
5LZE | electron microscopy | 3.50 | K | 1-122 | [»] | |
5LZF | electron microscopy | 4.60 | K | 1-122 | [»] | |
5MDV | electron microscopy | 2.97 | K | 1-123 | [»] | |
5MDW | electron microscopy | 3.06 | K | 1-123 | [»] | |
5MDY | electron microscopy | 3.35 | K | 1-123 | [»] | |
5MDZ | electron microscopy | 3.10 | K | 1-123 | [»] | |
5MGP | electron microscopy | 3.10 | K | 1-122 | [»] | |
5NCO | electron microscopy | 4.80 | L | 1-123 | [»] | |
5NP6 | electron microscopy | 3.60 | i | 1-122 | [»] | |
5NWY | electron microscopy | 2.93 | X | 1-123 | [»] | |
5O2R | electron microscopy | 3.40 | K | 1-122 | [»] | |
5U4I | electron microscopy | 3.50 | L | 1-123 | [»] | |
5U9F | electron microscopy | 3.20 | 13 | 1-123 | [»] | |
5U9G | electron microscopy | 3.20 | 13 | 1-123 | [»] | |
5UYK | electron microscopy | 3.90 | 13 | 1-122 | [»] | |
5UYL | electron microscopy | 3.60 | 13 | 1-122 | [»] | |
5UYM | electron microscopy | 3.20 | 13 | 1-122 | [»] | |
5UYN | electron microscopy | 4.00 | 13 | 1-122 | [»] | |
5UYP | electron microscopy | 3.90 | 13 | 1-122 | [»] | |
5UYQ | electron microscopy | 3.80 | 13 | 1-122 | [»] | |
5WDT | electron microscopy | 3.00 | K | 1-122 | [»] | |
5WE4 | electron microscopy | 3.10 | K | 1-122 | [»] | |
5WFK | electron microscopy | 3.40 | K | 1-122 | [»] | |
6BU8 | electron microscopy | 3.50 | 13 | 1-122 | [»] | |
6BY1 | X-ray | 3.94 | CK/DK | 1-122 | [»] | |
6C4I | electron microscopy | 3.24 | L | 1-123 | [»] | |
6ENF | electron microscopy | 3.20 | K | 1-122 | [»] | |
6ENJ | electron microscopy | 3.70 | K | 1-122 | [»] | |
6ENU | electron microscopy | 3.10 | K | 1-122 | [»] | |
6GBZ | electron microscopy | 3.80 | K | 1-122 | [»] | |
6GC0 | electron microscopy | 3.80 | K | 1-122 | [»] | |
6GC4 | electron microscopy | 4.30 | K | 1-122 | [»] | |
6GC6 | electron microscopy | 4.30 | K | 1-122 | [»] | |
6GC7 | electron microscopy | 4.30 | K | 1-122 | [»] | |
6GC8 | electron microscopy | 3.80 | K | 1-122 | [»] | |
6GWT | electron microscopy | 3.80 | K | 1-122 | [»] | |
6GXM | electron microscopy | 3.80 | K | 1-122 | [»] | |
6GXN | electron microscopy | 3.90 | K | 1-122 | [»] | |
6GXO | electron microscopy | 3.90 | K | 1-122 | [»] | |
6GXP | electron microscopy | 4.40 | K | 1-122 | [»] | |
6H4N | electron microscopy | 3.00 | K | 1-122 | [»] | |
6H58 | electron microscopy | 7.90 | K/KK | 1-122 | [»] | |
6HRM | electron microscopy | 2.96 | K | 1-123 | [»] | |
6I0Y | electron microscopy | 3.20 | K | 1-122 | [»] | |
6I7V | X-ray | 2.90 | CL/DL | 1-123 | [»] | |
6O9J | electron microscopy | 3.90 | K | 2-122 | [»] | |
6O9K | electron microscopy | 4.00 | K | 1-122 | [»] | |
6OFX | electron microscopy | 3.30 | k | 1-122 | [»] | |
6OG7 | electron microscopy | 3.30 | k | 1-122 | [»] | |
6ORE | electron microscopy | 2.90 | K | 1-123 | [»] | |
6ORL | electron microscopy | 3.50 | K | 1-123 | [»] | |
6OST | electron microscopy | 4.20 | K | 1-123 | [»] | |
6OT3 | electron microscopy | 3.90 | K | 1-123 | [»] | |
6OUO | electron microscopy | 3.70 | K | 1-123 | [»] | |
6Q97 | electron microscopy | 3.90 | K | 1-123 | [»] | |
6Q98 | electron microscopy | 4.30 | K | 1-123 | [»] | |
6Q9A | electron microscopy | 3.70 | K | 1-123 | [»] | |
6QDW | electron microscopy | 2.83 | k | 1-123 | [»] | |
6QUL | electron microscopy | 3.00 | L | 1-123 | [»] | |
6S0K | electron microscopy | 3.10 | L | 1-123 | [»] | |
6SZS | electron microscopy | 3.06 | K | 1-123 | [»] | |
6TBV | electron microscopy | 2.70 | L141 | 1-123 | [»] | |
6TC3 | electron microscopy | 2.70 | L141 | 1-123 | [»] | |
6VWL | electron microscopy | 3.10 | I | 1-123 | [»] | |
6VWM | electron microscopy | 3.40 | I | 1-123 | [»] | |
6VWN | electron microscopy | 3.40 | I | 1-123 | [»] | |
6WD6 | electron microscopy | 3.70 | k | 1-122 | [»] | |
6WDB | electron microscopy | 4.00 | k | 1-122 | [»] | |
6WDC | electron microscopy | 4.20 | k | 1-122 | [»] | |
6WDD | electron microscopy | 3.20 | k | 1-122 | [»] | |
6WDE | electron microscopy | 3.00 | k | 1-122 | [»] | |
6WDF | electron microscopy | 3.30 | k | 1-122 | [»] | |
6WDG | electron microscopy | 3.30 | k | 1-122 | [»] | |
6WDH | electron microscopy | 4.30 | k | 1-122 | [»] | |
6WDI | electron microscopy | 4.00 | k | 1-122 | [»] | |
6WDJ | electron microscopy | 3.70 | k | 1-122 | [»] | |
6WDK | electron microscopy | 3.60 | k | 1-122 | [»] | |
6WDL | electron microscopy | 3.70 | k | 1-122 | [»] | |
6WDM | electron microscopy | 3.60 | k | 1-122 | [»] | |
6WNT | electron microscopy | 3.10 | k | 1-122 | [»] | |
6WNV | electron microscopy | 3.50 | k | 1-122 | [»] | |
6WNW | electron microscopy | 3.20 | k | 1-122 | [»] | |
6XZ7 | electron microscopy | 2.10 | K | 1-123 | [»] | |
6Y69 | electron microscopy | 2.86 | K | 1-122 | [»] | |
6YSR | electron microscopy | 3.10 | K | 1-123 | [»] | |
6YSS | electron microscopy | 2.60 | K | 1-123 | [»] | |
6YST | electron microscopy | 3.20 | K | 1-123 | [»] | |
6YSU | electron microscopy | 3.70 | K | 1-123 | [»] | |
7BV8 | electron microscopy | 3.14 | L | 1-123 | [»] | |
SMRi | P0ADY3 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 852121, 1 interactor |
ComplexPortali | CPX-3807, 50S large ribosomal subunit |
DIPi | DIP-35798N |
IntActi | P0ADY3, 53 interactors |
STRINGi | 511145.b3310 |
Protein family/group databases
MoonProti | P0ADY3 |
Proteomic databases
jPOSTi | P0ADY3 |
PaxDbi | P0ADY3 |
PRIDEi | P0ADY3 |
Genome annotation databases
EnsemblBacteriai | AAC76335; AAC76335; b3310 BAE77981; BAE77981; BAE77981 |
GeneIDi | 52075115 947809 |
KEGGi | ecj:JW3272 eco:b3310 |
PATRICi | fig|1411691.4.peg.3421 |
Organism-specific databases
EchoBASEi | EB0868 |
Phylogenomic databases
eggNOGi | COG0093, Bacteria |
HOGENOMi | CLU_095071_2_1_6 |
InParanoidi | P0ADY3 |
PhylomeDBi | P0ADY3 |
Enzyme and pathway databases
BioCyci | EcoCyc:EG10875-MONOMER MetaCyc:EG10875-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P0ADY3 |
PROi | PR:P0ADY3 |
Family and domain databases
Gene3Di | 2.40.150.20, 1 hit |
HAMAPi | MF_01367, Ribosomal_L14, 1 hit |
InterProi | View protein in InterPro IPR036853, Ribosomal_L14_sf IPR000218, Ribosomal_L14P IPR005745, Ribosomal_L14P_bac-type IPR019972, Ribosomal_L14P_CS |
PANTHERi | PTHR11761, PTHR11761, 1 hit |
Pfami | View protein in Pfam PF00238, Ribosomal_L14, 1 hit |
SMARTi | View protein in SMART SM01374, Ribosomal_L14, 1 hit |
SUPFAMi | SSF50193, SSF50193, 1 hit |
TIGRFAMsi | TIGR01067, rplN_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00049, RIBOSOMAL_L14, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | RL14_ECOLI | |
Accessioni | P0ADY3Primary (citable) accession number: P0ADY3 Secondary accession number(s): P02411, Q2M6X5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | April 1, 1988 | |
Last modified: | December 2, 2020 | |
This is version 143 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Ribosomal proteins
Ribosomal proteins families and list of entries