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Protein

50S ribosomal protein L21

Gene

rplU

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

This protein binds to 23S rRNA in the presence of protein L20.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG50001-MONOMER.
ECOL316407:JW3153-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L21UniRule annotation
Gene namesi
Name:rplUUniRule annotation
Ordered Locus Names:b3186, JW3153
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG50001. rplU.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10310350S ribosomal protein L21PRO_0000181000Add
BLAST

Proteomic databases

PaxDbiP0AG48.
PRIDEiP0AG48.

2D gel databases

SWISS-2DPAGEP0AG48.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Contacts protein L20.2 Publications

Protein-protein interaction databases

DIPiDIP-47852N.
IntActiP0AG48. 81 interactions.
MINTiMINT-1280768.
STRINGi511145.b3186.

Structurei

Secondary structure

1
103
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1412Combined sources
Beta strandi15 – 173Combined sources
Beta strandi19 – 235Combined sources
Beta strandi29 – 313Combined sources
Beta strandi32 – 354Combined sources
Beta strandi38 – 4811Combined sources
Beta strandi50 – 534Combined sources
Beta strandi58 – 6811Combined sources
Beta strandi72 – 787Combined sources
Turni79 – 824Combined sources
Beta strandi83 – 897Combined sources
Beta strandi92 – 10211Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00R1-103[»]
2RDOelectron microscopy9.10R1-103[»]
3BBXelectron microscopy10.00R1-103[»]
3J5Lelectron microscopy6.60R1-103[»]
3J7Zelectron microscopy3.90R1-103[»]
3J9Yelectron microscopy3.90R1-103[»]
4CSUelectron microscopy5.50R1-103[»]
4U1UX-ray2.95BR/DR1-103[»]
4U1VX-ray3.00BR/DR1-103[»]
4U20X-ray2.90BR/DR1-103[»]
4U24X-ray2.90BR/DR1-103[»]
4U25X-ray2.90BR/DR1-103[»]
4U26X-ray2.80BR/DR1-103[»]
4U27X-ray2.80BR/DR1-103[»]
4UY8electron microscopy3.80R1-103[»]
4V4HX-ray3.46BR/DR1-103[»]
4V4QX-ray3.46BR/DR1-103[»]
4V50X-ray3.22BR/DR1-103[»]
4V52X-ray3.21BR/DR1-103[»]
4V53X-ray3.54BR/DR1-103[»]
4V54X-ray3.30BR/DR1-103[»]
4V55X-ray4.00BR/DR1-103[»]
4V56X-ray3.93BR/DR1-103[»]
4V57X-ray3.50BR/DR1-103[»]
4V5BX-ray3.74AR/CR1-103[»]
4V5Helectron microscopy5.80BR1-103[»]
4V5YX-ray4.45BR/DR1-103[»]
4V64X-ray3.50BR/DR1-103[»]
4V65electron microscopy9.00BK1-103[»]
4V66electron microscopy9.00BK1-103[»]
4V69electron microscopy6.70BR1-103[»]
4V6CX-ray3.19BR/DR1-103[»]
4V6DX-ray3.81BR/DR1-103[»]
4V6EX-ray3.71BR/DR1-103[»]
4V6Kelectron microscopy8.25AS1-103[»]
4V6Lelectron microscopy13.20BS1-103[»]
4V6Melectron microscopy7.10BR1-103[»]
4V6Nelectron microscopy12.10AT1-103[»]
4V6Oelectron microscopy14.70BT1-103[»]
4V6Pelectron microscopy13.50BT1-103[»]
4V6Qelectron microscopy11.50BT1-103[»]
4V6Relectron microscopy11.50BT1-103[»]
4V6Selectron microscopy13.10AT1-103[»]
4V6Telectron microscopy8.30BR1-103[»]
4V6Velectron microscopy9.80BV1-103[»]
4V6Yelectron microscopy12.00BR1-103[»]
4V6Zelectron microscopy12.00BR1-103[»]
4V70electron microscopy17.00BR1-103[»]
4V71electron microscopy20.00BR1-103[»]
4V72electron microscopy13.00BR1-103[»]
4V73electron microscopy15.00BR1-103[»]
4V74electron microscopy17.00BR1-103[»]
4V75electron microscopy12.00BR1-103[»]
4V76electron microscopy17.00BR1-103[»]
4V77electron microscopy17.00BR1-103[»]
4V78electron microscopy20.00BR1-103[»]
4V79electron microscopy15.00BR1-103[»]
4V7Aelectron microscopy9.00BR1-103[»]
4V7Belectron microscopy6.80BR1-103[»]
4V7Celectron microscopy7.60BT1-103[»]
4V7Delectron microscopy7.60AU1-103[»]
4V7Ielectron microscopy9.60AR1-103[»]
4V7SX-ray3.25BR/DR1-103[»]
4V7TX-ray3.19BR/DR1-103[»]
4V7UX-ray3.10BR/DR1-103[»]
4V7VX-ray3.29BR/DR1-103[»]
4V85X-ray3.20V1-103[»]
4V89X-ray3.70BV1-103[»]
4V9CX-ray3.30BR/DR1-103[»]
4V9DX-ray3.00CR/DR1-103[»]
4V9OX-ray2.90AR/CR/ER/GR1-103[»]
4V9PX-ray2.90AR/CR/ER/GR1-103[»]
4WF1X-ray3.09BR/DR1-103[»]
4WWWX-ray3.10RR/YR1-103[»]
4YBBX-ray2.10CS/DS1-103[»]
5AFIelectron microscopy2.90R1-103[»]
5AKAelectron microscopy5.70R1-103[»]
ProteinModelPortaliP0AG48.
SMRiP0AG48. Positions 1-103.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG48.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L21P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0261.
HOGENOMiHOG000036265.
InParanoidiP0AG48.
KOiK02888.
OMAiQGHRQQY.
OrthoDBiEOG6TJ84X.
PhylomeDBiP0AG48.

Family and domain databases

HAMAPiMF_01363. Ribosomal_L21.
InterProiIPR028909. L21p-like.
IPR001787. Ribosomal_L21.
IPR018258. Ribosomal_L21_CS.
[Graphical view]
PfamiPF00829. Ribosomal_L21p. 1 hit.
[Graphical view]
SUPFAMiSSF141091. SSF141091. 1 hit.
TIGRFAMsiTIGR00061. L21. 1 hit.
PROSITEiPS01169. RIBOSOMAL_L21. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AG48-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYAVFQSGGK QHRVSEGQTV RLEKLDIATG ETVEFAEVLM IANGEEVKIG
60 70 80 90 100
VPFVDGGVIK AEVVAHGRGE KVKIVKFRRR KHYRKQQGHR QWFTDVKITG

ISA
Length:103
Mass (Da):11,564
Last modified:July 21, 1986 - v1
Checksum:i9221F104EC9C8CDB
GO

Mass spectrometryi

Molecular mass is 11562.7 Da from positions 1 - 103. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13267 Genomic DNA. Translation: BAA02525.1.
U18997 Genomic DNA. Translation: AAA57987.1.
U00096 Genomic DNA. Translation: AAC76218.1.
AP009048 Genomic DNA. Translation: BAE77230.1.
PIRiJS0766. R5EC21.
RefSeqiNP_417653.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAC76218; AAC76218; b3186.
BAE77230; BAE77230; BAE77230.
GeneIDi949057.
KEGGiecj:Y75_p3106.
eco:b3186.
PATRICi32121792. VBIEscCol129921_3280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13267 Genomic DNA. Translation: BAA02525.1.
U18997 Genomic DNA. Translation: AAA57987.1.
U00096 Genomic DNA. Translation: AAC76218.1.
AP009048 Genomic DNA. Translation: BAE77230.1.
PIRiJS0766. R5EC21.
RefSeqiNP_417653.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00R1-103[»]
2RDOelectron microscopy9.10R1-103[»]
3BBXelectron microscopy10.00R1-103[»]
3J5Lelectron microscopy6.60R1-103[»]
3J7Zelectron microscopy3.90R1-103[»]
3J9Yelectron microscopy3.90R1-103[»]
4CSUelectron microscopy5.50R1-103[»]
4U1UX-ray2.95BR/DR1-103[»]
4U1VX-ray3.00BR/DR1-103[»]
4U20X-ray2.90BR/DR1-103[»]
4U24X-ray2.90BR/DR1-103[»]
4U25X-ray2.90BR/DR1-103[»]
4U26X-ray2.80BR/DR1-103[»]
4U27X-ray2.80BR/DR1-103[»]
4UY8electron microscopy3.80R1-103[»]
4V4HX-ray3.46BR/DR1-103[»]
4V4QX-ray3.46BR/DR1-103[»]
4V50X-ray3.22BR/DR1-103[»]
4V52X-ray3.21BR/DR1-103[»]
4V53X-ray3.54BR/DR1-103[»]
4V54X-ray3.30BR/DR1-103[»]
4V55X-ray4.00BR/DR1-103[»]
4V56X-ray3.93BR/DR1-103[»]
4V57X-ray3.50BR/DR1-103[»]
4V5BX-ray3.74AR/CR1-103[»]
4V5Helectron microscopy5.80BR1-103[»]
4V5YX-ray4.45BR/DR1-103[»]
4V64X-ray3.50BR/DR1-103[»]
4V65electron microscopy9.00BK1-103[»]
4V66electron microscopy9.00BK1-103[»]
4V69electron microscopy6.70BR1-103[»]
4V6CX-ray3.19BR/DR1-103[»]
4V6DX-ray3.81BR/DR1-103[»]
4V6EX-ray3.71BR/DR1-103[»]
4V6Kelectron microscopy8.25AS1-103[»]
4V6Lelectron microscopy13.20BS1-103[»]
4V6Melectron microscopy7.10BR1-103[»]
4V6Nelectron microscopy12.10AT1-103[»]
4V6Oelectron microscopy14.70BT1-103[»]
4V6Pelectron microscopy13.50BT1-103[»]
4V6Qelectron microscopy11.50BT1-103[»]
4V6Relectron microscopy11.50BT1-103[»]
4V6Selectron microscopy13.10AT1-103[»]
4V6Telectron microscopy8.30BR1-103[»]
4V6Velectron microscopy9.80BV1-103[»]
4V6Yelectron microscopy12.00BR1-103[»]
4V6Zelectron microscopy12.00BR1-103[»]
4V70electron microscopy17.00BR1-103[»]
4V71electron microscopy20.00BR1-103[»]
4V72electron microscopy13.00BR1-103[»]
4V73electron microscopy15.00BR1-103[»]
4V74electron microscopy17.00BR1-103[»]
4V75electron microscopy12.00BR1-103[»]
4V76electron microscopy17.00BR1-103[»]
4V77electron microscopy17.00BR1-103[»]
4V78electron microscopy20.00BR1-103[»]
4V79electron microscopy15.00BR1-103[»]
4V7Aelectron microscopy9.00BR1-103[»]
4V7Belectron microscopy6.80BR1-103[»]
4V7Celectron microscopy7.60BT1-103[»]
4V7Delectron microscopy7.60AU1-103[»]
4V7Ielectron microscopy9.60AR1-103[»]
4V7SX-ray3.25BR/DR1-103[»]
4V7TX-ray3.19BR/DR1-103[»]
4V7UX-ray3.10BR/DR1-103[»]
4V7VX-ray3.29BR/DR1-103[»]
4V85X-ray3.20V1-103[»]
4V89X-ray3.70BV1-103[»]
4V9CX-ray3.30BR/DR1-103[»]
4V9DX-ray3.00CR/DR1-103[»]
4V9OX-ray2.90AR/CR/ER/GR1-103[»]
4V9PX-ray2.90AR/CR/ER/GR1-103[»]
4WF1X-ray3.09BR/DR1-103[»]
4WWWX-ray3.10RR/YR1-103[»]
4YBBX-ray2.10CS/DS1-103[»]
5AFIelectron microscopy2.90R1-103[»]
5AKAelectron microscopy5.70R1-103[»]
ProteinModelPortaliP0AG48.
SMRiP0AG48. Positions 1-103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-47852N.
IntActiP0AG48. 81 interactions.
MINTiMINT-1280768.
STRINGi511145.b3186.

Chemistry

ChEMBLiCHEMBL2363135.

2D gel databases

SWISS-2DPAGEP0AG48.

Proteomic databases

PaxDbiP0AG48.
PRIDEiP0AG48.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76218; AAC76218; b3186.
BAE77230; BAE77230; BAE77230.
GeneIDi949057.
KEGGiecj:Y75_p3106.
eco:b3186.
PATRICi32121792. VBIEscCol129921_3280.

Organism-specific databases

EchoBASEiEB4295.
EcoGeneiEG50001. rplU.

Phylogenomic databases

eggNOGiCOG0261.
HOGENOMiHOG000036265.
InParanoidiP0AG48.
KOiK02888.
OMAiQGHRQQY.
OrthoDBiEOG6TJ84X.
PhylomeDBiP0AG48.

Enzyme and pathway databases

BioCyciEcoCyc:EG50001-MONOMER.
ECOL316407:JW3153-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0AG48.
PROiP0AG48.

Family and domain databases

HAMAPiMF_01363. Ribosomal_L21.
InterProiIPR028909. L21p-like.
IPR001787. Ribosomal_L21.
IPR018258. Ribosomal_L21_CS.
[Graphical view]
PfamiPF00829. Ribosomal_L21p. 1 hit.
[Graphical view]
SUPFAMiSSF141091. SSF141091. 1 hit.
TIGRFAMsiTIGR00061. L21. 1 hit.
PROSITEiPS01169. RIBOSOMAL_L21. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequence of the ribosomal protein L21 of Escherichia coli."
    Heiland I., Wittmann-Liebold B.
    Biochemistry 18:4605-4612(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
  2. "Cloning and nucleotide sequencing of the genes, rpIU and rpmA, for ribosomal proteins L21 and L27 of Escherichia coli."
    Jeong J.H., Kitakawa M.S., Isono S., Isono K.
    DNA Seq. 4:59-67(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. Cited for: PROTEIN SEQUENCE OF 1-13.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "The use of 2-iminothiolane as an RNA-protein cross-linking agent in Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-linked to proteins L4, L6, L21, L23, L27 and L29."
    Wower I., Wower J., Meinke M., Brimacombe R.
    Nucleic Acids Res. 9:4285-4302(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO 23S RRNA.
    Strain: MRE-600.
  7. "Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli."
    Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G.
    Biochemistry 28:4099-4105(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINKING TO L20.
  8. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  9. "Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry."
    Arnold R.J., Reilly J.P.
    Anal. Biochem. 269:105-112(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
    Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.
  11. "Molecular basis for the ribosome functioning as an L-tryptophan sensor."
    Bischoff L., Berninghausen O., Beckmann R.
    Cell Rep. 9:469-475(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF TNAC-STALLED 50S RIBOSOMAL SUBUNIT.
    Strain: K12 / A19 / KC6.

Entry informationi

Entry nameiRL21_ECOLI
AccessioniPrimary (citable) accession number: P0AG48
Secondary accession number(s): P02422, Q2M926
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 24, 2015
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

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.