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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.
MetaCyc:EG50001-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG50001. rplU.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001810001 – 10350S ribosomal protein L21Add BLAST103

Proteomic databases

EPDiP0AG48.
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

BioGridi4261074. 217 interactors.
DIPiDIP-47852N.
IntActiP0AG48. 81 interactors.
MINTiMINT-1280768.
STRINGi511145.b3186.

Structurei

Secondary structure

1103
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 14Combined sources12
Beta strandi15 – 17Combined sources3
Beta strandi19 – 23Combined sources5
Beta strandi29 – 31Combined sources3
Beta strandi32 – 35Combined sources4
Beta strandi38 – 48Combined sources11
Beta strandi50 – 53Combined sources4
Beta strandi58 – 68Combined sources11
Beta strandi72 – 78Combined sources7
Turni79 – 82Combined sources4
Beta strandi83 – 89Combined sources7
Beta strandi92 – 102Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00R1-103[»]
2RDOelectron microscopy9.10R1-103[»]
3BBXelectron microscopy10.00R1-103[»]
3J5Lelectron microscopy6.60R1-103[»]
3J7Zelectron microscopy3.90R1-103[»]
3J8Gelectron microscopy5.00R1-103[»]
3J9Yelectron microscopy3.90R1-103[»]
3J9Zelectron microscopy3.60LP1-103[»]
3JA1electron microscopy3.60LT1-103[»]
3JBUelectron microscopy3.64r1-103[»]
3JBVelectron microscopy3.32r1-103[»]
3JCDelectron microscopy3.70R1-103[»]
3JCEelectron microscopy3.20R1-103[»]
3JCJelectron microscopy3.70Q1-103[»]
3JCNelectron microscopy4.60R1-103[»]
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[»]
4WOIX-ray3.00BR/CR1-103[»]
4WWWX-ray3.10RR/YR1-103[»]
4YBBX-ray2.10CS/DS1-103[»]
5ADYelectron microscopy4.50R1-103[»]
5AFIelectron microscopy2.90R1-103[»]
5AKAelectron microscopy5.70R1-103[»]
5GADelectron microscopy3.70S1-103[»]
5GAEelectron microscopy3.33S1-103[»]
5GAFelectron microscopy4.30S1-103[»]
5GAGelectron microscopy3.80S1-103[»]
5GAHelectron microscopy3.80S1-103[»]
5IQRelectron microscopy3.00R1-103[»]
5IT8X-ray3.12CS/DS1-103[»]
5J5BX-ray2.80CS/DS1-103[»]
5J7LX-ray3.00CS/DS1-103[»]
5J88X-ray3.32CS/DS1-103[»]
5J8AX-ray3.10CS/DS1-103[»]
5J91X-ray2.96CS/DS1-103[»]
5JC9X-ray3.03CS/DS1-103[»]
5JTEelectron microscopy3.60BR1-103[»]
5JU8electron microscopy3.60BR1-103[»]
5KCRelectron microscopy3.601V1-103[»]
5KCSelectron microscopy3.901V1-103[»]
5KPSelectron microscopy3.90R1-103[»]
5KPVelectron microscopy4.10Q1-103[»]
5KPWelectron microscopy3.90Q1-103[»]
5KPXelectron microscopy3.90Q1-103[»]
5L3Pelectron microscopy3.70V1-103[»]
ProteinModelPortaliP0AG48.
SMRiP0AG48.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AG48.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L21P family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0261. LUCA.
HOGENOMiHOG000036265.
InParanoidiP0AG48.
KOiK02888.
OMAiQGHRQPF.
PhylomeDBiP0AG48.

Family and domain databases

HAMAPiMF_01363. Ribosomal_L21. 1 hit.
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.
WP_000271401.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76218; AAC76218; b3186.
BAE77230; BAE77230; BAE77230.
GeneIDi949057.
KEGGiecj:JW3153.
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.
WP_000271401.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J28electron microscopy8.00R1-103[»]
2RDOelectron microscopy9.10R1-103[»]
3BBXelectron microscopy10.00R1-103[»]
3J5Lelectron microscopy6.60R1-103[»]
3J7Zelectron microscopy3.90R1-103[»]
3J8Gelectron microscopy5.00R1-103[»]
3J9Yelectron microscopy3.90R1-103[»]
3J9Zelectron microscopy3.60LP1-103[»]
3JA1electron microscopy3.60LT1-103[»]
3JBUelectron microscopy3.64r1-103[»]
3JBVelectron microscopy3.32r1-103[»]
3JCDelectron microscopy3.70R1-103[»]
3JCEelectron microscopy3.20R1-103[»]
3JCJelectron microscopy3.70Q1-103[»]
3JCNelectron microscopy4.60R1-103[»]
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[»]
4WOIX-ray3.00BR/CR1-103[»]
4WWWX-ray3.10RR/YR1-103[»]
4YBBX-ray2.10CS/DS1-103[»]
5ADYelectron microscopy4.50R1-103[»]
5AFIelectron microscopy2.90R1-103[»]
5AKAelectron microscopy5.70R1-103[»]
5GADelectron microscopy3.70S1-103[»]
5GAEelectron microscopy3.33S1-103[»]
5GAFelectron microscopy4.30S1-103[»]
5GAGelectron microscopy3.80S1-103[»]
5GAHelectron microscopy3.80S1-103[»]
5IQRelectron microscopy3.00R1-103[»]
5IT8X-ray3.12CS/DS1-103[»]
5J5BX-ray2.80CS/DS1-103[»]
5J7LX-ray3.00CS/DS1-103[»]
5J88X-ray3.32CS/DS1-103[»]
5J8AX-ray3.10CS/DS1-103[»]
5J91X-ray2.96CS/DS1-103[»]
5JC9X-ray3.03CS/DS1-103[»]
5JTEelectron microscopy3.60BR1-103[»]
5JU8electron microscopy3.60BR1-103[»]
5KCRelectron microscopy3.601V1-103[»]
5KCSelectron microscopy3.901V1-103[»]
5KPSelectron microscopy3.90R1-103[»]
5KPVelectron microscopy4.10Q1-103[»]
5KPWelectron microscopy3.90Q1-103[»]
5KPXelectron microscopy3.90Q1-103[»]
5L3Pelectron microscopy3.70V1-103[»]
ProteinModelPortaliP0AG48.
SMRiP0AG48.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261074. 217 interactors.
DIPiDIP-47852N.
IntActiP0AG48. 81 interactors.
MINTiMINT-1280768.
STRINGi511145.b3186.

2D gel databases

SWISS-2DPAGEP0AG48.

Proteomic databases

EPDiP0AG48.
PaxDbiP0AG48.
PRIDEiP0AG48.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76218; AAC76218; b3186.
BAE77230; BAE77230; BAE77230.
GeneIDi949057.
KEGGiecj:JW3153.
eco:b3186.
PATRICi32121792. VBIEscCol129921_3280.

Organism-specific databases

EchoBASEiEB4295.
EcoGeneiEG50001. rplU.

Phylogenomic databases

eggNOGiCOG0261. LUCA.
HOGENOMiHOG000036265.
InParanoidiP0AG48.
KOiK02888.
OMAiQGHRQPF.
PhylomeDBiP0AG48.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP0AG48.
PROiP0AG48.

Family and domain databases

HAMAPiMF_01363. Ribosomal_L21. 1 hit.
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...

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: November 30, 2016
This is version 108 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

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.