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P0AG48

- RL21_ECOLI

UniProt

P0AG48 - RL21_ECOLI

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Protein
50S ribosomal protein L21
Gene
rplU, b3186, JW3153
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

This protein binds to 23S rRNA in the presence of protein L20.UniRule annotation

GO - Molecular functioni

  1. rRNA binding Source: UniProtKB-HAMAP
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. translation Source: UniProtKB-HAMAP
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 L21
Gene namesi
Name:rplU
Ordered Locus Names:b3186, JW3153
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG50001. rplU.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10310350S ribosomal protein L21UniRule annotation
PRO_0000181000Add
BLAST

Proteomic databases

PaxDbiP0AG48.
PRIDEiP0AG48.

2D gel databases

SWISS-2DPAGEP0AG48.

Expressioni

Gene expression databases

GenevestigatoriP0AG48.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

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

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Beta strandi8 – 147
Beta strandi15 – 173
Beta strandi20 – 234
Beta strandi32 – 354
Beta strandi38 – 4811
Beta strandi50 – 534
Beta strandi58 – 6811
Beta strandi72 – 787
Turni79 – 824
Beta strandi83 – 897
Beta strandi92 – 965
Beta strandi100 – 1023

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VS6X-ray3.46R1-103[»]
1VS8X-ray3.46R1-103[»]
1VT2X-ray3.30R1-103[»]
2AW4X-ray3.46R1-103[»]
2AWBX-ray3.46R1-103[»]
2I2TX-ray3.22R1-103[»]
2I2VX-ray3.22R1-103[»]
2J28electron microscopy8.00R1-103[»]
2QAMX-ray3.21R1-103[»]
2QAOX-ray3.21R1-103[»]
2QBAX-ray3.54R1-103[»]
2QBCX-ray3.54R1-103[»]
2QBEX-ray3.30R1-103[»]
2QBGX-ray3.30R1-103[»]
2QBIX-ray4.00R1-103[»]
2QBKX-ray4.00R1-103[»]
2QOVX-ray3.93R1-103[»]
2QOXX-ray3.93R1-103[»]
2QOZX-ray3.50R1-103[»]
2QP1X-ray3.50R1-103[»]
2RDOelectron microscopy9.10R1-103[»]
2WWQelectron microscopy5.80R1-103[»]
2Z4LX-ray4.45R1-103[»]
2Z4NX-ray4.45R1-103[»]
3BBXelectron microscopy10.00R1-103[»]
3E1Belectron microscopy-K1-103[»]
3E1Delectron microscopy-K1-103[»]
3FIKelectron microscopy6.70R1-103[»]
3I1NX-ray3.19R1-103[»]
3I1PX-ray3.19R1-103[»]
3I1RX-ray3.81R1-103[»]
3I1TX-ray3.81R1-103[»]
3I20X-ray3.71R1-103[»]
3I22X-ray3.71R1-103[»]
3IZTelectron microscopy-S1-103[»]
3IZUelectron microscopy-S1-103[»]
3J01electron microscopy-R1-103[»]
3J0Telectron microscopy12.10T1-103[»]
3J0Welectron microscopy14.70T1-103[»]
3J0Yelectron microscopy13.50T1-103[»]
3J11electron microscopy13.10T1-103[»]
3J12electron microscopy11.50T1-103[»]
3J14electron microscopy11.50T1-103[»]
3J19electron microscopy8.30R1-103[»]
3J37electron microscopy9.80V1-103[»]
3J4Xelectron microscopy12.00R1-103[»]
3J50electron microscopy20.00R1-103[»]
3J51electron microscopy17.00R1-103[»]
3J52electron microscopy12.00R1-103[»]
3J54electron microscopy13.00R1-103[»]
3J56electron microscopy15.00R1-103[»]
3J58electron microscopy17.00R1-103[»]
3J5Aelectron microscopy12.00R1-103[»]
3J5Celectron microscopy17.00R1-103[»]
3J5Eelectron microscopy17.00R1-103[»]
3J5Gelectron microscopy20.00R1-103[»]
3J5Ielectron microscopy15.00R1-103[»]
3J5Kelectron microscopy9.00R1-103[»]
3J5Lelectron microscopy6.60R1-103[»]
3J5Oelectron microscopy6.80R1-103[»]
3J5Uelectron microscopy7.60T1-103[»]
3J5Welectron microscopy7.60U1-103[»]
3KCRelectron microscopy-R1-103[»]
3OASX-ray3.25R1-103[»]
3OATX-ray3.25R1-103[»]
3OFCX-ray3.19R1-103[»]
3OFDX-ray3.19R1-103[»]
3OFQX-ray3.10R1-103[»]
3OFRX-ray3.10R1-103[»]
3OFZX-ray3.29R1-103[»]
3OG0X-ray3.29R1-103[»]
3ORBX-ray3.30R1-103[»]
3R8SX-ray3.00R1-103[»]
3R8TX-ray3.00R1-103[»]
3SGFX-ray3.20V1-103[»]
3UOSX-ray3.70V1-103[»]
4CSUelectron microscopy5.50R1-103[»]
4GARX-ray3.30R1-103[»]
4GAUX-ray3.30R1-103[»]
4KIXX-ray2.90R1-103[»]
4KIZX-ray2.90R1-103[»]
4KJ1X-ray2.90R1-103[»]
4KJ3X-ray2.90R1-103[»]
4KJ5X-ray2.90R1-103[»]
4KJ7X-ray2.90R1-103[»]
4KJ9X-ray2.90R1-103[»]
4KJBX-ray2.90R1-103[»]
ProteinModelPortaliP0AG48.
SMRiP0AG48. Positions 1-103.

Miscellaneous databases

EvolutionaryTraceiP0AG48.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0261.
HOGENOMiHOG000036265.
KOiK02888.
OMAiQGRGDKV.
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

MYAVFQSGGK QHRVSEGQTV RLEKLDIATG ETVEFAEVLM IANGEEVKIG    50
VPFVDGGVIK AEVVAHGRGE KVKIVKFRRR KHYRKQQGHR QWFTDVKITG 100
ISA 103
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:
EMBL
GenBank
DDBJ
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.
YP_491371.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76218; AAC76218; b3186.
BAE77230; BAE77230; BAE77230.
GeneIDi12932080.
949057.
KEGGiecj:Y75_p3106.
eco:b3186.
PATRICi32121792. VBIEscCol129921_3280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi JS0766. R5EC21.
RefSeqi NP_417653.1. NC_000913.3.
YP_491371.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VS6 X-ray 3.46 R 1-103 [» ]
1VS8 X-ray 3.46 R 1-103 [» ]
1VT2 X-ray 3.30 R 1-103 [» ]
2AW4 X-ray 3.46 R 1-103 [» ]
2AWB X-ray 3.46 R 1-103 [» ]
2I2T X-ray 3.22 R 1-103 [» ]
2I2V X-ray 3.22 R 1-103 [» ]
2J28 electron microscopy 8.00 R 1-103 [» ]
2QAM X-ray 3.21 R 1-103 [» ]
2QAO X-ray 3.21 R 1-103 [» ]
2QBA X-ray 3.54 R 1-103 [» ]
2QBC X-ray 3.54 R 1-103 [» ]
2QBE X-ray 3.30 R 1-103 [» ]
2QBG X-ray 3.30 R 1-103 [» ]
2QBI X-ray 4.00 R 1-103 [» ]
2QBK X-ray 4.00 R 1-103 [» ]
2QOV X-ray 3.93 R 1-103 [» ]
2QOX X-ray 3.93 R 1-103 [» ]
2QOZ X-ray 3.50 R 1-103 [» ]
2QP1 X-ray 3.50 R 1-103 [» ]
2RDO electron microscopy 9.10 R 1-103 [» ]
2WWQ electron microscopy 5.80 R 1-103 [» ]
2Z4L X-ray 4.45 R 1-103 [» ]
2Z4N X-ray 4.45 R 1-103 [» ]
3BBX electron microscopy 10.00 R 1-103 [» ]
3E1B electron microscopy - K 1-103 [» ]
3E1D electron microscopy - K 1-103 [» ]
3FIK electron microscopy 6.70 R 1-103 [» ]
3I1N X-ray 3.19 R 1-103 [» ]
3I1P X-ray 3.19 R 1-103 [» ]
3I1R X-ray 3.81 R 1-103 [» ]
3I1T X-ray 3.81 R 1-103 [» ]
3I20 X-ray 3.71 R 1-103 [» ]
3I22 X-ray 3.71 R 1-103 [» ]
3IZT electron microscopy - S 1-103 [» ]
3IZU electron microscopy - S 1-103 [» ]
3J01 electron microscopy - R 1-103 [» ]
3J0T electron microscopy 12.10 T 1-103 [» ]
3J0W electron microscopy 14.70 T 1-103 [» ]
3J0Y electron microscopy 13.50 T 1-103 [» ]
3J11 electron microscopy 13.10 T 1-103 [» ]
3J12 electron microscopy 11.50 T 1-103 [» ]
3J14 electron microscopy 11.50 T 1-103 [» ]
3J19 electron microscopy 8.30 R 1-103 [» ]
3J37 electron microscopy 9.80 V 1-103 [» ]
3J4X electron microscopy 12.00 R 1-103 [» ]
3J50 electron microscopy 20.00 R 1-103 [» ]
3J51 electron microscopy 17.00 R 1-103 [» ]
3J52 electron microscopy 12.00 R 1-103 [» ]
3J54 electron microscopy 13.00 R 1-103 [» ]
3J56 electron microscopy 15.00 R 1-103 [» ]
3J58 electron microscopy 17.00 R 1-103 [» ]
3J5A electron microscopy 12.00 R 1-103 [» ]
3J5C electron microscopy 17.00 R 1-103 [» ]
3J5E electron microscopy 17.00 R 1-103 [» ]
3J5G electron microscopy 20.00 R 1-103 [» ]
3J5I electron microscopy 15.00 R 1-103 [» ]
3J5K electron microscopy 9.00 R 1-103 [» ]
3J5L electron microscopy 6.60 R 1-103 [» ]
3J5O electron microscopy 6.80 R 1-103 [» ]
3J5U electron microscopy 7.60 T 1-103 [» ]
3J5W electron microscopy 7.60 U 1-103 [» ]
3KCR electron microscopy - R 1-103 [» ]
3OAS X-ray 3.25 R 1-103 [» ]
3OAT X-ray 3.25 R 1-103 [» ]
3OFC X-ray 3.19 R 1-103 [» ]
3OFD X-ray 3.19 R 1-103 [» ]
3OFQ X-ray 3.10 R 1-103 [» ]
3OFR X-ray 3.10 R 1-103 [» ]
3OFZ X-ray 3.29 R 1-103 [» ]
3OG0 X-ray 3.29 R 1-103 [» ]
3ORB X-ray 3.30 R 1-103 [» ]
3R8S X-ray 3.00 R 1-103 [» ]
3R8T X-ray 3.00 R 1-103 [» ]
3SGF X-ray 3.20 V 1-103 [» ]
3UOS X-ray 3.70 V 1-103 [» ]
4CSU electron microscopy 5.50 R 1-103 [» ]
4GAR X-ray 3.30 R 1-103 [» ]
4GAU X-ray 3.30 R 1-103 [» ]
4KIX X-ray 2.90 R 1-103 [» ]
4KIZ X-ray 2.90 R 1-103 [» ]
4KJ1 X-ray 2.90 R 1-103 [» ]
4KJ3 X-ray 2.90 R 1-103 [» ]
4KJ5 X-ray 2.90 R 1-103 [» ]
4KJ7 X-ray 2.90 R 1-103 [» ]
4KJ9 X-ray 2.90 R 1-103 [» ]
4KJB X-ray 2.90 R 1-103 [» ]
ProteinModelPortali P0AG48.
SMRi P0AG48. Positions 1-103.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-47852N.
IntActi P0AG48. 81 interactions.
MINTi MINT-1280768.
STRINGi 511145.b3186.

Chemistry

ChEMBLi CHEMBL2363135.

2D gel databases

SWISS-2DPAGE P0AG48.

Proteomic databases

PaxDbi P0AG48.
PRIDEi P0AG48.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76218 ; AAC76218 ; b3186 .
BAE77230 ; BAE77230 ; BAE77230 .
GeneIDi 12932080.
949057.
KEGGi ecj:Y75_p3106.
eco:b3186.
PATRICi 32121792. VBIEscCol129921_3280.

Organism-specific databases

EchoBASEi EB4295.
EcoGenei EG50001. rplU.

Phylogenomic databases

eggNOGi COG0261.
HOGENOMi HOG000036265.
KOi K02888.
OMAi QGRGDKV.
OrthoDBi EOG6TJ84X.
PhylomeDBi P0AG48.

Enzyme and pathway databases

BioCyci EcoCyc:EG50001-MONOMER.
ECOL316407:JW3153-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0AG48.
PROi P0AG48.

Gene expression databases

Genevestigatori P0AG48.

Family and domain databases

HAMAPi MF_01363. Ribosomal_L21.
InterProi IPR028909. L21p-like.
IPR001787. Ribosomal_L21.
IPR018258. Ribosomal_L21_CS.
[Graphical view ]
Pfami PF00829. Ribosomal_L21p. 1 hit.
[Graphical view ]
SUPFAMi SSF141091. SSF141091. 1 hit.
TIGRFAMsi TIGR00061. L21. 1 hit.
PROSITEi PS01169. RIBOSOMAL_L21. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.

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: September 3, 2014
This is version 85 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

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