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P60422

- RL2_ECOLI

UniProt

P60422 - RL2_ECOLI

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Protein

50S ribosomal protein L2

Gene
rplB, b3317, JW3279
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

One of the primary rRNA binding proteins. Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is highly controversial.UniRule annotation
In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, 1 Publication); these contacts are broken in the model with bound EF-G.UniRule annotation

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. rRNA binding Source: UniProtKB-HAMAP
  3. structural constituent of ribosome Source: InterPro
  4. transferase activity Source: InterPro
  5. zinc ion binding Source: EcoliWiki

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:EG10865-MONOMER.
ECOL316407:JW3279-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L2
Gene namesi
Name:rplB
Ordered Locus Names:b3317, JW3279
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10865. rplB.

Subcellular locationi

GO - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi230 – 2301H → Q: Loss of peptidyltransferase activity in reconstituted ribosomes. No change in rRNA binding or assembly into ribosomes. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 27327250S ribosomal protein L2UniRule annotationPRO_0000129559Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei242 – 2421N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP60422.
PRIDEiP60422.

Expressioni

Gene expression databases

GenevestigatoriP60422.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Forms a bridge to the 30S subunit in the 70S ribosome, contacting the 16S rRNA. Interacts weakly with S6 in one of the 3.5 A resolved structures.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaAP030044EBI-543515,EBI-548951
gspEP457592EBI-543515,EBI-1132437
metGP009592EBI-543515,EBI-909268
rpoAP0A7Z45EBI-543515,EBI-544985

Protein-protein interaction databases

BioGridi852132. 1 interaction.
DIPiDIP-35747N.
IntActiP60422. 362 interactions.
MINTiMINT-1322809.
STRINGi511145.b3317.

Structurei

Secondary structure

1
273
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53
Beta strandi8 – 103
Turni11 – 155
Beta strandi17 – 193
Beta strandi22 – 243
Helixi31 – 333
Beta strandi34 – 363
Beta strandi47 – 493
Beta strandi51 – 544
Beta strandi61 – 633
Beta strandi72 – 743
Beta strandi76 – 783
Beta strandi80 – 823
Beta strandi87 – 893
Beta strandi91 – 933
Beta strandi96 – 994
Beta strandi101 – 1055
Beta strandi107 – 1093
Beta strandi112 – 1154
Beta strandi116 – 1227
Beta strandi125 – 1273
Beta strandi129 – 1313
Helixi132 – 1343
Beta strandi142 – 1443
Beta strandi145 – 1473
Turni148 – 1503
Beta strandi157 – 1593
Beta strandi163 – 1664
Beta strandi169 – 1713
Beta strandi172 – 1754
Beta strandi177 – 1793
Beta strandi181 – 1844
Beta strandi186 – 1883
Beta strandi189 – 1913
Helixi199 – 2024
Helixi208 – 2125
Turni213 – 2153
Helixi222 – 2243
Turni227 – 2293
Beta strandi230 – 2323
Beta strandi236 – 2383
Beta strandi245 – 2484
Beta strandi251 – 2544
Beta strandi258 – 2603
Beta strandi261 – 2633
Helixi264 – 2663
Beta strandi267 – 2693

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P85electron microscopy12.30A2-273[»]
1P86electron microscopy11.50A2-273[»]
1VS6X-ray3.46C1-273[»]
1VS8X-ray3.46C1-273[»]
1VT2X-ray3.30C1-273[»]
2AW4X-ray3.46C1-273[»]
2AWBX-ray3.46C1-273[»]
2GYAelectron microscopy15.00A39-265[»]
2GYCelectron microscopy15.00A39-265[»]
2I2TX-ray3.22C2-273[»]
2I2VX-ray3.22C2-273[»]
2J28electron microscopy8.00C4-270[»]
2QAMX-ray3.21C2-273[»]
2QAOX-ray3.21C2-273[»]
2QBAX-ray3.54C2-273[»]
2QBCX-ray3.54C2-273[»]
2QBEX-ray3.30C2-273[»]
2QBGX-ray3.30C2-273[»]
2QBIX-ray4.00C2-273[»]
2QBKX-ray4.00C2-273[»]
2QOVX-ray3.93C2-273[»]
2QOXX-ray3.93C2-273[»]
2QOZX-ray3.50C2-273[»]
2QP1X-ray3.50C2-273[»]
2RDOelectron microscopy9.10C2-273[»]
2VHMX-ray3.74C1-273[»]
2VHNX-ray3.74C1-273[»]
2WWQelectron microscopy5.80C2-272[»]
2Z4LX-ray4.45C2-273[»]
2Z4NX-ray4.45C2-273[»]
3BBXelectron microscopy10.00C1-273[»]
3DF2X-ray3.50C1-273[»]
3DF4X-ray3.50C1-273[»]
3E1Belectron microscopy-N1-270[»]
3E1Delectron microscopy-N1-270[»]
3FIKelectron microscopy6.70C2-272[»]
3I1NX-ray3.19C1-273[»]
3I1PX-ray3.19C1-273[»]
3I1RX-ray3.81C1-273[»]
3I1TX-ray3.81C1-273[»]
3I20X-ray3.71C1-273[»]
3I22X-ray3.71C1-273[»]
3IZTelectron microscopy-D1-273[»]
3IZUelectron microscopy-D1-273[»]
3J01electron microscopy-62-273[»]
3J0Telectron microscopy12.10D2-273[»]
3J0Welectron microscopy14.70D2-273[»]
3J0Yelectron microscopy13.50D2-273[»]
3J11electron microscopy13.10D2-273[»]
3J12electron microscopy11.50D2-273[»]
3J14electron microscopy11.50D2-273[»]
3J19electron microscopy8.30C2-272[»]
3J37electron microscopy9.80D2-273[»]
3J4Xelectron microscopy12.00C1-272[»]
3J50electron microscopy20.00C1-272[»]
3J51electron microscopy17.00C1-272[»]
3J52electron microscopy12.00C1-272[»]
3J54electron microscopy13.00C1-272[»]
3J56electron microscopy15.00C1-272[»]
3J58electron microscopy17.00C1-272[»]
3J5Aelectron microscopy12.00C1-272[»]
3J5Celectron microscopy17.00C1-272[»]
3J5Eelectron microscopy17.00C1-272[»]
3J5Gelectron microscopy20.00C1-272[»]
3J5Ielectron microscopy15.00C1-272[»]
3J5Kelectron microscopy9.00C1-272[»]
3J5Lelectron microscopy6.60C2-272[»]
3J5Oelectron microscopy6.80C1-273[»]
3J5Uelectron microscopy7.60D2-273[»]
3J5Welectron microscopy7.60D2-273[»]
3KCRelectron microscopy-61-273[»]
3OASX-ray3.25C2-272[»]
3OATX-ray3.25C2-272[»]
3OFCX-ray3.19C2-272[»]
3OFDX-ray3.19C2-272[»]
3OFQX-ray3.10C2-272[»]
3OFRX-ray3.10C2-272[»]
3OFZX-ray3.29C2-272[»]
3OG0X-ray3.29C2-272[»]
3ORBX-ray3.30C1-273[»]
3R8SX-ray3.00C2-272[»]
3R8TX-ray3.00C2-272[»]
3SGFX-ray3.20C1-273[»]
3UOSX-ray3.70C1-273[»]
487Delectron microscopy7.50I62-172[»]
4CSUelectron microscopy5.50C2-273[»]
4GARX-ray3.30C1-273[»]
4GAUX-ray3.30C1-273[»]
4KIXX-ray2.90C1-273[»]
4KIZX-ray2.90C1-273[»]
4KJ1X-ray2.90C1-273[»]
4KJ3X-ray2.90C1-273[»]
4KJ5X-ray2.90C1-273[»]
4KJ7X-ray2.90C1-273[»]
4KJ9X-ray2.90C1-273[»]
4KJBX-ray2.90C1-273[»]
ProteinModelPortaliP60422.

Miscellaneous databases

EvolutionaryTraceiP60422.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0090.
HOGENOMiHOG000232982.
KOiK02886.
OMAiSAMNPID.
OrthoDBiEOG6TR0J1.
PhylomeDBiP60422.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
HAMAPiMF_01320_B. Ribosomal_L2_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR005880. Ribosomal_L2_bac/org-type.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR13691. PTHR13691. 1 hit.
PTHR13691:SF5. PTHR13691:SF5. 1 hit.
PfamiPF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002158. Ribosomal_L2. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR01171. rplB_bact. 1 hit.
PROSITEiPS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P60422-1 [UniParc]FASTAAdd to Basket

« Hide

MAVVKCKPTS PGRRHVVKVV NPELHKGKPF APLLEKNSKS GGRNNNGRIT    50
TRHIGGGHKQ AYRIVDFKRN KDGIPAVVER LEYDPNRSAN IALVLYKDGE 100
RRYILAPKGL KAGDQIQSGV DAAIKPGNTL PMRNIPVGST VHNVEMKPGK 150
GGQLARSAGT YVQIVARDGA YVTLRLRSGE MRKVEADCRA TLGEVGNAEH 200
MLRVLGKAGA ARWRGVRPTV RGTAMNPVDH PHGGGEGRNF GKHPVTPWGV 250
QTKGKKTRSN KRTDKFIVRR RSK 273
Length:273
Mass (Da):29,860
Last modified:January 23, 2007 - v2
Checksum:i1010BDE8D8C68B9B
GO

Mass spectrometryi

Molecular mass is 29732.3 Da from positions 2 - 273. Determined by MALDI. 1 Publication

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti232 – 2354HGGG → GGGH AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02613 Genomic DNA. Translation: CAA26463.1.
U18997 Genomic DNA. Translation: AAA58114.1.
U00096 Genomic DNA. Translation: AAC76342.1.
AP009048 Genomic DNA. Translation: BAE77974.1.
PIRiE23129. R5EC2.
RefSeqiNP_417776.1. NC_000913.3.
YP_492115.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76342; AAC76342; b3317.
BAE77974; BAE77974; BAE77974.
GeneIDi12932295.
947820.
KEGGiecj:Y75_p3859.
eco:b3317.
PATRICi32122066. VBIEscCol129921_3410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02613 Genomic DNA. Translation: CAA26463.1 .
U18997 Genomic DNA. Translation: AAA58114.1 .
U00096 Genomic DNA. Translation: AAC76342.1 .
AP009048 Genomic DNA. Translation: BAE77974.1 .
PIRi E23129. R5EC2.
RefSeqi NP_417776.1. NC_000913.3.
YP_492115.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P85 electron microscopy 12.30 A 2-273 [» ]
1P86 electron microscopy 11.50 A 2-273 [» ]
1VS6 X-ray 3.46 C 1-273 [» ]
1VS8 X-ray 3.46 C 1-273 [» ]
1VT2 X-ray 3.30 C 1-273 [» ]
2AW4 X-ray 3.46 C 1-273 [» ]
2AWB X-ray 3.46 C 1-273 [» ]
2GYA electron microscopy 15.00 A 39-265 [» ]
2GYC electron microscopy 15.00 A 39-265 [» ]
2I2T X-ray 3.22 C 2-273 [» ]
2I2V X-ray 3.22 C 2-273 [» ]
2J28 electron microscopy 8.00 C 4-270 [» ]
2QAM X-ray 3.21 C 2-273 [» ]
2QAO X-ray 3.21 C 2-273 [» ]
2QBA X-ray 3.54 C 2-273 [» ]
2QBC X-ray 3.54 C 2-273 [» ]
2QBE X-ray 3.30 C 2-273 [» ]
2QBG X-ray 3.30 C 2-273 [» ]
2QBI X-ray 4.00 C 2-273 [» ]
2QBK X-ray 4.00 C 2-273 [» ]
2QOV X-ray 3.93 C 2-273 [» ]
2QOX X-ray 3.93 C 2-273 [» ]
2QOZ X-ray 3.50 C 2-273 [» ]
2QP1 X-ray 3.50 C 2-273 [» ]
2RDO electron microscopy 9.10 C 2-273 [» ]
2VHM X-ray 3.74 C 1-273 [» ]
2VHN X-ray 3.74 C 1-273 [» ]
2WWQ electron microscopy 5.80 C 2-272 [» ]
2Z4L X-ray 4.45 C 2-273 [» ]
2Z4N X-ray 4.45 C 2-273 [» ]
3BBX electron microscopy 10.00 C 1-273 [» ]
3DF2 X-ray 3.50 C 1-273 [» ]
3DF4 X-ray 3.50 C 1-273 [» ]
3E1B electron microscopy - N 1-270 [» ]
3E1D electron microscopy - N 1-270 [» ]
3FIK electron microscopy 6.70 C 2-272 [» ]
3I1N X-ray 3.19 C 1-273 [» ]
3I1P X-ray 3.19 C 1-273 [» ]
3I1R X-ray 3.81 C 1-273 [» ]
3I1T X-ray 3.81 C 1-273 [» ]
3I20 X-ray 3.71 C 1-273 [» ]
3I22 X-ray 3.71 C 1-273 [» ]
3IZT electron microscopy - D 1-273 [» ]
3IZU electron microscopy - D 1-273 [» ]
3J01 electron microscopy - 6 2-273 [» ]
3J0T electron microscopy 12.10 D 2-273 [» ]
3J0W electron microscopy 14.70 D 2-273 [» ]
3J0Y electron microscopy 13.50 D 2-273 [» ]
3J11 electron microscopy 13.10 D 2-273 [» ]
3J12 electron microscopy 11.50 D 2-273 [» ]
3J14 electron microscopy 11.50 D 2-273 [» ]
3J19 electron microscopy 8.30 C 2-272 [» ]
3J37 electron microscopy 9.80 D 2-273 [» ]
3J4X electron microscopy 12.00 C 1-272 [» ]
3J50 electron microscopy 20.00 C 1-272 [» ]
3J51 electron microscopy 17.00 C 1-272 [» ]
3J52 electron microscopy 12.00 C 1-272 [» ]
3J54 electron microscopy 13.00 C 1-272 [» ]
3J56 electron microscopy 15.00 C 1-272 [» ]
3J58 electron microscopy 17.00 C 1-272 [» ]
3J5A electron microscopy 12.00 C 1-272 [» ]
3J5C electron microscopy 17.00 C 1-272 [» ]
3J5E electron microscopy 17.00 C 1-272 [» ]
3J5G electron microscopy 20.00 C 1-272 [» ]
3J5I electron microscopy 15.00 C 1-272 [» ]
3J5K electron microscopy 9.00 C 1-272 [» ]
3J5L electron microscopy 6.60 C 2-272 [» ]
3J5O electron microscopy 6.80 C 1-273 [» ]
3J5U electron microscopy 7.60 D 2-273 [» ]
3J5W electron microscopy 7.60 D 2-273 [» ]
3KCR electron microscopy - 6 1-273 [» ]
3OAS X-ray 3.25 C 2-272 [» ]
3OAT X-ray 3.25 C 2-272 [» ]
3OFC X-ray 3.19 C 2-272 [» ]
3OFD X-ray 3.19 C 2-272 [» ]
3OFQ X-ray 3.10 C 2-272 [» ]
3OFR X-ray 3.10 C 2-272 [» ]
3OFZ X-ray 3.29 C 2-272 [» ]
3OG0 X-ray 3.29 C 2-272 [» ]
3ORB X-ray 3.30 C 1-273 [» ]
3R8S X-ray 3.00 C 2-272 [» ]
3R8T X-ray 3.00 C 2-272 [» ]
3SGF X-ray 3.20 C 1-273 [» ]
3UOS X-ray 3.70 C 1-273 [» ]
487D electron microscopy 7.50 I 62-172 [» ]
4CSU electron microscopy 5.50 C 2-273 [» ]
4GAR X-ray 3.30 C 1-273 [» ]
4GAU X-ray 3.30 C 1-273 [» ]
4KIX X-ray 2.90 C 1-273 [» ]
4KIZ X-ray 2.90 C 1-273 [» ]
4KJ1 X-ray 2.90 C 1-273 [» ]
4KJ3 X-ray 2.90 C 1-273 [» ]
4KJ5 X-ray 2.90 C 1-273 [» ]
4KJ7 X-ray 2.90 C 1-273 [» ]
4KJ9 X-ray 2.90 C 1-273 [» ]
4KJB X-ray 2.90 C 1-273 [» ]
ProteinModelPortali P60422.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 852132. 1 interaction.
DIPi DIP-35747N.
IntActi P60422. 362 interactions.
MINTi MINT-1322809.
STRINGi 511145.b3317.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P60422.
PRIDEi P60422.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76342 ; AAC76342 ; b3317 .
BAE77974 ; BAE77974 ; BAE77974 .
GeneIDi 12932295.
947820.
KEGGi ecj:Y75_p3859.
eco:b3317.
PATRICi 32122066. VBIEscCol129921_3410.

Organism-specific databases

EchoBASEi EB0858.
EcoGenei EG10865. rplB.

Phylogenomic databases

eggNOGi COG0090.
HOGENOMi HOG000232982.
KOi K02886.
OMAi SAMNPID.
OrthoDBi EOG6TR0J1.
PhylomeDBi P60422.

Enzyme and pathway databases

BioCyci EcoCyc:EG10865-MONOMER.
ECOL316407:JW3279-MONOMER.

Miscellaneous databases

EvolutionaryTracei P60422.
PROi P60422.

Gene expression databases

Genevestigatori P60422.

Family and domain databases

Gene3Di 2.30.30.30. 1 hit.
2.40.50.140. 1 hit.
4.10.950.10. 1 hit.
HAMAPi MF_01320_B. Ribosomal_L2_B.
InterProi IPR012340. NA-bd_OB-fold.
IPR022666. Rbsml_prot_L2_RNA-bd_dom.
IPR014722. Rib_L2_dom2.
IPR002171. Ribosomal_L2.
IPR005880. Ribosomal_L2_bac/org-type.
IPR022669. Ribosomal_L2_C.
IPR022671. Ribosomal_L2_CS.
IPR014726. Ribosomal_L2_dom3.
IPR008991. Translation_prot_SH3-like.
[Graphical view ]
PANTHERi PTHR13691. PTHR13691. 1 hit.
PTHR13691:SF5. PTHR13691:SF5. 1 hit.
Pfami PF00181. Ribosomal_L2. 1 hit.
PF03947. Ribosomal_L2_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF002158. Ribosomal_L2. 1 hit.
SUPFAMi SSF50104. SSF50104. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR01171. rplB_bact. 1 hit.
PROSITEi PS00467. RIBOSOMAL_L2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the Escherichia coli S10 ribosomal protein operon."
    Zurawski G., Zurawski S.M.
    Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "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.
  4. "The primary structure of protein L2 from the Escherichia coli ribosome."
    Kimura M., Mende L., Wittmann-Liebold B.
    FEBS Lett. 149:304-312(1982)
    Cited for: PROTEIN SEQUENCE OF 2-273.
  5. "Protein-rRNA binding features and their structural and functional implications in ribosomes as determined by cross-linking studies."
    Urlaub H., Kruft V., Bischof O., Mueller E.-C., Wittmann-Liebold B.
    EMBO J. 14:4578-4588(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 60-71 AND 200-208, CROSS-LINKING TO RRNA.
    Strain: MRE-600.
  6. "Incorporation of six additional proteins to complete the assembly map of the 50 S subunit from Escherichia coli ribosomes."
    Herold M., Nierhaus K.H.
    J. Biol. Chem. 262:8826-8833(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSEMBLY MAP OF THE 50S SUBUNIT.
    Strain: K12.
  7. "Histidine 229 in protein L2 is apparently essential for 50S peptidyl transferase activity."
    Cooperman B.S., Wooten T., Romero D.P., Traut R.R.
    Biochem. Cell Biol. 73:1087-1094(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF HIS-230.
  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. "Functional implications of ribosomal protein L2 in protein biosynthesis as shown by in vivo replacement studies."
    Uehlein M., Wegloehner W., Urlaub H., Wittmann-Liebold B.
    Biochem. J. 331:423-430(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN REPLACEMENT STUDIES.
  10. "Ribosomal protein L2 is involved in the association of the ribosomal subunits, tRNA binding to A and P sites and peptidyl transfer."
    Diedrich G., Spahn C.M.T., Stelzl U., Schaefer M.A., Wooten T., Bochkariov D.E., Cooperman B.S., Traut R.R., Nierhaus K.H.
    EMBO J. 19:5241-5250(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REQUIREMENT FOR 70S RIBOSOME FORMATION, TRNA-BINDING, MUTAGENESIS OF CONSERVED RESIDUES.
  11. "Localization of the protein L2 in the 50 S subunit and the 70 S E. coli ribosome."
    Willumeit R., Forthmann S., Beckmann J., Diedrich G., Ratering R., Stuhrmann H.B., Nierhaus K.H.
    J. Mol. Biol. 305:167-177(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSITION IN THE 50S SUBUNIT AND 70S RIBOSOME.
    Strain: MRE-600.
  12. "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.
  13. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
    Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
    Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-242, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
  14. "The 3D arrangement of the 23 S and 5 S rRNA in the Escherichia coli 50 S ribosomal subunit based on a cryo-electron microscopic reconstruction at 7.5 A resolution."
    Mueller F., Sommer I., Baranov P., Matadeen R., Stoldt M., Woehnert J., Goerlach M., van Heel M., Brimacombe R.
    J. Mol. Biol. 298:35-59(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  15. "Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement."
    Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.
    Cell 113:789-801(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), INTERSUBUNIT BRIDGE FORMATION.
    Strain: MRE-600.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL2_ECOLI
AccessioniPrimary (citable) accession number: P60422
Secondary accession number(s): P02387, Q2M6Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein can be partially replaced in vivo by its H.marismortui (HmaL2) or human (L8, from the 60S cytoplasmic ribosome) homolog.

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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