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P60438

- RL3_ECOLI

UniProt

P60438 - RL3_ECOLI

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Protein

50S ribosomal protein L3

Gene

rplC

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

One of two assembly initiator proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.

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:EG10866-MONOMER.
ECOL316407:JW3282-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
50S ribosomal protein L3
Gene namesi
Name:rplC
Ordered Locus Names:b3320, JW3282
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10866. rplC.

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 – 20920950S ribosomal protein L3PRO_0000077098Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei38 – 381N6-succinyllysine1 Publication
Modified residuei150 – 1501N5-methylglutamine1 Publication

Post-translational modificationi

Methylated by PrmB.By similarity

Keywords - PTMi

Methylation

Proteomic databases

PaxDbiP60438.
PRIDEiP60438.

Expressioni

Gene expression databases

GenevestigatoriP60438.

Interactioni

Subunit structurei

Part of the 50S ribosomal subunit. Forms a cluster with proteins L14 and L19.

Protein-protein interaction databases

DIPiDIP-10744N.
IntActiP60438. 144 interactions.
MINTiMINT-1302843.
STRINGi511145.b3320.

Structurei

Secondary structure

1
209
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Beta strandi12 – 154Combined sources
Turni17 – 193Combined sources
Beta strandi21 – 288Combined sources
Beta strandi32 – 387Combined sources
Turni41 – 433Combined sources
Beta strandi47 – 515Combined sources
Helixi57 – 593Combined sources
Helixi62 – 698Combined sources
Beta strandi70 – 723Combined sources
Beta strandi80 – 834Combined sources
Turni91 – 933Combined sources
Helixi98 – 1014Combined sources
Beta strandi103 – 1053Combined sources
Beta strandi106 – 1127Combined sources
Beta strandi115 – 1184Combined sources
Turni121 – 1255Combined sources
Beta strandi132 – 1354Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi140 – 1423Combined sources
Turni150 – 1523Combined sources
Helixi155 – 1573Combined sources
Beta strandi162 – 1643Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi177 – 1815Combined sources
Turni182 – 1854Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi194 – 1963Combined sources
Beta strandi200 – 2034Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ML5electron microscopy14.00e2-209[»]
1P85electron microscopy12.30B1-209[»]
1P86electron microscopy11.50B1-209[»]
1VS6X-ray3.46D1-209[»]
1VS8X-ray3.46D1-209[»]
1VT2X-ray3.30D1-209[»]
2AW4X-ray3.46D1-209[»]
2AWBX-ray3.46D1-209[»]
2GYAelectron microscopy15.00B1-209[»]
2GYCelectron microscopy15.00B1-209[»]
2I2TX-ray3.22D1-209[»]
2I2VX-ray3.22D1-209[»]
2J28electron microscopy8.00D1-209[»]
2QAMX-ray3.21D1-209[»]
2QAOX-ray3.21D1-209[»]
2QBAX-ray3.54D1-209[»]
2QBCX-ray3.54D1-209[»]
2QBEX-ray3.30D1-209[»]
2QBGX-ray3.30D1-209[»]
2QBIX-ray4.00D1-209[»]
2QBKX-ray4.00D1-209[»]
2QOVX-ray3.93D1-209[»]
2QOXX-ray3.93D1-209[»]
2QOZX-ray3.50D1-209[»]
2QP1X-ray3.50D1-209[»]
2RDOelectron microscopy9.10D1-209[»]
2VHMX-ray3.74D1-209[»]
2VHNX-ray3.74D1-209[»]
2WWQelectron microscopy5.80D1-209[»]
2Z4LX-ray4.45D1-209[»]
2Z4NX-ray4.45D1-209[»]
3BBXelectron microscopy10.00D1-209[»]
3DF2X-ray3.50D1-209[»]
3DF4X-ray3.50D1-209[»]
3E1Belectron microscopy-Y1-209[»]
3E1Delectron microscopy-Y1-209[»]
3FIKelectron microscopy6.70D1-209[»]
3I1NX-ray3.19D1-209[»]
3I1PX-ray3.19D1-209[»]
3I1RX-ray3.81D1-209[»]
3I1TX-ray3.81D1-209[»]
3I20X-ray3.71D1-209[»]
3I22X-ray3.71D1-209[»]
3IZTelectron microscopy-E1-209[»]
3IZUelectron microscopy-E1-209[»]
3J01electron microscopy-D1-209[»]
3J0Telectron microscopy12.10E1-209[»]
3J0Welectron microscopy14.70E1-209[»]
3J0Yelectron microscopy13.50E1-209[»]
3J11electron microscopy13.10E1-209[»]
3J12electron microscopy11.50E1-209[»]
3J14electron microscopy11.50E1-209[»]
3J19electron microscopy8.30D1-209[»]
3J37electron microscopy9.80E1-209[»]
3J4Xelectron microscopy12.00D1-209[»]
3J50electron microscopy20.00D1-209[»]
3J51electron microscopy17.00D1-209[»]
3J52electron microscopy12.00D1-209[»]
3J54electron microscopy13.00D1-209[»]
3J56electron microscopy15.00D1-209[»]
3J58electron microscopy17.00D1-209[»]
3J5Aelectron microscopy12.00D1-209[»]
3J5Celectron microscopy17.00D1-209[»]
3J5Eelectron microscopy17.00D1-209[»]
3J5Gelectron microscopy20.00D1-209[»]
3J5Ielectron microscopy15.00D1-209[»]
3J5Kelectron microscopy9.00D1-209[»]
3J5Lelectron microscopy6.60D1-209[»]
3J5Oelectron microscopy6.80D1-209[»]
3J5Uelectron microscopy7.60E1-209[»]
3J5Welectron microscopy7.60E1-209[»]
3KCRelectron microscopy-D1-209[»]
3OASX-ray3.25D1-209[»]
3OATX-ray3.25D1-209[»]
3OFCX-ray3.19D1-209[»]
3OFDX-ray3.19D1-209[»]
3OFQX-ray3.10D1-209[»]
3OFRX-ray3.10D1-209[»]
3OFZX-ray3.29D1-209[»]
3OG0X-ray3.29D1-209[»]
3ORBX-ray3.30D1-209[»]
3R8SX-ray3.00D1-209[»]
3R8TX-ray3.00D1-209[»]
3SGFX-ray3.20D1-209[»]
3UOSX-ray3.70D1-209[»]
4CSUelectron microscopy5.50D1-209[»]
4GARX-ray3.30D1-209[»]
4GAUX-ray3.30D1-209[»]
4KIXX-ray2.90D1-209[»]
4KIZX-ray2.90D1-209[»]
4KJ1X-ray2.90D1-209[»]
4KJ3X-ray2.90D1-209[»]
4KJ5X-ray2.90D1-209[»]
4KJ7X-ray2.90D1-209[»]
4KJ9X-ray2.90D1-209[»]
4KJBX-ray2.90D1-209[»]
4PEBX-ray2.95D1-209[»]
4PECX-ray2.95D1-209[»]
4TOMX-ray3.00D1-209[»]
4TOOX-ray3.00D1-209[»]
4TOVX-ray2.90D1-209[»]
4TOXX-ray2.90D1-209[»]
4TP1X-ray2.90D1-209[»]
4TP3X-ray2.90D1-209[»]
4TP5X-ray2.90D1-209[»]
4TP7X-ray2.90D1-209[»]
4TP9X-ray2.80D1-209[»]
4TPBX-ray2.80D1-209[»]
4TPDX-ray2.80D1-209[»]
4TPFX-ray2.80D1-209[»]
ProteinModelPortaliP60438.
SMRiP60438. Positions 1-209.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60438.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L3P family.Curated

Phylogenomic databases

eggNOGiCOG0087.
HOGENOMiHOG000100368.
InParanoidiP60438.
KOiK02906.
OMAiSMQDATH.
OrthoDBiEOG6WDSMH.
PhylomeDBiP60438.

Family and domain databases

HAMAPiMF_01325_B. Ribosomal_L3_B.
InterProiIPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PANTHERiPTHR11229. PTHR11229. 1 hit.
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
TIGRFAMsiTIGR03625. L3_bact. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P60438-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIGLVGKKVG MTRIFTEDGV SIPVTVIEVE ANRVTQVKDL ANDGYRAIQV
60 70 80 90 100
TTGAKKANRV TKPEAGHFAK AGVEAGRGLW EFRLAEGEEF TVGQSISVEL
110 120 130 140 150
FADVKKVDVT GTSKGKGFAG TVKRWNFRTQ DATHGNSLSH RVPGSIGQNQ
160 170 180 190 200
TPGKVFKGKK MAGQMGNERV TVQSLDVVRV DAERNLLLVK GAVPGATGSD

LIVKPAVKA
Length:209
Mass (Da):22,244
Last modified:July 21, 1986 - v1
Checksum:iEA8E10EDD2C0A8FD
GO

Mass spectrometryi

Molecular mass is 22257.2 Da from positions 1 - 209. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02613 Genomic DNA. Translation: CAA26460.1.
U18997 Genomic DNA. Translation: AAA58117.1.
U00096 Genomic DNA. Translation: AAC76345.1.
AP009048 Genomic DNA. Translation: BAE77971.1.
V00344 Genomic DNA. Translation: CAA23634.1.
PIRiA02757. R5EC3.
RefSeqiNP_417779.1. NC_000913.3.
YP_492112.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76345; AAC76345; b3320.
BAE77971; BAE77971; BAE77971.
GeneIDi12932298.
947817.
KEGGiecj:Y75_p3856.
eco:b3320.
PATRICi32122072. VBIEscCol129921_3413.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X02613 Genomic DNA. Translation: CAA26460.1 .
U18997 Genomic DNA. Translation: AAA58117.1 .
U00096 Genomic DNA. Translation: AAC76345.1 .
AP009048 Genomic DNA. Translation: BAE77971.1 .
V00344 Genomic DNA. Translation: CAA23634.1 .
PIRi A02757. R5EC3.
RefSeqi NP_417779.1. NC_000913.3.
YP_492112.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ML5 electron microscopy 14.00 e 2-209 [» ]
1P85 electron microscopy 12.30 B 1-209 [» ]
1P86 electron microscopy 11.50 B 1-209 [» ]
1VS6 X-ray 3.46 D 1-209 [» ]
1VS8 X-ray 3.46 D 1-209 [» ]
1VT2 X-ray 3.30 D 1-209 [» ]
2AW4 X-ray 3.46 D 1-209 [» ]
2AWB X-ray 3.46 D 1-209 [» ]
2GYA electron microscopy 15.00 B 1-209 [» ]
2GYC electron microscopy 15.00 B 1-209 [» ]
2I2T X-ray 3.22 D 1-209 [» ]
2I2V X-ray 3.22 D 1-209 [» ]
2J28 electron microscopy 8.00 D 1-209 [» ]
2QAM X-ray 3.21 D 1-209 [» ]
2QAO X-ray 3.21 D 1-209 [» ]
2QBA X-ray 3.54 D 1-209 [» ]
2QBC X-ray 3.54 D 1-209 [» ]
2QBE X-ray 3.30 D 1-209 [» ]
2QBG X-ray 3.30 D 1-209 [» ]
2QBI X-ray 4.00 D 1-209 [» ]
2QBK X-ray 4.00 D 1-209 [» ]
2QOV X-ray 3.93 D 1-209 [» ]
2QOX X-ray 3.93 D 1-209 [» ]
2QOZ X-ray 3.50 D 1-209 [» ]
2QP1 X-ray 3.50 D 1-209 [» ]
2RDO electron microscopy 9.10 D 1-209 [» ]
2VHM X-ray 3.74 D 1-209 [» ]
2VHN X-ray 3.74 D 1-209 [» ]
2WWQ electron microscopy 5.80 D 1-209 [» ]
2Z4L X-ray 4.45 D 1-209 [» ]
2Z4N X-ray 4.45 D 1-209 [» ]
3BBX electron microscopy 10.00 D 1-209 [» ]
3DF2 X-ray 3.50 D 1-209 [» ]
3DF4 X-ray 3.50 D 1-209 [» ]
3E1B electron microscopy - Y 1-209 [» ]
3E1D electron microscopy - Y 1-209 [» ]
3FIK electron microscopy 6.70 D 1-209 [» ]
3I1N X-ray 3.19 D 1-209 [» ]
3I1P X-ray 3.19 D 1-209 [» ]
3I1R X-ray 3.81 D 1-209 [» ]
3I1T X-ray 3.81 D 1-209 [» ]
3I20 X-ray 3.71 D 1-209 [» ]
3I22 X-ray 3.71 D 1-209 [» ]
3IZT electron microscopy - E 1-209 [» ]
3IZU electron microscopy - E 1-209 [» ]
3J01 electron microscopy - D 1-209 [» ]
3J0T electron microscopy 12.10 E 1-209 [» ]
3J0W electron microscopy 14.70 E 1-209 [» ]
3J0Y electron microscopy 13.50 E 1-209 [» ]
3J11 electron microscopy 13.10 E 1-209 [» ]
3J12 electron microscopy 11.50 E 1-209 [» ]
3J14 electron microscopy 11.50 E 1-209 [» ]
3J19 electron microscopy 8.30 D 1-209 [» ]
3J37 electron microscopy 9.80 E 1-209 [» ]
3J4X electron microscopy 12.00 D 1-209 [» ]
3J50 electron microscopy 20.00 D 1-209 [» ]
3J51 electron microscopy 17.00 D 1-209 [» ]
3J52 electron microscopy 12.00 D 1-209 [» ]
3J54 electron microscopy 13.00 D 1-209 [» ]
3J56 electron microscopy 15.00 D 1-209 [» ]
3J58 electron microscopy 17.00 D 1-209 [» ]
3J5A electron microscopy 12.00 D 1-209 [» ]
3J5C electron microscopy 17.00 D 1-209 [» ]
3J5E electron microscopy 17.00 D 1-209 [» ]
3J5G electron microscopy 20.00 D 1-209 [» ]
3J5I electron microscopy 15.00 D 1-209 [» ]
3J5K electron microscopy 9.00 D 1-209 [» ]
3J5L electron microscopy 6.60 D 1-209 [» ]
3J5O electron microscopy 6.80 D 1-209 [» ]
3J5U electron microscopy 7.60 E 1-209 [» ]
3J5W electron microscopy 7.60 E 1-209 [» ]
3KCR electron microscopy - D 1-209 [» ]
3OAS X-ray 3.25 D 1-209 [» ]
3OAT X-ray 3.25 D 1-209 [» ]
3OFC X-ray 3.19 D 1-209 [» ]
3OFD X-ray 3.19 D 1-209 [» ]
3OFQ X-ray 3.10 D 1-209 [» ]
3OFR X-ray 3.10 D 1-209 [» ]
3OFZ X-ray 3.29 D 1-209 [» ]
3OG0 X-ray 3.29 D 1-209 [» ]
3ORB X-ray 3.30 D 1-209 [» ]
3R8S X-ray 3.00 D 1-209 [» ]
3R8T X-ray 3.00 D 1-209 [» ]
3SGF X-ray 3.20 D 1-209 [» ]
3UOS X-ray 3.70 D 1-209 [» ]
4CSU electron microscopy 5.50 D 1-209 [» ]
4GAR X-ray 3.30 D 1-209 [» ]
4GAU X-ray 3.30 D 1-209 [» ]
4KIX X-ray 2.90 D 1-209 [» ]
4KIZ X-ray 2.90 D 1-209 [» ]
4KJ1 X-ray 2.90 D 1-209 [» ]
4KJ3 X-ray 2.90 D 1-209 [» ]
4KJ5 X-ray 2.90 D 1-209 [» ]
4KJ7 X-ray 2.90 D 1-209 [» ]
4KJ9 X-ray 2.90 D 1-209 [» ]
4KJB X-ray 2.90 D 1-209 [» ]
4PEB X-ray 2.95 D 1-209 [» ]
4PEC X-ray 2.95 D 1-209 [» ]
4TOM X-ray 3.00 D 1-209 [» ]
4TOO X-ray 3.00 D 1-209 [» ]
4TOV X-ray 2.90 D 1-209 [» ]
4TOX X-ray 2.90 D 1-209 [» ]
4TP1 X-ray 2.90 D 1-209 [» ]
4TP3 X-ray 2.90 D 1-209 [» ]
4TP5 X-ray 2.90 D 1-209 [» ]
4TP7 X-ray 2.90 D 1-209 [» ]
4TP9 X-ray 2.80 D 1-209 [» ]
4TPB X-ray 2.80 D 1-209 [» ]
4TPD X-ray 2.80 D 1-209 [» ]
4TPF X-ray 2.80 D 1-209 [» ]
ProteinModelPortali P60438.
SMRi P60438. Positions 1-209.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10744N.
IntActi P60438. 144 interactions.
MINTi MINT-1302843.
STRINGi 511145.b3320.

Chemistry

ChEMBLi CHEMBL2363135.

Proteomic databases

PaxDbi P60438.
PRIDEi P60438.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76345 ; AAC76345 ; b3320 .
BAE77971 ; BAE77971 ; BAE77971 .
GeneIDi 12932298.
947817.
KEGGi ecj:Y75_p3856.
eco:b3320.
PATRICi 32122072. VBIEscCol129921_3413.

Organism-specific databases

EchoBASEi EB0859.
EcoGenei EG10866. rplC.

Phylogenomic databases

eggNOGi COG0087.
HOGENOMi HOG000100368.
InParanoidi P60438.
KOi K02906.
OMAi SMQDATH.
OrthoDBi EOG6WDSMH.
PhylomeDBi P60438.

Enzyme and pathway databases

BioCyci EcoCyc:EG10866-MONOMER.
ECOL316407:JW3282-MONOMER.

Miscellaneous databases

EvolutionaryTracei P60438.
PROi P60438.

Gene expression databases

Genevestigatori P60438.

Family and domain databases

HAMAPi MF_01325_B. Ribosomal_L3_B.
InterProi IPR000597. Ribosomal_L3.
IPR019927. Ribosomal_L3_bac/org-type.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view ]
PANTHERi PTHR11229. PTHR11229. 1 hit.
Pfami PF00297. Ribosomal_L3. 1 hit.
[Graphical view ]
SUPFAMi SSF50447. SSF50447. 1 hit.
TIGRFAMsi TIGR03625. L3_bact. 1 hit.
PROSITEi PS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of ribosomal protein L3 from Escherichia coli 70 S ribosomes."
    Muranova T.A., Muranov A.V., Markova L.F., Ovchinnikov Y.A.
    FEBS Lett. 96:301-305(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, METHYLATION AT GLN-150.
    Strain: MRE-600.
  2. "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].
  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. "Regulation of the S10 ribosomal protein operon in E. coli: nucleotide sequence at the start of the operon."
    Olins P.O., Nomura M.
    Cell 26:205-211(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-80.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-12.
    Strain: K12 / EMG2.
  7. "Initiator proteins for the assembly of the 50S subunit from Escherichia coli ribosomes."
    Nowotny V., Nierhaus K.H.
    Proc. Natl. Acad. Sci. U.S.A. 79:7238-7242(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS AN ASSEMBLY INITIATOR PROTEIN.
  8. "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.
  9. "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.
  10. "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.
  11. "The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors."
    Heurgue-Hamard V., Champ S., Engstroem A., Ehrenberg M., Buckingham R.H.
    EMBO J. 21:769-778(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION BY PRMB.
    Strain: K12.
  12. "Identification of lysine succinylation as a new post-translational modification."
    Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
    Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION AT LYS-38.
    Strain: K12.
  13. "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).
    Strain: MRE-600.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES.
    Strain: MRE-600.

Entry informationi

Entry nameiRL3_ECOLI
AccessioniPrimary (citable) accession number: P60438
Secondary accession number(s): P02386, Q2M6Y5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 115 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