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P60438

- RL3_ECOLI

UniProt

P60438 - RL3_ECOLI

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
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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

    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

    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-methylglutamine2 Publications

    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 – 85
    Beta strandi12 – 154
    Turni17 – 193
    Beta strandi21 – 288
    Beta strandi32 – 387
    Turni41 – 433
    Beta strandi47 – 515
    Helixi57 – 593
    Helixi62 – 698
    Beta strandi70 – 723
    Beta strandi80 – 834
    Turni91 – 933
    Helixi98 – 1014
    Beta strandi103 – 1053
    Beta strandi106 – 1127
    Beta strandi115 – 1184
    Turni121 – 1255
    Beta strandi132 – 1354
    Beta strandi136 – 1383
    Beta strandi140 – 1423
    Turni150 – 1523
    Helixi155 – 1573
    Beta strandi162 – 1643
    Beta strandi166 – 1683
    Beta strandi177 – 1815
    Turni182 – 1854
    Beta strandi186 – 1916
    Beta strandi194 – 1963
    Beta strandi200 – 2034

    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[»]
    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.
    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

    MIGLVGKKVG MTRIFTEDGV SIPVTVIEVE ANRVTQVKDL ANDGYRAIQV    50
    TTGAKKANRV TKPEAGHFAK AGVEAGRGLW EFRLAEGEEF TVGQSISVEL 100
    FADVKKVDVT GTSKGKGFAG TVKRWNFRTQ DATHGNSLSH RVPGSIGQNQ 150
    TPGKVFKGKK MAGQMGNERV TVQSLDVVRV DAERNLLLVK GAVPGATGSD 200
    LIVKPAVKA 209
    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 [» ]
    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.
    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

    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 1, 2014
    This is version 114 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