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  1. 1
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3992 other entries.

  2. 2
    "An FHA phosphoprotein recognition domain mediates protein EmbR phosphorylation by PknH, a Ser/Thr protein kinase from Mycobacterium tuberculosis."
    Molle V., Kremer L., Girard-Blanc C., Besra G.S., Cozzone A.J., Prost J.F.
    Biochemistry 42:15300-15309(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, PHOSPHORYLATION AT THR-170, MUTAGENESIS OF LYS-45 AND THR-170.
    Category: Function, Pathology & Biotech, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  3. 3
    "PknH, a transmembrane Hank's type serine/threonine kinase from Mycobacterium tuberculosis is differentially expressed under stress conditions."
    Sharma K., Chandra H., Gupta P.K., Pathak M., Narayan A., Meena L.S., D'Souza R.C., Chopra P., Ramachandran S., Singh Y.
    FEMS Microbiol. Lett. 233:107-113(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, SUBCELLULAR LOCATION, INDUCTION, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-45.
    Category: Function, Subcellular Location, Pathology & Biotech, PTM / Processing, Expression.
    Source: UniProtKB/Swiss-Prot (reviewed).
  4. 4
    "Deletion of the Mycobacterium tuberculosis pknH gene confers a higher bacillary load during the chronic phase of infection in BALB/c mice."
    Papavinasasundaram K.G., Chan B., Chung J.H., Colston M.J., Davis E.O., Av-Gay Y.
    J. Bacteriol. 187:5751-5760(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Category: Function, Pathology & Biotech.
    Source: UniProtKB/Swiss-Prot (reviewed).
  5. 5
    "EmbR, a regulatory protein with ATPase activity, is a substrate of multiple serine/threonine kinases and phosphatase in Mycobacterium tuberculosis."
    Sharma K., Gupta M., Krupa A., Srinivasan N., Singh Y.
    FEBS J. 273:2711-2721(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A KINASE WITH EMBR AS SUBSTRATE, DEPHOSPHORYLATION BY PSTP.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3 other entries.

  6. 6
    "Transcriptional control of the mycobacterial embCAB operon by PknH through a regulatory protein, EmbR, in vivo."
    Sharma K., Gupta M., Pathak M., Gupta N., Koul A., Sarangi S., Baweja R., Singh Y.
    J. Bacteriol. 188:2936-2944(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INDUCTION.
    Category: Function, Expression.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 4 other entries.

  7. 7
    "Characterization of the phosphorylation sites of Mycobacterium tuberculosis serine/threonine protein kinases, PknA, PknD, PknE, and PknH by mass spectrometry."
    Molle V., Zanella-Cleon I., Robin J.P., Mallejac S., Cozzone A.J., Becchi M.
    Proteomics 6:3754-3766(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
    Category: PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3 other entries.

  8. 8
    "Novel substrates of Mycobacterium tuberculosis PknH Ser/Thr kinase."
    Zheng X., Papavinasasundaram K.G., Av-Gay Y.
    Biochem. Biophys. Res. Commun. 355:162-168(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  9. 9
    "Convergence of Ser/Thr and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis."
    Chao J.D., Papavinasasundaram K.G., Zheng X., Chavez-Steenbock A., Wang X., Lee G.Q., Av-Gay Y.
    J. Biol. Chem. 285:29239-29246(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  10. 10
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2871 other entries.

  11. 11
    "Structure of the sensor domain of Mycobacterium tuberculosis PknH receptor kinase reveals a conserved binding cleft."
    Cavazos A., Prigozhin D.M., Alber T.
    J. Mol. Biol. 422:488-494(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 435-626, DISULFIDE BONDS.
    Category: PTM / Processing, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  12. 12
    "An improved method to unravel phosphoacceptors in Ser/Thr protein kinase-phosphorylated substrates."
    Molle V., Leiba J., Zanella-Cleon I., Becchi M., Kremer L.
    Proteomics 10:3910-3915(2010) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:P9WI71.

    This publication is mapped to 7 other entries.

1 to 12 of 12  Show
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