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  1. 1
    "Identification of two novel human putative serine/threonine kinases, VRK1 and VRK2, with structural similarity to Vaccinia virus B1R kinase."
    Nezu J., Oku A., Jones M.H., Shimane M.
    Genomics 45:327-331(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Category: Expression, Sequences.
    Tissue: Fetal liver.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  2. 2
    "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Category: Sequences.
    Tissue: Brain and Lung.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 50477 other entries.

  3. 3
    "The human vaccinia-related kinase 1 (VRK1) phosphorylates threonine-18 within the mdm-2 binding site of the p53 tumour suppressor protein."
    Lopez-Borges S., Lazo P.A.
    Oncogene 19:3656-3664(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, MUTAGENESIS OF SER-14; THR-102; SER-125; SER-150; SER-158; SER-239; THR-305; THR-312; THR-355 AND THR-390.
    Category: Function, Subcellular Location, Pathology & Biotech, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 and mapped to 11 other entries.

  4. 4
    "Kinetic properties of p53 phosphorylation by the human vaccinia-related kinase 1."
    Barcia R., Lopez-Borges S., Vega F.M., Lazo P.A.
    Arch. Biochem. Biophys. 399:1-5(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-355, ACTIVITY REGULATION.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is mapped to 1 other entry.

  5. 5
    "Characterization of three paralogous members of the Mammalian vaccinia related kinase family."
    Nichols R.J., Traktman P.
    J. Biol. Chem. 279:7934-7946(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    Category: Function, Subcellular Location, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 5 and mapped to 28 other entries.

  6. 6
    "Human vaccinia-related kinase 1 (VRK1) activates the ATF2 transcriptional activity by novel phosphorylation on Thr-73 and Ser-62 and cooperates with JNK."
    Sevilla A., Santos C.R., Vega F.M., Lazo P.A.
    J. Biol. Chem. 279:27458-27465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
    Category: Function, Subcellular Location.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  7. 7
    "The subcellular localization of vaccinia-related kinase-2 (VRK2) isoforms determines their different effect on p53 stability in tumour cell lines."
    Blanco S., Klimcakova L., Vega F.M., Lazo P.A.
    FEBS J. 273:2487-2504(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
    Category: Subcellular Location.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3 and mapped to 150 other entries.

  8. 8
    "The vaccinia-related kinases phosphorylate the N' terminus of BAF, regulating its interaction with DNA and its retention in the nucleus."
    Nichols R.J., Wiebe M.S., Traktman P.
    Mol. Biol. Cell 17:2451-2464(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 and mapped to 5 other entries.

  9. 9
    "Proteomics identification of nuclear Ran GTPase as an inhibitor of human VRK1 and VRK2 (vaccinia-related kinase) activities."
    Sanz-Garcia M., Lopez-Sanchez I., Lazo P.A.
    Mol. Cell. Proteomics 7:2199-2214(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAN, ACTIVITY REGULATION.
    Category: Function, Subcellular Location, Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3 and mapped to 7 other entries.

  10. 10
    "Spinal muscular atrophy with pontocerebellar hypoplasia is caused by a mutation in the VRK1 gene."
    Renbaum P., Kellerman E., Jaron R., Geiger D., Segel R., Lee M., King M.C., Levy-Lahad E.
    Am. J. Hum. Genet. 85:281-289(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN PCH1A.
    Category: Pathology & Biotech.
    Source: UniProtKB/Swiss-Prot (reviewed).
  11. 11
    "Plk3 interacts with and specifically phosphorylates VRK1 in Ser342, a downstream target in a pathway that induces Golgi fragmentation."
    Lopez-Sanchez I., Sanz-Garcia M., Lazo P.A.
    Mol. Cell. Biol. 29:1189-1201(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-342, MUTAGENESIS OF LYS-179 AND SER-342.
    Category: Function, Pathology & Biotech, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 and mapped to 3 other entries.

  12. 12
    "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 7259 and mapped to 5 other entries.

  13. 13
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 18098 other entries.

  14. 14
    "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342; SER-376 AND THR-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: PTM / Processing, Sequences.
    Tissue: Erythroleukemia.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 13318 other entries.

  15. 15
    "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: Sequences.
    Tissue: Liver.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 11541 other entries.

  16. 16
    "Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation."
    Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., Nielsen M.L.
    Nat. Struct. Mol. Biol. 24:325-336(2017) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Category: PTM / Processing, Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3540 other entries.

  17. 17
    "Human vaccinia-related kinase 1."
    Structural genomics consortium (SGC)
    Submitted (SEP-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 3-364 IN COMPLEX WITH INHIBITOR.
    Category: Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  18. 18
    "NMR solution structure of human vaccinia-related kinase 1 (VRK1) reveals the C-terminal tail essential for its structural stability and autocatalytic activity."
    Shin J., Chakraborty G., Bharatham N., Kang C., Tochio N., Koshiba S., Kigawa T., Kim W., Kim K.T., Yoon H.S.
    J. Biol. Chem. 286:22131-22138(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-342 AND THR-353, AUTOPHOSPHORYLATION.
    Category: Function, Pathology & Biotech, PTM / Processing, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).
  19. 19
    "Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex."
    Zheng R., Ghirlando R., Lee M.S., Mizuuchi K., Krause M., Craigie R.
    Proc. Natl. Acad. Sci. U.S.A. 97:8997-9002(2000) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: PathwayImported.
    Source: Reactome:R-HSA-2528998.

    This publication is mapped to 8 other entries.

  20. 20
    "LAP2 binds to BAF.DNA complexes: requirement for the LEM domain and modulation by variable regions."
    Shumaker D.K., Lee K.K., Tanhehco Y.C., Craigie R., Wilson K.L.
    EMBO J. 20:1754-1764(2001) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: PathwayImported.
    Source: Reactome:R-HSA-2528998.

    This publication is mapped to 8 other entries.

  21. 21
    "BAF is required for emerin assembly into the reforming nuclear envelope."
    Haraguchi T., Koujin T., Segura-Totten M., Lee K.K., Matsuoka Y., Yoneda Y., Wilson K.L., Hiraoka Y.
    J. Cell Sci. 114:4575-4585(2001) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: PathwayImported.
    Source: Reactome:R-HSA-2528998.

    This publication is cited by 1 and mapped to 8 other entries.

  22. 22
    "Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro."
    Holaska J.M., Lee K.K., Kowalski A.K., Wilson K.L.
    J. Biol. Chem. 278:6969-6975(2003) [PubMed] [Europe PMC] [Abstract]
    Category: Function.
    Annotation: PathwayImported.
    Source: Reactome:R-HSA-2528998.

    This publication is cited by 1 and mapped to 11 other entries.

  23. 23
    "Members of a novel family of mammalian protein kinases complement the DNA-negative phenotype of a vaccinia virus ts mutant defective in the B1 kinase."
    Boyle K.A., Traktman P.
    J. Virol. 78:1992-2005(2004) [PubMed] [Europe PMC] [Abstract]
    Category: Function, Pathology & Biotech.
    Annotation: can perform the functions of B1 kinase required for vaccinia virus genome replication most likely due to overlapping specificity for cellular and/or viral substratesImported.
    Source: GeneRIF:7443.

    This publication is mapped to 5 other entries.

  24. 24
    "c-Jun phosphorylation by the human vaccinia-related kinase 1 (VRK1) and its cooperation with the N-terminal kinase of c-Jun (JNK)."
    Sevilla A., Santos C.R., Barcia R., Vega F.M., Lazo P.A.
    Oncogene 23:8950-8958(2004) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Annotation: c-Jun is phosphorylated by the human vaccinia-related kinase 1 (VRK1) and cooperates with the N-terminal kinase of c-Jun (JNK)Imported.
    Source: GeneRIF:7443, IntAct:Q99986.

    This publication is mapped to 3 other entries.

  25. 25
    "p53 Stabilization and accumulation induced by human vaccinia-related kinase 1."
    Vega F.M., Sevilla A., Lazo P.A.
    Mol. Cell. Biol. 24:10366-10380(2004) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Annotation: VRK1 is the first step in a new pathway regulating p53 activity during cell proliferationImported.
    Source: GeneRIF:7443, IntAct:Q99986.

    This publication is mapped to 145 other entries.

1 to 25 of 70  Show
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