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1 to 25 of 1,378  Show
  1. 1
    "Extracellular signal-regulated kinases in T cells: characterization of human ERK1 and ERK2 cDNAs."
    Owaki H., Makar R., Boulton T.G., Cobb M.H., Geppert T.D.
    Biochem. Biophys. Res. Commun. 182:1416-1422(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  2. 2
    "Heterogeneous expression of four MAP kinase isoforms in human tissues."
    Gonzalez F.A., Raden D.L., Rigby M.R., Davis R.J.
    FEBS Lett. 304:170-178(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 other entries.

  3. 3
    "Identification of dominant negative Erk1/2 variants in cancer cells."
    Cheng H., Ren S., Qiu R., Wang M., Feng Y.H.
    Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).
  4. 4
    "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1545 other entries.

  5. 5
    "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] (ISOFORM 1).
    Category: Sequences.
    Tissue: Lung.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 50495 other entries.

  6. 6
    "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-15, ACETYLATION AT ALA-2.
    Category: PTM / Processing, Sequences.
    Tissue: Platelet.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 204 other entries.

  7. 7
    "ERF: an ETS domain protein with strong transcriptional repressor activity, can suppress ets-associated tumorigenesis and is regulated by phosphorylation during cell cycle and mitogenic stimulation."
    Sgouras D.N., Athanasiou M.A., Beal G.J. Jr., Fisher R.J., Blair D.G., Mavrothalassitis G.J.
    EMBO J. 14:4781-4793(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ERF.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  8. 8
    "3pK, a new mitogen-activated protein kinase-activated protein kinase located in the small cell lung cancer tumor suppressor gene region."
    Sithanandam G., Latif F., Duh F.-M., Bernal R., Smola U., Li H., Kuzmin I., Wixler V., Geil L., Shrestha S., Lloyd P.A., Bader S., Sekido Y., Tartof K.D., Kashuba V.I., Zabarovsky E.R., Dean M., Klein G.
    , Lerman M.I., Minna J.D., Rapp U.R., Allikmets R.
    Mol. Cell. Biol. 16:868-876(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MAPKAPK3.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  9. 9
    "Human immunodeficiency virus type 1 Nef binds directly to LCK and mitogen-activated protein kinase, inhibiting kinase activity."
    Greenway A.L., Azad A., Mills J., McPhee D.A.
    J. Virol. 70:6701-6708(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 NEF.
    Category: Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 3 other entries.

  10. 10
    "MAPKAPK5, a novel mitogen-activated protein kinase (MAPK)-activated protein kinase, is a substrate of the extracellular-regulated kinase (ERK) and p38 kinase."
    Ni H., Wang X.S., Diener K., Yao Z.
    Biochem. Biophys. Res. Commun. 243:492-496(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MAPKAPK5.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 and mapped to 3 other entries.

  11. 11
    "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB."
    Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.
    EMBO J. 17:4426-4441(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RPS6KA5/MSK1.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 6 and mapped to 11 other entries.

  12. 12
    "Antigen receptor signaling induces MAP kinase-mediated phosphorylation and degradation of the BCL-6 transcription factor."
    Niu H., Ye B.H., Dalla-Favera R.
    Genes Dev. 12:1953-1961(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BCL6.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  13. 13
    "Catalytic activation of the phosphatase MKP-3 by ERK2 mitogen-activated protein kinase."
    Camps M., Nichols A., Gillieron C., Antonsson B., Muda M., Chabert C., Boschert U., Arkinstall S.
    Science 280:1262-1265(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DUSP6, FUNCTION.
    Category: Function, Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).
  14. 14
    "Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway."
    Todd J.L., Tanner K.G., Denu J.M.
    J. Biol. Chem. 274:13271-13280(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEPHOSPHORYLATION BY DUSP3.
    Category: PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 other entries.

  15. 15
    "ERK activation induces phosphorylation of Elk-1 at multiple S/T-P motifs to high stoichiometry."
    Cruzalegui F.H., Cano E., Treisman R.
    Oncogene 18:7948-7957(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ELK1.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  16. 16
    "Reduced MAP kinase phosphatase-1 degradation after p42/p44MAPK-dependent phosphorylation."
    Brondello J.M., Pouyssegur J., McKenzie F.R.
    Science 286:2514-2517(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DUSP1.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 other entries.

  17. 17
    "The mitogen-activated protein kinase signal-integrating kinase Mnk2 is a eukaryotic initiation factor 4E kinase with high levels of basal activity in mammalian cells."
    Scheper G.C., Morrice N.A., Kleijn M., Proud C.G.
    Mol. Cell. Biol. 21:743-754(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS MKNK2 KINASE.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 6 other entries.

  18. 18
    "Growth factors can activate ATF2 via a two-step mechanism: phosphorylation of Thr71 through the Ras-MEK-ERK pathway and of Thr69 through RalGDS-Src-p38."
    Ouwens D.M., de Ruiter N.D., van der Zon G.C., Carter A.P., Schouten J., van der Burgt C., Kooistra K., Bos J.L., Maassen J.A., van Dam H.
    EMBO J. 21:3782-3793(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF ATF2.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 and mapped to 4 other entries.

  19. 19
    "IEX-1: a new ERK substrate involved in both ERK survival activity and ERK activation."
    Garcia J., Ye Y., Arranz V., Letourneux C., Pezeron G., Porteu F.
    EMBO J. 21:5151-5163(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF IER3, INTERACTION WITH IER3, ENZYME REGULATION.
    Category: Function, PTM / Processing, Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 other entries.

  20. 20
    "Insulin receptor substrate 4 associates with the protein IRAS."
    Sano H., Liu S.C.H., Lane W.S., Piletz J.E., Lienhard G.E.
    J. Biol. Chem. 277:19439-19447(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NISCH.
    Category: Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 6 and mapped to 3 other entries.

  21. 21
    "EGFR and FGFR signaling through FRS2 is subject to negative feedback control by ERK1/2."
    Wu Y., Chen Z., Ullrich A.
    Biol. Chem. 384:1215-1226(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF FRS2.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 other entries.

  22. 22
    "Activation of ERK induces phosphorylation of MAPK phosphatase-7, a JNK specific phosphatase, at Ser-446."
    Masuda K., Shima H., Katagiri C., Kikuchi K.
    J. Biol. Chem. 278:32448-32456(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF DUSP16.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  23. 23
    "Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK MAPK."
    Allan L.A., Morrice N., Brady S., Magee G., Pathak S., Clarke P.R.
    Nat. Cell Biol. 5:647-654(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CASP9.
    Category: Function, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  24. 24
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH NEK2.
    Category: Subcellular Location, Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  25. 25
    "Signal transduction via the stem cell factor receptor/c-Kit."
    Ronnstrand L.
    Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON ROLE IN KIT SIGNALING.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 18 and mapped to 4 other entries.

1 to 25 of 1,378  Show