PROTEIN SEQUENCE OF 228-241 AND 297-310, PHOSPHORYLATION AT SER-230 BY CAMK2, PHOSPHORYLATION AT SER-303 AND SER-307, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-230, DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY
PHOSPHORYLATION AT SER-303 AND SER-307, FUNCTION, DOMAIN, MUTAGENESIS OF ARG-296; VAL-297; LYS-298; GLU-299; GLU-300; SER-303; SER-307; ARG-309 AND GLU-311, IDENTIFICATION BY MASS SPECTROMETRY
PHOSPHORYLATION AT SER-275; SER-303 BY GSK3B AND SER-307 BY MAPK3, FUNCTION, DNA-BINDING, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-275; SER-303 AND SER-307
INTERACTION WITH MAPK3 AND MAPK8, PHOSPHORYLATION AT SER-363 BY MAPK8, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF SER-363, IDENTIFICATION BY MASS SPECTROMETRY
SUMOYLATION AT LYS-298, PHOSPHORYLATION AT SER-303, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-91; LYS-126; LYS-150; LYS-162; SER-230; LYS-298; SER-303; SER-307; SER-363 AND LYS-381, IDENTIFICATION BY MASS SPECTROMETRY
PHOSPHORYLATION AT SER-121; SER-230; SER-292; SER-303; SER-307; SER-314; SER-319; SER-326; SER-344; SER-363; SER-419 AND SER-444, MUTAGENESIS OF SER-326, IDENTIFICATION BY MASS SPECTROMETRY
INTERACTION WITH PLK1 AND HSP90 PROTEINS, PHOSPHORYLATION AT SER-419 BY PLK1, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-292; SER-314; SER-319; SER-326 AND SER-419
PHOSPHORYLATION AT SER-121 BY MAPKAPK2, FUNCTION, INTERACTION WITH HSP90 PROTEINS AND MAPKAPK2, MUTAGENESIS OF THR-120; SER-121; SER-123; THR-124; THR-527 AND SER-529, IDENTIFICATION BY MASS SPECTROMETRY
FUNCTION IN MITOTIC PROGRESSION REGULATION, INTERACTION WITH BTRC; CDC20; MAD2L1 AND PLK1, PHOSPHORYLATION AT SER-216 BY PLK1, SUBCELLULAR LOCATION, UBIQUITINATION, PROTEASOMAL DEGRADATION, MUTAGENESIS OF SER-216; SER-230; SER-303; SER-307 AND SER-419
ACETYLATION AT LYS-80; LYS-91; LYS-118; LYS-150; LYS-188; LYS-208; LYS-298 AND LYS-524, PHOSPHORYLATION, UBIQUITINATION, PROTEASOMAL DEGRADATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-80; LYS-118; LYS-208 AND LYS-298, IDENTIFICATION BY MASS SPECTROMETRY
DEPHOSPHORYLATION AT SER-121; SER-307; SER-314; THR-323 AND THR-367 BY PPP2CA, ACETYLATION AT LYS-118, IDENTIFICATION IN COMPLEX WITH IER5 AND PPP2CA, INTERACTION WITH HSP90AA1 AND IER5, FUNCTION, SUBUNIT, DNA-BINDING, MUTAGENESIS OF SER-121; SER-307; SER-314; THR-323 AND THR-367
These findings indicate that activation of HSF1 at Ser326 residue and transcription of HSP27 is related to the maintenance of gynecological CSCs/CICs., Phosphorylation
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