A7E56F29C4D985B227868DCAE3CA685AE7B93392092B7DD500FB708D9363638D1A9019DB60F9FAB5638378C66A1510F1

Phosphorylation on serine residues enhances its DNA-binding activity and stimulates transcription repression. Acetylation of Lys-130 contributes to its nuclear localization and enhances its interaction with KPNB1. Deacetylated by HDAC3. Poly-ADP-ribosylation reduces its DNA-binding activity (By similarity).

Source:http://purl.uniprot.org/SHA-384/A7E56F29C4D985B227868DCAE3CA685AE7B93392092B7DD500FB708D9363638D1A9019DB60F9FAB5638378C66A1510F1

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Statements in which the resource exists as a object.
Subject	Predicate
uniprot-protein:Q03255, uniprot-protein:Q863D9, uniprot-protein:Q863C2, uniprot-protein:Q863B7, uniprot-protein:Q863C0, uniprot-protein:P36389, uniprot-protein:Q864R2, uniprot-protein:Q864R1, uniprot-protein:Q864R0, uniprot-protein:Q864Q9, uniprot-protein:Q8SPQ2, uniprot-protein:Q27949, uniprot-protein:Q7JGF9, uniprot-protein:Q7JGF7, uniprot-protein:Q8SPQ1, uniprot-protein:Q9XS37, uniprot-protein:Q69FB1, uniprot-protein:Q9BH08, uniprot-protein:Q864P9, uniprot-protein:Q864Q3, uniprot-protein:Q864P4, uniprot-protein:Q864P7, uniprot-protein:Q864Q5, uniprot-protein:Q864P8, uniprot-protein:Q864Q8, uniprot-protein:Q864Q4, uniprot-protein:Q67EX7, uniprot-protein:Q67EX6, uniprot-protein:Q864Q0	uniprot:annotation