Q8VIB2
uniprot
Q8VIB2
canonical
amino_acid_sequence
MATDDSIIVLDDDDEDEAAAQPGPSNPASNPVSPGPEASGPSESHGDGGSSNSGSRKCYKLENEKLFEEFLELCKMQTSDHPEVVPFLHKLQQRAQSAFLASAEFRNILSRVLSRSRNRPAKLYVYINELCTVLKAHSIKKKLNLAPAASAESSGDNPPTDPPSDLTNTETTASEASRTRGSRRQIQRLEQLLALYVAEIQRLQEKELDLSELDDPDSSYLQEARLKRKLIRLFGRLCDLKDCSSLTGKVIEQRIPYRGTRYPEVNRRIERLINKPGPDTFPDYGDVLRAVEKAATRHSLGLPRQQLQLLAQDAFRDVGVRLQERRHLDLIYNFGCHLTDDYRPGVDPALTDPTLARRLRENRTLAMSRLDEVISKYAMMQDKSEEGERQKRRARLLATSQSSDLPKASSDSGEGPSGVASQEDPTTPKAETEDEEDDEESDDEEEEEEEEEEEATEDEDEDLEQLQEDQDDEEEEEGDNEDDKSPASPSPIFRRKEFSNPQKGSGPQEEQQERGLTGTPASPLEASPGLPSTDAESSGEQLQERLLAGESPVSQLSELDMEALPEETIPSPEERGISSSRRKSDSSLPTILENGAAMVTSTSFNGRVSSHPCRDASPPSKRFRKEKKQLGPGPLGNSYVKKQTMAQQDSGWKISVLSTPSSPLASVGPVADSSTRVDSPSHELVTSSLCNPSPSLILQTPQSQSPRPCIYKTSVATQCDPEEIIVLSDSD
uniprot
proteins
function
FUNCTION: Transcription corepressor known to repress transcriptional potential of several sumoylated transcription factors. Down-regulates basal and activated transcription. Its transcription repressor activity is modulated by recruiting it to subnuclear compartments like the nucleolus or PML/POD/ND10 nuclear bodies through interactions with MCSR1 and PML, respectively. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional activation of PAX3 and ETS1 through direct protein-protein interactions. Modulates PAX5 activity; the function seems to involve CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by regulating the RING-finger E3 ligase MDM2 ubiquitination activity. Under non-stress condition, in association with the deubiquitinating USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3 ligase activity of MDM2 towards TP53, thereby promoting TP53 ubiquitination and subsequent proteasomal degradation. Upon DNA damage, its association with MDM2 and USP7 is disrupted, resulting in increased MDM2 autoubiquitination and consequently, MDM2 degradation, which leads to TP53 stabilization. Acts as a histone chaperone that facilitates deposition of histone H3.3. Acts as a targeting component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Does not affect the ATPase activity of ATRX but alleviates its transcription repression activity. Upon neuronal activation associates with regulatory elements of selected immediate early genes where it promotes deposition of histone H3.3 which may be linked to transcriptional induction of these genes. Required for the recruitment of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested to function as regulatory sites for the incorporation of newly synthesized histone H3.3 into chromatin. Proposed to mediate activation of the JNK pathway and apoptosis via MAP3K5 in response to signaling from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis. In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated apoptosis may not involve DAXX. Plays a role as a positive regulator of the heat shock transcription factor HSF1 activity during the stress protein response (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9UER7}.
uniprot
proteins
mass_dalton
80687
uniprot
proteins
post_translational_modification
PTM: Sumoylated with SUMO1 on multiple lysine residues. {ECO:0000250}.; PTM: Repressor activity is down-regulated upon Ser-661 phosphorylation. Upon neuronal activation dephosphorylated by calcineurin in a Ca2+ dependent manner at Ser-661; dephosphorylation positively affects histone H3.3 loading and transcriptional activation (By similarity). {ECO:0000250}.; PTM: Polyubiquitinated; which is promoted by CUL3 and SPOP and results in proteasomal degradation. Ubiquitinated by MDM2; inducing its degradation. Deubiquitinated by USP7; leading to stabilize it (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
DAXX family
uniprot
proteins
pubmed
22673903
uniprot
proteins
sequence_length
731
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UER7}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9UER7}. Nucleus, PML body {ECO:0000250|UniProtKB:Q9UER7}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q9UER7}. Chromosome, centromere {ECO:0000250|UniProtKB:Q9UER7}. Note=Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear bodies. Colocalizes with a subset of interphase centromeres, but is absent from mitotic centromeres. Detected in cytoplasmic punctate structures. Translocates from the nucleus to the cytoplasm upon glucose deprivation or oxidative stress. Colocalizes with RASSF1 in the nucleus. Colocalizes with USP7 in nucleoplasma with accumulation in speckled structures. {ECO:0000250|UniProtKB:Q9UER7}.
uniprot
proteins