DAXX_MOUSE
ID DAXX_MOUSE Reviewed; 739 AA.
AC O35613; Q9QWT8; Q9QWV3;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Death domain-associated protein 6;
DE AltName: Full=Daxx;
GN Name=Daxx;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=9215629; DOI=10.1016/s0092-8674(00)80294-9;
RA Yang X., Khosravi-Far R., Chang H.Y., Baltimore D.;
RT "Daxx, a novel Fas-binding protein that activates JNK and apoptosis.";
RL Cell 89:1067-1076(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J.,
RA Lasky S., Hood L.;
RT "Sequence of the mouse major histocompatibility complex class II region.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PML.
RX PubMed=10684855; DOI=10.1084/jem.191.4.631;
RA Zhong S., Salomoni P., Ronchetti S., Guo A., Ruggero D., Pandolfi P.P.;
RT "Promyelocytic leukemia protein (PML) and Daxx participate in a novel
RT nuclear pathway for apoptosis.";
RL J. Exp. Med. 191:631-640(2000).
RN [4]
RP INTERACTION WITH HIPK3.
RX PubMed=11034606; DOI=10.1084/jem.192.8.1165;
RA Rochat-Steiner V., Becker K., Micheau O., Schneider P., Burns K.,
RA Tschopp J.;
RT "FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces
RT FADD phosphorylation and inhibits Fas-mediated Jun NH2-terminal kinase
RT activation.";
RL J. Exp. Med. 192:1165-1174(2000).
RN [5]
RP INTERACTION WITH PAX5.
RX PubMed=11799127; DOI=10.1074/jbc.m111763200;
RA Emelyanov A.V., Kovac C.R., Sepulveda M.A., Birshtein B.K.;
RT "The interaction of Pax5 (BSAP) with Daxx can result in transcriptional
RT activation in B cells.";
RL J. Biol. Chem. 277:11156-11164(2002).
RN [6]
RP INTERACTION WITH HIPK1, MUTAGENESIS OF SER-502 AND SER-669, PHOSPHORYLATION
RP AT SER-219; THR-472; SER-502; SER-515; THR-523; SER-626 AND SER-669, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12529400; DOI=10.1128/mcb.23.3.950-960.2003;
RA Ecsedy J.A., Michaelson J.S., Leder P.;
RT "Homeodomain-interacting protein kinase 1 modulates Daxx localization,
RT phosphorylation, and transcriptional activity.";
RL Mol. Cell. Biol. 23:950-960(2003).
RN [7]
RP INTERACTION WITH CBP.
RX PubMed=16287980; DOI=10.1073/pnas.0504460102;
RA Kuo H.-Y., Chang C.-C., Jeng J.-C., Hu H.-M., Lin D.-Y., Maul G.G.,
RA Kwok R.P.S., Shih H.-M.;
RT "SUMO modification negatively modulates the transcriptional activity of
RT CREB-binding protein via the recruitment of Daxx.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:16973-16978(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-687; SER-736 AND SER-738, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH HISTONE H3.3.
RX PubMed=20504901; DOI=10.1101/gad.566910;
RA Drane P., Ouararhni K., Depaux A., Shuaib M., Hamiche A.;
RT "The death-associated protein DAXX is a novel histone chaperone involved in
RT the replication-independent deposition of H3.3.";
RL Genes Dev. 24:1253-1265(2010).
RN [10]
RP FUNCTION AS HISTONE CHAPERONE.
RX PubMed=20651253; DOI=10.1073/pnas.1008850107;
RA Lewis P.W., Elsaesser S.J., Noh K.M., Stadler S.C., Allis C.D.;
RT "Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in
RT replication-independent chromatin assembly at telomeres.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:14075-14080(2010).
RN [11]
RP FUNCTION IN HISTONE H3.3 DEPOSITION, SUBCELLULAR LOCATION,
RP DEPHOSPHORYLATION AT SER-669 BY CALCINEURIN, AND DEVELOPMENTAL STAGE.
RX PubMed=22500635; DOI=10.1016/j.neuron.2012.02.021;
RA Michod D., Bartesaghi S., Khelifi A., Bellodi C., Berliocchi L.,
RA Nicotera P., Salomoni P.;
RT "Calcium-dependent dephosphorylation of the histone chaperone DAXX
RT regulates H3.3 loading and transcription upon neuronal activation.";
RL Neuron 74:122-135(2012).
CC -!- FUNCTION: Transcription corepressor known to repress transcriptional
CC potential of several sumoylated transcription factors. Down-regulates
CC basal and activated transcription. Its transcription repressor activity
CC is modulated by recruiting it to subnuclear compartments like the
CC nucleolus or PML/POD/ND10 nuclear bodies through interactions with
CC MCSR1 and PML, respectively. Seems to regulate transcription in
CC PML/POD/ND10 nuclear bodies together with PML and may influence
CC TNFRSF6-dependent apoptosis thereby. Inhibits transcriptional
CC activation of PAX3 and ETS1 through direct protein-protein
CC interactions. Modulates PAX5 activity; the function seems to involve
CC CREBBP. Acts as an adapter protein in a MDM2-DAXX-USP7 complex by
CC regulating the RING-finger E3 ligase MDM2 ubiquitination activity.
CC Under non-stress condition, in association with the deubiquitinating
CC USP7, prevents MDM2 self-ubiquitination and enhances the intrinsic E3
CC ligase activity of MDM2 towards TP53, thereby promoting TP53
CC ubiquitination and subsequent proteasomal degradation. Upon DNA damage,
CC its association with MDM2 and USP7 is disrupted, resulting in increased
CC MDM2 autoubiquitination and consequently, MDM2 degradation, which leads
CC to TP53 stabilization. Acts as histone chaperone that facilitates
CC deposition of histone H3.3. Acts as targeting component of the
CC chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA
CC translocase activity and catalyzes the replication-independent
CC deposition of histone H3.3 in pericentric DNA repeats outside S-phase
CC and telomeres, and the in vitro remodeling of H3.3-containing
CC nucleosomes. Does not affect the ATPase activity of ATRX but alleviates
CC its transcription repression activity. Upon neuronal activation
CC associates with regulatory elements of selected immediate early genes
CC where it promotes deposition of histone H3.3 which may be linked to
CC transcriptional induction of these genes. Required for the recruitment
CC of histone H3.3:H4 dimers to PML-nuclear bodies (PML-NBs); the process
CC is independent of ATRX and facilitated by ASF1A; PML-NBs are suggested
CC to function as regulatory sites for the incorporation of newly
CC synthesized histone H3.3 into chromatin. Proposed to mediate activation
CC of the JNK pathway and apoptosis via MAP3K5 in response to signaling
CC from TNFRSF6 and TGFBR2. Interaction with HSPB1/HSP27 may prevent
CC interaction with TNFRSF6 and MAP3K5 and block DAXX-mediated apoptosis.
CC In contrast, in lymphoid cells JNC activation and TNFRSF6-mediated
CC apoptosis may not involve DAXX. Plays a role as a positive regulator of
CC the heat shock transcription factor HSF1 activity during the stress
CC protein response (By similarity). {ECO:0000250|UniProtKB:Q9UER7,
CC ECO:0000269|PubMed:10684855, ECO:0000269|PubMed:20651253,
CC ECO:0000269|PubMed:22500635}.
CC -!- SUBUNIT: Homomultimer. Interacts (via C-terminus) with TNFRSF6 (via
CC death domain). Interacts with PAX5, SLC2A4/GLUT4, MAP3K5, TGFBR2,
CC phosphorylated dimeric HSPB1/HSP27, CENPC, ETS1, sumoylated PML, UBE2I,
CC MCRS1 and TP53. Interacts (via N-terminus) with HIPK2 and HIPK3.
CC Interacts with HIPK1, which induces translocation from PML/POD/ND10
CC nuclear bodies to chromatin and enhances association with HDAC1.
CC Interacts (non-phosphorylated) with PAX3, PAX7, DEK, HDAC1, HDAC2,
CC HDAC3, acetylated histone H4 and histones H2A, H2B, H3, H3.3 and H4.
CC Interacts with SPOP; mediating CUL3-dependent proteosomal degradation.
CC Interacts with CBP; the interaction is dependent the sumoylation of CBP
CC and suppresses CBP transcriptional activity via recruitment of HDAC2
CC directly in the complex with TP53 and HIPK2. Interacts with AXIN1; the
CC interaction stimulates the interaction of DAXX with TP53, stimulates
CC 'Ser-46' phosphorylation of TP53 on and induces cell death on UV
CC irradiation. Interacts with MDM2; the interaction is direct. Interacts
CC with USP7; the interaction is direct and independent of MDM2 and TP53.
CC Part of a complex with DAXX, MDM2 and USP7 under non-stress conditions.
CC Interacts (via N-terminus) with RASSF1 (via C-terminus); the
CC interaction is independent of MDM2 and TP53; RASSF1 isoform A disrupts
CC interactions among MDM2, DAXX and USP7, thus contributing to the
CC efficient activation of TP53 by promoting MDM2 self-ubiquitination in
CC cell-cycle checkpoint control in response to DNA damage. Interacts with
CC ATRX to form the chromatin remodeling complex ATRX:DAXX. Interacts with
CC HSF1 (via homotrimeric form preferentially); this interaction relieves
CC homotrimeric HSF1 from repression of its transcriptional activity by
CC HSP90-dependent multichaperone complex upon heat shock (By similarity).
CC {ECO:0000250|UniProtKB:Q9UER7, ECO:0000269|PubMed:10684855,
CC ECO:0000269|PubMed:11034606, ECO:0000269|PubMed:11799127,
CC ECO:0000269|PubMed:12529400, ECO:0000269|PubMed:16287980,
CC ECO:0000269|PubMed:20504901}.
CC -!- INTERACTION:
CC O35613; O54784: Dapk3; NbExp=2; IntAct=EBI-77304, EBI-77359;
CC O35613; P25446: Fas; NbExp=2; IntAct=EBI-77304, EBI-296206;
CC O35613; O88904: Hipk1; NbExp=3; IntAct=EBI-77304, EBI-692945;
CC O35613; Q62318: Trim28; NbExp=2; IntAct=EBI-77304, EBI-346909;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10684855}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:22500635}. Nucleus, PML body
CC {ECO:0000269|PubMed:10684855}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9UER7}. Chromosome, centromere
CC {ECO:0000250|UniProtKB:Q9UER7}. Note=Dispersed throughout the
CC nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli.
CC Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuclear
CC bodies. Colocalizes with a subset of interphase centromeres, but is
CC absent from mitotic centromeres. Detected in cytoplasmic punctate
CC structures. Translocates from the nucleus to the cytoplasm upon glucose
CC deprivation or oxidative stress. Colocalizes with RASSF1 in the
CC nucleus. Colocalizes with USP7 in nucleoplasma with accumulation in
CC speckled structures. {ECO:0000250|UniProtKB:Q9UER7}.
CC -!- DEVELOPMENTAL STAGE: Expressed as early as 12.5 dpc in the
CC neuroepithelium (ventricular zone). At 17.5 dpc, expression becomes
CC more pronounced in postmitotic cells of the cortical plate (CP). Early
CC postnatally (postnatal day 2 [P2]) and in the adult brain (P30)
CC expressed both in the cortex and in the hippocampus.
CC {ECO:0000269|PubMed:22500635}.
CC -!- DOMAIN: The Sumo interaction motif mediates Sumo binding, and is
CC required both for sumoylation and binding to sumoylated targets.
CC {ECO:0000250}.
CC -!- PTM: Sumoylated with SUMO1 on multiple lysine residues. {ECO:0000250}.
CC -!- PTM: Repressor activity is down-regulated upon Ser-669 phosphorylation.
CC Upon neuronal activation dephosphorylated by calcineurin in a Ca2+
CC dependent manner at Ser-669; dephosphorylation positively affects
CC histone H3.3 loading and transcriptional activation.
CC {ECO:0000269|PubMed:12529400}.
CC -!- PTM: Polyubiquitinated; which is promoted by CUL3 and SPOP and results
CC in proteasomal degradation. Ubiquitinated by MDM2; inducing its
CC degradation. Deubiquitinated by USP7; leading to stabilize it (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DAXX family. {ECO:0000305}.
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DR EMBL; AF006040; AAC53284.1; -; mRNA.
DR EMBL; AF110520; AAC97971.1; -; Genomic_DNA.
DR EMBL; AF100956; AAC69891.1; -; Genomic_DNA.
DR RefSeq; NP_001186662.1; NM_001199733.1.
DR RefSeq; NP_031855.3; NM_007829.4.
DR RefSeq; XP_006523643.1; XM_006523580.2.
DR RefSeq; XP_006523644.1; XM_006523581.2.
DR RefSeq; XP_006523645.1; XM_006523582.2.
DR AlphaFoldDB; O35613; -.
DR BMRB; O35613; -.
DR SMR; O35613; -.
DR BioGRID; 199054; 26.
DR CORUM; O35613; -.
DR DIP; DIP-30972N; -.
DR IntAct; O35613; 18.
DR MINT; O35613; -.
DR STRING; 10090.ENSMUSP00000128504; -.
DR iPTMnet; O35613; -.
DR PhosphoSitePlus; O35613; -.
DR EPD; O35613; -.
DR jPOST; O35613; -.
DR MaxQB; O35613; -.
DR PaxDb; O35613; -.
DR PeptideAtlas; O35613; -.
DR PRIDE; O35613; -.
DR ProteomicsDB; 279877; -.
DR DNASU; 13163; -.
DR GeneID; 13163; -.
DR KEGG; mmu:13163; -.
DR CTD; 1616; -.
DR MGI; MGI:1197015; Daxx.
DR eggNOG; ENOG502QRS6; Eukaryota.
DR InParanoid; O35613; -.
DR OrthoDB; 557255at2759; -.
DR PhylomeDB; O35613; -.
DR Reactome; R-MMU-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
DR Reactome; R-MMU-9670095; Inhibition of DNA recombination at telomere.
DR BioGRID-ORCS; 13163; 10 hits in 75 CRISPR screens.
DR ChiTaRS; Daxx; mouse.
DR PRO; PR:O35613; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35613; protein.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0001741; C:XY body; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0008432; F:JUN kinase binding; ISO:MGI.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0140037; F:sumo-dependent protein binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0030521; P:androgen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0071276; P:cellular response to cadmium ion; ISS:UniProtKB.
DR GO; GO:0071280; P:cellular response to copper ion; ISS:UniProtKB.
DR GO; GO:0072738; P:cellular response to diamide; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:1903936; P:cellular response to sodium arsenite; ISS:UniProtKB.
DR GO; GO:0034620; P:cellular response to unfolded protein; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0007254; P:JNK cascade; ISO:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0006334; P:nucleosome assembly; IMP:UniProtKB.
DR GO; GO:0030578; P:PML body organization; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:MGI.
DR GO; GO:0033129; P:positive regulation of histone phosphorylation; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0071168; P:protein localization to chromatin; IMP:CAFA.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR CDD; cd13151; DAXX_helical_bundle; 1.
DR CDD; cd13150; DAXX_histone_binding; 1.
DR DisProt; DP00708; -.
DR Gene3D; 1.10.8.810; -; 1.
DR Gene3D; 1.20.58.2170; -; 1.
DR InterPro; IPR005012; Daxx.
DR InterPro; IPR046378; DAXX_histone_binding.
DR InterPro; IPR046426; DAXX_histone_binding_sf.
DR InterPro; IPR031333; Daxx_N.
DR InterPro; IPR038298; Daxx_N_sf.
DR PANTHER; PTHR12766:SF7; PTHR12766:SF7; 1.
DR Pfam; PF03344; Daxx; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Centromere; Chaperone; Chromatin regulator; Chromosome;
KW Coiled coil; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..739
FT /note="Death domain-associated protein 6"
FT /id="PRO_0000151259"
FT REGION 1..166
FT /note="Necessary for interaction with USP7 and ATRX"
FT /evidence="ECO:0000250"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 189..423
FT /note="Interaction with histone H3.3"
FT /evidence="ECO:0000250"
FT REGION 353..576
FT /note="Necessary for interaction with USP7"
FT /evidence="ECO:0000250"
FT REGION 405..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..739
FT /note="Interaction with SPOP"
FT /evidence="ECO:0000250"
FT REGION 732..739
FT /note="Sumo interaction motif (SIM)"
FT /evidence="ECO:0000250"
FT COILED 185..223
FT /evidence="ECO:0000255"
FT COILED 364..403
FT /evidence="ECO:0000255"
FT COILED 445..488
FT /evidence="ECO:0000255"
FT MOTIF 391..395
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 622..628
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 36..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..498
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UER7"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12529400"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UER7"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UER7"
FT MOD_RES 472
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:12529400"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12529400"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VIB2"
FT MOD_RES 507
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VIB2"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12529400"
FT MOD_RES 523
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:12529400"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VIB2"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VIB2"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12529400"
FT MOD_RES 669
FT /note="Phosphoserine; by HIPK1"
FT /evidence="ECO:0000269|PubMed:12529400"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UER7"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UER7"
FT CROSSLNK 630
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q9UER7"
FT MUTAGEN 502
FT /note="S->A: No effect on phosphorylation by HIPK1."
FT /evidence="ECO:0000269|PubMed:12529400"
FT MUTAGEN 669
FT /note="S->A: Diminishes phosphorylation by HIPK1."
FT /evidence="ECO:0000269|PubMed:12529400"
FT CONFLICT 416
FT /note="Q -> K (in Ref. 2; AAC97971)"
FT /evidence="ECO:0000305"
FT CONFLICT 452
FT /note="D -> DD (in Ref. 2; AAC97971)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="P -> S (in Ref. 2; AAC97971)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 739 AA; 81489 MW; 8407D5788528AC2D CRC64;
MATDDSIIVL DDDDEDEAAA QPGPSNLPPN PASTGPGPGL SQQATGLSEP RVDGGSSNSG
SRKCYKLDNE KLFEEFLELC KTETSDHPEV VPFLHKLQQR AQSVFLASAE FCNILSRVLA
RSRKRPAKIY VYINELCTVL KAHSIKKKLN LAPAASTTSE ASGPNPPTEP PSDLTNTENT
ASEASRTRGS RRQIQRLEQL LALYVAEIRR LQEKELDLSE LDDPDSSYLQ EARLKRKLIR
LFGRLCELKD CSSLTGRVIE QRIPYRGTRY PEVNRRIERL INKPGLDTFP DYGDVLRAVE
KAATRHSLGL PRQQLQLLAQ DAFRDVGVRL QERRHLDLIY NFGCHLTDDY RPGVDPALSD
PTLARRLREN RTLAMNRLDE VISKYAMMQD KTEEGERQKR RARLLGTAPQ PSDPPQASSE
SGEGPSGMAS QECPTTSKAE TDDDDDDDDD DDEDNEESEE EEEEEEEEKE ATEDEDEDLE
QLQEDQGGDE EEEGGDNEGN ESPTSPSDFF HRRNSEPAEG LRTPEGQQKR GLTETPASPP
GASLDPPSTD AESSGEQLLE PLLGDESPVS QLAELEMEAL PEERDISSPR KKSEDSLPTI
LENGAAVVTS TSVNGRVSSH TWRDASPPSK RFRKEKKQLG SGLLGNSYIK EPMAQQDSGQ
NTSVQPMPSP PLASVASVAD SSTRVDSPSH ELVTSSLCSP SPSLLLQTPQ AQSLRQCIYK
TSVATQCDPE EIIVLSDSD
