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 24-JAN-2024, entry version 186. 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 a histone chaperone that facilitates CC deposition of histone H3.3. Acts as a 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 proteasomal 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000128504; -. DR PeptideAtlas; O35613; -. DR ProteomicsDB; 279877; -. DR Pumba; O35613; -. DR DNASU; 13163; -. DR GeneID; 13163; -. DR KEGG; mmu:13163; -. DR AGR; MGI:1197015; -. DR CTD; 1616; -. DR MGI; MGI:1197015; Daxx. DR eggNOG; ENOG502QRS6; Eukaryota. DR InParanoid; O35613; -. DR OrthoDB; 2920075at2759; -. 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; 11 hits in 81 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:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0000792; C:heterochromatin; IDA:MGI. DR GO; GO:0005874; C:microtubule; 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:0140693; F:molecular condensate scaffold activity; 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: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:0071346; P:cellular response to type II interferon; ISO:MGI. 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:1900038; P:negative regulation of cellular response to hypoxia; ISO:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA: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:0036480; P:neuron intrinsic apoptotic signaling pathway in response to oxidative stress; ISO: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: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:0006355; P:regulation of DNA-templated transcription; ISO:MGI. 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 CDD; cd13151; DAXX_helical_bundle; 1. DR CDD; cd13150; DAXX_histone_binding; 1. DR DisProt; DP00708; -. DR Gene3D; 1.20.58.2170; -; 1. DR Gene3D; 1.10.8.810; Daxx helical bundle domain; 1. DR InterPro; IPR046378; DAXX_histone-bd. DR InterPro; IPR046426; DAXX_histone-bd_sf. DR InterPro; IPR031333; Daxx_N. DR InterPro; IPR038298; Daxx_N_sf. DR PANTHER; PTHR12766:SF9; DEATH DOMAIN-ASSOCIATED PROTEIN 6; 1. DR PANTHER; PTHR12766; DEATH DOMAIN-ASSOCIATED PROTEIN 6 DAXX; 1. DR Pfam; PF03344; Daxx; 1. DR Pfam; PF20920; DAXX_hist_bd; 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 //