DAXX_MOUSE - dbPTM
DAXX_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DAXX_MOUSE
UniProt AC O35613
Protein Name Death domain-associated protein 6
Gene Name Daxx
Organism Mus musculus (Mouse).
Sequence Length 739
Subcellular Localization Cytoplasm . Nucleus, nucleoplasm . Nucleus, PML body . Nucleus, nucleolus . Chromosome, centromere . Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. Colocalizes with histone H3.3, ATRX, HIRA and ASF1A at PML-nuc
Protein Description 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 histone chaperone that facilitates deposition of histone H3.3. Acts as 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)..
Protein Sequence MATDDSIIVLDDDDEDEAAAQPGPSNLPPNPASTGPGPGLSQQATGLSEPRVDGGSSNSGSRKCYKLDNEKLFEEFLELCKTETSDHPEVVPFLHKLQQRAQSVFLASAEFCNILSRVLARSRKRPAKIYVYINELCTVLKAHSIKKKLNLAPAASTTSEASGPNPPTEPPSDLTNTENTASEASRTRGSRRQIQRLEQLLALYVAEIRRLQEKELDLSELDDPDSSYLQEARLKRKLIRLFGRLCELKDCSSLTGRVIEQRIPYRGTRYPEVNRRIERLINKPGLDTFPDYGDVLRAVEKAATRHSLGLPRQQLQLLAQDAFRDVGVRLQERRHLDLIYNFGCHLTDDYRPGVDPALSDPTLARRLRENRTLAMNRLDEVISKYAMMQDKTEEGERQKRRARLLGTAPQPSDPPQASSESGEGPSGMASQECPTTSKAETDDDDDDDDDDDEDNEESEEEEEEEEEEKEATEDEDEDLEQLQEDQGGDEEEEGGDNEGNESPTSPSDFFHRRNSEPAEGLRTPEGQQKRGLTETPASPPGASLDPPSTDAESSGEQLLEPLLGDESPVSQLAELEMEALPEERDISSPRKKSEDSLPTILENGAAVVTSTSVNGRVSSHTWRDASPPSKRFRKEKKQLGSGLLGNSYIKEPMAQQDSGQNTSVQPMPSPPLASVASVADSSTRVDSPSHELVTSSLCSPSPSLLLQTPQAQSLRQCIYKTSVATQCDPEEIIVLSDSD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
25PhosphorylationAAAQPGPSNLPPNPA
HHHCCCCCCCCCCCC		57.84-
219PhosphorylationQEKELDLSELDDPDS
HHHCCCHHHCCCCCC		35.4627566939
249UbiquitinationFGRLCELKDCSSLTG
HHHHHHCCCHHHHCC		34.10-
372PhosphorylationRRLRENRTLAMNRLD
HHHHHCHHHHHHHHH		30.3725177544
418PhosphorylationPSDPPQASSESGEGP
CCCCCCCCCCCCCCC		29.41-
430PhosphorylationEGPSGMASQECPTTS
CCCCCCCCCCCCCCC		20.02-
441PhosphorylationPTTSKAETDDDDDDD
CCCCCCCCCCCCCCC		49.9829514104
458PhosphorylationDDEDNEESEEEEEEE
CCCCCHHHHHHHHHH		44.0925195567
472PhosphorylationEEEEKEATEDEDEDL
HHHHHHHHCCCCHHH		45.0912529400
502PhosphorylationGDNEGNESPTSPSDF
CCCCCCCCCCCHHHH		37.1612529400
504PhosphorylationNEGNESPTSPSDFFH
CCCCCCCCCHHHHCH		63.6525293948
505PhosphorylationEGNESPTSPSDFFHR
CCCCCCCCHHHHCHH		26.2825293948
507PhosphorylationNESPTSPSDFFHRRN
CCCCCCHHHHCHHCC		46.9825293948
515PhosphorylationDFFHRRNSEPAEGLR
HHCHHCCCCCCCCCC		43.0526824392
516PhosphorylationFFHRRNSEPAEGLRT
HCHHCCCCCCCCCCC		52.6724719451
523PhosphorylationEPAEGLRTPEGQQKR
CCCCCCCCCCHHHCC		30.6326824392
533PhosphorylationGQQKRGLTETPASPP
HHHCCCCCCCCCCCC		40.4123649490
535PhosphorylationQKRGLTETPASPPGA
HCCCCCCCCCCCCCC		20.9419854140
538PhosphorylationGLTETPASPPGASLD
CCCCCCCCCCCCCCC		32.6027180971
543PhosphorylationPASPPGASLDPPSTD
CCCCCCCCCCCCCCC		38.9423649490
567PhosphorylationEPLLGDESPVSQLAE
HHHHCCCCHHHHHHH		35.0323649490
570PhosphorylationLGDESPVSQLAELEM
HCCCCHHHHHHHHHH		23.9023649490
593PhosphorylationISSPRKKSEDSLPTI
CCCCCCCCCCCCCCH		50.0726160508
596PhosphorylationPRKKSEDSLPTILEN
CCCCCCCCCCCHHHC		32.0026160508
599PhosphorylationKSEDSLPTILENGAA
CCCCCCCCHHHCCCE		43.4126160508
609PhosphorylationENGAAVVTSTSVNGR
HCCCEEEEECCCCCE		21.4930635358
610PhosphorylationNGAAVVTSTSVNGRV
CCCEEEEECCCCCEE		13.6930635358
611PhosphorylationGAAVVTSTSVNGRVS
CCEEEEECCCCCEEC		27.5930635358
612PhosphorylationAAVVTSTSVNGRVSS
CEEEEECCCCCEECC		17.2230635358
618PhosphorylationTSVNGRVSSHTWRDA
CCCCCEECCCCCCCC		18.2930635358
619PhosphorylationSVNGRVSSHTWRDAS
CCCCEECCCCCCCCC		23.2926643407
621PhosphorylationNGRVSSHTWRDASPP
CCEECCCCCCCCCCC		24.9226643407
626PhosphorylationSHTWRDASPPSKRFR
CCCCCCCCCCCHHHH		41.4525266776
627PhosphorylationHTWRDASPPSKRFRK
CCCCCCCCCCHHHHH		38.6124719451
629PhosphorylationWRDASPPSKRFRKEK
CCCCCCCCHHHHHHH		39.5926745281
658PhosphorylationEPMAQQDSGQNTSVQ
CCCCCCCCCCCCCCC		37.6325777480
662PhosphorylationQQDSGQNTSVQPMPS
CCCCCCCCCCCCCCC		23.5325777480
663PhosphorylationQDSGQNTSVQPMPSP
CCCCCCCCCCCCCCC		26.7229472430
669PhosphorylationTSVQPMPSPPLASVA
CCCCCCCCCCCCHHH		32.6627087446
674PhosphorylationMPSPPLASVASVADS
CCCCCCCHHHHHCCC		26.3729472430
677PhosphorylationPPLASVASVADSSTR
CCCCHHHHHCCCCCC		18.7125293948
681PhosphorylationSVASVADSSTRVDSP
HHHHHCCCCCCCCCC		24.7025777480
682PhosphorylationVASVADSSTRVDSPS
HHHHCCCCCCCCCCC		22.3025777480
683PhosphorylationASVADSSTRVDSPSH
HHHCCCCCCCCCCCC		38.3725777480
687PhosphorylationDSSTRVDSPSHELVT
CCCCCCCCCCCHHHH		25.9922942356
689PhosphorylationSTRVDSPSHELVTSS
CCCCCCCCCHHHHHH		33.2822942356
694PhosphorylationSPSHELVTSSLCSPS
CCCCHHHHHHHCCCC		25.8125159016
695PhosphorylationPSHELVTSSLCSPSP
CCCHHHHHHHCCCCH		17.5225159016
696PhosphorylationSHELVTSSLCSPSPS
CCHHHHHHHCCCCHH		24.8325159016
699PhosphorylationLVTSSLCSPSPSLLL
HHHHHHCCCCHHHHH		33.4325159016
701PhosphorylationTSSLCSPSPSLLLQT
HHHHCCCCHHHHHCC		15.7225159016
703PhosphorylationSLCSPSPSLLLQTPQ
HHCCCCHHHHHCCCC		35.6725293948
736PhosphorylationPEEIIVLSDSD----
HHHEEEEECCC----		24.9521082442
738PhosphorylationEIIVLSDSD------
HEEEEECCC------		41.6721082442
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
669SPhosphorylationKinaseHIPK1O88904
Uniprot
-KUbiquitinationE3 ubiquitin ligaseSpopQ6ZWS8
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
669SPhosphorylation

12529400
669SPhosphorylation

12529400
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DAXX_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RASF1_MOUSERassf1physical
18566590
MDM2_MOUSEMdm2physical
18566590
P53_MOUSETrp53physical
18566590
CR3L1_MOUSECreb3l1physical
20211142
DMAP1_MOUSEDmap1physical
20211142
DMAP1_MOUSEDmap1physical
14978102
SUMO1_MOUSESumo1physical
21383010
SUMO2_MOUSESumo2physical
21383010
KINH_MOUSEKif5bphysical
18932217
P53_MOUSETrp53physical
15364927
MDM2_MOUSEMdm2physical
15364927
STK4_MOUSEStk4physical
21572393
TGFR2_HUMANTGFBR2physical
11483955
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DAXX_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736, AND MASSSPECTROMETRY.
"Homeodomain-interacting protein kinase 1 modulates Daxx localization,phosphorylation, and transcriptional activity.";
Ecsedy J.A., Michaelson J.S., Leder P.;
Mol. Cell. Biol. 23:950-960(2003).
Cited for: INTERACTION WITH HIPK1, MUTAGENESIS OF SER-502 AND SER-669,PHOSPHORYLATION AT SER-219; THR-472; SER-502; SER-515; THR-523;SER-626 AND SER-669, AND MASS SPECTROMETRY.

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