HUMAN:DAXX

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	DAXX (synonyms: BING2, DAP6)
Protein Name(s)	Death domain-associated protein 6 Daxx hDaxx ETS1-associated protein 1 EAP1 Fas death domain-associated protein
External Links
UniProt	Q9UER7
EMBL	AF039136 AF006041 AF015956 AF050179 AF097742 AB015051 AK303854 CR457085 AL662827 AL662820 BX248088 CR759793 CR759817 CR759786 Z97183 Z97184 Z97184 Z97183 CH471081 BC000220 BC109073 BC109074
CCDS	CCDS4776.1 CCDS59008.1
PIR	T03847
RefSeq	NP_001135441.1 NP_001241646.1 NP_001341.1
UniGene	Hs.336916
PDB	2KQS 2KZS 2KZU 4H9N 4H9O 4H9P 4H9Q 4H9R 4H9S 4HGA
PDBsum	2KQS 2KZS 2KZU 4H9N 4H9O 4H9P 4H9Q 4H9R 4H9S 4HGA
DisProt	DP00707
ProteinModelPortal	Q9UER7
SMR	Q9UER7
BioGrid	107985
DIP	DIP-27628N
IntAct	Q9UER7
MINT	MINT-122943
STRING	9606.ENSP00000266000
PhosphoSite	Q9UER7
DMDM	24636785
MaxQB	Q9UER7
PaxDb	Q9UER7
PeptideAtlas	Q9UER7
PRIDE	Q9UER7
DNASU	1616
Ensembl	ENST00000266000 ENST00000374542 ENST00000383062 ENST00000383194 ENST00000399060 ENST00000399344 ENST00000414083 ENST00000433482 ENST00000436311 ENST00000445009 ENST00000455860 ENST00000612868 ENST00000612888 ENST00000617660
GeneID	1616
KEGG	hsa:1616
UCSC	uc003oec.3
CTD	1616
GeneCards	GC06M033286 GC06Mj33207 GC06Mk33264 GC06Mm33456 GC06Mn33215
HGNC	HGNC:2681
HPA	CAB002224 CAB025546 HPA008736 HPA008797
MIM	603186
neXtProt	NX_Q9UER7
PharmGKB	PA27148
eggNOG	NOG39676
GeneTree	ENSGT00390000009448
HOGENOM	HOG000112148
HOVERGEN	HBG031495
InParanoid	Q9UER7
KO	K02308
OMA	DGDKSPM
PhylomeDB	Q9UER7
TreeFam	TF325803
SignaLink	Q9UER7
ChiTaRS	DAXX
EvolutionaryTrace	Q9UER7
GeneWiki	Death-associated_protein_6
GenomeRNAi	1616
NextBio	6638
PRO	PR:Q9UER7
Proteomes	UP000005640 UP000005640
Bgee	Q9UER7
CleanEx	HS_DAXX
ExpressionAtlas	Q9UER7
Genevestigator	Q9UER7
GO	GO:0000775 GO:0005737 GO:0005829 GO:0000792 GO:0005730 GO:0005634 GO:0016605 GO:0070603 GO:0050681 GO:0019899 GO:0031072 GO:0042393 GO:0002039 GO:0042803 GO:0030295 GO:0019901 GO:0047485 GO:0005057 GO:0003714 GO:0008134 GO:0031625 GO:0007257 GO:0030521 GO:0006915 GO:0006338 GO:0008625 GO:0000281 GO:0045892 GO:0006334 GO:2001235 GO:1901216 GO:0045860 GO:0001934 GO:0031396 GO:0006355 GO:0006351 GO:0016032
InterPro	IPR005012
PANTHER	PTHR12766
Pfam	PF03344

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
enables	GO:0032183	SUMO binding	PMID:17081986^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P61956	F		Seeded From UniProt	complete
enables	GO:0032183	SUMO binding	PMID:17081986^[1]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P63165	F		Seeded From UniProt	complete
involved_in	GO:0072738	cellular response to diamide	PMID:15016915^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903936	cellular response to sodium arsenite	PMID:15016915^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071280	cellular response to copper ion	PMID:15016915^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071276	cellular response to cadmium ion	PMID:15016915^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034620	cellular response to unfolded protein	PMID:15016915^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034605	cellular response to heat	PMID:15016915^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0003713	transcription coactivator activity	PMID:15016915^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0000775	chromosome, centromeric region	PMID:10504293^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1901216	positive regulation of neuron death	PMID:15983381^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q99683	P		Seeded From UniProt	complete
involved_in	GO:0045860	positive regulation of protein kinase activity	PMID:15983381^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q99683	P	has_regulation_target:(UniProtKB:Q99683)	Seeded From UniProt	complete
enables	GO:0030295	protein kinase activator activity	PMID:15983381^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q99683	F	has_regulation_target:(UniProtKB:Q99683)	Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:15983381^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q99683	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15983381^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0001934	positive regulation of protein phosphorylation	PMID:15983381^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q99683	P		Seeded From UniProt	complete
enables	GO:0042393	histone binding	PMID:20211137^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0046982	protein heterodimerization activity	PMID:21134643^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0003714	transcription corepressor activity	PMID:17081986^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_regulation_target:(UniProtKB:P04150)	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17081986^[1]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0050681	androgen receptor binding	PMID:15572661^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P10275	F		Seeded From UniProt	complete
enables	GO:0047485	protein N-terminus binding	PMID:18566590^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q9NS23	F		Seeded From UniProt	complete
enables	GO:0047485	protein N-terminus binding	PMID:15572661^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P10275	F		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:15572661^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:12140263^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042393	histone binding	PMID:20504901^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042393	histone binding	PMID:12140263^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0031625	ubiquitin protein ligase binding	PMID:16845383^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q00987	F		Seeded From UniProt	complete
involved_in	GO:0031396	regulation of protein ubiquitination	PMID:18566590^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030521	androgen receptor signaling pathway	PMID:15572661^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
	GO:0000775	chromosome, centromeric region	PMID:10504293^[3]	ECO:0000314			C		Fig.1	complete CACAO 7328
enables	GO:0019899	enzyme binding	PMID:16845383^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q93009	F		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:18566590^[8]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006338	chromatin remodeling	PMID:20651253^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006334	nucleosome assembly	PMID:20651253^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006334	nucleosome assembly	PMID:20504901^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:O35613	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15572661^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0003714	transcription corepressor activity	PMID:12140263^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0002039	p53 binding	PMID:16845383^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04637	F		Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	PMID:15878163^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15878163^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016604	nuclear body	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1903508	positive regulation of nucleic acid-templated transcription	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0003713	P		Seeded From UniProt	complete
involved_in	GO:0045892	negative regulation of transcription, DNA-templated	PMID:10698492^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:10698492^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:10669754^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0008134	transcription factor binding	PMID:10698492^[14]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:10698492^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008625	extrinsic apoptotic signaling pathway via death domain receptors	PMID:9215629^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0007257	activation of JUN kinase activity	PMID:9215629^[16]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0016605	PML body	PMID:15247905^[17]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0031072	heat shock protein binding	PMID:15572661^[7]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	PMID:15572661^[7]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15572661^[7]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-HSA-4085992 Reactome:R-HSA-3222072 Reactome:R-HSA-3215295	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005694	chromosome	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0158	C		Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0053	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
involved_in	GO:0006325	chromatin organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0156	P		Seeded From UniProt	complete
part_of	GO:0000775	chromosome, centromeric region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0137 UniProtKB-SubCell:SL-0047	C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0190	C		Seeded From UniProt	complete
part_of	GO:0005730	nucleolus	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0188	C		Seeded From UniProt	complete
part_of	GO:0016605	PML body	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0465	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 Lin, DY et al. (2006) Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol. Cell 24 341-54 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 Boellmann, F et al. (2004) DAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activity. Proc. Natl. Acad. Sci. U.S.A. 101 4100-5 PubMed GONUTS page
↑ ^3.0 ^3.1 Everett, RD et al. (1999) A dynamic connection between centromeres and ND10 proteins. J. Cell. Sci. 112 ( Pt 20) 3443-54 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 Junn, E et al. (2005) Interaction of DJ-1 with Daxx inhibits apoptosis signal-regulating kinase 1 activity and cell death. Proc. Natl. Acad. Sci. U.S.A. 102 9691-6 PubMed GONUTS page
↑ Goldberg, AD et al. (2010) Distinct factors control histone variant H3.3 localization at specific genomic regions. Cell 140 678-91 PubMed GONUTS page
↑ Escobar-Cabrera, E et al. (2010) Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. Structure 18 1642-53 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 ^7.7 Lin, DY et al. (2004) Negative modulation of androgen receptor transcriptional activity by Daxx. Mol. Cell. Biol. 24 10529-41 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Song, MS et al. (2008) The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex. EMBO J. 27 1863-74 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Hollenbach, AD et al. (2002) Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek. J. Cell. Sci. 115 3319-30 PubMed GONUTS page
↑ ^10.0 ^10.1 Drané, P et al. (2010) The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3. Genes Dev. 24 1253-65 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Tang, J et al. (2006) Critical role for Daxx in regulating Mdm2. Nat. Cell Biol. 8 855-62 PubMed GONUTS page
↑ ^12.0 ^12.1 Lewis, PW et al. (2010) Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proc. Natl. Acad. Sci. U.S.A. 107 14075-80 PubMed GONUTS page
↑ ^13.0 ^13.1 Tang, J et al. (2005) The death domain-associated protein modulates activity of the transcription co-factor Skip/NcoA62. FEBS Lett. 579 2883-90 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 ^14.3 Li, R et al. (2000) EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes. Oncogene 19 745-53 PubMed GONUTS page
↑ Li, H et al. (2000) Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol. Cell. Biol. 20 1784-96 PubMed GONUTS page
↑ ^16.0 ^16.1 Yang, X et al. (1997) Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell 89 1067-76 PubMed GONUTS page
↑ Yordy, JS et al. (2004) SP100 expression modulates ETS1 transcriptional activity and inhibits cell invasion. Oncogene 23 6654-65 PubMed GONUTS page

[PMID:17081986-1] 1.0 ^1.1 ^1.2 ^1.3 Lin, DY et al. (2006) Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol. Cell 24 341-54 PubMed GONUTS page

[PMID:15016915-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 Boellmann, F et al. (2004) DAXX interacts with heat shock factor 1 during stress activation and enhances its transcriptional activity. Proc. Natl. Acad. Sci. U.S.A. 101 4100-5 PubMed GONUTS page

[PMID:10504293-3] 3.0 ^3.1 Everett, RD et al. (1999) A dynamic connection between centromeres and ND10 proteins. J. Cell. Sci. 112 ( Pt 20) 3443-54 PubMed GONUTS page

[PMID:15983381-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 Junn, E et al. (2005) Interaction of DJ-1 with Daxx inhibits apoptosis signal-regulating kinase 1 activity and cell death. Proc. Natl. Acad. Sci. U.S.A. 102 9691-6 PubMed GONUTS page

[PMID:20211137-5] Goldberg, AD et al. (2010) Distinct factors control histone variant H3.3 localization at specific genomic regions. Cell 140 678-91 PubMed GONUTS page

[PMID:21134643-6] Escobar-Cabrera, E et al. (2010) Structural characterization of the DAXX N-terminal helical bundle domain and its complex with Rassf1C. Structure 18 1642-53 PubMed GONUTS page

[PMID:15572661-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 ^7.6 ^7.7 Lin, DY et al. (2004) Negative modulation of androgen receptor transcriptional activity by Daxx. Mol. Cell. Biol. 24 10529-41 PubMed GONUTS page

[PMID:18566590-8] 8.0 ^8.1 ^8.2 Song, MS et al. (2008) The tumour suppressor RASSF1A promotes MDM2 self-ubiquitination by disrupting the MDM2-DAXX-HAUSP complex. EMBO J. 27 1863-74 PubMed GONUTS page

[PMID:12140263-9] 9.0 ^9.1 ^9.2 Hollenbach, AD et al. (2002) Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek. J. Cell. Sci. 115 3319-30 PubMed GONUTS page

[PMID:20504901-10] 10.0 ^10.1 Drané, P et al. (2010) The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3. Genes Dev. 24 1253-65 PubMed GONUTS page

[PMID:16845383-11] 11.0 ^11.1 ^11.2 Tang, J et al. (2006) Critical role for Daxx in regulating Mdm2. Nat. Cell Biol. 8 855-62 PubMed GONUTS page

[PMID:20651253-12] 12.0 ^12.1 Lewis, PW et al. (2010) Daxx is an H3.3-specific histone chaperone and cooperates with ATRX in replication-independent chromatin assembly at telomeres. Proc. Natl. Acad. Sci. U.S.A. 107 14075-80 PubMed GONUTS page

[PMID:15878163-13] 13.0 ^13.1 Tang, J et al. (2005) The death domain-associated protein modulates activity of the transcription co-factor Skip/NcoA62. FEBS Lett. 579 2883-90 PubMed GONUTS page

[PMID:10698492-14] 14.0 ^14.1 ^14.2 ^14.3 Li, R et al. (2000) EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes. Oncogene 19 745-53 PubMed GONUTS page

[PMID:10669754-15] Li, H et al. (2000) Sequestration and inhibition of Daxx-mediated transcriptional repression by PML. Mol. Cell. Biol. 20 1784-96 PubMed GONUTS page

[PMID:9215629-16] 16.0 ^16.1 Yang, X et al. (1997) Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell 89 1067-76 PubMed GONUTS page

[PMID:15247905-17] Yordy, JS et al. (2004) SP100 expression modulates ETS1 transcriptional activity and inhibits cell invasion. Oncogene 23 6654-65 PubMed GONUTS page

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HUMAN:DAXX

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References

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