Reviewed, UniProtKB/Swiss-Prot Q9UER7 (DAXX_HUMAN)

Names and origin

Protein names

Recommended name:
    Death domain-associated protein 6
Alternative name(s):
    Daxx
    hDaxx
    Fas death domain-associated protein
    ETS1-associated protein 1
      Short name=EAP1

Gene names

Name:	DAXX
Synonyms:	BING2, DAP6

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	740 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Seems to regulate transcription in PML/POD/ND10 nuclear bodies together with PML and may influence TNFRSF6-dependent apoptosis thereby. Down-regulates basal and activated transcription. Seems to act as a transcriptional co-repressor and inhibits PAX3 and ETS1 through direct protein-protein interaction. Modulates PAX5 activity. 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.
Subunit structure	Homomultimer. Binds to the TNFRSF6 death domain via its C-terminus and to PAX5. Binds to SLC2A4/GLUT4, MAP3K5, TGFBR2, phosphorylated dimeric HSPB1/HSP27, CENPC1, ETS1, sumoylated PML, UBE2I and MCRS1. Is part of a complex containing PAX5 and CREBBP. Interacts with HIPK2 and HIPK3 via its N-terminus. Interacts with HIPK1, which induces translocation from PML/POD/ND10 nuclear bodies to chromatin and enhances association with HDAC1 By similarity. The non-phosphorylated form binds to PAX3, PAX7, DEK, HDAC1, HDAC2, HDAC3, acetylated histone H4 and histones H2A, H2B, H3 and H4. Interacts with SPOP. Part of a complex consisting of DAXX, CUL3 and SPOP.
Subcellular location	Nucleus. Cytoplasm. Note= Dispersed throughout the nucleoplasm, in PML/POD/ND10 nuclear bodies, and in nucleoli. 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.
Tissue specificity	Ubiquitous.
Induction	Upon mitogenic stimulation by concanavalin A.
Post-translational modification	Sumoylated. Phosphorylated upon DNA damage, probably by ATM or ATR. Phosphorylated by HIPK1 upon glucose deprivation. Polyubiquitinated; which is promoted by CUL3 and SPOP and results in proteasomal degradation.
Sequence similarities	Belongs to the DAXX family.

Ontologies

Keywords
Biological process	Apoptosis Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
PTM	Phosphoprotein Ubl conjugation
Gene Ontology (GO)
Biological process	activation of JNK activity Ref.1 Traceable author statement. Source: ProtInc androgen receptor signaling pathway Inferred from direct assay. Source: UniProtKB induction of apoptosis via death domain receptors Ref.1 Traceable author statement. Source: ProtInc negative regulation of transcription, DNA-dependent Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasm Traceable author statement. Source: UniProtKB nucleus Inferred from direct assay. Source: UniProtKB
Molecular function	androgen receptor binding Inferred from physical interaction. Source: UniProtKB heat shock protein binding Traceable author statement. Source: UniProtKB identical protein binding Ref.5 Inferred from physical interaction. Source: IntAct protein N-terminus binding Inferred from physical interaction. Source: UniProtKB receptor signaling protein activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-287635,EBI-287635
AR	P10275	2	EBI-77321,EBI-608057
ATRX	P46100	1	EBI-77321,EBI-396461
CREBBP	Q92793	1	EBI-77321,EBI-81215
DAPK3	O43293	1	EBI-77321,EBI-77293
ETS1	P14921	2	EBI-287635,EBI-913209
ETS1	P14921-1	1	EBI-287635,EBI-913224
ETS1	P14921-2	1	EBI-287635,EBI-913228
FAS	P25445	2	EBI-77321,EBI-494743
Fas	P25446	4	EBI-77321,EBI-296206	From a different organism.
HDAC1	Q13547	1	EBI-77321,EBI-301834
HDAC2	Q92769	1	EBI-77321,EBI-301821
HIPK1	Q86Z02	1	EBI-77321,EBI-692891
Hipk1	O88904	1	EBI-77321,EBI-692945	From a different organism.
HSPB1	P04792	1	EBI-77321,EBI-352682
HSPB1	P15991	2	EBI-77321,EBI-1559114	From a different organism.
MAP3K5	Q99683	4	EBI-77321,EBI-476263
MCRS1	Q96EZ8	2	EBI-77321,EBI-348259
MDM2	Q00987	3	EBI-77321,EBI-389668
PARK7	Q99497	1	EBI-77321,EBI-1164361
Pax5	Q02650	2	EBI-77321,EBI-296260	From a different organism.
PML	P29590	1	EBI-77321,EBI-295890
SLC2A4	P14672	3	EBI-77321,EBI-367146
STAT3	P40763	2	EBI-77321,EBI-518675
SUMO1	P63165	4	EBI-77321,EBI-80140
TCF7L2	Q9NQB0	3	EBI-77321,EBI-924724
TGFBR2	P37173	1	EBI-77321,EBI-296151
TP53	P04637	3	EBI-77321,EBI-366083
TSG101	Q99816	1	EBI-77321,EBI-346882
USP7	Q93009	4	EBI-77321,EBI-302474

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UER7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UER7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     696-740: SSLCIPSPARLSQTPHSQPPRPGTCKTSVATQCDPEEIIVLSDSD → PAKNLGRRRSKQDQG

Notes: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 740	740	Death domain-associated protein 6
Regions
	Region	501 – 625	125	Interaction with MAP3K5
	Region	626 – 740	115	Interaction with SPOP
	Coiled coil	180 – 217	38	Potential
	Coiled coil	358 – 399	42	Potential
	Coiled coil	430 – 489	60	Potential
	Motif	391 – 395	5	Nuclear localization signal Potential
	Motif	628 – 634	7	Nuclear localization signal Potential
	Compositional bias	11 – 16	6	Poly-Asp
	Compositional bias	434 – 572	139	Asp/Glu-rich (acidic)
Amino acid modifications
	Modified residue	178	1	Phosphoserine
	Modified residue	213	1	Phosphoserine By similarity
	Modified residue	459	1	Phosphothreonine By similarity
	Modified residue	495	1	Phosphoserine By similarity
	Modified residue	648	1	Phosphotyrosine
	Modified residue	668	1	Phosphoserine Probable
	Modified residue	671	1	Phosphoserine
	Modified residue	688	1	Phosphoserine
	Modified residue	690	1	Phosphoserine
	Modified residue	702	1	Phosphoserine
	Modified residue	709	1	Phosphothreonine
	Modified residue	712	1	Phosphoserine
	Modified residue	737	1	Phosphoserine
	Modified residue	739	1	Phosphoserine
Natural variations
	Alternative sequence	696 – 740	45	SSLCI…LSDSD → PAKNLGRRRSKQDQG in isoform 2.
Experimental info
	Mutagenesis	630	1	K → A: Abolishes sumoylation
	Mutagenesis	631	1	K → A: Abolishes sumoylation
	Mutagenesis	668	1	S → A: No translocation to the cytosol upon glucose deprivation
	Mutagenesis	671	1	S → A: No effect on cytosol translocation. upon glucose deprivation
	Sequence conflict	177	1	Q → R in AAB66585. Ref.2
	Sequence conflict	263	1	R → H in AAC72843. Ref.5
	Sequence conflict	323	1	R → W in AAB66585. Ref.2
	Sequence conflict	365	1	R → Q in AAB66585. Ref.2
	Sequence conflict	382	1	L → S in AAB66585. Ref.2
	Sequence conflict	647	1	S → R Ref.4 Ref.7
	Sequence conflict	722	1	T → A Ref.4 Ref.7
	Sequence conflict	731 – 732	2	EE → KK in AAC72843. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 2002. Version 2. Checksum: 1B309ADDAA878040	FASTA	740	81,373
	10 20 30 40 50 60 MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS SSSGGKKCYK 70 80 90 100 110 120 LENEKLFEEF LELCKMQTAD HPEVVPFLYN RQQRAHSLFL ASAEFCNILS RVLSRARSRP 130 140 150 160 170 180 AKLYVYINEL CTVLKAHSAK KKLNLAPAAT TSNEPSGNNP PTHLSLDPTN AENTASQSPR 190 200 210 220 230 240 TRGSRRQIQR LEQLLALYVA EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC 250 260 270 280 290 300 ELKDCSSLTG RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH 310 320 330 340 350 360 SLGLPRQQLQ LMAQDAFRDV GIRLQERRHL DLIYNFGCHL TDDYRPGVDP ALSDPVLARR 370 380 390 400 410 420 LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG TSSHSADTPE ASLDSGEGPS 430 440 450 460 470 480 GMASQGCPSA SRAETDDEDD EESDEEEEEE EEEEEEEATD SEEEEDLEQM QEGQEDDEEE 490 500 510 520 530 540 DEEEEAAAGK DGDKSPMSSL QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP 550 560 570 580 590 600 SSIDAESNGE QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV 610 620 630 640 650 660 LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSYVE RQRSVHEKNG 670 680 690 700 710 720 KKICTLPSPP SPLASLAPVA DSSTRVDSPS HGLVTSSLCI PSPARLSQTP HSQPPRPGTC 730 740 KTSVATQCDP EEIIVLSDSD
	Isoform 2 [UniParc]. Checksum: 47E099676EB7315C		710	78,333
	10 20 30 40 50 60 MATANSIIVL DDDDEDEAAA QPGPSHPLPN AASPGAEAPS SSEPHGARGS SSSGGKKCYK 70 80 90 100 110 120 LENEKLFEEF LELCKMQTAD HPEVVPFLYN RQQRAHSLFL ASAEFCNILS RVLSRARSRP 130 140 150 160 170 180 AKLYVYINEL CTVLKAHSAK KKLNLAPAAT TSNEPSGNNP PTHLSLDPTN AENTASQSPR 190 200 210 220 230 240 TRGSRRQIQR LEQLLALYVA EIRRLQEKEL DLSELDDPDS AYLQEARLKR KLIRLFGRLC 250 260 270 280 290 300 ELKDCSSLTG RVIEQRIPYR GTRYPEVNRR IERLINKPGP DTFPDYGDVL RAVEKAAARH 310 320 330 340 350 360 SLGLPRQQLQ LMAQDAFRDV GIRLQERRHL DLIYNFGCHL TDDYRPGVDP ALSDPVLARR 370 380 390 400 410 420 LRENRSLAMS RLDEVISKYA MLQDKSEEGE RKKRRARLQG TSSHSADTPE ASLDSGEGPS 430 440 450 460 470 480 GMASQGCPSA SRAETDDEDD EESDEEEEEE EEEEEEEATD SEEEEDLEQM QEGQEDDEEE 490 500 510 520 530 540 DEEEEAAAGK DGDKSPMSSL QISNEKNLEP GKQISRSSGE QQNKGRIVSP SLLSEEPLAP 550 560 570 580 590 600 SSIDAESNGE QPEELTLEEE SPVSQLFELE IEALPLDTPS SVETDISSSR KQSEEPFTTV 610 620 630 640 650 660 LENGAGMVSS TSFNGGVSPH NWGDSGPPCK KSRKEKKQTG SGPLGNSYVE RQRSVHEKNG 670 680 690 700 710 KKICTLPSPP SPLASLAPVA DSSTRVDSPS HGLVTPAKNL GRRRSKQDQG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Daxx, a novel Fas-binding protein that activates JNK and apoptosis." Yang X., Khosravi-Far R., Chang H.Y., Baltimore D. Cell 89:1067-1076(1997) [PubMed: 9215629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Cloning and expression of primate Daxx cDNAs and mapping of the human gene to chromosome 6p21.3 in the MHC region." Kiriakidou M., Driscoll D.A., Lopez-Guisa J.M., Strauss J.F. III DNA Cell Biol. 16:1289-1298(1997) [PubMed: 9407001] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION. Tissue: Placenta.
[3]	"Interphase-specific association of intrinsic centromere protein CENP-C with HDaxx, a death domain-binding protein implicated in Fas-mediated cell death." Pluta A.F., Earnshaw W.C., Goldberg I.G. J. Cell Sci. 111:2029-2041(1998) [PubMed: 9645950] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CENPC1, SUBCELLULAR LOCATION. Tissue: Cervix carcinoma.
[4]	"TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense cluster at the centromeric end of the MHC." Herberg J.A., Beck S., Trowsdale J. J. Mol. Biol. 277:839-857(1998) [PubMed: 9545376] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[5]	"EAP1/Daxx interacts with ETS1 and represses transcriptional activation of ETS1 target genes." Li R., Pei H., Watson D.K., Papas T.S. Oncogene 19:745-753(2000) [PubMed: 10698492] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: T-cell.
[6]	Usui T. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 334-740 (ISOFORM 2). Tissue: Eye.
[9]	"The Pax3-FKHR oncoprotein is unresponsive to the Pax3-associated repressor hDaxx." Hollenbach A.D., Sublett J.E., McPherson C.J., Grosveld G. EMBO J. 18:3702-3711(1999) [PubMed: 10393185] [Abstract] Cited for: INTERACTION WITH PAX3 AND PAX7, PHOSPHORYLATION.
[10]	"Promyelocytic leukemia protein (PML) and Daxx participate in a novel nuclear pathway for apoptosis." Zhong S., Salomoni P., Ronchetti S., Guo A., Ruggero D., Pandolfi P.P. J. Exp. Med. 191:631-640(2000) [PubMed: 10684855] [Abstract] Cited for: INTERACTION WITH PML.
[11]	"Sequestration and inhibition of Daxx-mediated transcriptional repression by PML." Li H., Leo C., Zhu J., Wu X., O'Neil J., Park E.-J., Chen J.D. Mol. Cell. Biol. 20:1784-1796(2000) [PubMed: 10669754] [Abstract] Cited for: INTERACTION WITH SUMOYLATED PML; HDAC1; HDAC2 AND HDAC3.
[12]	"Inhibition of Daxx-mediated apoptosis by heat shock protein 27." Charette S.J., Lavoie J.N., Lambert H., Landry J. Mol. Cell. Biol. 20:7602-7612(2000) [PubMed: 11003656] [Abstract] Cited for: INTERACTION WITH HSPB1.
[13]	"Apoptosis signal-regulating kinase 1 controls the proapoptotic function of death-associated protein (Daxx) in the cytoplasm." Ko Y.-G., Kang Y.-S., Park H., Seol W., Kim J., Kim T., Park H.-S., Choi E.-J., Kim S. J. Biol. Chem. 276:39103-39106(2001) [PubMed: 11495919] [Abstract] Cited for: INTERACTION WITH MAP3K5, SUBCELLULAR LOCATION.
[14]	"TGF-beta-induced apoptosis is mediated by the adapter protein Daxx that facilitates JNK activation." Perlman R., Schiemann W.P., Brooks M.W., Lodish H.F., Weinberg R.A. Nat. Cell Biol. 3:708-714(2001) [PubMed: 11483955] [Abstract] Cited for: INTERACTION WITH TGFBR2.
[15]	"Modification of Daxx by small ubiquitin-related modifier-1." Jang M.-S., Ryu S.-W., Kim E. Biochem. Biophys. Res. Commun. 295:495-500(2002) [PubMed: 12150977] [Abstract] Cited for: SUMOYLATION, MUTAGENESIS OF LYS-630 AND LYS-631.
[16]	"The insulin-sensitive glucose transporter, GLUT4, interacts physically with Daxx. Two proteins with capacity to bind Ubc9 and conjugated to SUMO1." Lalioti V.S., Vergarajauregui S., Pulido D., Sandoval I.V. J. Biol. Chem. 277:19783-19791(2002) [PubMed: 11842083] [Abstract] Cited for: INTERACTION WITH SLC2A4 AND UBE2I, SUMOYLATION, SUBCELLULAR LOCATION.
[17]	"Essential role of the 58-kDa microspherule protein in the modulation of Daxx-dependent transcriptional repression as revealed by nucleolar sequestration." Lin D.-Y., Shih H.-M. J. Biol. Chem. 277:25446-25456(2002) [PubMed: 11948183] [Abstract] Cited for: INTERACTION WITH MCRS1.
[18]	"Daxx and histone deacetylase II associate with chromatin through an interaction with core histones and the chromatin-associated protein Dek." Hollenbach A.D., McPherson C.J., Mientjes E.J., Iyengar R., Grosveld G. J. Cell Sci. 115:3319-3330(2002) [PubMed: 12140263] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH HDAC2; HISTONES AND DEK.
[19]	"HIPK2 regulates transforming growth factor-beta-induced c-Jun NH(2)-terminal kinase activation and apoptosis in human hepatoma cells." Hofmann T.G., Stollberg N., Schmitz M.L., Will H. Cancer Res. 63:8271-8277(2003) [PubMed: 14678985] [Abstract] Cited for: INTERACTION WITH HIPK2.
[20]	"Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1 oligomerization." Song J.J., Lee Y.J. J. Biol. Chem. 278:47245-47252(2003) [PubMed: 12968034] [Abstract] Cited for: OLIGOMERIZATION, SUBCELLULAR LOCATION, INTERACTION WITH MAP3K5, MUTAGENESIS OF SER-668 AND SER-671, PHOSPHORYLATION AT SER-668.
[21]	"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) [PubMed: 12529400] [Abstract] Cited for: INTERACTION WITH HIPK1.
[22]	"Daxx-mediated transcriptional repression of MMP1 gene is reversed by SPOP." La M., Kim K., Park J., Won J., Lee J.-H., Fu Y.M., Meadows G.G., Joe C.O. Biochem. Biophys. Res. Commun. 320:760-765(2004) [PubMed: 15240113] [Abstract] Cited for: INTERACTION WITH SPOP.
[23]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-671, MASS SPECTROMETRY.