Reviewed, UniProtKB/Swiss-Prot Q15047 (SETB1_HUMAN)

Names and origin

Protein names

Recommended name:
    Histone-lysine N-methyltransferase SETDB1
    EC=2.1.1.43
Alternative name(s):
    SET domain bifurcated 1
    ERG-associated protein with SET domain
      Short name=ESET
    Histone H3-K9 methyltransferase 4
    H3-K9-HMTase 4
    Lysine N-methyltransferase 1E

Gene names

Name:	SETDB1
Synonyms:	KIAA0067, KMT1E

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	1291 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3. H3 'Lys-9' trimethylation represents a specific tag for epigenetic transcriptional repression by recruiting HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. H3 'Lys-9' trimethylation is coordinated with DNA methylation. Probably forms a complex with MBD1 and ATF7IP that represses transcription and couples DNA methylation and histone 'Lys-9' trimethylation. Its activity is dependent on MBD1 and is heritably maintained through DNA replication by being recruited by CAF-1. SETDB1 is targeted to histone H3 by TRIM28/TIF1B, a factor recruited by KRAB zinc-finger proteins.
Catalytic activity	S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine.
Subunit structure	Interacts with MBD1; interaction is abolished when MBD1 is sumoylated. Interacts with ATF7IP and ATF7IP2; the interaction with ATF7IP is required to stimulate histone methyltransferase activity and facilitate the conversion of dimethylated to trimethylated H3 'Lys-9'. During DNA replication, it is recruited by SETDB1 to form a S phase-specific complex that facilitates methylation of H3 'Lys-9' during replication-coupled chromatin assembly and is at least composed of the CAF-1 subunit CHAF1A, MBD1 and SETDB1. Interacts with ERG, TRIM28/TIF1B, CBX1, CBX5, DNMT3A, HDAC1, HDAC2, SIN3A, SIN3B, DNMT3B and SUMO2.
Subcellular location	Nucleus. Note= Associated with non-pericentromeric regions of chromatin. Excluded from nucleoli and islands of condensed chromatin.
Tissue specificity	Widely expressed. High expression in testis.
Domain	The pre-SET, SET and post-SET domains are all required for methyltransferase activity. The 347-amino-acid insertion in the SET domain has no effect on the catalytic activity.
Miscellaneous	Isoform 2 lacks all domains required for histone methyltransferase activity. Highly up-regulated in Huntington disease patients, suggesting that participates in the altered chromatin modulation and transcription dysfunction observed in Huntington disease. Its down-regulation has salubrious effects on patients, suggesting that it may be a promising treatment in Huntington disease patients.
Sequence similarities	Belongs to the histone-lysine methyltransferase family. Suvar3-9 subfamily. Contains 1 MBD (methyl-CpG-binding) domain. Contains 1 post-SET domain. Contains 1 pre-SET domain. Contains 1 SET domain. Contains 2 Tudor domains.
Sequence caution	The sequence CAI13325.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAI13326.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Chromosomal protein Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Repressor Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	chromatin modification Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chromosome Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: InterPro
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro histone-lysine N-methyltransferase activity Inferred from electronic annotation. Source: InterPro protein binding Ref.13 Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AKT1	P31749	6	EBI-79691,EBI-296087
AKT2	P31751	1	EBI-79691,EBI-296058
DNMT3A	Q9Y6K1	2	EBI-79691,EBI-923653
DNMT3B	Q9UBC3-2	1	EBI-79691,EBI-287723
DNMT3B	Q9UBC3-3	1	EBI-79691,EBI-287726
ERG	P11308	1	EBI-79691,EBI-79704

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15047-1)

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: Q15047-2)

The sequence of this isoform differs from the canonical sequence as follows:
     381-397: DDKRCEWIYRGSTRLEP → VLFFSTILEAEVGGGGT
     398-1291: Missing.

Notes: No experimental confirmation available.

Isoform 3 (identifier: Q15047-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1254-1254: Missing.

Notes: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1291	1291	Histone-lysine N-methyltransferase SETDB1		PRO_0000186064
Regions
	Domain	257 – 320	64	Tudor 1
	Domain	347 – 403	57	Tudor 2
	Domain	594 – 665	72	MBD
	Domain	727 – 800	74	Pre-SET
	Domain	802 – 1270	469	SET
	Domain	1275 – 1291	17	Post-SET
	Coiled coil	18 – 64	47	Potential
Amino acid modifications
	Modified residue	838	1	Phosphothreonine
	Modified residue	1066	1	Phosphoserine
	Modified residue	1179	1	Phosphoserine
	Modified residue	1180	1	Phosphothreonine
	Modified residue	1190	1	Phosphoserine
Natural variations
	Alternative sequence	381 – 397	17	DDKRC…TRLEP → VLFFSTILEAEVGGGGT in isoform 2.		VSP_002217
	Alternative sequence	398 – 1291	894	Missing in isoform 2.		VSP_002218
	Alternative sequence	1254	1	Missing in isoform 3.		VSP_034600
	Natural variant	236	1	N → S: dbSNP rs2271075.		VAR_014284
	Natural variant	506	1	P → S: dbSNP rs17852587.		VAR_031281
	Natural variant	824	1	A → G: dbSNP rs2691551.		VAR_014286
	Natural variant	824	1	A → P: dbSNP rs2814054.		VAR_014285
Experimental info
	Mutagenesis	729 – 731	3	CDC → LDP: Abolishes methyltransferase activity
	Mutagenesis	1224	1	H → K: Abolishes methyltransferase activity
	Mutagenesis	1226	1	C → A: Abolishes methyltransferase activity
	Mutagenesis	1279	1	C → Y: Abolishes methyltransferase activity

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: D8841B4C41B911C5	FASTA	1,291	143,157
	10 20 30 40 50 60 MSSLPGCIGL DAATATVESE EIAELQQAVV EELGISMEEL RHFIDEELEK MDCVQQRKKQ 70 80 90 100 110 120 LAELETWVIQ KESEVAHVDQ LFDDASRAVT NCESLVKDFY SKLGLQYRDS SSEDESSRPT 130 140 150 160 170 180 EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL REAMAALRKS AQDVQKFMDA VNKKSSSQDL 190 200 210 220 230 240 HKGTLSQMSG ELSKDGDLIV SMRILGKKRT KTWHKGTLIA IQTVGPGKKY KVKFDNKGKS 250 260 270 280 290 300 LLSGNHIAYD YHPPADKLYV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG 310 320 330 340 350 360 YASYVTQSEL YPICRPLKKT WEDIEDISCR DFIEEYVTAY PNRPMVLLKS GQLIKTEWEG 370 380 390 400 410 420 TWWKSRVEEV DGSLVRILFL DDKRCEWIYR GSTRLEPMFS MKTSSASALE KKQGQLRTRP 430 440 450 460 470 480 NMGAVRSKGP VVQYTQDLTG TGTQFKPVEP PQPTAPPAPP FPPAPPLSPQ AGDSDLESQL 490 500 510 520 530 540 AQSRKQVAKK STSFRPGSVG SGHSSPTSPA LSENVSGGKP GINQTYRSPL GSTASAPAPS 550 560 570 580 590 600 ALPAPPAPPV FHGMLERAPA EPSYRAPMEK LFYLPHVCSY TCLSRVRPMR NEQYRGKNPL 610 620 630 640 650 660 LVPLLYDFRR MTARRRVNRK MGFHVIYKTP CGLCLRTMQE IERYLFETGC DFLFLEMFCL 670 680 690 700 710 720 DPYVLVDRKF QPYKPFYYIL DITYGKEDVP LSCVNEIDTT PPPQVAYSKE RIPGKGVFIN 730 740 750 760 770 780 TGPEFLVGCD CKDGCRDKSK CACHQLTIQA TACTPGGQIN PNSGYQYKRL EECLPTGVYE 790 800 810 820 830 840 CNKRCKCDPN MCTNRLVQHG LQVRLQLFKT QNKGWGIRCL DDIAKGSFVC IYAGKILTDD 850 860 870 880 890 900 FADKEGLEMG DEYFANLDHI ESVENFKEGY ESDAPCSSDS SGVDLKDQED GNSGTEDPEE 910 920 930 940 950 960 SNDDSSDDNF CKDEDFSTSS VWRSYATRRQ TRGQKENGLS ETTSKDSHPP DLGPPHIPVP 970 980 990 1000 1010 1020 PSIPVGGCNP PSSEETPKNK VASWLSCNSV SEGGFADSDS HSSFKTNEGG EGRAGGSRME 1030 1040 1050 1060 1070 1080 AEKASTSGLG IKDEGDIKQA KKEDTDDRNK MSVVTESSRN YGYNPSPVKP EGLRRPPSKT 1090 1100 1110 1120 1130 1140 SMHQSRRLMA SAQSNPDDVL TLSSSTESEG ESGTSRKPTA GQTSATAVDS DDIQTISSGS 1150 1160 1170 1180 1190 1200 EGDDFEDKKN MTGPMKRQVA VKSTRGFALK STHGIAIKST NMASVDKGES APVRKNTRQF 1210 1220 1230 1240 1250 1260 YDGEESCYII DAKLEGNLGR YLNHSCSPNL FVQNVFVDTH DLRFPWVAFF ASKRIRAGTE 1270 1280 1290 LTWDYNYEVG SVEGKELLCC CGAIECRGRL L
	Isoform 2 [UniParc]. Checksum: A880C9152E11A900		397	44,689
	10 20 30 40 50 60 MSSLPGCIGL DAATATVESE EIAELQQAVV EELGISMEEL RHFIDEELEK MDCVQQRKKQ 70 80 90 100 110 120 LAELETWVIQ KESEVAHVDQ LFDDASRAVT NCESLVKDFY SKLGLQYRDS SSEDESSRPT 130 140 150 160 170 180 EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL REAMAALRKS AQDVQKFMDA VNKKSSSQDL 190 200 210 220 230 240 HKGTLSQMSG ELSKDGDLIV SMRILGKKRT KTWHKGTLIA IQTVGPGKKY KVKFDNKGKS 250 260 270 280 290 300 LLSGNHIAYD YHPPADKLYV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG 310 320 330 340 350 360 YASYVTQSEL YPICRPLKKT WEDIEDISCR DFIEEYVTAY PNRPMVLLKS GQLIKTEWEG 370 380 390 TWWKSRVEEV DGSLVRILFL VLFFSTILEA EVGGGGT
	Isoform 3 [UniParc]. Checksum: BBF5516339BE6C17		1,290	143,001
	10 20 30 40 50 60 MSSLPGCIGL DAATATVESE EIAELQQAVV EELGISMEEL RHFIDEELEK MDCVQQRKKQ 70 80 90 100 110 120 LAELETWVIQ KESEVAHVDQ LFDDASRAVT NCESLVKDFY SKLGLQYRDS SSEDESSRPT 130 140 150 160 170 180 EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL REAMAALRKS AQDVQKFMDA VNKKSSSQDL 190 200 210 220 230 240 HKGTLSQMSG ELSKDGDLIV SMRILGKKRT KTWHKGTLIA IQTVGPGKKY KVKFDNKGKS 250 260 270 280 290 300 LLSGNHIAYD YHPPADKLYV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG 310 320 330 340 350 360 YASYVTQSEL YPICRPLKKT WEDIEDISCR DFIEEYVTAY PNRPMVLLKS GQLIKTEWEG 370 380 390 400 410 420 TWWKSRVEEV DGSLVRILFL DDKRCEWIYR GSTRLEPMFS MKTSSASALE KKQGQLRTRP 430 440 450 460 470 480 NMGAVRSKGP VVQYTQDLTG TGTQFKPVEP PQPTAPPAPP FPPAPPLSPQ AGDSDLESQL 490 500 510 520 530 540 AQSRKQVAKK STSFRPGSVG SGHSSPTSPA LSENVSGGKP GINQTYRSPL GSTASAPAPS 550 560 570 580 590 600 ALPAPPAPPV FHGMLERAPA EPSYRAPMEK LFYLPHVCSY TCLSRVRPMR NEQYRGKNPL 610 620 630 640 650 660 LVPLLYDFRR MTARRRVNRK MGFHVIYKTP CGLCLRTMQE IERYLFETGC DFLFLEMFCL 670 680 690 700 710 720 DPYVLVDRKF QPYKPFYYIL DITYGKEDVP LSCVNEIDTT PPPQVAYSKE RIPGKGVFIN 730 740 750 760 770 780 TGPEFLVGCD CKDGCRDKSK CACHQLTIQA TACTPGGQIN PNSGYQYKRL EECLPTGVYE 790 800 810 820 830 840 CNKRCKCDPN MCTNRLVQHG LQVRLQLFKT QNKGWGIRCL DDIAKGSFVC IYAGKILTDD 850 860 870 880 890 900 FADKEGLEMG DEYFANLDHI ESVENFKEGY ESDAPCSSDS SGVDLKDQED GNSGTEDPEE 910 920 930 940 950 960 SNDDSSDDNF CKDEDFSTSS VWRSYATRRQ TRGQKENGLS ETTSKDSHPP DLGPPHIPVP 970 980 990 1000 1010 1020 PSIPVGGCNP PSSEETPKNK VASWLSCNSV SEGGFADSDS HSSFKTNEGG EGRAGGSRME 1030 1040 1050 1060 1070 1080 AEKASTSGLG IKDEGDIKQA KKEDTDDRNK MSVVTESSRN YGYNPSPVKP EGLRRPPSKT 1090 1100 1110 1120 1130 1140 SMHQSRRLMA SAQSNPDDVL TLSSSTESEG ESGTSRKPTA GQTSATAVDS DDIQTISSGS 1150 1160 1170 1180 1190 1200 EGDDFEDKKN MTGPMKRQVA VKSTRGFALK STHGIAIKST NMASVDKGES APVRKNTRQF 1210 1220 1230 1240 1250 1260 YDGEESCYII DAKLEGNLGR YLNHSCSPNL FVQNVFVDTH DLRFPWVAFF ASKIRAGTEL 1270 1280 1290 TWDYNYEVGS VEGKELLCCC GAIECRGRLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1." Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S. DNA Res. 1:223-229(1994) [PubMed: 7584044] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Bone marrow.
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] (ISOFORMS 1; 2 AND 3), VARIANT SER-506. Tissue: Muscle and Uterus.
[5]	"SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins." Schultz D.C., Ayyanathan K., Negorev D., Maul G.G., Rauscher F.J. III Genes Dev. 16:919-932(2002) [PubMed: 11959841] [Abstract] Cited for: CHARACTERIZATION, MUTAGENESIS OF 729-CYS--CYS-731; HIS-1224; CYS-1226 AND CYS-1279, INTERACTION WITH TRIM28.
[6]	"Regulated recruitment of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: a mammalian cell culture model of gene variegation." Ayyanathan K., Lechner M.S., Bell P., Maul G.G., Schultz D.C., Yamada Y., Tanaka K., Torigoe K., Rauscher F.J. III Genes Dev. 17:1855-1869(2003) [PubMed: 12869583] [Abstract] Cited for: FUNCTION.
[7]	"mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression." Wang H., An W., Cao R., Xia L., Erdjument-Bromage H., Chatton B., Tempst P., Roeder R.G., Zhang Y. Mol. Cell 12:475-487(2003) [PubMed: 14536086] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH ATF7IP.
[8]	"Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly." Sarraf S.A., Stancheva I. Mol. Cell 15:595-605(2004) [PubMed: 15327775] [Abstract] Cited for: FUNCTION, INTERACTION WITH MBD1 AND CHAF1A.
[9]	"In vivo HP1 targeting causes large-scale chromatin condensation and enhanced histone lysine methylation." Verschure P.J., van der Kraan I., de Leeuw W., van der Vlag J., Carpenter A.E., Belmont A.S., van Driel R. Mol. Cell. Biol. 25:4552-4564(2005) [PubMed: 15899859] [Abstract] Cited for: INTERACTION WITH CBX1 AND CBX5.
[10]	"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC." Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J. Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-838, MASS SPECTROMETRY. Tissue: Hepatocyte.
[11]	"Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins." Lyst M.J., Nan X., Stancheva I. EMBO J. 25:5317-5328(2006) [PubMed: 17066076] [Abstract] Cited for: INTERACTION WITH MBD1.
[12]	"Transcriptional repression and heterochromatin formation by MBD1 and MCAF/AM family proteins." Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M. J. Biol. Chem. 280:13928-13935(2005) [PubMed: 15691849] [Abstract] Cited for: INTERACTION WITH ATF7IP AND ATF7IP2.
[13]	"The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A interact directly and localize to promoters silenced in cancer cells." Li H., Rauch T., Chen Z.-X., Szabo P.E., Riggs A.D., Pfeifer G.P. J. Biol. Chem. 281:19489-19500(2006) [PubMed: 16682412] [Abstract] Cited for: INTERACTION WITH DNMT3A AND DNMT3B.
[14]	"NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression." Rosendorff A., Sakakibara S., Lu S., Kieff E., Xuan Y., DiBacco A., Shi Y., Shi Y., Gill G. Proc. Natl. Acad. Sci. U.S.A. 103:5308-5313(2006) [PubMed: 16567619] [Abstract] Cited for: INTERACTION WITH SUMO2.
[15]	"ESET/SETDB1 gene expression and histone H3 (K9) trimethylation in Huntington's disease." Ryu H., Lee J., Hagerty S.W., Soh B.Y., McAlpin S.E., Cormier K.A., Smith K.M., Ferrante R.J. Proc. Natl. Acad. Sci. U.S.A. 103:19176-19181(2006) [PubMed: 17142323] [Abstract] Cited for: EXPRESSION IN HUNTINGTON DISEASE.
[16]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1179; THR-1180 AND SER-1190, MASS SPECTROMETRY.
[17]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, MASS SPECTROMETRY.
[18]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBLGenBankDDBJ

D31891 mRNA. Translation: BAA06689.2. Different initiation.
AL590133 Genomic DNA. Translation: CAI13325.1. Sequence problems.
AL590133 Genomic DNA. Translation: CAI13326.1. Sequence problems.
AL590133 Genomic DNA. Translation: CAI13327.1.
AL590133 Genomic DNA. Translation: CAI13328.1.
CH471121 Genomic DNA. Translation: EAW53506.1.
BC009362 mRNA. Translation: AAH09362.1.
BC028671 mRNA. Translation: AAH28671.1.

RefSeq

NP_036564.2.

UniGene

Hs.643565

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3DLM	X-ray	1.77	A	196-402	[»]

ModBase

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