Q15047 (SETB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone-lysine N-methyltransferase SETDB1
EC=2.1.1.43

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

Gene names

Name:	SETDB1
Synonyms:	KIAA0067, KMT1E

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1291 AA.
Sequence status	Complete.
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. Ref.6 Ref.7 Ref.8 Ref.15
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
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, CHD7, DNMT3A, HDAC1, HDAC2, NLK, PPARG, SIN3A, SIN3B, DNMT3B and SUMO2. Interacts with MPHOSPH8. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.18
Subcellular location	Nucleus. Chromosome. 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. Isoform 2 lacks all domains required for histone methyltransferase activity.
Miscellaneous	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 BAA06689.2 differs from that shown. Reason: Erroneous initiation. 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	Chromosome Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
Ligand	S-adenosyl-L-methionine
Molecular function	Chromatin regulator Methyltransferase Repressor Transferase
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inner cell mass cell proliferation Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA chromosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro histone-lysine N-methyltransferase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AKT1	P31749	9	EBI-79691,EBI-296087
DNMT3A	Q9Y6K1	7	EBI-79691,EBI-923653

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.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q15047-3)

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

Note: 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

976

1

Phosphothreonine; by NLK Probable

Modified residue

1066

1

Phosphoserine Ref.16 Ref.17 Ref.20

Cross-link

182

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

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.
Corresponds to variant rs2271075 [ dbSNP | Ensembl ].

VAR_014284

Natural variant

506

1

P → S. Ref.4
Corresponds to variant rs17852587 [ dbSNP | Ensembl ].

VAR_031281

Natural variant

824

1

A → G.
Corresponds to variant rs2691551 [ dbSNP | Ensembl ].

VAR_014286

Natural variant

824

1

A → P.
Corresponds to variant rs2814054 [ dbSNP | Ensembl ].

VAR_014285

Experimental info

Mutagenesis

729 – 731

3

CDC → LDP: Abolishes methyltransferase activity. Ref.5

Mutagenesis

976

1

T → A: Abrogates interaction with CHD7, NLK and PPARG. Reduces phosphorylation by NLK. Reduces transcriptional repression. Ref.15

Mutagenesis

1224

1

H → K: Abolishes methyltransferase activity. Ref.5

Mutagenesis

1226

1

C → A: Abolishes methyltransferase activity. Ref.5

Mutagenesis

1279

1

C → Y: Abolishes methyltransferase activity. Ref.5

Secondary structure

1

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1291

Helix Strand Turn

Details...

Beta strand

203 – 207

5

Beta strand

213 – 224

12

Beta strand

227 – 237

11

Beta strand

239 – 242

4

Helix

244 – 246

3

Beta strand

247 – 251

5

Helix

255 – 257

3

Beta strand

263 – 269

7

Beta strand

274 – 283

10

Turn

287 – 290

4

Beta strand

293 – 297

5

Beta strand

302 – 305

4

Helix

307 – 309

3

Beta strand

310 – 315

6

Helix

320 – 323

4

Helix

327 – 339

13

Beta strand

353 – 358

6

Beta strand

361 – 371

11

Beta strand

374 – 379

6

Turn

380 – 383

4

Beta strand

384 – 389

6

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	FASTA	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	FASTA	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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CBX1 AND CBX5.
[10]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MBD1.
[11]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ATF7IP AND ATF7IP2.
[12]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DNMT3A AND DNMT3B.
[13]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SUMO2.
[14]	"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] [Europe PMC] [Abstract] Cited for: EXPRESSION IN HUNTINGTON DISEASE.
[15]	"A histone lysine methyltransferase activated by non-canonical Wnt signalling suppresses PPAR-gamma transactivation." Takada I., Mihara M., Suzawa M., Ohtake F., Kobayashi S., Igarashi M., Youn M.Y., Takeyama K., Nakamura T., Mezaki Y., Takezawa S., Yogiashi Y., Kitagawa H., Yamada G., Takada S., Minami Y., Shibuya H., Matsumoto K., Kato S. Nat. Cell Biol. 9:1273-1285(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CHD7; NLK1 AND PPARG, PHOSPHORYLATION AT THR-976, MUTAGENESIS OF THR-976.
[16]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing and promotes tumour cell motility and invasion." Kokura K., Sun L., Bedford M.T., Fang J. EMBO J. 29:3673-3687(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MPHOSPH8.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, MASS SPECTROMETRY.
[21]	"The crystal structure of Tudor domain of human histone-lysine N-methyltransferase SETDB1." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 196-402.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00018321.
IPI00218321.
IPI00879832.

RefSeq

NP_001138887.1. NM_001145415.1.
NP_001230420.1. NM_001243491.1.
NP_036564.3. NM_012432.3.

UniGene

Hs.643565.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

Q15047.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31029N.

IntAct

Q15047. 81 interactions.

MINT

MINT-1184137.

STRING

9606.ENSP00000357965.

PTM databases

PhosphoSite

Q15047.

Polymorphism databases

DMDM

25091210.

Proteomic databases

PaxDb

Q15047.

PRIDE

Q15047.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000271640; ENSP00000271640; ENSG00000143379.
ENST00000368962; ENSP00000357958; ENSG00000143379.
ENST00000368963; ENSP00000357959; ENSG00000143379.
ENST00000368969; ENSP00000357965; ENSG00000143379.
ENST00000423081; ENSP00000407831; ENSG00000143379.

GeneID

9869.

KEGG

hsa:9869.

UCSC

uc001evu.2. human.
uc001evv.2. human.
uc001evw.4. human.

Organism-specific databases

CTD

9869.

GeneCards

GC01P150898.

HGNC

HGNC:10761. SETDB1.

HPA

HPA018142.

MIM

604396. gene.

neXtProt

NX_Q15047.

PharmGKB

PA35679.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2940.

HOVERGEN

HBG061013.

InParanoid

Q15047.

KO

K11421.

OMA

PSKTSMH.

OrthoDB

EOG46Q6RR.

Gene expression databases

ArrayExpress

Q15047.

Bgee

Q15047.

CleanEx

HS_SETDB1.

Genevestigator

Q15047.

GermOnline

ENSG00000143379. Homo sapiens.

Family and domain databases

InterPro

IPR016177. DNA-bd_integrase-typ.
IPR025796. Hist-Lys_N-MeTrfase_SETDB1.
IPR001739. Methyl_CpG_DNA-bd.
IPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR003606. Pre-SET_Zn-bd_sub.
IPR001214. SET_dom.
IPR002999. Tudor.
[Graphical view]

Pfam

PF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]

SMART

SM00391. MBD. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
SM00333. TUDOR. 2 hits.
[Graphical view]

SUPFAM

SSF54171. DNA-binding_integrase-type. 1 hit.

PROSITE

PS50982. MBD. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
PS50304. TUDOR. False negative.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SETDB1. human.

EvolutionaryTrace

Q15047.

GenomeRNAi

9869.

NextBio

37203.

SOURCE

Search...

Entry information

Entry name

SETB1_HUMAN

Accession

Primary (citable) accession number: Q15047
Secondary accession number(s): A6NEW2 , Q5SZD8, Q5SZD9, Q5SZE0, Q5SZE7, Q96GM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 15, 2002
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 146 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.