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Q15047

- SETB1_HUMAN

UniProt

Q15047 - SETB1_HUMAN

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Protein

Histone-lysine N-methyltransferase SETDB1

Gene

SETDB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi729 – 7291Zinc 1By similarity
Metal bindingi729 – 7291Zinc 2By similarity
Metal bindingi731 – 7311Zinc 1By similarity
Metal bindingi735 – 7351Zinc 1By similarity
Metal bindingi735 – 7351Zinc 3By similarity
Metal bindingi741 – 7411Zinc 1By similarity
Metal bindingi743 – 7431Zinc 2By similarity
Metal bindingi781 – 7811Zinc 2By similarity
Metal bindingi781 – 7811Zinc 3By similarity
Metal bindingi785 – 7851Zinc 2By similarity
Metal bindingi787 – 7871Zinc 3By similarity
Metal bindingi792 – 7921Zinc 3By similarity
Binding sitei851 – 8511S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei853 – 8531S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei1220 – 12201S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi1226 – 12261Zinc 4By similarity
Metal bindingi1279 – 12791Zinc 4By similarity
Metal bindingi1281 – 12811Zinc 4By similarity
Metal bindingi1286 – 12861Zinc 4By similarity

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
  3. zinc ion binding Source: InterPro

GO - Biological processi

  1. bone development Source: Ensembl
  2. histone H3-K9 trimethylation Source: Ensembl
  3. inner cell mass cell proliferation Source: Ensembl
  4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:SETDB1
Synonyms:KIAA0067, KMT1E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10761. SETDB1.

Subcellular locationi

Nucleus. Chromosome
Note: Associated with non-pericentromeric regions of chromatin. Excluded from nucleoli and islands of condensed chromatin.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. Golgi apparatus Source: HPA
  3. nuclear chromatin Source: Ensembl
  4. nucleus Source: HPA
  5. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi729 – 7313CDC → LDP: Abolishes methyltransferase activity. 1 Publication
Mutagenesisi976 – 9761T → A: Abrogates interaction with CHD7, NLK and PPARG. Reduces phosphorylation by NLK. Reduces transcriptional repression. 1 Publication
Mutagenesisi1224 – 12241H → K: Abolishes methyltransferase activity. 1 Publication
Mutagenesisi1226 – 12261C → A: Abolishes methyltransferase activity. 1 Publication
Mutagenesisi1279 – 12791C → Y: Abolishes methyltransferase activity. 1 Publication

Organism-specific databases

PharmGKBiPA35679.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12911291Histone-lysine N-methyltransferase SETDB1PRO_0000186064Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki182 – 182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei976 – 9761Phosphothreonine; by NLK1 Publication
Modified residuei1066 – 10661Phosphoserine3 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ15047.
PaxDbiQ15047.
PRIDEiQ15047.

PTM databases

PhosphoSiteiQ15047.

Expressioni

Tissue specificityi

Widely expressed. High expression in testis.

Gene expression databases

BgeeiQ15047.
CleanExiHS_SETDB1.
ExpressionAtlasiQ15047. baseline and differential.
GenevestigatoriQ15047.

Organism-specific databases

HPAiHPA018142.

Interactioni

Subunit structurei

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. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AKT1P317499EBI-79691,EBI-296087
DNMT3AQ9Y6K17EBI-79691,EBI-923653
MBD1Q9UIS93EBI-79691,EBI-867196
MPHOSPH8Q995492EBI-79691,EBI-2653928
ZDHHC17Q8IUH53EBI-9090795,EBI-524753

Protein-protein interaction databases

BioGridi115202. 126 interactions.
DIPiDIP-31029N.
IntActiQ15047. 108 interactions.
MINTiMINT-1184137.
STRINGi9606.ENSP00000357965.

Structurei

Secondary structure

1
1291
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi203 – 2075Combined sources
Beta strandi213 – 22412Combined sources
Beta strandi227 – 23711Combined sources
Beta strandi239 – 2424Combined sources
Helixi244 – 2463Combined sources
Beta strandi247 – 2515Combined sources
Helixi255 – 2573Combined sources
Beta strandi263 – 2697Combined sources
Beta strandi274 – 28310Combined sources
Turni287 – 2904Combined sources
Beta strandi293 – 2975Combined sources
Beta strandi302 – 3054Combined sources
Helixi307 – 3093Combined sources
Beta strandi310 – 3156Combined sources
Helixi320 – 3234Combined sources
Helixi327 – 33913Combined sources
Beta strandi353 – 3586Combined sources
Beta strandi361 – 37111Combined sources
Beta strandi374 – 3796Combined sources
Turni380 – 3834Combined sources
Beta strandi384 – 3896Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DLMX-ray1.77A196-402[»]
ProteinModelPortaliQ15047.
SMRiQ15047. Positions 196-397, 681-881, 1134-1291.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15047.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini257 – 32064Tudor 1Add
BLAST
Domaini347 – 40357Tudor 2Add
BLAST
Domaini594 – 66572MBDPROSITE-ProRule annotationAdd
BLAST
Domaini727 – 80074Pre-SETPROSITE-ProRule annotationAdd
BLAST
Domaini803 – 1266464SETPROSITE-ProRule annotationAdd
BLAST
Domaini1275 – 129117Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni813 – 8153S-adenosyl-L-methionine bindingBy similarity
Regioni1223 – 12242S-adenosyl-L-methionine bindingBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili18 – 6447Sequence AnalysisAdd
BLAST

Domaini

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.
In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.By similarity

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
Contains 1 MBD (methyl-CpG-binding) domain.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 pre-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation
Contains 2 Tudor domains.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000119330.
HOVERGENiHBG061013.
InParanoidiQ15047.
KOiK11421.
OMAiGSVGSGH.
OrthoDBiEOG7ZD1TG.
PhylomeDBiQ15047.
TreeFamiTF106411.

Family and domain databases

InterProiIPR016177. DNA-bd_dom.
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]
PfamiPF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00391. MBD. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
SM00333. TUDOR. 2 hits.
[Graphical view]
SUPFAMiSSF54171. SSF54171. 1 hit.
PROSITEiPS50982. MBD. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS51573. SAM_MT43_SUVAR39_1. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15047-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSSLPGCIGL DAATATVESE EIAELQQAVV EELGISMEEL RHFIDEELEK
60 70 80 90 100
MDCVQQRKKQ LAELETWVIQ KESEVAHVDQ LFDDASRAVT NCESLVKDFY
110 120 130 140 150
SKLGLQYRDS SSEDESSRPT EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL
160 170 180 190 200
REAMAALRKS AQDVQKFMDA VNKKSSSQDL HKGTLSQMSG ELSKDGDLIV
210 220 230 240 250
SMRILGKKRT KTWHKGTLIA IQTVGPGKKY KVKFDNKGKS LLSGNHIAYD
260 270 280 290 300
YHPPADKLYV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG
310 320 330 340 350
YASYVTQSEL YPICRPLKKT WEDIEDISCR DFIEEYVTAY PNRPMVLLKS
360 370 380 390 400
GQLIKTEWEG TWWKSRVEEV DGSLVRILFL DDKRCEWIYR GSTRLEPMFS
410 420 430 440 450
MKTSSASALE KKQGQLRTRP NMGAVRSKGP VVQYTQDLTG TGTQFKPVEP
460 470 480 490 500
PQPTAPPAPP FPPAPPLSPQ AGDSDLESQL AQSRKQVAKK STSFRPGSVG
510 520 530 540 550
SGHSSPTSPA LSENVSGGKP GINQTYRSPL GSTASAPAPS ALPAPPAPPV
560 570 580 590 600
FHGMLERAPA EPSYRAPMEK LFYLPHVCSY TCLSRVRPMR NEQYRGKNPL
610 620 630 640 650
LVPLLYDFRR MTARRRVNRK MGFHVIYKTP CGLCLRTMQE IERYLFETGC
660 670 680 690 700
DFLFLEMFCL DPYVLVDRKF QPYKPFYYIL DITYGKEDVP LSCVNEIDTT
710 720 730 740 750
PPPQVAYSKE RIPGKGVFIN TGPEFLVGCD CKDGCRDKSK CACHQLTIQA
760 770 780 790 800
TACTPGGQIN PNSGYQYKRL EECLPTGVYE CNKRCKCDPN MCTNRLVQHG
810 820 830 840 850
LQVRLQLFKT QNKGWGIRCL DDIAKGSFVC IYAGKILTDD FADKEGLEMG
860 870 880 890 900
DEYFANLDHI ESVENFKEGY ESDAPCSSDS SGVDLKDQED GNSGTEDPEE
910 920 930 940 950
SNDDSSDDNF CKDEDFSTSS VWRSYATRRQ TRGQKENGLS ETTSKDSHPP
960 970 980 990 1000
DLGPPHIPVP PSIPVGGCNP PSSEETPKNK VASWLSCNSV SEGGFADSDS
1010 1020 1030 1040 1050
HSSFKTNEGG EGRAGGSRME AEKASTSGLG IKDEGDIKQA KKEDTDDRNK
1060 1070 1080 1090 1100
MSVVTESSRN YGYNPSPVKP EGLRRPPSKT SMHQSRRLMA SAQSNPDDVL
1110 1120 1130 1140 1150
TLSSSTESEG ESGTSRKPTA GQTSATAVDS DDIQTISSGS EGDDFEDKKN
1160 1170 1180 1190 1200
MTGPMKRQVA VKSTRGFALK STHGIAIKST NMASVDKGES APVRKNTRQF
1210 1220 1230 1240 1250
YDGEESCYII DAKLEGNLGR YLNHSCSPNL FVQNVFVDTH DLRFPWVAFF
1260 1270 1280 1290
ASKRIRAGTE LTWDYNYEVG SVEGKELLCC CGAIECRGRL L
Length:1,291
Mass (Da):143,157
Last modified:November 1, 1996 - v1
Checksum:iD8841B4C41B911C5
GO
Isoform 2 (identifier: Q15047-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:397
Mass (Da):44,689
Checksum:iA880C9152E11A900
GO
Isoform 3 (identifier: Q15047-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:1,290
Mass (Da):143,001
Checksum:iBBF5516339BE6C17
GO

Sequence cautioni

The sequence BAA06689.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAI13325.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI13326.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti236 – 2361N → S.
Corresponds to variant rs2271075 [ dbSNP | Ensembl ].
VAR_014284
Natural varianti506 – 5061P → S.1 Publication
Corresponds to variant rs17852587 [ dbSNP | Ensembl ].
VAR_031281
Natural varianti824 – 8241A → G.
Corresponds to variant rs2691551 [ dbSNP | Ensembl ].
VAR_014286
Natural varianti824 – 8241A → P.
Corresponds to variant rs2814054 [ dbSNP | Ensembl ].
VAR_014285

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei381 – 39717DDKRC…TRLEP → VLFFSTILEAEVGGGGT in isoform 2. 1 PublicationVSP_002217Add
BLAST
Alternative sequencei398 – 1291894Missing in isoform 2. 1 PublicationVSP_002218Add
BLAST
Alternative sequencei1254 – 12541Missing in isoform 3. 1 PublicationVSP_034600

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44217.1. [Q15047-1]
CCDS58026.1. [Q15047-2]
CCDS972.1. [Q15047-3]
RefSeqiNP_001138887.1. NM_001145415.1. [Q15047-1]
NP_001230420.1. NM_001243491.1. [Q15047-2]
NP_036564.3. NM_012432.3. [Q15047-3]
UniGeneiHs.643565.

Genome annotation databases

EnsembliENST00000271640; ENSP00000271640; ENSG00000143379. [Q15047-1]
ENST00000368962; ENSP00000357958; ENSG00000143379. [Q15047-2]
ENST00000368969; ENSP00000357965; ENSG00000143379. [Q15047-3]
GeneIDi9869.
KEGGihsa:9869.
UCSCiuc001evu.2. human. [Q15047-1]
uc001evv.2. human. [Q15047-3]
uc001evw.4. human. [Q15047-2]

Polymorphism databases

DMDMi25091210.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS44217.1. [Q15047-1 ]
CCDS58026.1. [Q15047-2 ]
CCDS972.1. [Q15047-3 ]
RefSeqi NP_001138887.1. NM_001145415.1. [Q15047-1 ]
NP_001230420.1. NM_001243491.1. [Q15047-2 ]
NP_036564.3. NM_012432.3. [Q15047-3 ]
UniGenei Hs.643565.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DLM X-ray 1.77 A 196-402 [» ]
ProteinModelPortali Q15047.
SMRi Q15047. Positions 196-397, 681-881, 1134-1291.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115202. 126 interactions.
DIPi DIP-31029N.
IntActi Q15047. 108 interactions.
MINTi MINT-1184137.
STRINGi 9606.ENSP00000357965.

Chemistry

ChEMBLi CHEMBL2321646.

PTM databases

PhosphoSitei Q15047.

Polymorphism databases

DMDMi 25091210.

Proteomic databases

MaxQBi Q15047.
PaxDbi Q15047.
PRIDEi Q15047.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000271640 ; ENSP00000271640 ; ENSG00000143379 . [Q15047-1 ]
ENST00000368962 ; ENSP00000357958 ; ENSG00000143379 . [Q15047-2 ]
ENST00000368969 ; ENSP00000357965 ; ENSG00000143379 . [Q15047-3 ]
GeneIDi 9869.
KEGGi hsa:9869.
UCSCi uc001evu.2. human. [Q15047-1 ]
uc001evv.2. human. [Q15047-3 ]
uc001evw.4. human. [Q15047-2 ]

Organism-specific databases

CTDi 9869.
GeneCardsi GC01P150898.
HGNCi HGNC:10761. SETDB1.
HPAi HPA018142.
MIMi 604396. gene.
neXtProti NX_Q15047.
PharmGKBi PA35679.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00760000119330.
HOVERGENi HBG061013.
InParanoidi Q15047.
KOi K11421.
OMAi GSVGSGH.
OrthoDBi EOG7ZD1TG.
PhylomeDBi Q15047.
TreeFami TF106411.

Miscellaneous databases

ChiTaRSi SETDB1. human.
EvolutionaryTracei Q15047.
GeneWikii SETDB1.
GenomeRNAii 9869.
NextBioi 37203.
PROi Q15047.
SOURCEi Search...

Gene expression databases

Bgeei Q15047.
CleanExi HS_SETDB1.
ExpressionAtlasi Q15047. baseline and differential.
Genevestigatori Q15047.

Family and domain databases

InterProi IPR016177. DNA-bd_dom.
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 ]
Pfami PF01429. MBD. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00391. MBD. 1 hit.
SM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
SM00333. TUDOR. 2 hits.
[Graphical view ]
SUPFAMi SSF54171. SSF54171. 1 hit.
PROSITEi PS50982. MBD. 1 hit.
PS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS51573. SAM_MT43_SUVAR39_1. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
    Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
    Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH REST; CDYL; WIZ; EHMT1 AND EHMT2.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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.

Entry informationi

Entry nameiSETB1_HUMAN
AccessioniPrimary (citable) accession number: Q15047
Secondary accession number(s): A6NEW2
, Q5SZD8, Q5SZD9, Q5SZE0, Q5SZE7, Q96GM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 1, 1996
Last modified: November 26, 2014
This is version 161 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3