Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone-lysine N-methyltransferase SETDB1

Gene

SETDB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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. Probably forms a corepressor complex required for activated KRAS-mediated promoter hypermethylation and transcriptional silencing of tumor suppressor genes (TSGs) or other tumor-related genes in colorectal cancer (CRC) cells (PubMed:24623306). Also required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (PubMed:24623306). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing (PubMed:24623306). The SETDB1-TRIM28-ZNF274 complex may play a role in recruiting ATRX to the 3'-exons of zinc-finger coding genes with atypical chromatin signatures to establish or maintain/protect H3K9me3 at these transcriptionally active regions (PubMed:27029610).6 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)DescriptionActionsGraphical viewLength
Metal bindingi729Zinc 1By similarity1
Metal bindingi729Zinc 2By similarity1
Metal bindingi731Zinc 1By similarity1
Metal bindingi735Zinc 1By similarity1
Metal bindingi735Zinc 3By similarity1
Metal bindingi741Zinc 1By similarity1
Metal bindingi743Zinc 2By similarity1
Metal bindingi781Zinc 2By similarity1
Metal bindingi781Zinc 3By similarity1
Metal bindingi785Zinc 2By similarity1
Metal bindingi787Zinc 3By similarity1
Metal bindingi792Zinc 3By similarity1
Binding sitei851S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei853S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei1220S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi1226Zinc 4By similarity1
Metal bindingi1279Zinc 4By similarity1
Metal bindingi1281Zinc 4By similarity1
Metal bindingi1286Zinc 4By similarity1

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • DNA binding Source: InterPro
  • histone-lysine N-methyltransferase activity Source: UniProtKB-EC
  • promoter-specific chromatin binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • positive regulation of methylation-dependent chromatin silencing Source: UniProtKB
  • Ras protein signal transduction Source: UniProtKB
  • response to ethanol Source: Ensembl
  • response to vitamin Source: Ensembl
  • 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

Enzyme and pathway databases

BioCyciZFISH:HS07042-MONOMER.
ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.

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
Proteomesi
  • UP000005640 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi729 – 731CDC → LDP: Abolishes methyltransferase activity. 1 Publication3
Mutagenesisi976T → A: Abrogates interaction with CHD7, NLK and PPARG. Reduces phosphorylation by NLK. Reduces transcriptional repression. 1 Publication1
Mutagenesisi1224H → K: Abolishes methyltransferase activity. 1 Publication1
Mutagenesisi1226C → A: Abolishes methyltransferase activity. 1 Publication1
Mutagenesisi1279C → Y: Abolishes methyltransferase activity. 1 Publication1

Organism-specific databases

DisGeNETi9869.
OpenTargetsiENSG00000143379.
PharmGKBiPA35679.

Chemistry databases

ChEMBLiCHEMBL2321646.

Polymorphism and mutation databases

BioMutaiSETDB1.
DMDMi25091210.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001860641 – 1291Histone-lysine N-methyltransferase SETDB1Add BLAST1291

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei112PhosphoserineBy similarity1
Modified residuei117PhosphoserineBy similarity1
Modified residuei120PhosphothreonineBy similarity1
Cross-linki182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Modified residuei976Phosphothreonine; by NLK1 Publication1
Modified residuei1025PhosphoserineCombined sources1
Cross-linki1032Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki1032Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1066PhosphoserineCombined sources1
Cross-linki1069Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1170N6,N6,N6-trimethyllysine; alternateCombined sources1
Modified residuei1170N6,N6-dimethyllysine; alternateCombined sources1
Modified residuei1178N6,N6,N6-trimethyllysine; alternateCombined sources1
Modified residuei1178N6,N6-dimethyllysine; alternateCombined sources1

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ15047.
MaxQBiQ15047.
PaxDbiQ15047.
PeptideAtlasiQ15047.
PRIDEiQ15047.

PTM databases

iPTMnetiQ15047.
PhosphoSitePlusiQ15047.

Expressioni

Tissue specificityi

Widely expressed. High expression in testis.

Gene expression databases

BgeeiENSG00000143379.
CleanExiHS_SETDB1.
ExpressionAtlasiQ15047. baseline and differential.
GenevisibleiQ15047. HS.

Organism-specific databases

HPAiHPA018142.
HPA058484.

Interactioni

Subunit structurei

Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2 (PubMed:19061646). 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 (PubMed:15327775). Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1 (PubMed:24623306). Interacts with TRIM28/TIF1B (PubMed:11959841). 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' (PubMed:14536086, PubMed:15691849). Interacts with MBD1; interaction is abolished when MBD1 is sumoylated (PubMed:15327775, PubMed:17066076). Interacts with CBX1 and CBX5 (PubMed:15899859). Interacts with DNMT3A and DNMT3B (PubMed:16682412). Interacts with SUMO2. Interacts with CHD7, NLK1 and PPARG (PubMed:17952062). Interacts with MPHOSPH8 (PubMed:20871592). Interacts with ERG (By similarity). Interacts with HDAC1, HDAC2, SIN3A and SIN3B (By similarity). Interacts with ATRX. Forms a complex with ATRX, TRIM28 and ZNF274 (PubMed:27029610).By similarity13 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. 133 interactors.
DIPiDIP-31029N.
IntActiQ15047. 113 interactors.
MINTiMINT-1184137.
STRINGi9606.ENSP00000271640.

Chemistry databases

BindingDBiQ15047.

Structurei

Secondary structure

11291
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi203 – 207Combined sources5
Beta strandi213 – 224Combined sources12
Beta strandi227 – 234Combined sources8
Beta strandi239 – 242Combined sources4
Helixi244 – 246Combined sources3
Beta strandi247 – 251Combined sources5
Helixi255 – 257Combined sources3
Beta strandi263 – 270Combined sources8
Beta strandi273 – 283Combined sources11
Turni287 – 290Combined sources4
Beta strandi293 – 297Combined sources5
Beta strandi302 – 305Combined sources4
Helixi307 – 309Combined sources3
Beta strandi310 – 315Combined sources6
Helixi320 – 323Combined sources4
Helixi327 – 339Combined sources13
Beta strandi353 – 358Combined sources6
Beta strandi361 – 371Combined sources11
Beta strandi374 – 379Combined sources6
Turni380 – 383Combined sources4
Beta strandi384 – 389Combined sources6
Helixi396 – 399Combined sources4
Beta strandi1167 – 1172Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DLMX-ray1.77A196-402[»]
4X3SX-ray1.60C/D1165-1174[»]
5KCHX-ray1.70A196-403[»]
5KCOX-ray1.47A196-403[»]
5KE2X-ray1.56A196-402[»]
5KE3X-ray1.70A196-402[»]
5KH6X-ray2.05A196-400[»]
ProteinModelPortaliQ15047.
SMRiQ15047.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15047.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini257 – 320Tudor 1Add BLAST64
Domaini347 – 403Tudor 2Add BLAST57
Domaini594 – 665MBDPROSITE-ProRule annotationAdd BLAST72
Domaini727 – 800Pre-SETPROSITE-ProRule annotationAdd BLAST74
Domaini803 – 1266SETPROSITE-ProRule annotationAdd BLAST464
Domaini1275 – 1291Post-SETPROSITE-ProRule annotationAdd BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni813 – 815S-adenosyl-L-methionine bindingBy similarity3
Regioni1223 – 1224S-adenosyl-L-methionine bindingBy similarity2

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili18 – 64Sequence analysisAdd BLAST47

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

eggNOGiKOG1141. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOVERGENiHBG061013.
InParanoidiQ15047.
KOiK11421.
OMAiIRAVTNC.
OrthoDBiEOG091G014F.
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.
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.
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. AlignAdd to basket

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_014284236N → S.Corresponds to variant rs2271075dbSNPEnsembl.1
Natural variantiVAR_031281506P → S.1 PublicationCorresponds to variant rs17852587dbSNPEnsembl.1
Natural variantiVAR_014286824A → G.Corresponds to variant rs2691551dbSNPEnsembl.1
Natural variantiVAR_014285824A → P.Corresponds to variant rs2814054dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002217381 – 397DDKRC…TRLEP → VLFFSTILEAEVGGGGT in isoform 2. 1 PublicationAdd BLAST17
Alternative sequenceiVSP_002218398 – 1291Missing in isoform 2. 1 PublicationAdd BLAST894
Alternative sequenceiVSP_0346001254Missing in isoform 3. 1 Publication1

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]
XP_016858444.1. XM_017002955.1. [Q15047-2]
UniGeneiHs.643565.

Genome annotation databases

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

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.
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]
XP_016858444.1. XM_017002955.1. [Q15047-2]
UniGeneiHs.643565.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3DLMX-ray1.77A196-402[»]
4X3SX-ray1.60C/D1165-1174[»]
5KCHX-ray1.70A196-403[»]
5KCOX-ray1.47A196-403[»]
5KE2X-ray1.56A196-402[»]
5KE3X-ray1.70A196-402[»]
5KH6X-ray2.05A196-400[»]
ProteinModelPortaliQ15047.
SMRiQ15047.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115202. 133 interactors.
DIPiDIP-31029N.
IntActiQ15047. 113 interactors.
MINTiMINT-1184137.
STRINGi9606.ENSP00000271640.

Chemistry databases

BindingDBiQ15047.
ChEMBLiCHEMBL2321646.

PTM databases

iPTMnetiQ15047.
PhosphoSitePlusiQ15047.

Polymorphism and mutation databases

BioMutaiSETDB1.
DMDMi25091210.

Proteomic databases

EPDiQ15047.
MaxQBiQ15047.
PaxDbiQ15047.
PeptideAtlasiQ15047.
PRIDEiQ15047.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9869.
DisGeNETi9869.
GeneCardsiSETDB1.
HGNCiHGNC:10761. SETDB1.
HPAiHPA018142.
HPA058484.
MIMi604396. gene.
neXtProtiNX_Q15047.
OpenTargetsiENSG00000143379.
PharmGKBiPA35679.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1141. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOVERGENiHBG061013.
InParanoidiQ15047.
KOiK11421.
OMAiIRAVTNC.
OrthoDBiEOG091G014F.
PhylomeDBiQ15047.
TreeFamiTF106411.

Enzyme and pathway databases

BioCyciZFISH:HS07042-MONOMER.
ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.

Miscellaneous databases

ChiTaRSiSETDB1. human.
EvolutionaryTraceiQ15047.
GeneWikiiSETDB1.
GenomeRNAii9869.
PROiQ15047.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143379.
CleanExiHS_SETDB1.
ExpressionAtlasiQ15047. baseline and differential.
GenevisibleiQ15047. HS.

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.
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.
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]
ProtoNetiSearch...

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 30, 2016
This is version 183 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.