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Q15047

- SETB1_HUMAN

UniProt

Q15047 - SETB1_HUMAN

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Protein
Histone-lysine N-methyltransferase SETDB1
Gene
SETDB1, KIAA0067, KMT1E
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].

Sites

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

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
  3. protein binding Source: IntAct
  4. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. bone development Source: Ensembl
  2. inner cell mass cell proliferation Source: Ensembl
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. 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. Golgi apparatus Source: HPA
  2. chromosome Source: UniProtKB-SubCell
  3. cytoplasm Source: HPA
  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 SETDB1
PRO_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 NLK Inferred
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

ArrayExpressiQ15047.
BgeeiQ15047.
CleanExiHS_SETDB1.
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. 115 interactions.
DIPiDIP-31029N.
IntActiQ15047. 99 interactions.
MINTiMINT-1184137.
STRINGi9606.ENSP00000357965.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DLMX-ray1.77A196-402[»]
ProteinModelPortaliQ15047.
SMRiQ15047. Positions 196-397, 605-662, 681-881, 1165-1290.

Miscellaneous databases

EvolutionaryTraceiQ15047.

Family & Domainsi

Domains and Repeats

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

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili18 – 6447 Reviewed prediction
Add
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

Contains 1 post-SET domain.
Contains 1 pre-SET domain.
Contains 1 SET domain.
Contains 2 Tudor domains.

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiCOG2940.
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

MSSLPGCIGL DAATATVESE EIAELQQAVV EELGISMEEL RHFIDEELEK     50
MDCVQQRKKQ LAELETWVIQ KESEVAHVDQ LFDDASRAVT NCESLVKDFY 100
SKLGLQYRDS SSEDESSRPT EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL 150
REAMAALRKS AQDVQKFMDA VNKKSSSQDL HKGTLSQMSG ELSKDGDLIV 200
SMRILGKKRT KTWHKGTLIA IQTVGPGKKY KVKFDNKGKS LLSGNHIAYD 250
YHPPADKLYV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG 300
YASYVTQSEL YPICRPLKKT WEDIEDISCR DFIEEYVTAY PNRPMVLLKS 350
GQLIKTEWEG TWWKSRVEEV DGSLVRILFL DDKRCEWIYR GSTRLEPMFS 400
MKTSSASALE KKQGQLRTRP NMGAVRSKGP VVQYTQDLTG TGTQFKPVEP 450
PQPTAPPAPP FPPAPPLSPQ AGDSDLESQL AQSRKQVAKK STSFRPGSVG 500
SGHSSPTSPA LSENVSGGKP GINQTYRSPL GSTASAPAPS ALPAPPAPPV 550
FHGMLERAPA EPSYRAPMEK LFYLPHVCSY TCLSRVRPMR NEQYRGKNPL 600
LVPLLYDFRR MTARRRVNRK MGFHVIYKTP CGLCLRTMQE IERYLFETGC 650
DFLFLEMFCL DPYVLVDRKF QPYKPFYYIL DITYGKEDVP LSCVNEIDTT 700
PPPQVAYSKE RIPGKGVFIN TGPEFLVGCD CKDGCRDKSK CACHQLTIQA 750
TACTPGGQIN PNSGYQYKRL EECLPTGVYE CNKRCKCDPN MCTNRLVQHG 800
LQVRLQLFKT QNKGWGIRCL DDIAKGSFVC IYAGKILTDD FADKEGLEMG 850
DEYFANLDHI ESVENFKEGY ESDAPCSSDS SGVDLKDQED GNSGTEDPEE 900
SNDDSSDDNF CKDEDFSTSS VWRSYATRRQ TRGQKENGLS ETTSKDSHPP 950
DLGPPHIPVP PSIPVGGCNP PSSEETPKNK VASWLSCNSV SEGGFADSDS 1000
HSSFKTNEGG EGRAGGSRME AEKASTSGLG IKDEGDIKQA KKEDTDDRNK 1050
MSVVTESSRN YGYNPSPVKP EGLRRPPSKT SMHQSRRLMA SAQSNPDDVL 1100
TLSSSTESEG ESGTSRKPTA GQTSATAVDS DDIQTISSGS EGDDFEDKKN 1150
MTGPMKRQVA VKSTRGFALK STHGIAIKST NMASVDKGES APVRKNTRQF 1200
YDGEESCYII DAKLEGNLGR YLNHSCSPNL FVQNVFVDTH DLRFPWVAFF 1250
ASKRIRAGTE LTWDYNYEVG SVEGKELLCC CGAIECRGRL L 1291
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.
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.

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.
VSP_002217Add
BLAST
Alternative sequencei398 – 1291894Missing in isoform 2.
VSP_002218Add
BLAST
Alternative sequencei1254 – 12541Missing in isoform 3.
VSP_034600

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3DLM X-ray 1.77 A 196-402 [» ]
ProteinModelPortali Q15047.
SMRi Q15047. Positions 196-397, 605-662, 681-881, 1165-1290.
ModBasei Search...

Protein-protein interaction databases

BioGridi 115202. 115 interactions.
DIPi DIP-31029N.
IntActi Q15047. 99 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.
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

ArrayExpressi Q15047.
Bgeei Q15047.
CleanExi HS_SETDB1.
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: July 9, 2014
This is version 158 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

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