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Protein

Histone-lysine N-methyltransferase SETDB1

Gene

SETDB1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChromatin regulator, Methyltransferase, Repressor, Transferase
Biological processTranscription, Transcription regulation
LigandMetal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-3214841 PKMTs methylate histone lysines

SIGNOR Signaling Network Open Resource

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SIGNORi
Q15047

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SETDB1
Synonyms:KIAA0067, KMT1E
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000143379.12

Human Gene Nomenclature Database

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HGNCi
HGNC:10761 SETDB1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
604396 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q15047

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

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DisGeNETi
9869

Open Targets

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OpenTargetsi
ENSG00000143379

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA35679

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2321646

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
SETDB1

Domain mapping of disease mutations (DMDM)

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DMDMi
25091210

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001860641 – 1291Histone-lysine N-methyltransferase SETDB1Add BLAST1291

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei112PhosphoserineBy similarity1
Modified residuei117PhosphoserineBy similarity1
Modified residuei120PhosphothreonineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei976Phosphothreonine; by NLK1 Publication1
Modified residuei1025PhosphoserineCombined sources1
Cross-linki1032Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki1032Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki1038Glycyl 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
Cross-linki1149Glycyl 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

Encyclopedia of Proteome Dynamics

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EPDi
Q15047

MaxQB - The MaxQuant DataBase

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MaxQBi
Q15047

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q15047

PeptideAtlas

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PeptideAtlasi
Q15047

PRoteomics IDEntifications database

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PRIDEi
Q15047

ProteomicsDB human proteome resource

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ProteomicsDBi
60397
60398 [Q15047-2]
60399 [Q15047-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q15047

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q15047

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed. High expression in testis.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000143379 Expressed in 215 organ(s), highest expression level in testis

CleanEx database of gene expression profiles

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CleanExi
HS_SETDB1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q15047 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q15047 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA018142
HPA058484

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
115202, 140 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q15047

Database of interacting proteins

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DIPi
DIP-31029N

Protein interaction database and analysis system

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IntActi
Q15047, 121 interactors

Molecular INTeraction database

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MINTi
Q15047

STRING: functional protein association networks

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STRINGi
9606.ENSP00000271640

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q15047

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11291
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q15047

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q15047

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q15047

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni813 – 815S-adenosyl-L-methionine bindingBy similarity3
Regioni1223 – 1224S-adenosyl-L-methionine bindingBy similarity2

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili18 – 64Sequence analysisAdd BLAST47

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1141 Eukaryota
COG2940 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157471

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG061013

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q15047

KEGG Orthology (KO)

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KOi
K11421

Identification of Orthologs from Complete Genome Data

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OMAi
KNMSGPM

Database of Orthologous Groups

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OrthoDBi
EOG091G014F

Database for complete collections of gene phylogenies

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PhylomeDBi
Q15047

TreeFam database of animal gene trees

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TreeFami
TF106411

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR016177 DNA-bd_dom_sf
IPR025796 Hist-Lys_N-MeTrfase_SETDB1
IPR001739 Methyl_CpG_DNA-bd
IPR003616 Post-SET_dom
IPR007728 Pre-SET_dom
IPR001214 SET_dom
IPR002999 Tudor

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01429 MBD, 1 hit
PF05033 Pre-SET, 1 hit
PF00856 SET, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00391 MBD, 1 hit
SM00468 PreSET, 1 hit
SM00317 SET, 1 hit
SM00333 TUDOR, 2 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54171 SSF54171, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PRF4E9PRF4_HUMAN
Histone-lysine N-methyltransferase
SETDB1
1,259Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PQM8E9PQM8_HUMAN
Histone-lysine N-methyltransferase ...
SETDB1
636Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B0QZE6B0QZE6_HUMAN
Histone-lysine N-methyltransferase ...
SETDB1
156Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PS59E9PS59_HUMAN
Histone-lysine N-methyltransferase ...
SETDB1
163Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
X6R732X6R732_HUMAN
Histone-lysine N-methyltransferase ...
SETDB1
249Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PAP1E9PAP1_HUMAN
Histone-lysine N-methyltransferase ...
SETDB1
111Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
X6RHV1X6RHV1_HUMAN
Histone-lysine N-methyltransferase ...
SETDB1
150Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA06689 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014284236N → S. Corresponds to variant dbSNP:rs2271075Ensembl.1
Natural variantiVAR_031281506P → S1 PublicationCorresponds to variant dbSNP:rs17852587Ensembl.1
Natural variantiVAR_014286824A → G. Corresponds to variant dbSNP:rs2691551Ensembl.1
Natural variantiVAR_014285824A → P. Corresponds to variant dbSNP:rs2814054Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D31891 mRNA Translation: BAA06689.2 Different initiation.
AL590133 Genomic DNA No translation available.
CH471121 Genomic DNA Translation: EAW53506.1
BC009362 mRNA Translation: AAH09362.1
BC028671 mRNA Translation: AAH28671.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS44217.1 [Q15047-1]
CCDS58026.1 [Q15047-2]
CCDS972.1 [Q15047-3]

NCBI Reference Sequences

More...
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]
XP_016858444.1, XM_017002955.1 [Q15047-2]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.643565

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000271640; ENSP00000271640; ENSG00000143379 [Q15047-1]
ENST00000368962; ENSP00000357958; ENSG00000143379 [Q15047-2]
ENST00000368969; ENSP00000357965; ENSG00000143379 [Q15047-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
9869

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:9869

UCSC genome browser

More...
UCSCi
uc001evu.3 human [Q15047-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D31891 mRNA Translation: BAA06689.2 Different initiation.
AL590133 Genomic DNA No translation available.
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:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
6AU2X-ray1.63A196-402[»]
6AU3X-ray1.80A196-402[»]
6BHDX-ray1.25A190-410[»]
6BHEX-ray1.35A190-410[»]
6BHGX-ray1.45A190-410[»]
6BHHX-ray1.85A190-410[»]
6BHIX-ray1.40A190-410[»]
6BPIX-ray1.64A196-402[»]
ProteinModelPortaliQ15047
SMRiQ15047
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115202, 140 interactors
CORUMiQ15047
DIPiDIP-31029N
IntActiQ15047, 121 interactors
MINTiQ15047
STRINGi9606.ENSP00000271640

Chemistry databases

BindingDBiQ15047
ChEMBLiCHEMBL2321646

PTM databases

iPTMnetiQ15047
PhosphoSitePlusiQ15047

Polymorphism and mutation databases

BioMutaiSETDB1
DMDMi25091210

Proteomic databases

EPDiQ15047
MaxQBiQ15047
PaxDbiQ15047
PeptideAtlasiQ15047
PRIDEiQ15047
ProteomicsDBi60397
60398 [Q15047-2]
60399 [Q15047-3]

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

Comparative Toxicogenomics Database

More...
CTDi
9869
DisGeNETi9869
EuPathDBiHostDB:ENSG00000143379.12

GeneCards: human genes, protein and diseases

More...
GeneCardsi
SETDB1
HGNCiHGNC:10761 SETDB1
HPAiHPA018142
HPA058484
MIMi604396 gene
neXtProtiNX_Q15047
OpenTargetsiENSG00000143379
PharmGKBiPA35679

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1141 Eukaryota
COG2940 LUCA
GeneTreeiENSGT00940000157471
HOVERGENiHBG061013
InParanoidiQ15047
KOiK11421
OMAiKNMSGPM
OrthoDBiEOG091G014F
PhylomeDBiQ15047
TreeFamiTF106411

Enzyme and pathway databases

ReactomeiR-HSA-3214841 PKMTs methylate histone lysines
SIGNORiQ15047

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
SETDB1 human
EvolutionaryTraceiQ15047

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
SETDB1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
9869

Protein Ontology

More...
PROi
PR:Q15047

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000143379 Expressed in 215 organ(s), highest expression level in testis
CleanExiHS_SETDB1
ExpressionAtlasiQ15047 baseline and differential
GenevisibleiQ15047 HS

Family and domain databases

InterProiView protein in InterPro
IPR016177 DNA-bd_dom_sf
IPR025796 Hist-Lys_N-MeTrfase_SETDB1
IPR001739 Methyl_CpG_DNA-bd
IPR003616 Post-SET_dom
IPR007728 Pre-SET_dom
IPR001214 SET_dom
IPR002999 Tudor
PfamiView protein in Pfam
PF01429 MBD, 1 hit
PF05033 Pre-SET, 1 hit
PF00856 SET, 1 hit
SMARTiView protein in SMART
SM00391 MBD, 1 hit
SM00468 PreSET, 1 hit
SM00317 SET, 1 hit
SM00333 TUDOR, 2 hits
SUPFAMiSSF54171 SSF54171, 1 hit
PROSITEiView protein in PROSITE
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSETB1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q15047
Secondary accession number(s): A6NEW2
, Q5SZD8, Q5SZD9, Q5SZE0, Q5SZE7, Q96GM9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 1, 1996
Last modified: December 5, 2018
This is version 202 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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