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Entry version 162 (08 May 2019)
Sequence version 1 (01 Nov 1998)
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Protein

Histone-lysine N-methyltransferase SETDB1

Gene

Setdb1

Organism
Mus musculus (Mouse)
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 (PubMed:11791185, PubMed:22939622). 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 (By similarity). Required to maintain a transcriptionally repressive state of genes in undifferentiated embryonic stem cells (ESCs) (By similarity). In ESCs, in collaboration with TRIM28, is also required for H3K9me3 and silencing of endogenous and introduced retroviruses in a DNA-methylation independent-pathway (PubMed:20164836, PubMed:29728365). Associates at promoter regions of tumor suppressor genes (TSGs) leading to their gene silencing. 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 (By similarity).By similarity4 Publications

<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 bindingi746Zinc 1By similarity1
Metal bindingi746Zinc 2By similarity1
Metal bindingi748Zinc 1By similarity1
Metal bindingi752Zinc 1By similarity1
Metal bindingi752Zinc 3By similarity1
Metal bindingi758Zinc 1By similarity1
Metal bindingi760Zinc 2By similarity1
Metal bindingi798Zinc 2By similarity1
Metal bindingi798Zinc 3By similarity1
Metal bindingi802Zinc 2By similarity1
Metal bindingi804Zinc 3By similarity1
Metal bindingi809Zinc 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 sitei868S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei870S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei1236S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi1242Zinc 4By similarity1
Metal bindingi1295Zinc 4By similarity1
Metal bindingi1297Zinc 4By similarity1
Metal bindingi1302Zinc 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

More...
Reactomei
R-MMU-3214841 PKMTs methylate histone lysines

<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 SETDB1Curated (EC:2.1.1.432 Publications)
Alternative name(s):
ERG-associated protein with SET domain
Short name:
ESET1 Publication
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:Setdb1Imported
Synonyms:Eset1 Publication, Kiaa0067
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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: Unplaced

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1934229 Setdb1

<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 & Seán O’Donoghue; 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>Mutagenesisi798C → T: Abolishes methyltransferase activity. 1 Publication1
Mutagenesisi1242C → A: Decreases endogenous retroviruses silencing and cell growth. 1 Publication1
Mutagenesisi1242C → T: Abolishes methyltransferase activity. 1 Publication1

<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_00001860651 – 1307Histone-lysine N-methyltransferase SETDB1Add BLAST1307

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 residuei112PhosphoserineCombined sources1
Modified residuei117PhosphoserineCombined sources1
Modified residuei120PhosphothreonineCombined sources1
<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); alternateBy similarity
Cross-linki182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei993Phosphothreonine; by NLKBy similarity1
Modified residuei1042PhosphoserineBy similarity1
Cross-linki1049Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki1049Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki1055Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1085Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki1165Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei1186N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei1186N6,N6-dimethyllysine; alternateBy similarity1
Modified residuei1194N6,N6,N6-trimethyllysine; alternateBy similarity1
Modified residuei1194N6,N6-dimethyllysine; alternateBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Degraded by the proteasome, shielded by interaction with ATF7IP.By similarity

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O88974

MaxQB - The MaxQuant DataBase

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MaxQBi
O88974

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

More...
PaxDbi
O88974

PeptideAtlas

More...
PeptideAtlasi
O88974

PRoteomics IDEntifications database

More...
PRIDEi
O88974

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O88974

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

More...
PhosphoSitePlusi
O88974

<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

Ubiquitously expressed. Strong expression in liver and testis.1 Publication

<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, SETDB1, EHMT1 and EHMT2. 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. Probably part of a corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1. Interacts with TRIM28/TIF1B. 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'. Interacts with MBD1; interaction is abolished when MBD1 is sumoylated. Interacts with CBX1 and CBX5. Interacts with DNMT3A and DNMT3B. Interacts with SUMO2. Interacts with CHD7, NLK1 and PPARG. Interacts with MPHOSPH8 (By similarity). Interacts with ERG (PubMed:11791185). Interacts with HDAC1, HDAC2, SIN3A, SIN3B (PubMed:12398767). Interacts with ATRX. Forms a complex with ATRX, TRIM28 and ZNF274 (By similarity). Interacts with RESF1 (PubMed:29728365). Interacts with ZNF638 (By similarity).By similarity3 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

WithEntry#Exp.IntActNotes
ErgP812703EBI-79658,EBI-79647

Protein-protein interaction databases

Protein interaction database and analysis system

More...
IntActi
O88974, 9 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000015841

<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

3D structure databases

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

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SMRi
O88974

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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
Domaini611 – 682MBDPROSITE-ProRule annotationAdd BLAST72
Domaini744 – 817Pre-SETPROSITE-ProRule annotationAdd BLAST74
Domaini820 – 1282SETPROSITE-ProRule annotationAdd BLAST463
Domaini1291 – 1307Post-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>Regioni830 – 832S-adenosyl-L-methionine bindingBy similarity3
Regioni1239 – 1240S-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 coili30 – 65Sequence analysisAdd BLAST36

<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.
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

More...
eggNOGi
KOG1141 Eukaryota
COG2940 LUCA

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O88974

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
IPR040880 DUF5604
IPR025796 Hist-Lys_N-MeTrfase_SETDB1
IPR001739 Methyl_CpG_DNA-bd
IPR003616 Post-SET_dom
IPR007728 Pre-SET_dom
IPR001214 SET_dom
IPR002999 Tudor
IPR041292 Tudor_4
IPR041291 TUDOR_5

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF18300 DUF5604, 1 hit
PF01429 MBD, 1 hit
PF05033 Pre-SET, 1 hit
PF00856 SET, 1 hit
PF18358 Tudor_4, 1 hit
PF18359 TUDOR_5, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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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

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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 (7+)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 7 <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
Note: Experimental confirmation may be lacking for some isoforms.

This entry has 7 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O88974-1) [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
MSSLPGCMSL AAAPAAADSA EIAELQQAVV EELGISMEEL RQYIDEELEK
60 70 80 90 100
MDCIQQRKKQ LAELETWVLQ KESEVAYVDR LFDDASREVT NCESLVKDFY
110 120 130 140 150
SKLGLQYHDS SSEDEASRPT EIIEIPDEDD DVLSIDSGDA GSRTPKDQKL
160 170 180 190 200
REAMAALRKS AQDVQKFMDA VNKKSSSQDL HKGTLGQVSG ELSKDGDLIV
210 220 230 240 250
SMRILGKKRT KTWHKGTLIA IQTVGLGKKY KVKFDNKGKS LLSGNHIAYD
260 270 280 290 300
YHPPADKLFV GSRVVAKYKD GNQVWLYAGI VAETPNVKNK LRFLIFFDDG
310 320 330 340 350
YASYVTQSEL YPICRPLKKT WEDIEDSSCR DFIEEYITAY PNRPMVLLKS
360 370 380 390 400
GQLIKTEWEG TWWKSRVEEV DGSLVRILFL DDKRCEWIYR GSTRLEPMFS
410 420 430 440 450
MKTSSASAME KKQGGQLRTR PNMGAVRSKG PVVQYTQDLT GTGIQFKPME
460 470 480 490 500
PLQPIAPPAP LPIPPLSPQA ADTDLESQLA QSRKQVAKKS TSFRPGSVGS
510 520 530 540 550
GHSSPTSSTL SENVSAGKLG INQTYRSPLA SVTSTPASAA PPVPPVPPGP
560 570 580 590 600
PTPPGPPAPP GPLAPPAFHG MLERAPAEPS YRAPMEKLFY LPHVCSYTCL
610 620 630 640 650
SRIRPMRNEQ YRGKNPLLVP LLYDFRRMTA RRRVNRKMGF HVIYKTPCGL
660 670 680 690 700
CLRTMQEIER YLFETGCDFL FLEMFCLDPY VLVDRKFQPF KPFYYILDIT
710 720 730 740 750
YGKEDVPLSC VNEIDTTPPP QVAYSKERIP GKGVFINTGP EFLVGCDCKD
760 770 780 790 800
GCRDKSKCAC HQLTIQATAC TPGGQVNPNS GYQYKRLEEC LPTGVYECNK
810 820 830 840 850
RCNCDPNMCT NRLVQHGLQV RLQLFKTQNK GWGIRCLDDI AKGSFVCIYA
860 870 880 890 900
GKILTDDFAD KEGLEMGDEY FANLDHIESV ENFKEGYESD VPTSSDSSGV
910 920 930 940 950
DMKDQEDGNS GSEDPEESND DSSDDNFCKD EDFSTSSVWR SYATRRQTRG
960 970 980 990 1000
QKENELSEMT SKDSRPPDLG PPHVPIPSSV SVGGCNPPSS EETPKNKVAS
1010 1020 1030 1040 1050
WLSCNSVSEG GFADSDSRSS FKTSEGGDGR AGGGRGEAER ASTSGLSFKD
1060 1070 1080 1090 1100
EGDNKQPKKE DPENRNKMPV VTEGSQNHGH NPPMKSEGLR RPASKMSVLQ
1110 1120 1130 1140 1150
SQRVVTSTQS NPDDILTLSS STESEGESGT SRKPTAGHTS ATAVDSDDIQ
1160 1170 1180 1190 1200
TISSGSDGDD FEDKKNLSGP TKRQVAVKST RGFALKSTHG IAIKSTNMAS
1210 1220 1230 1240 1250
VDKGESAPVR KNTRQFYDGE ESCYIIDAKL EGNLGRYLNH SCSPNLFVQN
1260 1270 1280 1290 1300
VFVDTHDLRF PWVAFFASKR IRAGTELTWD YNYEVGSVEG KELLCCCGAI

ECRGRLL
Length:1,307
Mass (Da):144,549
Last modified:November 1, 1998 - 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:i326AED6371D156C2
GO
Isoform 2 (identifier: O88974-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     482-486: SRKQV → AQSQK
     489-1307: Missing.

Show »
Length:488
Mass (Da):54,696
Checksum:i8874BF6A963B5415
GO
Isoform 3 (identifier: O88974-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-807: Missing.

Show »
Length:500
Mass (Da):54,477
Checksum:i164B400024020B2F
GO
Isoform 4 (identifier: O88974-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     474-474: D → ES

Show »
Length:1,308
Mass (Da):144,650
Checksum:iE224818F50D56E25
GO
Isoform 5 (identifier: O88974-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     527-1307: Missing.

Show »
Length:526
Mass (Da):58,617
Checksum:iF5B6903C06D91D11
GO
Isoform 6 (identifier: O88974-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     474-474: D → ES
     527-1307: Missing.

Show »
Length:527
Mass (Da):58,719
Checksum:iF2B3561EAA10EC06
GO
Isoform 7 (identifier: O88974-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     756-1307: Missing.

Note: No experimental confirmation available.
Show »
Length:755
Mass (Da):84,400
Checksum:i3AE0FFE5C3542A60
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3YYC3D3YYC3_MOUSE
Histone-lysine N-methyltransferase
Setdb1
1,308Annotation 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>
G5E8N3G5E8N3_MOUSE
Histone-lysine N-methyltransferase
Setdb1 mCG_16729
1,307Annotation 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>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti463I → M in BAC40439 (PubMed:16141072).Curated1
Sequence conflicti1092P → S in BAC65480 (PubMed:12693553).Curated1

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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0022211 – 807Missing in isoform 3. 1 PublicationAdd BLAST807
Alternative sequenceiVSP_024031474D → ES in isoform 4 and isoform 6. 2 Publications1
Alternative sequenceiVSP_002219482 – 486SRKQV → AQSQK in isoform 2. 1 Publication5
Alternative sequenceiVSP_002220489 – 1307Missing in isoform 2. 1 PublicationAdd BLAST819
Alternative sequenceiVSP_024032527 – 1307Missing in isoform 5 and isoform 6. 1 PublicationAdd BLAST781
Alternative sequenceiVSP_024033756 – 1307Missing in isoform 7. 1 PublicationAdd BLAST552

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
AF091628 mRNA Translation: AAC43039.1
AY091600 mRNA Translation: AAM13922.1
AF546078 mRNA Translation: AAN52358.1
AY226577 Genomic DNA Translation: AAO73535.2
AY226577 Genomic DNA Translation: AAO73536.2
BC007176 mRNA Translation: AAH07176.1
BC079537 mRNA Translation: AAH79537.1
AK122198 Transcribed RNA Translation: BAC65480.3
AK088590 mRNA Translation: BAC40439.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS17613.1 [O88974-4]
CCDS50991.1 [O88974-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
T17453

Genome annotation databases

UCSC genome browser

More...
UCSCi
uc008qjo.2 mouse [O88974-5]

Keywords - Coding sequence diversityi

Alternative splicing

<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
AF091628 mRNA Translation: AAC43039.1
AY091600 mRNA Translation: AAM13922.1
AF546078 mRNA Translation: AAN52358.1
AY226577 Genomic DNA Translation: AAO73535.2
AY226577 Genomic DNA Translation: AAO73536.2
BC007176 mRNA Translation: AAH07176.1
BC079537 mRNA Translation: AAH79537.1
AK122198 Transcribed RNA Translation: BAC65480.3
AK088590 mRNA Translation: BAC40439.1
CCDSiCCDS17613.1 [O88974-4]
CCDS50991.1 [O88974-1]
PIRiT17453

3D structure databases

SMRiO88974
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO88974, 9 interactors
STRINGi10090.ENSMUSP00000015841

PTM databases

iPTMnetiO88974
PhosphoSitePlusiO88974

Proteomic databases

EPDiO88974
MaxQBiO88974
PaxDbiO88974
PeptideAtlasiO88974
PRIDEiO88974

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiuc008qjo.2 mouse [O88974-5]

Organism-specific databases

MGIiMGI:1934229 Setdb1

Rodent Unidentified Gene-Encoded large proteins database

More...
Rougei
Search...

Phylogenomic databases

eggNOGiKOG1141 Eukaryota
COG2940 LUCA
InParanoidiO88974

Enzyme and pathway databases

ReactomeiR-MMU-3214841 PKMTs methylate histone lysines

Miscellaneous databases

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

More...
ChiTaRSi
Setdb1 mouse

Protein Ontology

More...
PROi
PR:O88974

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Family and domain databases

InterProiView protein in InterPro
IPR016177 DNA-bd_dom_sf
IPR040880 DUF5604
IPR025796 Hist-Lys_N-MeTrfase_SETDB1
IPR001739 Methyl_CpG_DNA-bd
IPR003616 Post-SET_dom
IPR007728 Pre-SET_dom
IPR001214 SET_dom
IPR002999 Tudor
IPR041292 Tudor_4
IPR041291 TUDOR_5
PfamiView protein in Pfam
PF18300 DUF5604, 1 hit
PF01429 MBD, 1 hit
PF05033 Pre-SET, 1 hit
PF00856 SET, 1 hit
PF18358 Tudor_4, 1 hit
PF18359 TUDOR_5, 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_MOUSE
<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: O88974
Secondary accession number(s): Q6AXH8
, Q78N64, Q78N65, Q80U84, Q8BTV6, Q8CIX7, Q922K1
<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, 1998
Last modified: May 8, 2019
This is version 162 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

<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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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