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Protein

Histone-lysine N-methyltransferase SUV39H1

Gene

SUV39H1

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 using monomethylated H3 'Lys-9' as substrate. Also weakly methylates histone H1 (in vitro). 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 heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin at pericentric and telomere regions. H3 'Lys-9' trimethylation is also required to direct DNA methylation at pericentric repeats. SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD+/NADP+ ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. Recruited by the large PER complex to the E-box elements of the circadian target genes such as PER2 itself or PER1, contributes to the conversion of local chromatin to a heterochromatin-like repressive state through H3 'Lys-9' trimethylation.6 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

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by S-adenosyl-L-homocysteine. Negatively regulated by CCAR2.2 Publications

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 bindingi181Zinc 1By similarity1
Metal bindingi181Zinc 2By similarity1
Metal bindingi183Zinc 1By similarity1
Metal bindingi186Zinc 1By similarity1
Metal bindingi186Zinc 3By similarity1
Metal bindingi194Zinc 1By similarity1
Metal bindingi195Zinc 1By similarity1
Metal bindingi195Zinc 2By similarity1
Metal bindingi222Zinc 2By similarity1
Metal bindingi222Zinc 3By similarity1
Metal bindingi226Zinc 2By similarity1
Metal bindingi228Zinc 3By similarity1
Metal bindingi232Zinc 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 sitei297S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi326Zinc 4By similarity1
Metal bindingi400Zinc 4By similarity1
Metal bindingi402Zinc 4By similarity1
Metal bindingi407Zinc 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 processBiological rhythms, Cell cycle, Differentiation, Host-virus interaction, rRNA processing, Transcription, 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
R-HSA-427359 SIRT1 negatively regulates rRNA expression

SIGNOR Signaling Network Open Resource

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SIGNORi
O43463

<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 SUV39H1 (EC:2.1.1.43)
Alternative name(s):
Histone H3-K9 methyltransferase 1
Short name:
H3-K9-HMTase 1
Lysine N-methyltransferase 1A
Position-effect variegation 3-9 homolog
Suppressor of variegation 3-9 homolog 1
Short name:
Su(var)3-9 homolog 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:SUV39H1
Synonyms:KMT1A, SUV39H
<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 X

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000101945.16

Human Gene Nomenclature Database

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HGNCi
HGNC:11479 SUV39H1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
300254 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O43463

<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

Centromere, 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>Mutagenesisi64W → A: Abolishes methyltransferase activity. 1 Publication1
Mutagenesisi67Y → A: Abolishes methyltransferase activity. 1 Publication1
Mutagenesisi266K → A: Loss of SIRT1-mediated up-regulation of enzymatic activity. 1 Publication1
Mutagenesisi266K → Q: Significant loss of enzymatic activity. 1 Publication1
Mutagenesisi320H → R: Strongly increases methylation of histone H3. 1 Publication1
Mutagenesisi324H → L or K: Abolishes methylation of histone H3. 1 Publication1
Mutagenesisi326C → A: Abolishes methylation of histone H3. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
6839

Open Targets

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OpenTargetsi
ENSG00000101945

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA36264

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1795118

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
2715

<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_00001860571 – 412Histone-lysine N-methyltransferase SUV39H1Add BLAST412

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 residuei266N6-acetyllysine1 Publication1
Modified residuei391PhosphoserineCombined sources1

<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

Phosphorylated on serine residues, and to a lesser degree, on threonine residues. The phosphorylated form is stabilized by SBF1 and is less active in its transcriptional repressor function.1 Publication
Acetylated at Lys-266, leading to inhibition of enzyme activity. SIRT1-mediated deacetylation relieves this inhibition.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
O43463

MaxQB - The MaxQuant DataBase

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MaxQBi
O43463

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

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PaxDbi
O43463

PeptideAtlas

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PeptideAtlasi
O43463

PRoteomics IDEntifications database

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PRIDEi
O43463

ProteomicsDB human proteome resource

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ProteomicsDBi
48957

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O43463

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

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PhosphoSitePlusi
O43463

<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 the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Accumulates during mitosis at centromeres during prometaphase, but dissociates from the centromere at the meta- to anaphase transition.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000101945 Expressed in 166 organ(s), highest expression level in right lobe of liver

CleanEx database of gene expression profiles

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CleanExi
HS_SUV39H1

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O43463 HS

<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

Interacts with H3 and H4 histones. Interacts with GFI1B, DNMT3B, CBX1, CBX4, CCAR2, MBD1, RUNX1, RUNX3, MYOD1, SMAD5 and RB1. Interacts with SBF1 through the SET domain. Interacts with HDAC1 and HDAC2 through the N-terminus and associates with the core histone deacetylase complex composed of HDAC1, HDAC2, RBBP4 and RBBP7. Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8. Interacts (via SET domain) with MECOM; enhances MECOM transcriptional repression activity. Interacts with LMNA; the interaction increases stability of SUV39H1. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex.16 Publications
(Microbial infection) Interacts with HTLV-1 Tax protein, leading to abrogate Tax transactivation of HTLV-1 LTR.1 Publication

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
112706, 187 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-467 eNoSc complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O43463

Database of interacting proteins

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DIPi
DIP-32589N

Protein interaction database and analysis system

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IntActi
O43463, 137 interactors

Molecular INTeraction database

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MINTi
O43463

STRING: functional protein association networks

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STRINGi
9606.ENSP00000365877

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O43463

<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

1412
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
O43463

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

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SMRi
O43463

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...

<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>Domaini43 – 101ChromoPROSITE-ProRule annotationAdd BLAST59
Domaini179 – 240Pre-SETPROSITE-ProRule annotationAdd BLAST62
Domaini243 – 366SETPROSITE-ProRule annotationAdd BLAST124
Domaini396 – 412Post-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>Regioni1 – 89Interaction with SIRT1Add BLAST89
Regioni254 – 256S-adenosyl-L-methionine bindingBy similarity3
Regioni255 – 377Mediates interaction with MECOMBy similarityAdd BLAST123
Regioni323 – 324S-adenosyl-L-methionine bindingBy similarity2

<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

Although the SET domain contains the active site of enzymatic activity, both pre-SET and post-SET domains are required for methyltransferase activity. The SET domain also participates in stable binding to heterochromatin.1 Publication
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.1 Publication

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1082 Eukaryota
COG2940 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160063

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231244

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG055621

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O43463

KEGG Orthology (KO)

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KOi
K11419

Identification of Orthologs from Complete Genome Data

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OMAi
FDYKMQI

Database of Orthologous Groups

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OrthoDBi
EOG091G0Y4N

Database for complete collections of gene phylogenies

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PhylomeDBi
O43463

TreeFam database of animal gene trees

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TreeFami
TF106452

Family and domain databases

Conserved Domains Database

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CDDi
cd00024 CHROMO, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR016197 Chromo-like_dom_sf
IPR000953 Chromo/chromo_shadow_dom
IPR023780 Chromo_domain
IPR023779 Chromodomain_CS
IPR011381 Histone_H3-K9_MeTrfase
IPR003616 Post-SET_dom
IPR007728 Pre-SET_dom
IPR001214 SET_dom

Pfam protein domain database

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Pfami
View protein in Pfam
PF00385 Chromo, 1 hit
PF05033 Pre-SET, 1 hit
PF00856 SET, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF009343 SUV39_SET, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00298 CHROMO, 1 hit
SM00508 PostSET, 1 hit
SM00468 PreSET, 1 hit
SM00317 SET, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54160 SSF54160, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00598 CHROMO_1, 1 hit
PS50013 CHROMO_2, 1 hit
PS50868 POST_SET, 1 hit
PS50867 PRE_SET, 1 hit
PS51579 SAM_MT43_SUVAR39_3, 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 (2)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 2 <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
Isoform 1 (identifier: O43463-1) [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
MAENLKGCSV CCKSSWNQLQ DLCRLAKLSC PALGISKRNL YDFEVEYLCD
60 70 80 90 100
YKKIREQEYY LVKWRGYPDS ESTWEPRQNL KCVRILKQFH KDLERELLRR
110 120 130 140 150
HHRSKTPRHL DPSLANYLVQ KAKQRRALRR WEQELNAKRS HLGRITVENE
160 170 180 190 200
VDLDGPPRAF VYINEYRVGE GITLNQVAVG CECQDCLWAP TGGCCPGASL
210 220 230 240 250
HKFAYNDQGQ VRLRAGLPIY ECNSRCRCGY DCPNRVVQKG IRYDLCIFRT
260 270 280 290 300
DDGRGWGVRT LEKIRKNSFV MEYVGEIITS EEAERRGQIY DRQGATYLFD
310 320 330 340 350
LDYVEDVYTV DAAYYGNISH FVNHSCDPNL QVYNVFIDNL DERLPRIAFF
360 370 380 390 400
ATRTIRAGEE LTFDYNMQVD PVDMESTRMD SNFGLAGLPG SPKKRVRIEC
410
KCGTESCRKY LF
Length:412
Mass (Da):47,907
Last modified:June 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:iAF6F959AD20C6C76
GO
Isoform 2 (identifier: O43463-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MAENLK → MVGMSRLRNDRLADPLT

Note: No experimental confirmation available.
Show »
Length:423
Mass (Da):49,148
Checksum:i67729933D3ABC7CF
GO

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 conflicti213L → P in BAD96791 (Ref. 4) 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. 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_0542861 – 6MAENLK → MVGMSRLRNDRLADPLT in isoform 2. 1 Publication6

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF019968 mRNA Translation: AAB92224.1
CR541746 mRNA Translation: CAG46546.1
AK223071 mRNA Translation: BAD96791.1
AK299900 mRNA Translation: BAG61742.1
AK312547 mRNA Translation: BAG35445.1
AF196970 Genomic DNA No translation available.
CH471224 Genomic DNA Translation: EAW50756.1
CH471224 Genomic DNA Translation: EAW50757.1
BC006238 mRNA Translation: AAH06238.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS14304.1 [O43463-1]
CCDS65252.1 [O43463-2]

NCBI Reference Sequences

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RefSeqi
NP_001269095.1, NM_001282166.1 [O43463-2]
NP_003164.1, NM_003173.3 [O43463-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.522639

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000337852; ENSP00000337976; ENSG00000101945 [O43463-2]
ENST00000376687; ENSP00000365877; ENSG00000101945 [O43463-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
6839

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:6839

UCSC genome browser

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UCSCi
uc004dkn.5 human [O43463-1]

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
AF019968 mRNA Translation: AAB92224.1
CR541746 mRNA Translation: CAG46546.1
AK223071 mRNA Translation: BAD96791.1
AK299900 mRNA Translation: BAG61742.1
AK312547 mRNA Translation: BAG35445.1
AF196970 Genomic DNA No translation available.
CH471224 Genomic DNA Translation: EAW50756.1
CH471224 Genomic DNA Translation: EAW50757.1
BC006238 mRNA Translation: AAH06238.1
CCDSiCCDS14304.1 [O43463-1]
CCDS65252.1 [O43463-2]
RefSeqiNP_001269095.1, NM_001282166.1 [O43463-2]
NP_003164.1, NM_003173.3 [O43463-1]
UniGeneiHs.522639

3D structure databases

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MTSX-ray2.20A/B/C44-106[»]
ProteinModelPortaliO43463
SMRiO43463
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112706, 187 interactors
ComplexPortaliCPX-467 eNoSc complex
CORUMiO43463
DIPiDIP-32589N
IntActiO43463, 137 interactors
MINTiO43463
STRINGi9606.ENSP00000365877

Chemistry databases

BindingDBiO43463
ChEMBLiCHEMBL1795118
GuidetoPHARMACOLOGYi2715

PTM databases

iPTMnetiO43463
PhosphoSitePlusiO43463

Proteomic databases

EPDiO43463
MaxQBiO43463
PaxDbiO43463
PeptideAtlasiO43463
PRIDEiO43463
ProteomicsDBi48957

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
6839
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337852; ENSP00000337976; ENSG00000101945 [O43463-2]
ENST00000376687; ENSP00000365877; ENSG00000101945 [O43463-1]
GeneIDi6839
KEGGihsa:6839
UCSCiuc004dkn.5 human [O43463-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
6839
DisGeNETi6839
EuPathDBiHostDB:ENSG00000101945.16

GeneCards: human genes, protein and diseases

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GeneCardsi
SUV39H1
HGNCiHGNC:11479 SUV39H1
MIMi300254 gene
neXtProtiNX_O43463
OpenTargetsiENSG00000101945
PharmGKBiPA36264

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG1082 Eukaryota
COG2940 LUCA
GeneTreeiENSGT00940000160063
HOGENOMiHOG000231244
HOVERGENiHBG055621
InParanoidiO43463
KOiK11419
OMAiFDYKMQI
OrthoDBiEOG091G0Y4N
PhylomeDBiO43463
TreeFamiTF106452

Enzyme and pathway databases

ReactomeiR-HSA-3214841 PKMTs methylate histone lysines
R-HSA-427359 SIRT1 negatively regulates rRNA expression
SIGNORiO43463

Miscellaneous databases

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

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ChiTaRSi
SUV39H1 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
SUV39H1

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

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GenomeRNAii
6839

Protein Ontology

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PROi
PR:O43463

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000101945 Expressed in 166 organ(s), highest expression level in right lobe of liver
CleanExiHS_SUV39H1
GenevisibleiO43463 HS

Family and domain databases

CDDicd00024 CHROMO, 1 hit
InterProiView protein in InterPro
IPR016197 Chromo-like_dom_sf
IPR000953 Chromo/chromo_shadow_dom
IPR023780 Chromo_domain
IPR023779 Chromodomain_CS
IPR011381 Histone_H3-K9_MeTrfase
IPR003616 Post-SET_dom
IPR007728 Pre-SET_dom
IPR001214 SET_dom
PfamiView protein in Pfam
PF00385 Chromo, 1 hit
PF05033 Pre-SET, 1 hit
PF00856 SET, 1 hit
PIRSFiPIRSF009343 SUV39_SET, 1 hit
SMARTiView protein in SMART
SM00298 CHROMO, 1 hit
SM00508 PostSET, 1 hit
SM00468 PreSET, 1 hit
SM00317 SET, 1 hit
SUPFAMiSSF54160 SSF54160, 1 hit
PROSITEiView protein in PROSITE
PS00598 CHROMO_1, 1 hit
PS50013 CHROMO_2, 1 hit
PS50868 POST_SET, 1 hit
PS50867 PRE_SET, 1 hit
PS51579 SAM_MT43_SUVAR39_3, 1 hit
PS50280 SET, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiSUV91_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: O43463
Secondary accession number(s): B2R6E8
, B4DST0, Q53G60, Q6FHK6
<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: June 1, 1998
Last modified: December 5, 2018
This is version 192 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 X
    Human chromosome X: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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