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Entry version 168 (18 Sep 2019)
Sequence version 3 (18 May 2010)
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Protein

Histone-lysine N-methyltransferase SETD2

Gene

SETD2

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-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36' (H3K36me2) as substrate (PubMed:16118227, PubMed:19141475, PubMed:21526191, PubMed:21792193, PubMed:23043551, PubMed:27474439). Represents the main enzyme generating H3K36me3, a specific tag for epigenetic transcriptional activation (By similarity). Plays a role in chromatin structure modulation during elongation by coordinating recruitment of the FACT complex and by interacting with hyperphosphorylated POLR2A (PubMed:23325844). Acts as a key regulator of DNA mismatch repair in G1 and early S phase by generating H3K36me3, a mark required to recruit MSH6 subunit of the MutS alpha complex: early recruitment of the MutS alpha complex to chromatin to be replicated allows a quick identification of mismatch DNA to initiate the mismatch repair reaction (PubMed:23622243). Required for DNA double-strand break repair in response to DNA damage: acts by mediating formation of H3K36me3, promoting recruitment of RAD51 and DNA repair via homologous recombination (HR) (PubMed:24843002). Acts as a tumor suppressor (PubMed:24509477). H3K36me3 also plays an essential role in the maintenance of a heterochromatic state, by recruiting DNA methyltransferase DNMT3A (PubMed:27317772). H3K36me3 is also enhanced in intron-containing genes, suggesting that SETD2 recruitment is enhanced by splicing and that splicing is coupled to recruitment of elongating RNA polymerase (PubMed:21792193). Required during angiogenesis (By similarity). Required for endoderm development by promoting embryonic stem cell differentiation toward endoderm: acts by mediating formation of H3K36me3 in distal promoter regions of FGFR3, leading to regulate transcription initiation of FGFR3 (By similarity). In addition to histones, also mediates methylation of other proteins, such as tubulins and STAT1 (PubMed:27518565, PubMed:28753426). Trimethylates 'Lys-40' of alpha-tubulins such as TUBA1B (alpha-TubK40me3); alpha-TubK40me3 is required for normal mitosis and cytokinesis and may be a specific tag in cytoskeletal remodeling (PubMed:27518565). Involved in interferon-alpha-induced antiviral defense by mediating both monomethylation of STAT1 at 'Lys-525' and catalyzing H3K36me3 on promoters of some interferon-stimulated genes (ISGs) to activate gene transcription (PubMed:28753426).By similarity13 Publications
(Microbial infection) Recruited to the promoters of adenovirus 12 E1A gene in case of infection, possibly leading to regulate its expression.1 Publication

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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

Specifically inhibited by sinefungin derivatives. N-propyl sinefungin (Pr-SNF) interacts preferentially with SETD2.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 0.14 min(-1).1 Publication
  1. KM=1.21 µM for S-adenosyl-L-methionine1 Publication
  2. KM=0.42 µM for histone H31 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi1499Zinc 1Combined sources3 Publications1
    Metal bindingi1501Zinc 1Combined sources3 Publications1
    Metal bindingi1516Zinc 1Combined sources3 Publications1
    Metal bindingi1516Zinc 2Combined sources3 Publications1
    Metal bindingi1520Zinc 1Combined sources3 Publications1
    Metal bindingi1529Zinc 2Combined sources3 Publications1
    Metal bindingi1533Zinc 2Combined sources3 Publications1
    Metal bindingi1539Zinc 2Combined sources3 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei1625Inhibitor1 Publication1
    Metal bindingi1631Zinc 3Combined sources3 Publications1
    Binding sitei1676Inhibitor; alternate1 Publication1
    Binding sitei1676S-adenosyl-L-methionine; alternateCombined sources3 Publications1
    Metal bindingi1678Zinc 3Combined sources3 Publications1
    Binding sitei1679Inhibitor; via amide nitrogen; alternateCombined sources2 Publications1
    Binding sitei1679S-adenosyl-L-methionine; via amide nitrogen; alternateCombined sources3 Publications1
    Metal bindingi1680Zinc 3Combined sources3 Publications1
    Metal bindingi1685Zinc 3Combined sources3 Publications1

    <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 functionActivator, Chromatin regulator, Developmental protein, Methyltransferase, Transferase
    Biological processAntiviral defense, Differentiation, DNA damage, DNA repair, Immunity, Innate immunity, Transcription, Transcription regulation
    LigandMetal-binding, S-adenosyl-L-methionine, Zinc

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.1.1.43 2681

    Reactome - a knowledgebase of biological pathways and processes

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

    SignaLink: a signaling pathway resource with multi-layered regulatory networks

    More...
    SignaLinki
    Q9BYW2

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    Q9BYW2

    <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 SETD2Curated (EC:2.1.1.432 Publications)
    Alternative name(s):
    HIF-1
    Huntingtin yeast partner B1 Publication
    Huntingtin-interacting protein 1
    Short name:
    HIP-1
    Huntingtin-interacting protein B1 Publication
    Lysine N-methyltransferase 3A1 Publication
    Protein-lysine N-methyltransferase SETD2Curated (EC:2.1.1.-2 Publications)
    SET domain-containing protein 21 Publication
    Short name:
    hSET21 Publication
    p231HBP1 Publication
    <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:SETD2
    Synonyms:HIF1, HYPB1 Publication, KIAA17321 Publication, KMT3A1 Publication, SET22 Publications
    ORF Names:HSPC069
    <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 3

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:18420 SETD2

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    612778 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q9BYW2

    <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

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Renal cell carcinoma (RCC)4 Publications
    The disease may be caused by mutations affecting the gene represented in this entry. Defects of SETD2 are associated with loss of DNA methylation at non-promoter regions (PubMed:23792563). SETD2 defects lead to aberrant and reduced nucleosome compaction and chromatin association of key replication proteins, such as MCM7 and DNA polymerase delta, leading to hinder replication fork progression and prevent loading of RAD51 homologous recombination repair factor at DNA breaks (PubMed:25728682).2 Publications
    Disease descriptionRenal cell carcinoma is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma. Clear cell renal cell carcinoma is the most common subtype.
    Related information in OMIM
    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_0698121733N → D in RCC; defects in recruitment of the MutS alpha complex. 1 Publication1
    Natural variantiVAR_0698131769S → P in RCC; defects in recruitment of the MutS alpha complex. 1 Publication1
    Luscan-Lumish syndrome (LLS)4 Publications
    The disease may be caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn autosomal dominant syndrome with a variable phenotype. Clinical features include macrocephaly, distinctive facial appearance, postnatal overgrowth, various degrees of learning difficulties, autism spectrum disorder, and intellectual disability.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_0765361815L → W in LLS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs869025570EnsemblClinVar.1
    Leukemia, acute lymphoblastic (ALL)2 Publications
    The disease may be caused by mutations affecting distinct genetic loci, including the gene represented in this entry.
    Disease descriptionA subtype of acute leukemia, a cancer of the white blood cells. ALL is a malignant disease of bone marrow and the most common malignancy diagnosed in children. The malignant cells are lymphoid precursor cells (lymphoblasts) that are arrested in an early stage of development. The lymphoblasts replace the normal marrow elements, resulting in a marked decrease in the production of normal blood cells. Consequently, anemia, thrombocytopenia, and neutropenia occur to varying degrees. The lymphoblasts also proliferate in organs other than the marrow, particularly the liver, spleen, and lymphnodes.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_0790542K → R in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_07905519E → G in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_079057226P → S in ALL; unknown pathological significance; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs780963440Ensembl.1
    Natural variantiVAR_079058267V → I in ALL; unknown pathological significance; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs186148199EnsemblClinVar.1
    Natural variantiVAR_079059470S → P in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_079060499T → A in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_079061761M → I in ALL; unknown pathological significance; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs188887061EnsemblClinVar.1
    Natural variantiVAR_079062794 – 2564Missing in ALL; unknown pathological significance; somatic mutation. 1 PublicationAdd BLAST1771
    Natural variantiVAR_0790641076S → P in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790651093S → G in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790661171T → A in ALL; unknown pathological significance; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs540476365Ensembl.1
    Natural variantiVAR_0790671351D → G in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790681365G → E in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790701416 – 2564Missing in ALL; unknown pathological significance; somatic mutation. 1 PublicationAdd BLAST1149
    Natural variantiVAR_0790711453D → N in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790721493D → N in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790731496 – 2564Missing in ALL; unknown pathological significance; somatic mutation. 1 PublicationAdd BLAST1069
    Natural variantiVAR_0790741609L → P in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790751654K → Q in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790761663T → M in ALL; unknown pathological significance; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1478147351Ensembl.1
    Natural variantiVAR_0790781821L → P in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790791915V → A in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790801920E → V in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790812077 – 2564Missing in ALL; unknown pathological significance; somatic mutation. 1 PublicationAdd BLAST488
    Natural variantiVAR_0790832214T → A in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790852361P → S in ALL; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790872524 – 2564Missing in ALL; unknown pathological significance; somatic mutation. 1 PublicationAdd BLAST41
    Natural variantiVAR_0790882546 – 2564Missing in ALL; unknown pathological significance; somatic mutation. 1 PublicationAdd BLAST19
    Leukemia, acute myelogenous (AML)2 Publications
    The disease may be caused by mutations affecting distinct genetic loci, including the gene represented in this entry.
    Disease descriptionA subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_07905670 – 2564Missing in AML; unknown pathological significance; somatic mutation. 1 PublicationAdd BLAST2495
    Natural variantiVAR_079063800S → N in AML; unknown pathological significance; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1169288572Ensembl.1
    Natural variantiVAR_0790691397D → G in AML; unknown pathological significance; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs754921650Ensembl.1
    Natural variantiVAR_0790771804L → S in AML; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790822122R → W in AML; unknown pathological significance; somatic mutation. 1 Publication1
    Natural variantiVAR_0790842325 – 2564Missing in AML; unknown pathological significance; somatic mutation. 1 PublicationAdd BLAST240
    Natural variantiVAR_0790862505F → L in AML; Impairs interaction with hyperphosphorylated POLR2A; unknown pathological significance; somatic mutation. 2 Publications1

    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>Mutagenesisi1589F → A: Strongly reduced methyltransferase activity. 1 Publication1
    Mutagenesisi1604Y → A: Increased methyltransferase activity. 1 Publication1
    Mutagenesisi1625R → H or G: Loss of methyltransferase activity. Abolishes ability to monomethylate STAT1. 2 Publications1
    Mutagenesisi1631C → A: Does not affect methyltransferase activity. 1 Publication1
    Mutagenesisi1636E → A: Increased methyltransferase activity. 1 Publication1
    Mutagenesisi1637T → A: Increased methyltransferase activity. 1 Publication1
    Mutagenesisi1668F → A: Strongly reduced methyltransferase activity. 2 Publications1
    Mutagenesisi1669Q → A: Loss of methyltransferase activity. 1 Publication1
    Mutagenesisi1670R → A, V, L, I or F: Impaired methyltransferase activity. 1 Publication1
    Mutagenesisi1670R → P, W, K or Q: Loss of methyltransferase activity. 1 Publication1
    Mutagenesisi1671Y → A: Strongly reduced methyltransferase activity. 2 Publications1
    Mutagenesisi2475R → A: Does not affect interaction with hyperphosphorylated POLR2A. 1 Publication1
    Mutagenesisi2476K → A: Does not affect interaction with hyperphosphorylated POLR2A. 1 Publication1
    Mutagenesisi2480Q → A: Does not affect interaction with hyperphosphorylated POLR2A. 1 Publication1
    Mutagenesisi2481F → A: Does not affect interaction with hyperphosphorylated POLR2A. 1 Publication1
    Mutagenesisi2483V → A: Impairs interaction with hyperphosphorylated POLR2A. 1 Publication1
    Mutagenesisi2506K → A: Impairs interaction with hyperphosphorylated POLR2A. 1 Publication1
    Mutagenesisi2510R → A: Impairs interaction with hyperphosphorylated POLR2A. 1 Publication1
    Mutagenesisi2514H → A: Impairs interaction with hyperphosphorylated POLR2A. 1 Publication1
    Mutagenesisi2515G → A or T: Does not affect interaction with hyperphosphorylated POLR2A. 1 Publication1
    Mutagenesisi2528E → A: Increases interaction with hyperphosphorylated POLR2A; when associated with A-2531. 1 Publication1
    Mutagenesisi2531E → A: Increases interaction with hyperphosphorylated POLR2A; when associated with A-2528. 1 Publication1

    Keywords - Diseasei

    Autism spectrum disorder, Disease mutation, Mental retardation, Tumor suppressor

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    29072

    MalaCards human disease database

    More...
    MalaCardsi
    SETD2
    MIMi144700 phenotype
    601626 phenotype
    613065 phenotype
    616831 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000181555

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    821 Sotos syndrome

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA143485612

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3108647

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    SETD2

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    296452963

    <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_00002523671 – 2564Histone-lysine N-methyltransferase SETD2Add BLAST2564

    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 residuei131PhosphoserineCombined sources1
    Modified residuei321PhosphoserineCombined sources1
    Modified residuei323PhosphoserineCombined sources1
    Modified residuei344PhosphoserineCombined 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-linki359Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei422PhosphoserineCombined sources1
    Modified residuei532PhosphoserineCombined sources1
    Modified residuei614PhosphoserineCombined sources1
    Modified residuei624PhosphoserineCombined sources1
    Modified residuei626PhosphothreonineCombined sources1
    Cross-linki637Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei698PhosphoserineBy similarity1
    Modified residuei708PhosphoserineCombined sources1
    Modified residuei744PhosphoserineCombined sources1
    Modified residuei754PhosphoserineCombined sources1
    Cross-linki776Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Modified residuei1098PhosphoserineCombined sources1
    Modified residuei1228PhosphoserineCombined sources1
    Modified residuei1413PhosphoserineBy similarity1
    Modified residuei1415PhosphoserineBy similarity1
    Modified residuei1417PhosphoserineBy similarity1
    Modified residuei1696PhosphoserineCombined sources1
    Modified residuei1844PhosphoserineBy similarity1
    Modified residuei1845PhosphoserineBy similarity1
    Modified residuei1853PhosphothreonineCombined sources1
    Modified residuei1872PhosphothreonineCombined sources1
    Modified residuei1888PhosphoserineCombined sources1
    Modified residuei1952PhosphoserineCombined sources1
    Modified residuei1980PhosphoserineBy similarity1
    Modified residuei1988PhosphoserineBy similarity1
    Modified residuei1995PhosphoserineBy similarity1
    Modified residuei2080PhosphoserineCombined sources1
    Modified residuei2082PhosphoserineCombined 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

    May be automethylated.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q9BYW2

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q9BYW2

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    Q9BYW2

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q9BYW2

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

    More...
    PaxDbi
    Q9BYW2

    PeptideAtlas

    More...
    PeptideAtlasi
    Q9BYW2

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9BYW2

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    79730 [Q9BYW2-1]
    79731 [Q9BYW2-2]
    79732 [Q9BYW2-3]

    2D gel databases

    USC-OGP 2-DE database

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    OGPi
    Q9BYW2

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

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    iPTMneti
    Q9BYW2

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

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    PhosphoSitePlusi
    Q9BYW2

    <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.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

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    Bgeei
    ENSG00000181555 Expressed in 229 organ(s), highest expression level in oviduct epithelium

    ExpressionAtlas, Differential and Baseline Expression

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    ExpressionAtlasi
    Q9BYW2 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

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    Genevisiblei
    Q9BYW2 HS

    Organism-specific databases

    Human Protein Atlas

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    HPAi
    HPA042451

    <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

    Specifically interacts with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II large subunit (POLR2A): binds to CTD heptad repeats doubly phosphorylated on 'Ser-2' and 'Ser-5' of each heptad (PubMed:16118227, PubMed:16314571).

    Interacts with HTT (PubMed:11461154, PubMed:9700202, PubMed:10958656).

    Interacts with IWS1 (PubMed:19141475).

    Interacts with p53/TP53; leading to regulate p53/TP53 target genes (PubMed:18585004).

    Component of a complex with HNRNPL (PubMed:19332550).

    Interacts with TUBA1A; the interaction is independent on alpha-tubulin acetylation on 'Lys-40' (PubMed:27518565).

    Interacts with STAT1 (PubMed:28753426).

    10 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

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

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    BioGridi
    118845, 55 interactors

    Protein interaction database and analysis system

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    IntActi
    Q9BYW2, 31 interactors

    STRING: functional protein association networks

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    STRINGi
    9606.ENSP00000386759

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    Q9BYW2

    <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

    12564
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

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    SMRi
    Q9BYW2

    Database of comparative protein structure models

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    ModBasei
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

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    EvolutionaryTracei
    Q9BYW2

    <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>Domaini1494 – 1548AWSPROSITE-ProRule annotationAdd BLAST55
    Domaini1550 – 1667SETPROSITE-ProRule annotationAdd BLAST118
    Domaini1674 – 1690Post-SETPROSITE-ProRule annotationAdd BLAST17
    Domaini2389 – 2422WWPROSITE-ProRule annotationAdd BLAST34

    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>Regioni1418 – 1714Interaction with TUBA1A1 PublicationAdd BLAST297
    Regioni1560 – 1562Inhibitor binding1 Publication3
    Regioni1560 – 1562S-adenosyl-L-methionine bindingCombined sources3 Publications3
    Regioni1603 – 1605Inhibitor binding1 Publication3
    Regioni1603 – 1605S-adenosyl-L-methionine bindingCombined sources3 Publications3
    Regioni1628 – 1629Inhibitor binding1 Publication2
    Regioni1628 – 1629S-adenosyl-L-methionine bindingCombined sources3 Publications