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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 ‘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

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 ‘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 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 ‘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 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

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000181555.19

    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; 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.
    See also OMIM:144700
    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.
    See also OMIM:616831
    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.
    See also OMIM:613065
    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 Publication1
    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.
    See also OMIM:601626
    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

    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
    79731 [Q9BYW2-2]
    79732 [Q9BYW2-3]

    2D gel databases

    USC-OGP 2-DE database

    More...
    OGPi
    Q9BYW2

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9BYW2

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

    More...
    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

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

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_SETD2

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9BYW2 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9BYW2 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    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)

    More...
    BioGridi
    118845, 50 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    Q9BYW2, 16 interactors

    STRING: functional protein association networks

    More...
    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

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q9BYW2

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

    More...
    SMRi
    Q9BYW2

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    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 Publications2
    Regioni2137 – 2366Low charge region1 PublicationAdd BLAST230
    Regioni2457 – 2564Interaction with POLR2A1 PublicationAdd BLAST108

    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 coili2117 – 2146Sequence analysisAdd BLAST30

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi166 – 247Pro-richAdd BLAST82
    Compositional biasi385 – 456Arg-richAdd BLAST72
    Compositional biasi2149 – 2232Pro-richAdd BLAST84
    Compositional biasi2266 – 2365Gln-richAdd BLAST100

    <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 low charge region mediates the transcriptional activation activity.1 Publication
    The catalytic SET domain binds histone H3 (PubMed:27474439, PubMed:28256625). It is also able to bind oncogenic histone H3 K36M/I found in a number of cancer types, in which histone H3 'Lys-36' is replaced by a Met or an Ile residue. When binding the oncogenic variant histone H3 K36M/I, the SET domain undergoes dramatic conformational change to accommodate the histone H3 peptide, leading to sequester and inhibit SETD2 activity and block global H3K36 methylation (PubMed:27474439, PubMed:28256625).2 Publications

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG4442 Eukaryota
    COG2940 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000160086

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG093939

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9BYW2

    KEGG Orthology (KO)

    More...
    KOi
    K11423

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    FIGHDSH

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G040P

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9BYW2

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF106477

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00201 WW, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.1740.100, 1 hit
    1.20.930.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR006560 AWS_dom
    IPR003616 Post-SET_dom
    IPR001214 SET_dom
    IPR013257 SRI
    IPR038190 SRI_sf
    IPR035441 TFIIS/LEDGF_dom_sf
    IPR001202 WW_dom
    IPR036020 WW_dom_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00856 SET, 1 hit
    PF08236 SRI, 1 hit
    PF00397 WW, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00570 AWS, 1 hit
    SM00508 PostSET, 1 hit
    SM00317 SET, 1 hit
    SM00456 WW, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51045 SSF51045, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51215 AWS, 1 hit
    PS50868 POST_SET, 1 hit
    PS50280 SET, 1 hit
    PS01159 WW_DOMAIN_1, 1 hit
    PS50020 WW_DOMAIN_2, 1 hit

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

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

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

    This entry has 3 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: Q9BYW2-1) [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
    MKQLQPQPPP KMGDFYDPEH PTPEEEENEA KIENVQKTGF IKGPMFKGVA
    60 70 80 90 100
    SSRFLPKGTK TKVNLEEQGR QKVSFSFSLT KKTLQNRFLT ALGNEKQSDT
    110 120 130 140 150
    PNPPAVPLQV DSTPKMKMEI GDTLSTAEES SPPKSRVELG KIHFKKHLLH
    160 170 180 190 200
    VTSRPLLATT TAVASPPTHA APLPAVIAES TTVDSPPSSP PPPPPPAQAT
    210 220 230 240 250
    TLSSPAPVTE PVALPHTPIT VLMAAPVPLP VDVAVRSLKE PPIIIVPESL
    260 270 280 290 300
    EADTKQDTIS NSLEEHVTQI LNEQADISSK KEDSHIGKDE EIPDSSKISL
    310 320 330 340 350
    SCKKTGSKKK SSQSEGIFLG SESDEDSVRT SSSQRSHDLK FSASIEKERD
    360 370 380 390 400
    FKKSSAPLKS EDLGKPSRSK TDRDDKYFSY SKLERDTRYV SSRCRSERER
    410 420 430 440 450
    RRSRSHSRSE RGSRTNLSYS RSERSHYYDS DRRYHRSSPY RERTRYSRPY
    460 470 480 490 500
    TDNRARESSD SEEEYKKTYS RRTSSHSSSY RDLRTSSYSK SDRDCKTETS
    510 520 530 540 550
    YLEMERRGKY SSKLERESKR TSENEAIKRC CSPPNELGFR RGSSYSKHDS
    560 570 580 590 600
    SASRYKSTLS KPIPKSDKFK NSFCCTELNE EIKQSHSFSL QTPCSKGSEL
    610 620 630 640 650
    RMINKNPERE KAGSPAPSNR LNDSPTLKKL DELPIFKSEF ITHDSHDSIK
    660 670 680 690 700
    ELDSLSKVKN DQLRSFCPIE LNINGSPGAE SDLATFCTSK TDAVLMTSDD
    710 720 730 740 750
    SVTGSELSPL VKACMLSSNG FQNISRCKEK DLDDTCMLHK KSESPFRETE
    760 770 780 790 800
    PLVSPHQDKL MSMPVMTVDY SKTVVKEPVD TRVSCCKTKD SDIYCTLNDS
    810 820 830 840 850
    NPSLCNSEAE NIEPSVMKIS SNSFMNVHLE SKPVICDSRN LTDHSKFACE
    860 870 880 890 900
    EYKQSIGSTS SASVNHFDDL YQPIGSSGIA SSLQSLPPGI KVDSLTLLKC
    910 920 930 940 950
    GENTSPVLDA VLKSKKSSEF LKHAGKETIV EVGSDLPDSG KGFASRENRR
    960 970 980 990 1000
    NNGLSGKCLQ EAQEEGNSIL PERRGRPEIS LDERGEGGHV HTSDDSEVVF
    1010 1020 1030 1040 1050
    SSCDLNLTME DSDGVTYALK CDSSGHAPEI VSTVHEDYSG SSESSNDESD
    1060 1070 1080 1090 1100
    SEDTDSDDSS IPRNRLQSVV VVPKNSTLPM EETSPCSSRS SQSYRHYSDH
    1110 1120 1130 1140 1150
    WEDERLESRR HLYEEKFESI ASKACPQTDK FFLHKGTEKN PEISFTQSSR
    1160 1170 1180 1190 1200
    KQIDNRLPEL SHPQSDGVDS TSHTDVKSDP LGHPNSEETV KAKIPSRQQE
    1210 1220 1230 1240 1250
    ELPIYSSDFE DVPNKSWQQT TFQNRPDSRL GKTELSFSSS CEIPHVDGLH
    1260 1270 1280 1290 1300
    SSEELRNLGW DFSQEKPSTT YQQPDSSYGA CGGHKYQQNA EQYGGTRDYW
    1310 1320 1330 1340 1350
    QGNGYWDPRS GRPPGTGVVY DRTQGQVPDS LTDDREEEEN WDQQDGSHFS
    1360 1370 1380 1390 1400
    DQSDKFLLSL QKDKGSVQAP EISSNSIKDT LAVNEKKDFS KNLEKNDIKD
    1410 1420 1430 1440 1450
    RGPLKKRRQE IESDSESDGE LQDRKKVRVE VEQGETSVPP GSALVGPSCV
    1460 1470 1480 1490 1500
    MDDFRDPQRW KECAKQGKMP CYFDLIEENV YLTERKKNKS HRDIKRMQCE
    1510 1520 1530 1540 1550
    CTPLSKDERA QGEIACGEDC LNRLLMIECS SRCPNGDYCS NRRFQRKQHA
    1560 1570 1580 1590 1600
    DVEVILTEKK GWGLRAAKDL PSNTFVLEYC GEVLDHKEFK ARVKEYARNK
    1610 1620 1630 1640 1650
    NIHYYFMALK NDEIIDATQK GNCSRFMNHS CEPNCETQKW TVNGQLRVGF
    1660 1670 1680 1690 1700
    FTTKLVPSGS ELTFDYQFQR YGKEAQKCFC GSANCRGYLG GENRVSIRAA
    1710 1720 1730 1740 1750
    GGKMKKERSR KKDSVDGELE ALMENGEGLS DKNQVLSLSR LMVRIETLEQ
    1760 1770 1780 1790 1800
    KLTCLELIQN THSQSCLKSF LERHGLSLLW IWMAELGDGR ESNQKLQEEI
    1810 1820 1830 1840 1850
    IKTLEHLPIP TKNMLEESKV LPIIQRWSQT KTAVPPLSEG DGYSSENTSR
    1860 1870 1880 1890 1900
    AHTPLNTPDP STKLSTEADT DTPKKLMFRR LKIISENSMD SAISDATSEL
    1910 1920 1930 1940 1950
    EGKDGKEDLD QLENVPVEEE EELQSQQLLP QQLPECKVDS ETNIEASKLP
    1960 1970 1980 1990 2000
    TSEPEADAEI EPKESNGTKL EEPINEETPS QDEEEGVSDV ESERSQEQPD
    2010 2020 2030 2040 2050
    KTVDISDLAT KLLDSWKDLK EVYRIPKKSQ TEKENTTTER GRDAVGFRDQ
    2060 2070 2080 2090 2100
    TPAPKTPNRS RERDPDKQTQ NKEKRKRRSS LSPPSSAYER GTKRPDDRYD
    2110 2120 2130 2140 2150
    TPTSKKKVRI KDRNKLSTEE RRKLFEQEVA QREAQKQQQQ MQNLGMTSPL
    2160 2170 2180 2190 2200
    PYDSLGYNAP HHPFAGYPPG YPMQAYVDPS NPNAGKVLLP TPSMDPVCSP
    2210 2220 2230 2240 2250
    APYDHAQPLV GHSTEPLSAP PPVPVVPHVA APVEVSSSQY VAQSDGVVHQ
    2260 2270 2280 2290 2300
    DSSVAVLPVP APGPVQGQNY SVWDSNQQSV SVQQQYSPAQ SQATIYYQGQ
    2310 2320 2330 2340 2350
    TCPTVYGVTS PYSQTTPPIV QSYAQPSLQY IQGQQIFTAH PQGVVVQPAA
    2360 2370 2380 2390 2400
    AVTTIVAPGQ PQPLQPSEMV VTNNLLDLPP PSPPKPKTIV LPPNWKTARD
    2410 2420 2430 2440 2450
    PEGKIYYYHV ITRQTQWDPP TWESPGDDAS LEHEAEMDLG TPTYDENPMK
    2460 2470 2480 2490 2500
    ASKKPKTAEA DTSSELAKKS KEVFRKEMSQ FIVQCLNPYR KPDCKVGRIT
    2510 2520 2530 2540 2550
    TTEDFKHLAR KLTHGVMNKE LKYCKNPEDL ECNENVKHKT KEYIKKYMQK
    2560
    FGAVYKPKED TELE
    Length:2,564
    Mass (Da):287,597
    Last modified:May 18, 2010 - v3
    <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:i2B1BAE5867AB8EAB
    GO
    Isoform 2 (identifier: Q9BYW2-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1715-2564: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:1,714
    Mass (Da):192,342
    Checksum:iBD566E360FCF0E9B
    GO
    Isoform 3 (identifier: Q9BYW2-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1573-2564: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:1,572
    Mass (Da):175,982
    Checksum:i1FAC3FE752C0777C
    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 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    A0A1W2PPX9A0A1W2PPX9_HUMAN
    Histone-lysine N-methyltransferase ...
    SETD2
    591Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H7C3H4H7C3H4_HUMAN
    Histone-lysine N-methyltransferase ...
    SETD2
    1,675Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H7BZ93H7BZ93_HUMAN
    Histone-lysine N-methyltransferase ...
    SETD2
    1,290Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    C9JG86C9JG86_HUMAN
    Histone-lysine N-methyltransferase ...
    SETD2
    1,340Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    H7BXT4H7BXT4_HUMAN
    Histone-lysine N-methyltransferase ...
    SETD2
    1,365Annotation score:

    Annotation score:1 out of 5

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

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

    The sequence AAF29041 differs from that shown. Reason: Frameshift at several positions.Curated
    The sequence AAH72440 differs from that shown. Reason: Erroneous termination at position 463. Translated as Glu.Curated
    The sequence AAI17163 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAI17165 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAT77612 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAT77613 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAB15367 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
    The sequence BAB15367 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence BAC87131 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence CAC28349 differs from that shown. Reason: Erroneous termination at position 385. Translated as Arg.Curated
    The sequence CAD38601 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    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 conflicti448R → Q in BAD18522 (PubMed:14702039).Curated1
    Sequence conflicti455A → V in CAD38601 (PubMed:17974005).Curated1
    Sequence conflicti912L → P in BAB15367 (PubMed:14702039).Curated1
    Sequence conflicti964E → K in CAC28349 (PubMed:11461154).Curated1
    Sequence conflicti964E → K in AAT77612 (PubMed:16118227).Curated1
    Sequence conflicti964E → K in AAT77613 (Ref. 7) Curated1
    Sequence conflicti1080M → I in BAC87131 (PubMed:14702039).Curated1
    Sequence conflicti1080M → T in CAD38601 (PubMed:17974005).Curated1
    Sequence conflicti1212V → F in BAD18522 (PubMed:14702039).Curated1
    Sequence conflicti1269T → A in CAC28349 (PubMed:11461154).Curated1
    Sequence conflicti1269T → A in AAT77612 (PubMed:16118227).Curated1
    Sequence conflicti1269T → A in AAT77613 (Ref. 7) Curated1
    Sequence conflicti1338E → G in BAB15367 (PubMed:14702039).Curated1
    Sequence conflicti1498Q → R in CAD38601 (PubMed:17974005).Curated1
    Sequence conflicti1706K → N in AAF29041 (PubMed:11042152).Curated1
    Sequence conflicti1736L → P in CAC28349 (PubMed:11461154).Curated1
    Sequence conflicti1736L → P in AAT77612 (PubMed:16118227).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_0790542K → R in ALL; unknown pathological significance; somatic mutation. 1 Publication