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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-Experimental evidence at protein leveli

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

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N6-methyl-L-lysine-[histone].2 Publications
S-adenosyl-L-methionine + [protein]-L-lysine = S-adenosyl-L-homocysteine + [protein]-N6-methyl-L-lysine.1 Publication
3 S-adenosyl-L-methionine + [protein]-L-lysine = 3 S-adenosyl-L-homocysteine + [protein]-N6,N6,N6-methyl-L-lysine.1 Publication

Enzyme regulationi

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

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
    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
    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

    GO - Molecular functioni

    • alpha-tubulin binding Source: UniProtKB
    • histone-lysine N-methyltransferase activity Source: UniProtKB
    • histone methyltransferase activity (H3-K36 specific) Source: UniProtKB
    • protein-lysine N-methyltransferase activity Source: UniProtKB

    GO - Biological processi

    • angiogenesis Source: Ensembl
    • cell migration involved in vasculogenesis Source: Ensembl
    • coronary vasculature morphogenesis Source: Ensembl
    • defense response to virus Source: UniProtKB
    • embryonic cranial skeleton morphogenesis Source: Ensembl
    • embryonic placenta morphogenesis Source: Ensembl
    • endodermal cell differentiation Source: UniProtKB
    • forebrain development Source: Ensembl
    • histone H3-K36 dimethylation Source: HGNC
    • histone H3-K36 trimethylation Source: UniProtKB
    • mesoderm morphogenesis Source: Ensembl
    • microtubule cytoskeleton organization involved in mitosis Source: UniProtKB
    • mismatch repair Source: UniProtKB
    • morphogenesis of a branching structure Source: Ensembl
    • neural tube closure Source: Ensembl
    • nucleosome organization Source: UniProtKB
    • peptidyl-lysine monomethylation Source: UniProtKB
    • peptidyl-lysine trimethylation Source: UniProtKB
    • pericardium development Source: Ensembl
    • positive regulation of interferon-alpha production Source: UniProtKB
    • regulation of cytokinesis Source: UniProtKB
    • regulation of double-strand break repair via homologous recombination Source: UniProtKB
    • regulation of mRNA export from nucleus Source: UniProtKB
    • regulation of protein localization to chromatin Source: UniProtKB
    • regulation of transcription, DNA-templated Source: UniProtKB-KW
    • response to type I interferon Source: UniProtKB
    • stem cell development Source: Ensembl
    • stem cell differentiation Source: UniProtKB
    • transcription elongation from RNA polymerase II promoter Source: UniProtKB

    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

    BRENDAi2.1.1.43. 2681.
    ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.
    SignaLinkiQ9BYW2.
    SIGNORiQ9BYW2.

    Names & Taxonomyi

    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
    Gene namesi
    Name:SETD2
    Synonyms:HIF1, HYPB1 Publication, KIAA17321 Publication, KMT3A1 Publication, SET22 Publications
    ORF Names:HSPC069
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 3

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000181555.19.
    HGNCiHGNC:18420. SETD2.

    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

    Pathology & Biotechi

    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
    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:rs869025570Ensembl.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 Publication1
    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 Publication1
    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 Publication1
    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 Publication1
    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 Publication1
    Natural variantiVAR_0790691397D → G in AML; unknown pathological significance; somatic mutation. 1 Publication1
    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
    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

    DisGeNETi29072.
    MalaCardsiSETD2.
    MIMi144700. phenotype.
    601626. phenotype.
    613065. phenotype.
    616831. phenotype.
    OpenTargetsiENSG00000181555.
    Orphaneti821. Sotos syndrome.
    PharmGKBiPA143485612.

    Chemistry databases

    ChEMBLiCHEMBL3108647.

    Polymorphism and mutation databases

    BioMutaiSETD2.
    DMDMi296452963.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002523671 – 2564Histone-lysine N-methyltransferase SETD2Add BLAST2564

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei131PhosphoserineCombined sources1
    Modified residuei321PhosphoserineCombined sources1
    Modified residuei323PhosphoserineCombined sources1
    Modified residuei344PhosphoserineCombined sources1
    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

    Post-translational modificationi

    May be automethylated.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    EPDiQ9BYW2.
    MaxQBiQ9BYW2.
    PaxDbiQ9BYW2.
    PeptideAtlasiQ9BYW2.
    PRIDEiQ9BYW2.

    2D gel databases

    OGPiQ9BYW2.

    PTM databases

    iPTMnetiQ9BYW2.
    PhosphoSitePlusiQ9BYW2.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    BgeeiENSG00000181555.
    CleanExiHS_SETD2.
    ExpressionAtlasiQ9BYW2. baseline and differential.
    GenevisibleiQ9BYW2. HS.

    Organism-specific databases

    HPAiHPA042451.

    Interactioni

    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

    Binary interactionsi

    Show more details

    GO - Molecular functioni

    • alpha-tubulin binding Source: UniProtKB

    Protein-protein interaction databases

    BioGridi118845. 48 interactors.
    IntActiQ9BYW2. 15 interactors.
    MINTiMINT-1537591.
    STRINGi9606.ENSP00000386759.

    Chemistry databases

    BindingDBiQ9BYW2.

    Structurei

    Secondary structure

    12564
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi1448 – 1450Combined sources3
    Helixi1451 – 1455Combined sources5
    Helixi1457 – 1465Combined sources9
    Beta strandi1480 – 1483Combined sources4
    Helixi1506 – 1511Combined sources6
    Helixi1521 – 1524Combined sources4
    Beta strandi1531 – 1533Combined sources3
    Helixi1536 – 1538Combined sources3
    Beta strandi1539 – 1541Combined sources3
    Turni1543 – 1547Combined sources5
    Beta strandi1552 – 1556Combined sources5
    Beta strandi1558 – 1560Combined sources3
    Beta strandi1562 – 1568Combined sources7
    Beta strandi1575 – 1578Combined sources4
    Beta strandi1582 – 1584Combined sources3
    Helixi1586 – 1598Combined sources13
    Beta strandi1606 – 1610Combined sources5
    Beta strandi1613 – 1616Combined sources4
    Beta strandi1618 – 1621Combined sources4
    Helixi1623 – 1626Combined sources4
    Beta strandi1634 – 1642Combined sources9
    Beta strandi1645 – 1654Combined sources10
    Beta strandi1661 – 1664Combined sources4
    Helixi1667 – 1670Combined sources4
    Beta strandi1672 – 1674Combined sources3
    Beta strandi1675 – 1677Combined sources3
    Beta strandi1687 – 1691Combined sources5
    Helixi1697 – 1700Combined sources4
    Beta strandi2377 – 2379Combined sources3
    Helixi2386 – 2388Combined sources3
    Beta strandi2392 – 2399Combined sources8
    Turni2401 – 2403Combined sources3
    Beta strandi2405 – 2409Combined sources5
    Turni2410 – 2413Combined sources4
    Beta strandi2414 – 2419Combined sources6
    Beta strandi2424 – 2428Combined sources5
    Helixi2463 – 2486Combined sources24
    Turni2487 – 2489Combined sources3
    Beta strandi2495 – 2498Combined sources4
    Helixi2502 – 2524Combined sources23
    Helixi2527 – 2529Combined sources3
    Helixi2534 – 2548Combined sources15
    Turni2549 – 2551Combined sources3
    Helixi2557 – 2559Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2A7ONMR-A2457-2564[»]
    2MDCNMR-A2385-2430[»]
    2MDINMR-A2377-2430[»]
    2MDJNMR-A2377-2430[»]
    4FMUX-ray2.10A1434-1711[»]
    4H12X-ray1.99A1434-1711[»]
    5JJYX-ray2.05A1434-1711[»]
    5JLBX-ray1.50A1434-1711[»]
    5JLEX-ray2.40A1434-1711[»]
    5LSSX-ray1.79A1433-1711[»]
    5LSXX-ray2.90A1433-1711[»]
    5LSYX-ray1.62A1433-1711[»]
    5LSZX-ray1.62A1433-1711[»]
    5LT6X-ray2.05A/B1433-1711[»]
    5LT7X-ray1.51A1433-1711[»]
    5LT8X-ray1.57A1433-1711[»]
    5V21X-ray2.42A1435-1711[»]
    5V22X-ray2.40A1435-1711[»]
    ProteinModelPortaliQ9BYW2.
    SMRiQ9BYW2.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BYW2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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
    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
    Coiled coili2117 – 2146Sequence analysisAdd BLAST30

    Compositional bias

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Compositional biasi166 – 247Pro-richAdd BLAST82
    Compositional biasi385 – 456Arg-richAdd BLAST72
    Compositional biasi2149 – 2232Pro-richAdd BLAST