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Q9H9B1

- EHMT1_HUMAN

UniProt

Q9H9B1 - EHMT1_HUMAN

Protein

Histone-lysine N-methyltransferase EHMT1

Gene

EHMT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 4 (08 Mar 2011)
      Previous versions | rss
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    Functioni

    Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53.2 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 Publication

    Enzyme regulationi

    Methyltransferase activity is inhibited by BIX-01294. Efficiently inhibited by compound E72, a BIX-01294 derivative in which the diazepane ring and the benzyl are replaced with a 3-dimethylaminopropyl and a 5-aminopentyl group at sites B and C, respectively.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1062 – 10621Zinc 1
    Metal bindingi1062 – 10621Zinc 2
    Metal bindingi1064 – 10641Zinc 1
    Metal bindingi1068 – 10681Zinc 1
    Metal bindingi1068 – 10681Zinc 3
    Metal bindingi1073 – 10731Zinc 1
    Metal bindingi1075 – 10751Zinc 2
    Metal bindingi1105 – 11051Zinc 2
    Metal bindingi1105 – 11051Zinc 3
    Metal bindingi1109 – 11091Zinc 2
    Metal bindingi1111 – 11111Zinc 3
    Metal bindingi1115 – 11151Zinc 3
    Binding sitei1155 – 11551Histone H3K9me2 Publications
    Binding sitei1173 – 11731S-adenosyl-L-methionine
    Metal bindingi1203 – 12031Zinc 4
    Metal bindingi1256 – 12561Zinc 4
    Binding sitei1257 – 12571S-adenosyl-L-methionine; via amide nitrogen
    Metal bindingi1258 – 12581Zinc 4
    Metal bindingi1263 – 12631Zinc 4

    GO - Molecular functioni

    1. histone-lysine N-methyltransferase activity Source: UniProtKB
    2. histone methyltransferase activity (H3-K27 specific) Source: UniProtKB
    3. histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
    4. methyltransferase activity Source: UniProtKB
    5. p53 binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein-lysine N-methyltransferase activity Source: UniProtKB
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. chromatin modification Source: UniProtKB
    2. DNA methylation Source: UniProtKB
    3. embryo development Source: UniProtKB
    4. histone methylation Source: UniProtKB
    5. negative regulation of transcription, DNA-templated Source: UniProtKB
    6. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    7. peptidyl-lysine dimethylation Source: UniProtKB
    8. peptidyl-lysine monomethylation Source: UniProtKB

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Transferase

    Keywords - Ligandi

    Metal-binding, S-adenosyl-L-methionine, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_169168. Senescence-Associated Secretory Phenotype (SASP).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase EHMT1 (EC:2.1.1.-, EC:2.1.1.43)
    Alternative name(s):
    Euchromatic histone-lysine N-methyltransferase 1
    Short name:
    Eu-HMTase1
    G9a-like protein 1
    Short name:
    GLP
    Short name:
    GLP1
    Histone H3-K9 methyltransferase 5
    Short name:
    H3-K9-HMTase 5
    Lysine N-methyltransferase 1D
    Gene namesi
    Name:EHMT1
    Synonyms:EUHMTASE1, GLP, KIAA1876, KMT1D
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:24650. EHMT1.

    Subcellular locationi

    Nucleus. Chromosome
    Note: Associates with euchromatic regions.

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. cytoplasm Source: HPA
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Kleefstra syndrome (KLESTS) [MIM:610253]: A syndrome characterized by severe mental retardation, hypotonia, brachy(micro)cephaly, and facial dysmorphisms. Additionally, congenital heart defects, urogenital defects, epilepsy and behavioral problems are frequently observed.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry (PubMed:16826528). The syndrome can be either caused by intragenic EHMT1 mutations leading to haploinsufficiency of the EHMT1 gene or by a submicroscopic 9q34.3 deletion. Although it is not known if and to what extent other genes in the 9q34.3 region contribute to the syndrome observed in deletion cases, EHMT1 seems to be the major determinant of the core disease phenotype (PubMed:19264732).2 Publications
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1075 – 10751C → Y in KLESTS. 1 Publication
    VAR_069183

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi905 – 9051E → A: Abolishes binding to histone H3K9me. 1 Publication

    Keywords - Diseasei

    Disease mutation, Mental retardation

    Organism-specific databases

    MIMi610253. phenotype.
    Orphaneti96147. Kleefstra syndrome due to 9q34 microdeletion.
    261652. Kleefstra syndrome due to a point mutation.
    PharmGKBiPA134941393.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12981298Histone-lysine N-methyltransferase EHMT1PRO_0000186067Add
    BLAST

    Proteomic databases

    MaxQBiQ9H9B1.
    PaxDbiQ9H9B1.
    PRIDEiQ9H9B1.

    PTM databases

    PhosphoSiteiQ9H9B1.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9H9B1.
    BgeeiQ9H9B1.
    CleanExiHS_EHMT1.
    GenevestigatoriQ9H9B1.

    Organism-specific databases

    HPAiHPA053043.

    Interactioni

    Subunit structurei

    Heterodimer; heterodimerizes with EHMT2. Interacts with WIZ and EHMT2. Part of the E2F6.com-1 complex in G0 phase composed of E2F6, MGA, MAX, TFDP1, CBX3, BAT8, EHMT1, RING1, RNF2, MBLR, L3MBTL2 and YAF2. Interacts (via ANK repeats) with RELA (when monomethylated at 'Lys-310'). Interacts with MPHOSPH8. Interacts with CDYL. Interacts with REST only in the presence of CDYL. Part of a complex containing at least CDYL, REST, WIZ, SETB1, EHMT1 and EHMT2.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MPHOSPH8Q995492EBI-766087,EBI-2653928
    RELAQ042063EBI-766087,EBI-73886
    RelaQ042075EBI-766087,EBI-644400From a different organism.

    Protein-protein interaction databases

    BioGridi122908. 29 interactions.
    DIPiDIP-34585N.
    IntActiQ9H9B1. 13 interactions.
    MINTiMINT-7945009.
    STRINGi9606.ENSP00000417980.

    Structurei

    Secondary structure

    1
    1298
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi776 – 7838
    Helixi786 – 7949
    Helixi809 – 8157
    Helixi819 – 8268
    Turni827 – 8293
    Helixi842 – 8487
    Helixi852 – 8598
    Turni860 – 8623
    Helixi876 – 8827
    Helixi886 – 8949
    Helixi909 – 9168
    Helixi919 – 9268
    Turni927 – 9293
    Helixi942 – 9487
    Helixi952 – 9598
    Turni960 – 9623
    Helixi975 – 9784
    Helixi983 – 99412
    Beta strandi1008 – 10125
    Turni1014 – 10174
    Beta strandi1019 – 10213
    Beta strandi1025 – 10317
    Beta strandi1037 – 10404
    Beta strandi1045 – 10484
    Helixi1056 – 10583
    Beta strandi1065 – 10684
    Helixi1074 – 10785
    Beta strandi1096 – 10983
    Beta strandi1109 – 11113
    Beta strandi1115 – 11173
    Helixi1120 – 11223
    Beta strandi1128 – 11325
    Beta strandi1134 – 114411
    Beta strandi1151 – 11555
    Beta strandi1157 – 11615
    Helixi1162 – 11665
    Beta strandi1174 – 11774
    Beta strandi1180 – 11834
    Beta strandi1185 – 11939
    Helixi1195 – 11984
    Beta strandi1206 – 121510
    Beta strandi1223 – 12308
    Helixi1244 – 12507
    Turni1251 – 12533

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IGQX-ray2.00A/B982-1266[»]
    2RFIX-ray1.59A/B982-1266[»]
    3B7BX-ray2.99A/B765-999[»]
    3B95X-ray2.99A/B765-999[»]
    3FPDX-ray2.40A/B1006-1266[»]
    3HNAX-ray1.50A/B982-1266[»]
    3MO0X-ray2.78A/B982-1266[»]
    3MO2X-ray2.49A/B/C/D982-1266[»]
    3MO5X-ray2.14A/B/C/D982-1266[»]
    3SW9X-ray3.05A/B982-1266[»]
    3SWCX-ray2.33A/B982-1266[»]
    4I51X-ray1.90A/B982-1266[»]
    ProteinModelPortaliQ9H9B1.
    SMRiQ9H9B1. Positions 695-1266.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H9B1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati737 – 76630ANK 1Add
    BLAST
    Repeati772 – 80130ANK 2Add
    BLAST
    Repeati805 – 83430ANK 3Add
    BLAST
    Repeati838 – 86831ANK 4Add
    BLAST
    Repeati872 – 90130ANK 5Add
    BLAST
    Repeati905 – 93430ANK 6Add
    BLAST
    Repeati938 – 96730ANK 7Add
    BLAST
    Repeati971 – 100434ANK 8Add
    BLAST
    Domaini1060 – 112364Pre-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1126 – 1243118SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni905 – 9073Histone H3K9me binding
    Regioni1136 – 11383S-adenosyl-L-methionine binding
    Regioni1162 – 118120Interaction with histone H3Add
    BLAST
    Regioni1200 – 12012S-adenosyl-L-methionine binding
    Regioni1242 – 12454Interaction with histone H3

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi406 – 4094Poly-Glu
    Compositional biasi442 – 4498Poly-Arg
    Compositional biasi1292 – 12954Poly-Ala

    Domaini

    The ANK repeats recognize and bind RELA subunit of NF-kappa-B, when RELA is monomethylated at 'Lys-310' By similarity. They also specifically recognize and bind H3K9me1 and H3K9me2.By similarity1 Publication
    The SET domain mediates interaction with WIZ.1 Publication
    In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.1 Publication

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily.PROSITE-ProRule annotation
    Contains 8 ANK repeats.PROSITE-ProRule annotation
    Contains 1 pre-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOVERGENiHBG028394.
    InParanoidiQ9H9B1.
    KOiK11420.
    OMAiSDFGRQQ.
    OrthoDBiEOG744T8D.
    PhylomeDBiQ9H9B1.
    TreeFamiTF106443.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR001214. SET_dom.
    [Graphical view]
    PfamiPF00023. Ank. 1 hit.
    PF12796. Ank_2. 2 hits.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 7 hits.
    SM00468. PreSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 5 hits.
    PS50867. PRE_SET. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: Q9H9B1-1) [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

    MAAADAEAVP ARGEPQQDCC VKTELLGEET PMAADEGSAE KQAGEAHMAA     50
    DGETNGSCEN SDASSHANAA KHTQDSARVN PQDGTNTLTR IAENGVSERD 100
    SEAAKQNHVT ADDFVQTSVI GSNGYILNKP ALQAQPLRTT STLASSLPGH 150
    AAKTLPGGAG KGRTPSAFPQ TPAAPPATLG EGSADTEDRK LPAPGADVKV 200
    HRARKTMPKS VVGLHAASKD PREVREARDH KEPKEEINKN ISDFGRQQLL 250
    PPFPSLHQSL PQNQCYMATT KSQTACLPFV LAAAVSRKKK RRMGTYSLVP 300
    KKKTKVLKQR TVIEMFKSIT HSTVGSKGEK DLGASSLHVN GESLEMDSDE 350
    DDSEELEEDD GHGAEQAAAF PTEDSRTSKE SMSEADRAQK MDGESEEEQE 400
    SVDTGEEEEG GDESDLSSES SIKKKFLKRK GKTDSPWIKP ARKRRRRSRK 450
    KPSGALGSES YKSSAGSAEQ TAPGDSTGYM EVSLDSLDLR VKGILSSQAE 500
    GLANGPDVLE TDGLQEVPLC SCRMETPKSR EITTLANNQC MATESVDHEL 550
    GRCTNSVVKY ELMRPSNKAP LLVLCEDHRG RMVKHQCCPG CGYFCTAGNF 600
    MECQPESSIS HRFHKDCASR VNNASYCPHC GEESSKAKEV TIAKADTTST 650
    VTPVPGQEKG SALEGRADTT TGSAAGPPLS EDDKLQGAAS HVPEGFDPTG 700
    PAGLGRPTPG LSQGPGKETL ESALIALDSE KPKKLRFHPK QLYFSARQGE 750
    LQKVLLMLVD GIDPNFKMEH QNKRSPLHAA AEAGHVDICH MLVQAGANID 800
    TCSEDQRTPL MEAAENNHLE AVKYLIKAGA LVDPKDAEGS TCLHLAAKKG 850
    HYEVVQYLLS NGQMDVNCQD DGGWTPMIWA TEYKHVDLVK LLLSKGSDIN 900
    IRDNEENICL HWAAFSGCVD IAEILLAAKC DLHAVNIHGD SPLHIAAREN 950
    RYDCVVLFLS RDSDVTLKNK EGETPLQCAS LNSQVWSALQ MSKALQDSAP 1000
    DRPSPVERIV SRDIARGYER IPIPCVNAVD SEPCPSNYKY VSQNCVTSPM 1050
    NIDRNITHLQ YCVCIDDCSS SNCMCGQLSM RCWYDKDGRL LPEFNMAEPP 1100
    LIFECNHACS CWRNCRNRVV QNGLRARLQL YRTRDMGWGV RSLQDIPPGT 1150
    FVCEYVGELI SDSEADVREE DSYLFDLDNK DGEVYCIDAR FYGNVSRFIN 1200
    HHCEPNLVPV RVFMAHQDLR FPRIAFFSTR LIEAGEQLGF DYGERFWDIK 1250
    GKLFSCRCGS PKCRHSSAAL AQRQASAAQE AQEDGLPDTS SAAAADPL 1298
    Length:1,298
    Mass (Da):141,466
    Last modified:March 8, 2011 - v4
    Checksum:i071574F3FB3D371E
    GO
    Isoform 2 (identifier: Q9H9B1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         8-66: AVPARGEPQQ...SCENSDASSH → RHLWLPMKAQ...GSTPRMAPTH
         67-1298: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:66
    Mass (Da):7,540
    Checksum:i4882B9806F478473
    GO
    Isoform 3 (identifier: Q9H9B1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1181-1184: DGEV → ISSA
         1185-1298: Missing.

    Show »
    Length:1,184
    Mass (Da):128,689
    Checksum:i1382C5327D3579D7
    GO
    Isoform 4 (identifier: Q9H9B1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         795-808: AGANIDTCSEDQRT → FCRLGSPRSRGCLW
         809-1298: Missing.

    Show »
    Length:808
    Mass (Da):86,704
    Checksum:i2CA1BA8DACAE22A8
    GO

    Sequence cautioni

    The sequence CAD28534.1 differs from that shown. Reason: Intron retention.
    The sequence CAH71077.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI17354.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti555 – 5551N → D in AAH47504. (PubMed:15489334)Curated
    Sequence conflicti561 – 5611E → G in AAM09024. (PubMed:14702039)Curated
    Sequence conflicti561 – 5611E → G in BAB14321. (PubMed:15164053)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti43 – 431A → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036345
    Natural varianti388 – 3881A → T.
    Corresponds to variant rs11137198 [ dbSNP | Ensembl ].
    VAR_027642
    Natural varianti1075 – 10751C → Y in KLESTS. 1 Publication
    VAR_069183
    Natural varianti1173 – 11731Y → F in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036346

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei8 – 6659AVPAR…DASSH → RHLWLPMKAQQRNRQERPTW LRTVRPMGLVKTAMPAVMQM LQSTLRTAQGSTPRMAPTH in isoform 2. 1 PublicationVSP_002222Add
    BLAST
    Alternative sequencei67 – 12981232Missing in isoform 2. 1 PublicationVSP_002223Add
    BLAST
    Alternative sequencei795 – 80814AGANI…EDQRT → FCRLGSPRSRGCLW in isoform 4. 1 PublicationVSP_040717Add
    BLAST
    Alternative sequencei809 – 1298490Missing in isoform 4. 1 PublicationVSP_040718Add
    BLAST
    Alternative sequencei1181 – 11844DGEV → ISSA in isoform 3. 1 PublicationVSP_002224
    Alternative sequencei1185 – 1298114Missing in isoform 3. 1 PublicationVSP_002225Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK022941 mRNA. Translation: BAB14321.1. Sequence problems.
    AL590627, AL611925 Genomic DNA. Translation: CAI17354.1. Sequence problems.
    AL590627, AL611925 Genomic DNA. Translation: CAI17355.1.
    AL611925, AL590627 Genomic DNA. Translation: CAH71076.1.
    AL611925, AL590627 Genomic DNA. Translation: CAH71077.1. Sequence problems.
    BC011608 mRNA. Translation: AAH11608.2.
    BC047504 mRNA. Translation: AAH47504.1.
    AY083210 mRNA. Translation: AAM09024.1.
    AB028932 mRNA. Translation: BAB56104.1.
    AB058779 mRNA. Translation: BAB47505.2.
    AL713772 mRNA. Translation: CAD28534.1. Sequence problems.
    CCDSiCCDS56595.1. [Q9H9B1-4]
    CCDS7050.2. [Q9H9B1-1]
    RefSeqiNP_001138999.1. NM_001145527.1. [Q9H9B1-4]
    NP_079033.4. NM_024757.4. [Q9H9B1-1]
    UniGeneiHs.495511.

    Genome annotation databases

    EnsembliENST00000460843; ENSP00000417980; ENSG00000181090. [Q9H9B1-1]
    ENST00000462484; ENSP00000417328; ENSG00000181090. [Q9H9B1-4]
    ENST00000462942; ENSP00000436107; ENSG00000181090.
    GeneIDi79813.
    KEGGihsa:79813.
    UCSCiuc004coa.3. human. [Q9H9B1-4]
    uc004cob.1. human. [Q9H9B1-2]
    uc011mfc.2. human. [Q9H9B1-1]

    Polymorphism databases

    DMDMi325511404.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK022941 mRNA. Translation: BAB14321.1 . Sequence problems.
    AL590627 , AL611925 Genomic DNA. Translation: CAI17354.1 . Sequence problems.
    AL590627 , AL611925 Genomic DNA. Translation: CAI17355.1 .
    AL611925 , AL590627 Genomic DNA. Translation: CAH71076.1 .
    AL611925 , AL590627 Genomic DNA. Translation: CAH71077.1 . Sequence problems.
    BC011608 mRNA. Translation: AAH11608.2 .
    BC047504 mRNA. Translation: AAH47504.1 .
    AY083210 mRNA. Translation: AAM09024.1 .
    AB028932 mRNA. Translation: BAB56104.1 .
    AB058779 mRNA. Translation: BAB47505.2 .
    AL713772 mRNA. Translation: CAD28534.1 . Sequence problems.
    CCDSi CCDS56595.1. [Q9H9B1-4 ]
    CCDS7050.2. [Q9H9B1-1 ]
    RefSeqi NP_001138999.1. NM_001145527.1. [Q9H9B1-4 ]
    NP_079033.4. NM_024757.4. [Q9H9B1-1 ]
    UniGenei Hs.495511.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IGQ X-ray 2.00 A/B 982-1266 [» ]
    2RFI X-ray 1.59 A/B 982-1266 [» ]
    3B7B X-ray 2.99 A/B 765-999 [» ]
    3B95 X-ray 2.99 A/B 765-999 [» ]
    3FPD X-ray 2.40 A/B 1006-1266 [» ]
    3HNA X-ray 1.50 A/B 982-1266 [» ]
    3MO0 X-ray 2.78 A/B 982-1266 [» ]
    3MO2 X-ray 2.49 A/B/C/D 982-1266 [» ]
    3MO5 X-ray 2.14 A/B/C/D 982-1266 [» ]
    3SW9 X-ray 3.05 A/B 982-1266 [» ]
    3SWC X-ray 2.33 A/B 982-1266 [» ]
    4I51 X-ray 1.90 A/B 982-1266 [» ]
    ProteinModelPortali Q9H9B1.
    SMRi Q9H9B1. Positions 695-1266.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122908. 29 interactions.
    DIPi DIP-34585N.
    IntActi Q9H9B1. 13 interactions.
    MINTi MINT-7945009.
    STRINGi 9606.ENSP00000417980.

    Chemistry

    BindingDBi Q9H9B1.
    ChEMBLi CHEMBL6031.
    GuidetoPHARMACOLOGYi 2651.

    PTM databases

    PhosphoSitei Q9H9B1.

    Polymorphism databases

    DMDMi 325511404.

    Proteomic databases

    MaxQBi Q9H9B1.
    PaxDbi Q9H9B1.
    PRIDEi Q9H9B1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000460843 ; ENSP00000417980 ; ENSG00000181090 . [Q9H9B1-1 ]
    ENST00000462484 ; ENSP00000417328 ; ENSG00000181090 . [Q9H9B1-4 ]
    ENST00000462942 ; ENSP00000436107 ; ENSG00000181090 .
    GeneIDi 79813.
    KEGGi hsa:79813.
    UCSCi uc004coa.3. human. [Q9H9B1-4 ]
    uc004cob.1. human. [Q9H9B1-2 ]
    uc011mfc.2. human. [Q9H9B1-1 ]

    Organism-specific databases

    CTDi 79813.
    GeneCardsi GC09P140513.
    GeneReviewsi EHMT1.
    HGNCi HGNC:24650. EHMT1.
    HPAi HPA053043.
    MIMi 607001. gene.
    610253. phenotype.
    neXtProti NX_Q9H9B1.
    Orphaneti 96147. Kleefstra syndrome due to 9q34 microdeletion.
    261652. Kleefstra syndrome due to a point mutation.
    PharmGKBi PA134941393.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOVERGENi HBG028394.
    InParanoidi Q9H9B1.
    KOi K11420.
    OMAi SDFGRQQ.
    OrthoDBi EOG744T8D.
    PhylomeDBi Q9H9B1.
    TreeFami TF106443.

    Enzyme and pathway databases

    Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).

    Miscellaneous databases

    ChiTaRSi EHMT1. human.
    EvolutionaryTracei Q9H9B1.
    GeneWikii EHMT1.
    GenomeRNAii 79813.
    NextBioi 69410.
    PROi Q9H9B1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H9B1.
    Bgeei Q9H9B1.
    CleanExi HS_EHMT1.
    Genevestigatori Q9H9B1.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR001214. SET_dom.
    [Graphical view ]
    Pfami PF00023. Ank. 1 hit.
    PF12796. Ank_2. 2 hits.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 7 hits.
    SM00468. PreSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 5 hits.
    PS50867. PRE_SET. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Teratocarcinoma.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 583-1298 (ISOFORM 1).
      Tissue: Brain and Testis.
    4. "A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells."
      Ogawa H., Ishiguro K., Gaubatz S., Livingston D.M., Nakatani Y.
      Science 296:1132-1136(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-1298 (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; BAT8; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
      Tissue: Cervix carcinoma.
    5. Tsuritani K., Ukai Y., Yajima Y., Amemiya C., Yoshimoto M.
      Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 382-1298 (ISOFORM 1).
      Tissue: Brain.
    6. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
      DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 382-1298 (ISOFORM 3), TISSUE SPECIFICITY.
      Tissue: Brain.
    7. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1089-1298 (ISOFORM 1).
      Tissue: Lymph node.
    9. "Loss-of-function mutations in euchromatin histone methyl transferase 1 (EHMT1) cause the 9q34 subtelomeric deletion syndrome."
      Kleefstra T., Brunner H.G., Amiel J., Oudakker A.R., Nillesen W.M., Magee A., Genevieve D., Cormier-Daire V., van Esch H., Fryns J.-P., Hamel B.C.J., Sistermans E.A., de Vries B.B.A., van Bokhoven H.
      Am. J. Hum. Genet. 79:370-377(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN KLESTS.
    10. "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP."
      Ueda J., Tachibana M., Ikura T., Shinkai Y.
      J. Biol. Chem. 281:20120-20128(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WIZ AND EHMT2.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    12. "CDYL bridges REST and histone methyltransferases for gene repression and suppression of cellular transformation."
      Mulligan P., Westbrook T.F., Ottinger M., Pavlova N., Chang B., Macia E., Shi Y.J., Barretina J., Liu J., Howley P.M., Elledge S.J., Shi Y.
      Mol. Cell 32:718-726(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CDYL AND REST, IDENTIFICATION IN A COMPLEX WITH REST; CDYL; SETB1; EHMT2 AND WIZ.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Methyl-H3K9-binding protein MPP8 mediates E-cadherin gene silencing and promotes tumour cell motility and invasion."
      Kokura K., Sun L., Bedford M.T., Fang J.
      EMBO J. 29:3673-3687(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MPHOSPH8.
    15. Cited for: FUNCTION, INTERACTION WITH TP53.
    16. Erratum
      Huang J., Dorsey J., Chuikov S., Perez-Burgos L., Zhang X., Jenuwein T., Reinberg D., Berger S.L.
      J. Biol. Chem. 285:18122-18122(2010)
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "The ankyrin repeats of G9a and GLP histone methyltransferases are mono-and dimethyllysine binding modules."
      Collins R.E., Northrop J.P., Horton J.R., Lee D.Y., Zhang X., Stallcup M.R., Cheng X.
      Nat. Struct. Mol. Biol. 15:245-250(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS) OF 765-999 IN COMPLEX WITH HISTONE H3, DOMAIN ANK REPEATS, MUTAGENESIS OF GLU-905.
    20. "Adding a lysine mimic in the design of potent inhibitors of histone lysine methyltransferases."
      Chang Y., Ganesh T., Horton J.R., Spannhoff A., Liu J., Sun A., Zhang X., Bedford M.T., Shinkai Y., Snyder J.P., Cheng X.
      J. Mol. Biol. 400:1-7(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 982-1266 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE; ZINC ION AND E72 INHIBITOR, ENZYME REGULATION.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 982-1266 IN COMPLEX WITH HISTONE H3; S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS.
    22. Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-43 AND PHE-1173.
    23. Cited for: VARIANT KLESTS TYR-1075.

    Entry informationi

    Entry nameiEHMT1_HUMAN
    AccessioniPrimary (citable) accession number: Q9H9B1
    Secondary accession number(s): B1AQ58
    , B1AQ59, Q86X08, Q8TCN7, Q96F53, Q96JF1, Q96KH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: March 8, 2011
    Last modified: October 1, 2014
    This is version 149 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3