Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q96KQ7

- EHMT2_HUMAN

UniProt

Q96KQ7 - EHMT2_HUMAN

Protein

Histone-lysine N-methyltransferase EHMT2

Gene

EHMT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 mediates monomethylation of 'Lys-56' of histone H3 (H3K56me1) in G1 phase, leading to promote interaction between histone H3 and PCNA and regulating DNA replication. 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. May also methylate histone H1. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Also methylates CDYL, WIZ, ACIN1, DNMT1, HDAC1, ERCC6, KLF12 and itself.6 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi974 – 9741Zinc 1
    Metal bindingi974 – 9741Zinc 2
    Metal bindingi976 – 9761Zinc 1
    Metal bindingi980 – 9801Zinc 1
    Metal bindingi980 – 9801Zinc 3
    Metal bindingi985 – 9851Zinc 1
    Metal bindingi987 – 9871Zinc 2
    Metal bindingi1017 – 10171Zinc 2
    Metal bindingi1017 – 10171Zinc 3
    Metal bindingi1021 – 10211Zinc 2
    Metal bindingi1023 – 10231Zinc 3
    Metal bindingi1027 – 10271Zinc 3
    Binding sitei1067 – 10671Histone H3K9meBy similarity
    Binding sitei1085 – 10851S-adenosyl-L-methionine
    Metal bindingi1115 – 11151Zinc 4
    Metal bindingi1168 – 11681Zinc 4
    Binding sitei1169 – 11691S-adenosyl-L-methionine; via amide nitrogen
    Metal bindingi1170 – 11701Zinc 4
    Metal bindingi1175 – 11751Zinc 4

    GO - Molecular functioni

    1. C2H2 zinc finger domain binding Source: UniProt
    2. histone-lysine N-methyltransferase activity Source: UniProtKB
    3. histone methyltransferase activity (H3-K27 specific) Source: UniProtKB
    4. histone methyltransferase activity (H3-K9 specific) 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. DNA methylation Source: UniProtKB
    2. DNA methylation on cytosine within a CG sequence Source: Ensembl
    3. fertilization Source: Ensembl
    4. histone methylation Source: UniProtKB
    5. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. organ growth Source: Ensembl
    7. peptidyl-lysine dimethylation Source: UniProtKB
    8. regulation of DNA replication Source: UniProtKB
    9. spermatid development Source: Ensembl
    10. synaptonemal complex assembly Source: Ensembl

    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).
    REACT_953. RNA Polymerase I Transcription Initiation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase EHMT2 (EC:2.1.1.-, EC:2.1.1.43)
    Alternative name(s):
    Euchromatic histone-lysine N-methyltransferase 2
    HLA-B-associated transcript 8
    Histone H3-K9 methyltransferase 3
    Short name:
    H3-K9-HMTase 3
    Lysine N-methyltransferase 1C
    Protein G9a
    Gene namesi
    Name:EHMT2
    Synonyms:BAT8, C6orf30, G9A, KMT1C, NG36
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:14129. EHMT2.

    Subcellular locationi

    Nucleus 1 Publication. Chromosome 1 Publication
    Note: Associates with euchromatic regions. Does not associate with heterochromatin.

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi786 – 7861W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication
    Mutagenesisi791 – 7911W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication
    Mutagenesisi794 – 7941E → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication
    Mutagenesisi817 – 8171E → R: Impairs binding to histone H3K9me. 1 Publication
    Mutagenesisi824 – 8241W → A: Abolishes binding to histone H3K9me without affecting the histone methyltransferase activity. 1 Publication
    Mutagenesisi852 – 8521D → R: Impairs binding to histone H3K9me. 1 Publication

    Organism-specific databases

    PharmGKBiPA25267.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 12101209Histone-lysine N-methyltransferase EHMT2PRO_0000186068Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei140 – 1401Phosphoserine3 Publications
    Modified residuei173 – 1731Phosphoserine1 Publication
    Modified residuei185 – 1851N6,N6,N6-trimethyllysine; by EHMT2; alternate1 Publication
    Modified residuei185 – 1851N6,N6-dimethyllysine; by EHMT2; alternate1 Publication
    Modified residuei232 – 2321Phosphoserine3 Publications
    Modified residuei246 – 2461Phosphoserine4 Publications
    Modified residuei413 – 4131Phosphoserine1 Publication
    Modified residuei569 – 5691Phosphoserine1 Publication
    Modified residuei1204 – 12041Phosphoserine1 Publication
    Modified residuei1210 – 12101Phosphothreonine1 Publication

    Post-translational modificationi

    Methylated at Lys-185; automethylated.1 Publication

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ96KQ7.
    PaxDbiQ96KQ7.
    PRIDEiQ96KQ7.

    Expressioni

    Tissue specificityi

    Expressed in all tissues examined, with high levels in fetal liver, thymus, lymph node, spleen and peripheral blood leukocytes and lower level in bone marrow.1 Publication

    Gene expression databases

    ArrayExpressiQ96KQ7.
    BgeeiQ96KQ7.
    CleanExiHS_EHMT2.
    GenevestigatoriQ96KQ7.

    Organism-specific databases

    HPAiHPA050550.

    Interactioni

    Subunit structurei

    Heterodimer; heterodimerizes with EHMT1/GLP. Interacts with GFI1B and WIZ. 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. Part of a complex composed of TRIM28, HDAC1, HDAC2 and EHMT2. Interacts with UHRF1. 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
    GFI1Q996842EBI-744366,EBI-949368
    Gfi1Q071203EBI-744366,EBI-4289236From a different organism.
    HDAC1Q135473EBI-744366,EBI-301834
    KAT2BQ928313EBI-744366,EBI-477430
    PRDM5Q9NQX13EBI-744366,EBI-4292031
    PRRC2BQ5JSZ52EBI-744366,EBI-744891
    REREQ9P2R63EBI-744366,EBI-948076

    Protein-protein interaction databases

    BioGridi116123. 81 interactions.
    DIPiDIP-34461N.
    IntActiQ96KQ7. 38 interactions.
    MINTiMINT-1441977.
    STRINGi9606.ENSP00000397323.

    Structurei

    Secondary structure

    1
    1210
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi920 – 9245
    Turni926 – 9294
    Beta strandi931 – 9333
    Beta strandi937 – 9437
    Beta strandi949 – 9524
    Beta strandi957 – 9604
    Helixi968 – 9703
    Beta strandi977 – 9804
    Helixi986 – 9905
    Beta strandi1008 – 10103
    Beta strandi1021 – 10233
    Beta strandi1027 – 10293
    Helixi1032 – 10343
    Beta strandi1040 – 10445
    Beta strandi1046 – 105611
    Beta strandi1063 – 10675
    Beta strandi1069 – 10735
    Helixi1074 – 10774
    Beta strandi1086 – 10894
    Beta strandi1097 – 11059
    Helixi1107 – 11104
    Beta strandi1118 – 112710
    Beta strandi1135 – 11428
    Helixi1156 – 11627
    Turni1163 – 11653
    Beta strandi1176 – 11783
    Helixi1179 – 118810

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2O8JX-ray1.80A/B/C/D913-1193[»]
    3DM1X-ray2.40B/D/F/H179-190[»]
    3K5KX-ray1.70A/B913-1193[»]
    3RJWX-ray2.56A/B913-1193[»]
    4NVQX-ray2.03A/B913-1193[»]
    ProteinModelPortaliQ96KQ7.
    SMRiQ96KQ7. Positions 632-908, 922-1192.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96KQ7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati649 – 67830ANK 1Add
    BLAST
    Repeati684 – 71330ANK 2Add
    BLAST
    Repeati717 – 74630ANK 3Add
    BLAST
    Repeati750 – 78031ANK 4Add
    BLAST
    Repeati784 – 81330ANK 5Add
    BLAST
    Repeati817 – 84630ANK 6Add
    BLAST
    Repeati850 – 87930ANK 7Add
    BLAST
    Domaini972 – 103564Pre-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1038 – 1155118SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini1164 – 118017Post-SETAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni817 – 8193Histone H3K9me bindingBy similarity
    Regioni1048 – 10503S-adenosyl-L-methionine binding
    Regioni1074 – 109320Interaction with histone H3By similarityAdd
    BLAST
    Regioni1112 – 11132S-adenosyl-L-methionine binding
    Regioni1154 – 11574Interaction with histone H3By similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2 – 1312Poly-AlaAdd
    BLAST
    Compositional biasi160 – 1634Poly-Ala
    Compositional biasi300 – 32627Poly-GluAdd
    BLAST

    Domaini

    The SET domain mediates interaction with WIZ.1 Publication
    The ANK repeats bind H3K9me1 and H3K9me2.1 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. Histone-lysine methyltransferase family. Suvar3-9 subfamily.PROSITE-ProRule annotation
    Contains 7 ANK repeats.PROSITE-ProRule annotation
    Contains 1 post-SET domain.Curated
    Contains 1 pre-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOVERGENiHBG028394.
    KOiK11420.
    PhylomeDBiQ96KQ7.
    TreeFamiTF106443.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR001214. SET_dom.
    [Graphical view]
    PfamiPF00023. Ank. 6 hits.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 6 hits.
    SM00508. PostSET. 1 hit.
    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 (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q96KQ7-1) [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

    MAAAAGAAAA AAAEGEAPAE MGALLLEKET RGATERVHGS LGDTPRSEET     50
    LPKATPDSLE PAGPSSPASV TVTVGDEGAD TPVGATPLIG DESENLEGDG 100
    DLRGGRILLG HATKSFPSSP SKGGSCPSRA KMSMTGAGKS PPSVQSLAMR 150
    LLSMPGAQGA AAAGSEPPPA TTSPEGQPKV HRARKTMSKP GNGQPPVPEK 200
    RPPEIQHFRM SDDVHSLGKV TSDLAKRRKL NSGGGLSEEL GSARRSGEVT 250
    LTKGDPGSLE EWETVVGDDF SLYYDSYSVD ERVDSDSKSE VEALTEQLSE 300
    EEEEEEEEEE EEEEEEEEEE EEEDEESGNQ SDRSGSSGRR KAKKKWRKDS 350
    PWVKPSRKRR KREPPRAKEP RGVNGVGSSG PSEYMEVPLG SLELPSEGTL 400
    SPNHAGVSND TSSLETERGF EELPLCSCRM EAPKIDRISE RAGHKCMATE 450
    SVDGELSGCN AAILKRETMR PSSRVALMVL CETHRARMVK HHCCPGCGYF 500
    CTAGTFLECH PDFRVAHRFH KACVSQLNGM VFCPHCGEDA SEAQEVTIPR 550
    GDGVTPPAGT AAPAPPPLSQ DVPGRADTSQ PSARMRGHGE PRRPPCDPLA 600
    DTIDSSGPSL TLPNGGCLSA VGLPLGPGRE ALEKALVIQE SERRKKLRFH 650
    PRQLYLSVKQ GELQKVILML LDNLDPNFQS DQQSKRTPLH AAAQKGSVEI 700
    CHVLLQAGAN INAVDKQQRT PLMEAVVNNH LEVARYMVQR GGCVYSKEED 750
    GSTCLHHAAK IGNLEMVSLL LSTGQVDVNA QDSGGWTPII WAAEHKHIEV 800
    IRMLLTRGAD VTLTDNEENI CLHWASFTGS AAIAEVLLNA RCDLHAVNYH 850
    GDTPLHIAAR ESYHDCVLLF LSRGANPELR NKEGDTAWDL TPERSDVWFA 900
    LQLNRKLRLG VGNRAIRTEK IICRDVARGY ENVPIPCVNG VDGEPCPEDY 950
    KYISENCETS TMNIDRNITH LQHCTCVDDC SSSNCLCGQL SIRCWYDKDG 1000
    RLLQEFNKIE PPLIFECNQA CSCWRNCKNR VVQSGIKVRL QLYRTAKMGW 1050
    GVRALQTIPQ GTFICEYVGE LISDAEADVR EDDSYLFDLD NKDGEVYCID 1100
    ARYYGNISRF INHLCDPNII PVRVFMLHQD LRFPRIAFFS SRDIRTGEEL 1150
    GFDYGDRFWD IKSKYFTCQC GSEKCKHSAE AIALEQSRLA RLDPHPELLP 1200
    ELGSLPPVNT 1210
    Length:1,210
    Mass (Da):132,370
    Last modified:October 17, 2006 - v3
    Checksum:iA6C5DC6B72801520
    GO
    Isoform 2 (identifier: Q96KQ7-2) [UniParc]FASTAAdd to Basket

    Also known as: NG36G9a-SPI

    The sequence of this isoform differs from the canonical sequence as follows:
         373-406: Missing.

    Show »
    Length:1,176
    Mass (Da):129,019
    Checksum:i887FC5E322B772B9
    GO
    Isoform 3 (identifier: Q96KQ7-3) [UniParc]FASTAAdd to Basket

    Also known as: NG36

    The sequence of this isoform differs from the canonical sequence as follows:
         195-202: PPVPEKRP → VSGMGEMG
         203-1210: Missing.

    Show »
    Length:202
    Mass (Da):19,864
    Checksum:i339618C3DA895788
    GO

    Sequence cautioni

    The sequence AAH02686.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH09351.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence AAH18718.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH20970.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence CAA49491.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAD21811.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence AAD21812.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence BAB63294.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence BAB63295.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti178 – 1781P → S in CAC86666. (PubMed:14702039)Curated
    Sequence conflicti985 – 9851C → R in CAC86666. (PubMed:14702039)Curated
    Sequence conflicti994 – 9941C → R in CAA49491. (PubMed:8457211)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti55 – 551T → N.4 Publications
    Corresponds to variant rs7887 [ dbSNP | Ensembl ].
    VAR_027973
    Natural varianti1165 – 11651Y → F.
    Corresponds to variant rs13919 [ dbSNP | Ensembl ].
    VAR_027974

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei195 – 2028PPVPEKRP → VSGMGEMG in isoform 3. 1 PublicationVSP_002212
    Alternative sequencei203 – 12101008Missing in isoform 3. 1 PublicationVSP_002213Add
    BLAST
    Alternative sequencei373 – 40634Missing in isoform 2. CuratedVSP_002211Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ315532 mRNA. Translation: CAC86666.1.
    AK056936 mRNA. Translation: BAB71314.1.
    AF134726 Genomic DNA. Translation: AAD21811.1. Sequence problems.
    AF134726 Genomic DNA. Translation: AAD21812.1. Sequence problems.
    BA000025 Genomic DNA. Translation: BAB63294.1. Sequence problems.
    BA000025 Genomic DNA. Translation: BAB63295.1. Sequence problems.
    AL662834 Genomic DNA. Translation: CAI17747.2.
    AL662834 Genomic DNA. Translation: CAI17748.1.
    AL671762 Genomic DNA. Translation: CAI18224.2.
    AL671762 Genomic DNA. Translation: CAI18226.2.
    AL844853 Genomic DNA. Translation: CAI41852.1.
    AL844853 Genomic DNA. Translation: CAI41853.1.
    CR388219, CR388202 Genomic DNA. Translation: CAQ07473.1.
    CR388219, CR388202 Genomic DNA. Translation: CAQ07474.1.
    CR936237 Genomic DNA. Translation: CAQ09159.1.
    CR759784 Genomic DNA. Translation: CAQ09311.1.
    CR388202, CR388219 Genomic DNA. Translation: CAQ09508.1.
    CR388202, CR388219 Genomic DNA. Translation: CAQ09509.1.
    CH471081 Genomic DNA. Translation: EAX03542.1.
    BC002686 mRNA. Translation: AAH02686.2. Different initiation.
    BC009351 mRNA. Translation: AAH09351.1. Different initiation.
    BC018718 mRNA. Translation: AAH18718.1. Different initiation.
    BC020970 mRNA. Translation: AAH20970.2. Different initiation.
    X69838 mRNA. Translation: CAA49491.1. Different initiation.
    CCDSiCCDS4725.1. [Q96KQ7-1]
    CCDS4726.1. [Q96KQ7-2]
    RefSeqiNP_001276342.1. NM_001289413.1.
    NP_006700.3. NM_006709.4. [Q96KQ7-1]
    NP_079532.5. NM_025256.6. [Q96KQ7-2]
    UniGeneiHs.709218.

    Genome annotation databases

    EnsembliENST00000375530; ENSP00000364680; ENSG00000204371. [Q96KQ7-2]
    ENST00000375537; ENSP00000364687; ENSG00000204371. [Q96KQ7-1]
    ENST00000383372; ENSP00000372863; ENSG00000206376. [Q96KQ7-2]
    ENST00000383373; ENSP00000372864; ENSG00000206376. [Q96KQ7-1]
    ENST00000420336; ENSP00000396119; ENSG00000238134.
    ENST00000420874; ENSP00000411035; ENSG00000236759. [Q96KQ7-2]
    ENST00000421926; ENSP00000416957; ENSG00000232045.
    ENST00000429506; ENSP00000406110; ENSG00000227333. [Q96KQ7-1]
    ENST00000450075; ENSP00000392305; ENSG00000236759. [Q96KQ7-1]
    ENST00000450229; ENSP00000400838; ENSG00000227333. [Q96KQ7-2]
    GeneIDi10919.
    KEGGihsa:10919.
    UCSCiuc003nxz.1. human. [Q96KQ7-1]
    uc003nya.1. human. [Q96KQ7-2]
    uc003nyb.1. human. [Q96KQ7-3]

    Polymorphism databases

    DMDMi116241348.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ315532 mRNA. Translation: CAC86666.1 .
    AK056936 mRNA. Translation: BAB71314.1 .
    AF134726 Genomic DNA. Translation: AAD21811.1 . Sequence problems.
    AF134726 Genomic DNA. Translation: AAD21812.1 . Sequence problems.
    BA000025 Genomic DNA. Translation: BAB63294.1 . Sequence problems.
    BA000025 Genomic DNA. Translation: BAB63295.1 . Sequence problems.
    AL662834 Genomic DNA. Translation: CAI17747.2 .
    AL662834 Genomic DNA. Translation: CAI17748.1 .
    AL671762 Genomic DNA. Translation: CAI18224.2 .
    AL671762 Genomic DNA. Translation: CAI18226.2 .
    AL844853 Genomic DNA. Translation: CAI41852.1 .
    AL844853 Genomic DNA. Translation: CAI41853.1 .
    CR388219 , CR388202 Genomic DNA. Translation: CAQ07473.1 .
    CR388219 , CR388202 Genomic DNA. Translation: CAQ07474.1 .
    CR936237 Genomic DNA. Translation: CAQ09159.1 .
    CR759784 Genomic DNA. Translation: CAQ09311.1 .
    CR388202 , CR388219 Genomic DNA. Translation: CAQ09508.1 .
    CR388202 , CR388219 Genomic DNA. Translation: CAQ09509.1 .
    CH471081 Genomic DNA. Translation: EAX03542.1 .
    BC002686 mRNA. Translation: AAH02686.2 . Different initiation.
    BC009351 mRNA. Translation: AAH09351.1 . Different initiation.
    BC018718 mRNA. Translation: AAH18718.1 . Different initiation.
    BC020970 mRNA. Translation: AAH20970.2 . Different initiation.
    X69838 mRNA. Translation: CAA49491.1 . Different initiation.
    CCDSi CCDS4725.1. [Q96KQ7-1 ]
    CCDS4726.1. [Q96KQ7-2 ]
    RefSeqi NP_001276342.1. NM_001289413.1.
    NP_006700.3. NM_006709.4. [Q96KQ7-1 ]
    NP_079532.5. NM_025256.6. [Q96KQ7-2 ]
    UniGenei Hs.709218.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2O8J X-ray 1.80 A/B/C/D 913-1193 [» ]
    3DM1 X-ray 2.40 B/D/F/H 179-190 [» ]
    3K5K X-ray 1.70 A/B 913-1193 [» ]
    3RJW X-ray 2.56 A/B 913-1193 [» ]
    4NVQ X-ray 2.03 A/B 913-1193 [» ]
    ProteinModelPortali Q96KQ7.
    SMRi Q96KQ7. Positions 632-908, 922-1192.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116123. 81 interactions.
    DIPi DIP-34461N.
    IntActi Q96KQ7. 38 interactions.
    MINTi MINT-1441977.
    STRINGi 9606.ENSP00000397323.

    Chemistry

    BindingDBi Q96KQ7.
    ChEMBLi CHEMBL6032.
    GuidetoPHARMACOLOGYi 2652.

    Polymorphism databases

    DMDMi 116241348.

    Proteomic databases

    MaxQBi Q96KQ7.
    PaxDbi Q96KQ7.
    PRIDEi Q96KQ7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000375530 ; ENSP00000364680 ; ENSG00000204371 . [Q96KQ7-2 ]
    ENST00000375537 ; ENSP00000364687 ; ENSG00000204371 . [Q96KQ7-1 ]
    ENST00000383372 ; ENSP00000372863 ; ENSG00000206376 . [Q96KQ7-2 ]
    ENST00000383373 ; ENSP00000372864 ; ENSG00000206376 . [Q96KQ7-1 ]
    ENST00000420336 ; ENSP00000396119 ; ENSG00000238134 .
    ENST00000420874 ; ENSP00000411035 ; ENSG00000236759 . [Q96KQ7-2 ]
    ENST00000421926 ; ENSP00000416957 ; ENSG00000232045 .
    ENST00000429506 ; ENSP00000406110 ; ENSG00000227333 . [Q96KQ7-1 ]
    ENST00000450075 ; ENSP00000392305 ; ENSG00000236759 . [Q96KQ7-1 ]
    ENST00000450229 ; ENSP00000400838 ; ENSG00000227333 . [Q96KQ7-2 ]
    GeneIDi 10919.
    KEGGi hsa:10919.
    UCSCi uc003nxz.1. human. [Q96KQ7-1 ]
    uc003nya.1. human. [Q96KQ7-2 ]
    uc003nyb.1. human. [Q96KQ7-3 ]

    Organism-specific databases

    CTDi 10919.
    GeneCardsi GC06M031847.
    GC06Mi31858.
    GC06Mj31835.
    GC06Mk31829.
    GC06Mm31924.
    GC06Mn31837.
    H-InvDB HIX0166078.
    HIX0166345.
    HIX0167369.
    HIX0184162.
    HGNCi HGNC:14129. EHMT2.
    HPAi HPA050550.
    MIMi 604599. gene.
    neXtProti NX_Q96KQ7.
    PharmGKBi PA25267.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOVERGENi HBG028394.
    KOi K11420.
    PhylomeDBi Q96KQ7.
    TreeFami TF106443.

    Enzyme and pathway databases

    Reactomei REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_953. RNA Polymerase I Transcription Initiation.

    Miscellaneous databases

    ChiTaRSi EHMT2. human.
    EvolutionaryTracei Q96KQ7.
    GeneWikii EHMT2.
    GenomeRNAii 10919.
    NextBioi 41475.
    PROi Q96KQ7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96KQ7.
    Bgeei Q96KQ7.
    CleanExi HS_EHMT2.
    Genevestigatori Q96KQ7.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR003616. Post-SET_dom.
    IPR007728. Pre-SET_dom.
    IPR003606. Pre-SET_Zn-bd_sub.
    IPR001214. SET_dom.
    [Graphical view ]
    Pfami PF00023. Ank. 6 hits.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 6 hits.
    SM00508. PostSET. 1 hit.
    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. "Novel NG36/G9a gene products encoded within the human and mouse MHC class III regions."
      Brown S.E., Campbell R.D., Sanderson C.M.
      Mamm. Genome 12:916-924(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2), TISSUE SPECIFICITY, VARIANT ASN-55.
    2. "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 3).
      Tissue: Salivary gland.
    3. "Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
      Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
      Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."
      Hirakawa M., Yamaguchi H., Imai K., Shimada J., Shiina S., Tamiya G., Oka A., Inoko H.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-55.
    6. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-55.
    7. "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] OF 6-1210 (ISOFORM 1), VARIANT ASN-55.
      Tissue: Muscle and Uterus.
    8. "The G9a gene in the human major histocompatibility complex encodes a novel protein containing ankyrin-like repeats."
      Milner C.M., Campbell R.D.
      Biochem. J. 290:811-818(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 195-1210, FUNCTION.
      Tissue: Histiocytic lymphoma.
    9. "Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3."
      Tachibana M., Sugimoto K., Fukushima T., Shinkai Y.
      J. Biol. Chem. 276:25309-25317(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION.
    10. "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: IDENTIFICATION IN COMPLEX WITH E2F6; TFDP1; MAX; MGA; EHMT1; CBX3; RING1; RNF2; MBLR; L3MBTL2 AND YAF2.
    11. "Gfi1b alters histone methylation at target gene promoters and sites of gamma-satellite containing heterochromatin."
      Vassen L., Fiolka K., Moeroey T.
      EMBO J. 25:2409-2419(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GFI1B.
    12. "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 EHMT1.
    13. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    15. "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; EHMT1 AND WIZ.
    16. Cited for: FUNCTION, METHYLATION AT LYS-185, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "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: DOMAIN ANK REPEATS, MUTAGENESIS OF TRP-786; TRP-791; GLU-794; GLU-817; TRP-824 AND ASP-852.
    18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-173; SER-232; SER-246 AND THR-1210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    20. "UHRF1 binds G9a and participates in p21 transcriptional regulation in mammalian cells."
      Kim J.K., Esteve P.O., Jacobsen S.E., Pradhan S.
      Nucleic Acids Res. 37:493-505(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UHRF1.
    21. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. Cited for: FUNCTION, INTERACTION WITH TP53.
    23. 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)
    24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-232 AND SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "Maintenance of silent chromatin through replication requires SWI/SNF-like chromatin remodeler SMARCAD1."
      Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., Mermoud J.E.
      Mol. Cell 42:285-296(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMARCAD1.
    26. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140; SER-232; SER-246; SER-413 AND SER-1204, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Histone H3 lysine 56 methylation regulates DNA replication through its interaction with PCNA."
      Yu Y., Song C., Zhang Q., Dimaggio P.A., Garcia B.A., York A., Carey M.F., Grunstein M.
      Mol. Cell 46:7-17(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    28. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 913-1193 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiEHMT2_HUMAN
    AccessioniPrimary (citable) accession number: Q96KQ7
    Secondary accession number(s): B0UZY2
    , Q14349, Q5JP83, Q5JQ92, Q5JQA1, Q5JQG3, Q6PK06, Q96MH5, Q96QD0, Q9UQL8, Q9Y331
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 15, 2002
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 150 of the entry and version 3 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

    Caution

    While NG36 and G9a were originally thought to derive from 2 separate genes, all G9A transcripts also contain the in frame coding sequence of NG36.1 Publication
    It is uncertain whether Met-1 or Met-21 is the initiator methionine.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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