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Q9H9B1

- EHMT1_HUMAN

UniProt

Q9H9B1 - EHMT1_HUMAN

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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

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-lysine N-methyltransferase activity Source: UniProtKB
  7. 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
Complete GO annotation...

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-KW
  2. cytoplasm Source: HPA
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. plasma membrane Source: HPA
Complete GO annotation...

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

BgeeiQ9H9B1.
CleanExiHS_EHMT1.
ExpressionAtlasiQ9H9B1. baseline and differential.
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. 34 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 – 7838Combined sources
Helixi786 – 7949Combined sources
Helixi809 – 8157Combined sources
Helixi819 – 8268Combined sources
Turni827 – 8293Combined sources
Helixi842 – 8487Combined sources
Helixi852 – 8598Combined sources
Turni860 – 8623Combined sources
Helixi876 – 8827Combined sources
Helixi886 – 8949Combined sources
Helixi909 – 9168Combined sources
Helixi919 – 9268Combined sources
Turni927 – 9293Combined sources
Helixi942 – 9487Combined sources
Helixi952 – 9598Combined sources
Turni960 – 9623Combined sources
Helixi975 – 9784Combined sources
Helixi983 – 99412Combined sources
Beta strandi1008 – 10125Combined sources
Turni1014 – 10174Combined sources
Beta strandi1019 – 10213Combined sources
Beta strandi1025 – 10317Combined sources
Beta strandi1037 – 10404Combined sources
Beta strandi1045 – 10484Combined sources
Helixi1056 – 10583Combined sources
Beta strandi1065 – 10684Combined sources
Helixi1074 – 10785Combined sources
Beta strandi1096 – 10983Combined sources
Beta strandi1109 – 11113Combined sources
Beta strandi1115 – 11173Combined sources
Helixi1120 – 11223Combined sources
Beta strandi1128 – 11325Combined sources
Beta strandi1134 – 114411Combined sources
Beta strandi1151 – 11555Combined sources
Beta strandi1157 – 11615Combined sources
Helixi1162 – 11665Combined sources
Beta strandi1174 – 11774Combined sources
Beta strandi1180 – 11834Combined sources
Beta strandi1185 – 11939Combined sources
Helixi1195 – 11984Combined sources
Beta strandi1206 – 121510Combined sources
Beta strandi1223 – 12308Combined sources
Helixi1244 – 12507Combined sources
Turni1251 – 12533Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118855.
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

        10         20         30         40         50
MAAADAEAVP ARGEPQQDCC VKTELLGEET PMAADEGSAE KQAGEAHMAA
60 70 80 90 100
DGETNGSCEN SDASSHANAA KHTQDSARVN PQDGTNTLTR IAENGVSERD
110 120 130 140 150
SEAAKQNHVT ADDFVQTSVI GSNGYILNKP ALQAQPLRTT STLASSLPGH
160 170 180 190 200
AAKTLPGGAG KGRTPSAFPQ TPAAPPATLG EGSADTEDRK LPAPGADVKV
210 220 230 240 250
HRARKTMPKS VVGLHAASKD PREVREARDH KEPKEEINKN ISDFGRQQLL
260 270 280 290 300
PPFPSLHQSL PQNQCYMATT KSQTACLPFV LAAAVSRKKK RRMGTYSLVP
310 320 330 340 350
KKKTKVLKQR TVIEMFKSIT HSTVGSKGEK DLGASSLHVN GESLEMDSDE
360 370 380 390 400
DDSEELEEDD GHGAEQAAAF PTEDSRTSKE SMSEADRAQK MDGESEEEQE
410 420 430 440 450
SVDTGEEEEG GDESDLSSES SIKKKFLKRK GKTDSPWIKP ARKRRRRSRK
460 470 480 490 500
KPSGALGSES YKSSAGSAEQ TAPGDSTGYM EVSLDSLDLR VKGILSSQAE
510 520 530 540 550
GLANGPDVLE TDGLQEVPLC SCRMETPKSR EITTLANNQC MATESVDHEL
560 570 580 590 600
GRCTNSVVKY ELMRPSNKAP LLVLCEDHRG RMVKHQCCPG CGYFCTAGNF
610 620 630 640 650
MECQPESSIS HRFHKDCASR VNNASYCPHC GEESSKAKEV TIAKADTTST
660 670 680 690 700
VTPVPGQEKG SALEGRADTT TGSAAGPPLS EDDKLQGAAS HVPEGFDPTG
710 720 730 740 750
PAGLGRPTPG LSQGPGKETL ESALIALDSE KPKKLRFHPK QLYFSARQGE
760 770 780 790 800
LQKVLLMLVD GIDPNFKMEH QNKRSPLHAA AEAGHVDICH MLVQAGANID
810 820 830 840 850
TCSEDQRTPL MEAAENNHLE AVKYLIKAGA LVDPKDAEGS TCLHLAAKKG
860 870 880 890 900
HYEVVQYLLS NGQMDVNCQD DGGWTPMIWA TEYKHVDLVK LLLSKGSDIN
910 920 930 940 950
IRDNEENICL HWAAFSGCVD IAEILLAAKC DLHAVNIHGD SPLHIAAREN
960 970 980 990 1000
RYDCVVLFLS RDSDVTLKNK EGETPLQCAS LNSQVWSALQ MSKALQDSAP
1010 1020 1030 1040 1050
DRPSPVERIV SRDIARGYER IPIPCVNAVD SEPCPSNYKY VSQNCVTSPM
1060 1070 1080 1090 1100
NIDRNITHLQ YCVCIDDCSS SNCMCGQLSM RCWYDKDGRL LPEFNMAEPP
1110 1120 1130 1140 1150
LIFECNHACS CWRNCRNRVV QNGLRARLQL YRTRDMGWGV RSLQDIPPGT
1160 1170 1180 1190 1200
FVCEYVGELI SDSEADVREE DSYLFDLDNK DGEVYCIDAR FYGNVSRFIN
1210 1220 1230 1240 1250
HHCEPNLVPV RVFMAHQDLR FPRIAFFSTR LIEAGEQLGF DYGERFWDIK
1260 1270 1280 1290
GKLFSCRCGS PKCRHSSAAL AQRQASAAQE AQEDGLPDTS SAAAADPL
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.Curated
The sequence CAH71077.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI17354.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 34 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.
GeneTreei ENSGT00760000118855.
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

Bgeei Q9H9B1.
CleanExi HS_EHMT1.
ExpressionAtlasi Q9H9B1. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 151 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