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Protein

Histone-lysine N-methyltransferase EHMT1

Gene

EHMT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Metal bindingi1062Zinc 11
Metal bindingi1062Zinc 21
Metal bindingi1064Zinc 11
Metal bindingi1068Zinc 11
Metal bindingi1068Zinc 31
Metal bindingi1073Zinc 11
Metal bindingi1075Zinc 21
Metal bindingi1105Zinc 21
Metal bindingi1105Zinc 31
Metal bindingi1109Zinc 21
Metal bindingi1111Zinc 31
Metal bindingi1115Zinc 31
Binding sitei1155Histone H3K9me2 Publications1
Binding sitei1173S-adenosyl-L-methionine1
Metal bindingi1203Zinc 41
Metal bindingi1256Zinc 41
Binding sitei1257S-adenosyl-L-methionine; via amide nitrogen1
Metal bindingi1258Zinc 41
Metal bindingi1263Zinc 41

GO - Molecular functioni

  • histone-lysine N-methyltransferase activity Source: UniProtKB
  • histone methyltransferase activity (H3-K27 specific) Source: UniProtKB
  • histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
  • methyltransferase activity Source: UniProtKB
  • p53 binding Source: UniProtKB
  • protein-lysine N-methyltransferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciZFISH:HS09291-MONOMER.
ZFISH:HS17627-MONOMER.
ReactomeiR-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-6804760. Regulation of TP53 Activity through Methylation.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:24650. EHMT1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

Kleefstra syndrome (KLESTS)2 Publications
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
Disease descriptionA 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.
See also OMIM:610253
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0691831075C → Y in KLESTS. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi905E → A: Abolishes binding to histone H3K9me. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi79813.
MalaCardsiEHMT1.
MIMi610253. phenotype.
OpenTargetsiENSG00000181090.
Orphaneti96147. Kleefstra syndrome due to 9q34 microdeletion.
261652. Kleefstra syndrome due to a point mutation.
PharmGKBiPA134941393.

Chemistry databases

ChEMBLiCHEMBL6031.
GuidetoPHARMACOLOGYi2651.

Polymorphism and mutation databases

BioMutaiEHMT1.
DMDMi325511404.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001860671 – 1298Histone-lysine N-methyltransferase EHMT1Add BLAST1298

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki234Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki432Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei435PhosphoserineCombined sources1
Modified residuei483PhosphoserineCombined sources1
Cross-linki731Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1004PhosphoserineCombined sources1
Modified residuei1048PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9H9B1.
MaxQBiQ9H9B1.
PaxDbiQ9H9B1.
PeptideAtlasiQ9H9B1.
PRIDEiQ9H9B1.

PTM databases

iPTMnetiQ9H9B1.
PhosphoSitePlusiQ9H9B1.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000181090.
CleanExiHS_EHMT1.
ExpressionAtlasiQ9H9B1. baseline and differential.
GenevisibleiQ9H9B1. HS.

Organism-specific databases

HPAiHPA060022.

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
MPHOSPH8Q995493EBI-766087,EBI-2653928
RELAQ042063EBI-766087,EBI-73886
RelaQ042075EBI-766087,EBI-644400From a different organism.

GO - Molecular functioni

  • p53 binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122908. 44 interactors.
DIPiDIP-34585N.
IntActiQ9H9B1. 25 interactors.
MINTiMINT-7945009.
STRINGi9606.ENSP00000417980.

Chemistry databases

BindingDBiQ9H9B1.

Structurei

Secondary structure

11298
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi776 – 783Combined sources8
Helixi786 – 794Combined sources9
Helixi809 – 815Combined sources7
Helixi819 – 826Combined sources8
Turni827 – 829Combined sources3
Helixi842 – 848Combined sources7
Helixi852 – 859Combined sources8
Turni860 – 862Combined sources3
Helixi876 – 882Combined sources7
Helixi886 – 894Combined sources9
Helixi909 – 916Combined sources8
Helixi919 – 926Combined sources8
Turni927 – 929Combined sources3
Helixi942 – 948Combined sources7
Helixi952 – 959Combined sources8
Turni960 – 962Combined sources3
Helixi975 – 978Combined sources4
Helixi983 – 994Combined sources12
Beta strandi1008 – 1012Combined sources5
Turni1014 – 1017Combined sources4
Beta strandi1019 – 1021Combined sources3
Beta strandi1025 – 1031Combined sources7
Beta strandi1037 – 1040Combined sources4
Beta strandi1045 – 1048Combined sources4
Helixi1056 – 1058Combined sources3
Beta strandi1065 – 1068Combined sources4
Helixi1074 – 1078Combined sources5
Beta strandi1096 – 1098Combined sources3
Beta strandi1109 – 1111Combined sources3
Beta strandi1115 – 1117Combined sources3
Helixi1120 – 1122Combined sources3
Beta strandi1128 – 1132Combined sources5
Beta strandi1134 – 1144Combined sources11
Beta strandi1151 – 1155Combined sources5
Beta strandi1157 – 1161Combined sources5
Helixi1162 – 1166Combined sources5
Beta strandi1174 – 1177Combined sources4
Beta strandi1180 – 1183Combined sources4
Beta strandi1185 – 1193Combined sources9
Helixi1195 – 1198Combined sources4
Beta strandi1206 – 1215Combined sources10
Beta strandi1223 – 1230Combined sources8
Helixi1244 – 1250Combined sources7
Turni1251 – 1253Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H9B1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati737 – 766ANK 1Add BLAST30
Repeati772 – 801ANK 2Add BLAST30
Repeati805 – 834ANK 3Add BLAST30
Repeati838 – 868ANK 4Add BLAST31
Repeati872 – 901ANK 5Add BLAST30
Repeati905 – 934ANK 6Add BLAST30
Repeati938 – 967ANK 7Add BLAST30
Repeati971 – 1004ANK 8Add BLAST34
Domaini1060 – 1123Pre-SETPROSITE-ProRule annotationAdd BLAST64
Domaini1126 – 1243SETPROSITE-ProRule annotationAdd BLAST118

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni905 – 907Histone H3K9me binding3
Regioni1136 – 1138S-adenosyl-L-methionine binding3
Regioni1162 – 1181Interaction with histone H3Add BLAST20
Regioni1200 – 1201S-adenosyl-L-methionine binding2
Regioni1242 – 1245Interaction with histone H34

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi406 – 409Poly-Glu4
Compositional biasi442 – 449Poly-Arg8
Compositional biasi1292 – 1295Poly-Ala4

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

eggNOGiKOG1082. Eukaryota.
COG0666. LUCA.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOVERGENiHBG028394.
InParanoidiQ9H9B1.
KOiK11420.
OrthoDBiEOG091G00U6.
PhylomeDBiQ9H9B1.
TreeFamiTF106443.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamiPF12796. 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. AlignAdd to basket

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 BAB14321 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated
The sequence CAD28534 differs from that shown. Intron retention.Curated
The sequence CAH71077 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI17354 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti555N → D in AAH47504 (PubMed:15489334).Curated1
Sequence conflicti561E → G in AAM09024 (PubMed:14702039).Curated1
Sequence conflicti561E → G in BAB14321 (PubMed:15164053).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03634543A → V in a breast cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs79514677dbSNPEnsembl.1
Natural variantiVAR_027642388A → T.Corresponds to variant rs11137198dbSNPEnsembl.1
Natural variantiVAR_0691831075C → Y in KLESTS. 1 Publication1
Natural variantiVAR_0363461173Y → F in a breast cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0022228 – 66AVPAR…DASSH → RHLWLPMKAQQRNRQERPTW LRTVRPMGLVKTAMPAVMQM LQSTLRTAQGSTPRMAPTH in isoform 2. 1 PublicationAdd BLAST59
Alternative sequenceiVSP_00222367 – 1298Missing in isoform 2. 1 PublicationAdd BLAST1232
Alternative sequenceiVSP_040717795 – 808AGANI…EDQRT → FCRLGSPRSRGCLW in isoform 4. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_040718809 – 1298Missing in isoform 4. 1 PublicationAdd BLAST490
Alternative sequenceiVSP_0022241181 – 1184DGEV → ISSA in isoform 3. 1 Publication4
Alternative sequenceiVSP_0022251185 – 1298Missing in isoform 3. 1 PublicationAdd BLAST114

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

EnsembliENST00000371394; ENSP00000485945; ENSG00000181090. [Q9H9B1-2]
ENST00000460843; ENSP00000417980; ENSG00000181090. [Q9H9B1-1]
ENST00000462484; ENSP00000417328; ENSG00000181090. [Q9H9B1-4]
GeneIDi79813.
KEGGihsa:79813.
UCSCiuc004coa.3. human. [Q9H9B1-1]

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.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122908. 44 interactors.
DIPiDIP-34585N.
IntActiQ9H9B1. 25 interactors.
MINTiMINT-7945009.
STRINGi9606.ENSP00000417980.

Chemistry databases

BindingDBiQ9H9B1.
ChEMBLiCHEMBL6031.
GuidetoPHARMACOLOGYi2651.

PTM databases

iPTMnetiQ9H9B1.
PhosphoSitePlusiQ9H9B1.

Polymorphism and mutation databases

BioMutaiEHMT1.
DMDMi325511404.

Proteomic databases

EPDiQ9H9B1.
MaxQBiQ9H9B1.
PaxDbiQ9H9B1.
PeptideAtlasiQ9H9B1.
PRIDEiQ9H9B1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371394; ENSP00000485945; ENSG00000181090. [Q9H9B1-2]
ENST00000460843; ENSP00000417980; ENSG00000181090. [Q9H9B1-1]
ENST00000462484; ENSP00000417328; ENSG00000181090. [Q9H9B1-4]
GeneIDi79813.
KEGGihsa:79813.
UCSCiuc004coa.3. human. [Q9H9B1-1]

Organism-specific databases

CTDi79813.
DisGeNETi79813.
GeneCardsiEHMT1.
GeneReviewsiEHMT1.
HGNCiHGNC:24650. EHMT1.
HPAiHPA060022.
MalaCardsiEHMT1.
MIMi607001. gene.
610253. phenotype.
neXtProtiNX_Q9H9B1.
OpenTargetsiENSG00000181090.
Orphaneti96147. Kleefstra syndrome due to 9q34 microdeletion.
261652. Kleefstra syndrome due to a point mutation.
PharmGKBiPA134941393.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1082. Eukaryota.
COG0666. LUCA.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOVERGENiHBG028394.
InParanoidiQ9H9B1.
KOiK11420.
OrthoDBiEOG091G00U6.
PhylomeDBiQ9H9B1.
TreeFamiTF106443.

Enzyme and pathway databases

BioCyciZFISH:HS09291-MONOMER.
ZFISH:HS17627-MONOMER.
ReactomeiR-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-6804760. Regulation of TP53 Activity through Methylation.

Miscellaneous databases

ChiTaRSiEHMT1. human.
EvolutionaryTraceiQ9H9B1.
GeneWikiiEHMT1.
GenomeRNAii79813.
PROiQ9H9B1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000181090.
CleanExiHS_EHMT1.
ExpressionAtlasiQ9H9B1. baseline and differential.
GenevisibleiQ9H9B1. HS.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PfamiPF12796. 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]
ProtoNetiSearch...

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 30, 2016
This is version 174 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.