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Q5DW34

- EHMT1_MOUSE

UniProt

Q5DW34 - EHMT1_MOUSE

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Protein

Histone-lysine N-methyltransferase EHMT1

Gene

Ehmt1

Organism
Mus musculus (Mouse)
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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1060 – 10601Zinc 1By similarity
Metal bindingi1060 – 10601Zinc 2By similarity
Metal bindingi1062 – 10621Zinc 1By similarity
Metal bindingi1066 – 10661Zinc 1By similarity
Metal bindingi1066 – 10661Zinc 3By similarity
Metal bindingi1071 – 10711Zinc 1By similarity
Metal bindingi1073 – 10731Zinc 2By similarity
Metal bindingi1103 – 11031Zinc 2By similarity
Metal bindingi1103 – 11031Zinc 3By similarity
Metal bindingi1107 – 11071Zinc 2By similarity
Metal bindingi1109 – 11091Zinc 3By similarity
Metal bindingi1113 – 11131Zinc 3By similarity
Binding sitei1153 – 11531Histone H3K9meBy similarity
Binding sitei1171 – 11711S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi1201 – 12011Zinc 4By similarity
Metal bindingi1254 – 12541Zinc 4By similarity
Binding sitei1255 – 12551S-adenosyl-L-methionine; via amide nitrogenPROSITE-ProRule annotation
Metal bindingi1256 – 12561Zinc 4By similarity
Metal bindingi1261 – 12611Zinc 4By similarity

GO - Molecular functioni

  1. C2H2 zinc finger domain binding Source: UniProt
  2. histone methyltransferase activity (H3-K27 specific) Source: UniProtKB
  3. histone methyltransferase activity (H3-K9 specific) Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA methylation Source: UniProtKB
  2. embryo development Source: UniProtKB
  3. histone H3-K27 methylation Source: GOC
  4. histone H3-K9 methylation Source: GOC
  5. negative regulation of transcription, DNA-templated Source: UniProtKB
  6. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  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_206033. 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
Lysine N-methyltransferase 1D
Gene namesi
Name:Ehmt1
Synonyms:Euhmtase1, Glp, Kmt1d
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1924933. Ehmt1.

Subcellular locationi

Nucleus 1 Publication. Chromosome 1 Publication
Note: Associates with euchromatic regions.

GO - Cellular componenti

  1. chromosome Source: UniProtKB-KW
  2. cytoplasm Source: Ensembl
  3. nucleus Source: UniProtKB
  4. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryos die around E9.5. Levels of H3K9me1 and H3K9me2 are drastically reduced.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1153 – 11531Y → V in LM7; does not prevent methyltransferase activity; when associated with F-1240. 1 Publication
Mutagenesisi1198 – 12014Missing in LM3; does not form heterodimer with EHMT2 and is defective in mediating both H3K9me and DNA methylation. 1 Publication
Mutagenesisi1201 – 12011C → A in LM4; does not prevent methyltransferase activity. 1 Publication
Mutagenesisi1240 – 12401Y → F in LM7; does not prevent methyltransferase activity; when associated with V-1153. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12961296Histone-lysine N-methyltransferase EHMT1PRO_0000405844Add
BLAST

Proteomic databases

MaxQBiQ5DW34.
PaxDbiQ5DW34.
PRIDEiQ5DW34.

PTM databases

PhosphoSiteiQ5DW34.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ5DW34.
ExpressionAtlasiQ5DW34. baseline.
GenevestigatoriQ5DW34.

Interactioni

Subunit structurei

Interacts with 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. Interacts with MPHOSPH8 (By similarity). 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 (By similarity). Heterodimer; heterodimerizes with EHMT2. Interacts (via ANK repeats) with RELA (when monomethylated at 'Lys-310').By similarity2 Publications

Protein-protein interaction databases

BioGridi218847. 6 interactions.
DIPiDIP-49000N.
DIP-59572N.
IntActiQ5DW34. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ5DW34.
SMRiQ5DW34. Positions 718-1264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati735 – 76430ANK 1Add
BLAST
Repeati770 – 79930ANK 2Add
BLAST
Repeati803 – 83230ANK 3Add
BLAST
Repeati836 – 86631ANK 4Add
BLAST
Repeati870 – 89930ANK 5Add
BLAST
Repeati903 – 93230ANK 6Add
BLAST
Repeati936 – 96530ANK 7Add
BLAST
Repeati969 – 100234ANK 8Add
BLAST
Domaini1058 – 112164Pre-SETPROSITE-ProRule annotationAdd
BLAST
Domaini1124 – 1241118SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni903 – 9053Histone H3K9me bindingBy similarity
Regioni1134 – 11363S-adenosyl-L-methionine bindingBy similarity
Regioni1160 – 117920Interaction with histone H3By similarityAdd
BLAST
Regioni1198 – 11992S-adenosyl-L-methionine bindingBy similarity
Regioni1240 – 12434Interaction with histone H3By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi440 – 4478Poly-Arg
Compositional biasi1290 – 12934Poly-Ala

Domaini

The ANK repeats specifically recognize and bind H3K9me1 and H3K9me2 (By similarity). They also specifically recognize and bind RELA subunit of NF-kappa-B, when RELA is monomethylated at 'Lys-310'.By similarity1 Publication
The SET domain mediates interaction with WIZ.By similarity
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.By similarity

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.
HOGENOMiHOG000231216.
HOVERGENiHBG028394.
InParanoidiQ5DW34.
KOiK11420.
OMAiSDFGRQQ.
OrthoDBiEOG744T8D.
PhylomeDBiQ5DW34.
TreeFamiTF106443.

Family and domain databases

Gene3Di1.25.40.20. 3 hits.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5DW34-1) [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
MAAADAEQAV LAKQETKQDC CMKTELLRED TPMAADEGST EKQEGETPMA
60 70 80 90 100
ADGETNGSCE KSGDPSHLNA PKHTQENTRA SPQEGTNRVS RVAENGVSER
110 120 130 140 150
DTEVGKQNHV TADDFMQTSV IGSNGYFLNK PALQGQPLRT PNILTSSLPG
160 170 180 190 200
HAAKTLPGGA SKCRTLSALP QTPTTAPTVP GEGSADTEDR KPTASGTDVR
210 220 230 240 250
VHRARKTMPK SILGLHAASK DHREVQDHKE PKEDINRNIS ECGRQQLLPT
260 270 280 290 300
FPALHQSLPQ NQCYMATTKS QTACLPFVLA AAVSRKKKRR MGTYSLVPKK
310 320 330 340 350
KTKVLKQRTV IEMFKSITHS TVGAKGEKAL DDSALHVNGE SLEMDSEDED
360 370 380 390 400
SDELEDDEDH GAEQAAAFPT EDSRTSKESM SETDRAAKMD GDSEEEQESP
410 420 430 440 450
DTGEDEDGGD ESDLSSESSI KKKFLKRRGK TDSPWIKPAR KRRRRSRKKP
460 470 480 490 500
SSMLGSEACK SSPGSMEQAA LGDSAGYMEV SLDSLDLRVR GILSSQTENE
510 520 530 540 550
GLASGPDVLG TDGLQEVPLC SCRMETPKSR EISTLANNQC MATESVDHEL
560 570 580 590 600
GRCTNSVVKY ELMRPSNKAP LLVLCEDHRG RMVKHQCCPG CGYFCTAGNF
610 620 630 640 650
MECQPESSIS HRFHKDCASR VNNASYCPHC GEEASKAKEV TIAKADTTST
660 670 680 690 700
VTLAPGQEKS LAAEGRADTT TGSIAGAPED ERSQSTAPQA PECFDPAGPA
710 720 730 740 750
GLVRPTSGLS QGPGKETLES ALIALDSEKP KKLRFHPKQL YFSARQGELQ
760 770 780 790 800
KVLLMLVDGI DPNFKMEHQS KRSPLHAAAE AGHVDICHML VQAGANIDTC
810 820 830 840 850
SEDQRTPLME AAENNHLDAV KYLIKAGAQV DPKDAEGSTC LHLAAKKGHY
860 870 880 890 900
DVVQYLLSNG QMDVNCQDDG GWTPMIWATE YKHVELVKLL LSKGSDINIR
910 920 930 940 950
DNEENICLHW AAFSGCVDIA EILLAAKCDL HAVNIHGDSP LHIAARENRY
960 970 980 990 1000
DCVVLFLSRD SDVTLKNKEG ETPLQCASLS SQVWSALQMS KALRDSAPDK
1010 1020 1030 1040 1050
PVAVEKTVSR DIARGYERIP IPCVNAVDSE LCPTNYKYVS QNCVTSPMNI
1060 1070 1080 1090 1100
DRNITHLQYC VCVDDCSSST CMCGQLSMRC WYDKDGRLLP EFNMAEPPLI
1110 1120 1130 1140 1150
FECNHACSCW RNCRNRVVQN GLRARLQLYR TQDMGWGVRS LQDIPLGTFV
1160 1170 1180 1190 1200
CEYVGELISD SEADVREEDS YLFDLDNKDG EVYCIDARFY GNVSRFINHH
1210 1220 1230 1240 1250
CEPNLVPVRV FMSHQDLRFP RIAFFSTRLI QAGEQLGFDY GERFWDVKGK
1260 1270 1280 1290
LFSCRCGSSK CRHSSAALAQ RQASAAQEPQ ENGLPDTSSA AAADPL
Length:1,296
Mass (Da):141,999
Last modified:March 8, 2011 - v2
Checksum:iB7783B6F38D3C7CB
GO
Isoform 2 (identifier: Q5DW34-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     273-279: Missing.
     455-500: Missing.

Note: No experimental confirmation available.

Show »
Length:1,243
Mass (Da):136,496
Checksum:iAB666EE7F3CE9EC3
GO
Isoform 3 (identifier: Q5DW34-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     550-597: Missing.

Note: No experimental confirmation available.

Show »
Length:1,248
Mass (Da):136,631
Checksum:i6D881B82F181F36E
GO

Sequence cautioni

The sequence CAM22112.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti411 – 4111E → D in BAD90007. (PubMed:15774718)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei273 – 2797Missing in isoform 2. 1 PublicationVSP_040724
Alternative sequencei455 – 50046Missing in isoform 2. 1 PublicationVSP_040725Add
BLAST
Alternative sequencei550 – 59748Missing in isoform 3. 1 PublicationVSP_040726Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB205007 mRNA. Translation: BAD90007.1.
AL732525 Genomic DNA. Translation: CAM22112.1. Different initiation.
AL732525 Genomic DNA. Translation: CAM22113.1.
AL732525 Genomic DNA. Translation: CAM22114.1.
BC056938 mRNA. Translation: AAH56938.1.
BC089302 mRNA. Translation: AAH89302.1.
CCDSiCCDS15740.1. [Q5DW34-1]
CCDS59634.1. [Q5DW34-2]
CCDS59636.1. [Q5DW34-3]
RefSeqiNP_001012536.2. NM_001012518.3. [Q5DW34-1]
NP_001103156.1. NM_001109686.2. [Q5DW34-2]
NP_001103157.1. NM_001109687.2. [Q5DW34-3]
UniGeneiMm.24176.

Genome annotation databases

EnsembliENSMUST00000046227; ENSMUSP00000046077; ENSMUSG00000036893. [Q5DW34-3]
ENSMUST00000102938; ENSMUSP00000100002; ENSMUSG00000036893. [Q5DW34-1]
ENSMUST00000114432; ENSMUSP00000110075; ENSMUSG00000036893. [Q5DW34-2]
ENSMUST00000147147; ENSMUSP00000119057; ENSMUSG00000036893.
GeneIDi77683.
KEGGimmu:77683.
UCSCiuc008iph.3. mouse. [Q5DW34-3]
uc008ipi.3. mouse. [Q5DW34-1]
uc012brr.2. mouse. [Q5DW34-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB205007 mRNA. Translation: BAD90007.1 .
AL732525 Genomic DNA. Translation: CAM22112.1 . Different initiation.
AL732525 Genomic DNA. Translation: CAM22113.1 .
AL732525 Genomic DNA. Translation: CAM22114.1 .
BC056938 mRNA. Translation: AAH56938.1 .
BC089302 mRNA. Translation: AAH89302.1 .
CCDSi CCDS15740.1. [Q5DW34-1 ]
CCDS59634.1. [Q5DW34-2 ]
CCDS59636.1. [Q5DW34-3 ]
RefSeqi NP_001012536.2. NM_001012518.3. [Q5DW34-1 ]
NP_001103156.1. NM_001109686.2. [Q5DW34-2 ]
NP_001103157.1. NM_001109687.2. [Q5DW34-3 ]
UniGenei Mm.24176.

3D structure databases

ProteinModelPortali Q5DW34.
SMRi Q5DW34. Positions 718-1264.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 218847. 6 interactions.
DIPi DIP-49000N.
DIP-59572N.
IntActi Q5DW34. 4 interactions.

PTM databases

PhosphoSitei Q5DW34.

Proteomic databases

MaxQBi Q5DW34.
PaxDbi Q5DW34.
PRIDEi Q5DW34.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000046227 ; ENSMUSP00000046077 ; ENSMUSG00000036893 . [Q5DW34-3 ]
ENSMUST00000102938 ; ENSMUSP00000100002 ; ENSMUSG00000036893 . [Q5DW34-1 ]
ENSMUST00000114432 ; ENSMUSP00000110075 ; ENSMUSG00000036893 . [Q5DW34-2 ]
ENSMUST00000147147 ; ENSMUSP00000119057 ; ENSMUSG00000036893 .
GeneIDi 77683.
KEGGi mmu:77683.
UCSCi uc008iph.3. mouse. [Q5DW34-3 ]
uc008ipi.3. mouse. [Q5DW34-1 ]
uc012brr.2. mouse. [Q5DW34-2 ]

Organism-specific databases

CTDi 79813.
MGIi MGI:1924933. Ehmt1.

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00760000118855.
HOGENOMi HOG000231216.
HOVERGENi HBG028394.
InParanoidi Q5DW34.
KOi K11420.
OMAi SDFGRQQ.
OrthoDBi EOG744T8D.
PhylomeDBi Q5DW34.
TreeFami TF106443.

Enzyme and pathway databases

Reactomei REACT_206033. Senescence-Associated Secretory Phenotype (SASP).

Miscellaneous databases

ChiTaRSi Ehmt1. mouse.
NextBioi 347359.
PROi Q5DW34.
SOURCEi Search...

Gene expression databases

Bgeei Q5DW34.
ExpressionAtlasi Q5DW34. baseline.
Genevestigatori Q5DW34.

Family and domain databases

Gene3Di 1.25.40.20. 3 hits.
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. "Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9."
    Tachibana M., Ueda J., Fukuda M., Takeda N., Ohta T., Iwanari H., Sakihama T., Kodama T., Hamakubo T., Shinkai Y.
    Genes Dev. 19:815-826(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, INTERACTION WITH EHMT2, TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] OF 34-1296 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1296 (ISOFORM 3).
    Strain: C57BL/6.
    Tissue: Brain.
  4. "G9a/GLP complexes independently mediate H3K9 and DNA methylation to silence transcription."
    Tachibana M., Matsumura Y., Fukuda M., Kimura H., Shinkai Y.
    EMBO J. 27:2681-2690(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF TYR-1153; 1198-ASN--CYS-1201; CYS-1201 AND TYR-1240.
  5. "Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-kappaB signaling."
    Levy D., Kuo A.J., Chang Y., Schaefer U., Kitson C., Cheung P., Espejo A., Zee B.M., Liu C.L., Tangsombatvisit S., Tennen R.I., Kuo A.Y., Tanjing S., Cheung R., Chua K.F., Utz P.J., Shi X., Prinjha R.K.
    , Lee K., Garcia B.A., Bedford M.T., Tarakhovsky A., Cheng X., Gozani O.
    Nat. Immunol. 12:29-36(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN ANK REPEATS, INTERACTION WITH RELA.

Entry informationi

Entry nameiEHMT1_MOUSE
AccessioniPrimary (citable) accession number: Q5DW34
Secondary accession number(s): A2AIS3
, A2AIS4, Q5EBR1, Q6PGM0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: March 8, 2011
Last modified: November 26, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3