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UniProtKB/Swiss-Prot entry Q9Z148


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name EHMT2_MOUSE
Primary accession number Q9Z148
Secondary accession numbers Q6PE08 Q8K4R6 Q8K4R7 Q9Z149
Integrated into Swiss-Prot on November 15, 2002
Sequence was last modified on November 15, 2002 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 81)
Name and origin of the protein
Protein name Histone-lysine N-methyltransferase, H3 lysine-9 specific 3
Synonyms EC 2.1.1.43
Histone H3-K9 methyltransferase 3
H3-K9-HMTase 3
Euchromatic histone-lysine N-methyltransferase 2
HLA-B-associated transcript 8
Protein G9a
Gene name
Name: Ehmt2
Synonyms: Bat8, G9a, Ng36
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND MUTAGENESIS OF 1165-ASN--CYS-1168.
DOI=10.1101/gad.989402; PubMed=12130538 [NCBI, ExPASy, EBI, Israel, Japan]
Tachibana M., Sugimoto K., Nozaki M., Ueda J., Ohta T., Ohki M., Fukuda M., Takeda N., Niida H., Kato H., Shinkai Y.;
"G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesis.";
Genes Dev. 16:1779-1791(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=129;
DOI=10.1101/gr.1736803; PubMed=14656967 [NCBI, ExPASy, EBI, Israel, Japan]
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
ALTERNATIVE SPLICING (ISOFORM 2).
DOI=10.1007/s00335-001-3029-3; PubMed=11707778 [NCBI, ExPASy, EBI, Israel, Japan]
Brown S.E., Campbell R.D., Sanderson C.M.;
"Novel NG36/G9a gene products encoded within the human and mouse MHC class III regions.";
Mamm. Genome 12:916-924(2001).
[5]
ENZYME ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-1162.
DOI=10.1074/jbc.M101914200; PubMed=11316813 [NCBI, ExPASy, EBI, Israel, Japan]
Tachibana M., Sugimoto K., Fukushima T., Shinkai Y.;
"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.";
J. Biol. Chem. 276:25309-25317(2001).
[6]
INTERACTION WITH WIZ AND EHMT1.
DOI=10.1074/jbc.M603087200; PubMed=16702210 [NCBI, ExPASy, EBI, Israel, Japan]
Ueda J., Tachibana M., Ikura T., Shinkai Y.;
"Zinc finger protein Wiz links G9a/GLP histone methyltransferases to the co-repressor molecule CtBP.";
J. Biol. Chem. 281:20120-20128(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-608, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan]
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF109906; AAC84164.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109906; AAC84165.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB077209; BAC05482.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB077210; BAC05483.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC025539; AAH25539.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC058357; AAH58357.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_665829.1; -.
NP_671493.1; -.
UniGene Mm.35345
3D structure databases
HSSP Q8X225; 1ML9. [HSSP ENTRY / PDB]
SMR Q9Z148; 975-1245.
ModBase Q9Z148.
Protein-protein interaction databases
IntAct Q9Z148; -.
PTM databases
PhosphoSite Q9Z148; -.
Organism-specific databases
MGI MGI:2148922; Ehmt2.
Gene expression databases
ArrayExpress Q9Z148; -.
CleanEx MM_EHMT2; -.
GermOnline ENSMUSG00000013787; Mus musculus.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from direct assay from MGI).
GO:0018024; Molecular function: histone-lysine N-methyltransferase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0009566; Biological process: fertilization (inferred from mutant phenotype from MGI).
GO:0007281; Biological process: germ cell development (inferred from mutant phenotype from MGI).
GO:0051567; Biological process: histone H3-K9 methylation (inferred from mutant phenotype from MGI).
GO:0000122; Biological process: negative regulation of transcription from RNA polymerase II promoter (inferred from mutant phenotype from MGI).
GO:0035265; Biological process: organ growth (inferred from mutant phenotype from MGI).
GO:0000239; Biological process: pachytene (inferred from mutant phenotype from MGI).
GO:0007286; Biological process: spermatid development (inferred from mutant phenotype from MGI).
GO:0007130; Biological process: synaptonemal complex assembly (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR002110; ANK.
IPR003616; Post-SET_Zn_bd.
IPR007728; Pre-SET_Zn_bd.
IPR003606; Pre-SET_Zn_bd_sub.
IPR001214; SET.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.20; ANK; 1.
Pfam PF00023; Ank; 6.
PF05033; Pre-SET; 1.
PF00856; SET; 1.
Pfam graphical view of domain structure.
PRINTS PR01415; ANKYRIN.
SMART SM00248; ANK; 6.
SM00508; PostSET; 1.
SM00468; PreSET; 1.
SM00317; SET; 1.
SMART graphical view of domain structure.
PROSITE PS50297; ANK_REP_REGION; 1.
PS50088; ANK_REPEAT; 5.
PS50868; POST_SET; FALSE_NEG.
PS50867; PRE_SET; 1.
PS50280; SET; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9Z148.
Genome annotation databases
Ensembl ENSMUSG00000013787; Mus musculus. [Contig view]
GeneID 110147; -.
KEGG mmu:110147; -.
Phylogenomic databases
HOGENOM Q9Z148; -.
HOVERGEN Q9Z148; -.
Other
NextBio 363413; -.
SOURCE Ehmt2; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ANK repeat; Chromatin regulator; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; Repeat; S-adenosyl-L-methionine; Transferase; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1263  1263     Histone-lysine N-methyltransferase, H3 lysine-9 specific 3. PRO_0000186069
REPEAT   702    731  30     ANK 1. 
REPEAT   737    766  30     ANK 2. 
REPEAT   770    799  30     ANK 3. 
REPEAT   803    833  31     ANK 4. 
REPEAT   837    866  30     ANK 5. 
REPEAT   870    899  30     ANK 6. 
REPEAT   903    932  30     ANK 7. 
DOMAIN   1025   1088  64     Pre-SET. 
DOMAIN   1090   1212  123     SET. 
DOMAIN   1217   1233  17     Post-SET. 
REGION   1101   1103  3     S-adenosyl-L-methionine binding (By similarity). 
REGION   1165   1166  2     S-adenosyl-L-methionine binding (By similarity). 
COMPBIAS   352    379  28     Poly-Glu. 
METAL   1027   1027        Zinc 1 (By similarity). 
METAL   1027   1027        Zinc 2 (By similarity). 
METAL   1029   1029        Zinc 1 (By similarity). 
METAL   1033   1033        Zinc 1 (By similarity). 
METAL   1033   1033        Zinc 3 (By similarity). 
METAL   1038   1038        Zinc 1 (By similarity). 
METAL   1040   1040        Zinc 2 (By similarity). 
METAL   1070   1070        Zinc 2 (By similarity). 
METAL   1070   1070        Zinc 3 (By similarity). 
METAL   1074   1074        Zinc 2 (By similarity). 
METAL   1076   1076        Zinc 3 (By similarity). 
METAL   1080   1080        Zinc 3 (By similarity). 
METAL   1168   1168        Zinc 4 (By similarity). 
METAL   1221   1221        Zinc 4 (By similarity). 
METAL   1223   1223        Zinc 4 (By similarity). 
METAL   1228   1228        Zinc 4 (By similarity). 
BINDING   1138   1138        S-adenosyl-L-methionine (By similarity). 
MOD_RES   193    193        Phosphoserine (By similarity). 
MOD_RES   285    285        Phosphoserine (By similarity). 
MOD_RES   298    298        Phosphoserine (By similarity). 
MOD_RES   608    608        Phosphothreonine. 
MOD_RES   1263   1263        Phosphothreonine (By similarity). 
VAR_SEQ   1     57        Missing (in isoform 2 and isoform 3). VSP_002214
VAR_SEQ   58     71        AGLTGPPVPCLPSQ -> MAAAAGAAAAAAAE (in isoform 2 and isoform 3). VSP_002215
VAR_SEQ   426    459        Missing (in isoform 2). VSP_002216
MUTAGEN   1162   1162        R->H: Strongly reduces histone methyltransferase activity. 
MUTAGEN   1165   1168        Missing: Abolishes histone methyltransferase activity and subsequent repression. 
Sequence information
Length: 1263 AA [This is the length of the unprocessed precursor] Molecular weight: 138039 Da [This is the MW of the unprocessed precursor] CRC64: 74DBFF9A36769589 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRGLPRGRGL MRARGRGRAA PTGGRGRGRG GAHRGRGRPR SLLSLPRAQA SWAPQLPAGL 

        70         80         90        100        110        120 
TGPPVPCLPS QGEAPAEMGA LLLEKEPRGA AERVHSSLGD TPQSEETLPK ANPDSLEPAG 

       130        140        150        160        170        180 
PSSPASVTVT VGDEGADTPV GAASLIGDEP ESLEGDGGRI VLGHATKSFP SSPSKGGACP 

       190        200        210        220        230        240 
SRAKMSMTGA GKSPPSVQSL AMRLLSMPGA QGAATAGPEP SPATTAAQEG QPKVHRARKT 

       250        260        270        280        290        300 
MSKPSNGQPP IPEKRPPEVQ HFRMSDDMHL GKVTSDVAKR RKLNSGSLSE DLGSAGGSGD 

       310        320        330        340        350        360 
IILEKGEPRP LEEWETVVGD DFSLYYDAYS VDERVDSDSK SEVEALAEQL SEEEEEEEEE 

       370        380        390        400        410        420 
EEEEEEEEEE EEEEEEDEES GNQSDRSGSS GRRKAKKKWR KDSPWVKPSR KRRKREPPRA 

       430        440        450        460        470        480 
KEPRGVNGVG SSGPSEYMEV PLGSLELPSE GTLSPNHAGV SNDTSSLETE RGFEELPLCS 

       490        500        510        520        530        540 
CRMEAPKIDR ISERAGHKCM ATESVDGELL GCNAAILKRE TMRPSSRVAL MVLCEAHRAR 

       550        560        570        580        590        600 
MVKHHCCPGC GYFCTAGTFL ECHPDFRVAH RFHKACVSQL NGMVFCPHCG EDASEAQEVT 

       610        620        630        640        650        660 
IPRGDGGTPP IGTAAPALPP LAHDAPGRAD TSQPSARMRG HGEPRRPPCD PLADTIDSSG 

       670        680        690        700        710        720 
PSLTLPNGGC LSAVGLPPGP GREALEKALV IQESERRKKL RFHPRQLYLS VKQGELQKVI 

       730        740        750        760        770        780 
LMLLDNLDPN FQSDQQSKRT PLHAAAQKGS VEICHVLLQA GANINAVDKQ QRTPLMEAVV 

       790        800        810        820        830        840 
NNHLEVARYM VQLGGCVYSK EEDGSTCLHH AAKIGNLEMV SLLLSTGQVD VNAQDSGGWT 

       850        860        870        880        890        900 
PIIWAAEHKH IDVIRMLLTR GADVTLTDNE ENICLHWASF TGSAAIAEVL LNAQCDLHAV 

       910        920        930        940        950        960 
NYHGDTPLHI AARESYHDCV LLFLSRGANP ELRNKEGDTA WDLTPERSDV WFALQLNRKL 

       970        980        990       1000       1010       1020 
RLGVGNRAVR TEKIICRDVA RGYENVPIPC VNGVDGEPCP EDYKYISENC ETSTMNIDRN 

      1030       1040       1050       1060       1070       1080 
ITHLQHCTCV DDCSSSNCLC GQLSIRCWYD KDGRLLQEFN KIEPPLIFEC NQACSCWRSC 

      1090       1100       1110       1120       1130       1140 
KNRVVQSGIK VRLQLYRTAK MGWGVRALQT IPQGTFICEY VGELISDAEA DVREDDSYLF 

      1150       1160       1170       1180       1190       1200 
DLDNKDGEVY CIDARYYGNI SRFINHLCDP NIIPVRVFML HQDLRFPRIA FFSSRDIRTG 

      1210       1220       1230       1240       1250       1260 
EELGFDYGDR FWDIKSKYFT CQCGSEKCKH SAEAIALEQS RLARLDPHPE LLPDLSSLPP 


INT 

Q9Z148 in FASTA format

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