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UniProtKB/Swiss-Prot entry Q9Y6K1


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

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Entry information
Entry name DNM3A_HUMAN
Primary accession number Q9Y6K1
Secondary accession numbers Q86XF5 Q8IZV0 Q8WXU9
Integrated into Swiss-Prot on September 26, 2001
Sequence was last modified on January 15, 2008 (Sequence version 4)
Annotations were last modified on    November 25, 2008 (Entry version 70)
Name and origin of the protein
Protein name DNA (cytosine-5)-methyltransferase 3A
Synonyms Dnmt3a
EC 2.1.1.37
DNA methyltransferase HsaIIIA
DNA MTase HsaIIIA
M.HsaIIIA
Gene name
Name: DNMT3A
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal testis;
DOI=10.1016/S0378-1119(99)00252-8; PubMed=10433969 [NCBI, ExPASy, EBI, Israel, Japan]
Xie S., Wang Z., Okano M., Nogami M., Li Y., He W.-W., Okumura K., Li E.;
"Cloning, expression and chromosome locations of the human DNMT3 gene family.";
Gene 236:87-95(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
DOI=10.1074/jbc.M205312200; PubMed=12138111 [NCBI, ExPASy, EBI, Israel, Japan]
Chen T., Ueda Y., Xie S., Li E.;
"A novel Dnmt3a isoform produced from an alternative promoter localizes to euchromatin and its expression correlates with active de novo methylation.";
J. Biol. Chem. 277:38746-38754(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DNMT1 AND DNMT3B, AND SUBCELLULAR LOCATION.
DOI=10.1093/emboj/cdf401; PubMed=12145218 [NCBI, ExPASy, EBI, Israel, Japan]
Kim G.-D., Ni J., Kelesoglu N., Roberts R.J., Pradhan S.;
"Co-operation and communication between the human maintenance and de novo DNA (cytosine-5) methyltransferases.";
EMBO J. 21:4183-4195(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
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).
[7]
TISSUE SPECIFICITY.
DOI=10.1093/nar/27.11.2291; PubMed=10325416 [NCBI, ExPASy, EBI, Israel, Japan]
Robertson K.D., Uzvolgyi E., Liang G., Talmadge C., Sumegi J., Gonzales F.A., Jones P.A.;
"The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA expression in normal tissues and overexpression in tumors.";
Nucleic Acids Res. 27:2291-2298(1999).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[9]
INTERACTION WITH SETDB1.
DOI=10.1074/jbc.M513249200; PubMed=16682412 [NCBI, ExPASy, EBI, Israel, Japan]
Li H., Rauch T., Chen Z.-X., Szabo P.E., Riggs A.D., Pfeifer G.P.;
"The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A interact directly and localize to promoters silenced in cancer cells.";
J. Biol. Chem. 281:19489-19500(2006).
[10]
FUNCTION, AND INTERACTION WITH THE PRC2/EED-EZH2 COMPLEX.
DOI=10.1038/nature04431; PubMed=16357870 [NCBI, ExPASy, EBI, Israel, Japan]
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C., Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M., Esteller M., Di Croce L., de Launoit Y., Fuks F.;
"The Polycomb group protein EZH2 directly controls DNA methylation.";
Nature 439:871-874(2006).
[11]
ERRATUM.
Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C., Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M., Esteller M., Di Croce L., de Launoit Y., Fuks F.;
Nature 446:824-824(2006).
[12]
DE NOVO DNA METHYLATION OF TARGET GENES.
DOI=10.1038/ng1950; PubMed=17200670 [NCBI, ExPASy, EBI, Israel, Japan]
Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M., Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E., Bergman Y., Simon I., Cedar H.;
"Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer.";
Nat. Genet. 39:232-236(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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
AF067972; AAD33084.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF480163; AAN40037.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF331856; AAL57039.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC012074; AAY14761.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471053; EAX00727.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC043617; AAH43617.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_072046.2; -.
NP_715640.2; -.
NP_783328.1; -.
UniGene Hs.515840
3D structure databases
PDB
2QRV; X-ray; 2.89 A; A/D/E/H=626-912.[ExPASy / RCSB / EBI]
PDBsum 2QRV; -.
ModBase Q9Y6K1.
Protein-protein interaction databases
IntAct Q9Y6K1; -.
Protein family/group databases
REBASE 4119; M.HsaDnmt3A.
PTM databases
PhosphoSite Q9Y6K1; -.
Organism-specific databases
HGNC HGNC:2978; DNMT3A.
GenAtlas DNMT3A.
HPA CAB009469; -.
MIM 602769; gene. [NCBI / EBI]
PharmGKB PA27445; -.
GeneCards Q9Y6K1.
Gene expression databases
ArrayExpress Q9Y6K1; -.
CleanEx HS_DNMT3A; -.
GermOnline ENSG00000119772; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from sequence or structural similarity from UniProtKB).
GO:0000791; Cellular component: euchromatin (inferred from sequence or structural similarity from UniProtKB).
GO:0016363; Cellular component: nuclear matrix (inferred from sequence or structural similarity from UniProtKB).
GO:0003886; Molecular function: DNA (cytosine-5-)-methyltransferase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0003677; Molecular function: DNA binding (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006306; Biological process: DNA methylation (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR001525; C5_DNA_meth.
IPR000313; PWWP.
Graphical view of domain structure.
Pfam PF00145; DNA_methylase; 1.
PF00855; PWWP; 1.
Pfam graphical view of domain structure.
SMART SM00293; PWWP; 1.
SMART graphical view of domain structure.
PROSITE PS00094; C5_MTASE_1; 1.
PS00095; C5_MTASE_2; FALSE_NEG.
PS50812; PWWP; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9Y6K1.
Genome annotation databases
Ensembl ENSG00000119772; Homo sapiens. [Contig view]
GeneID 1788; -.
KEGG hsa:1788; -.
Phylogenomic databases
HOVERGEN Q9Y6K1; -.
Other
NextBio 7279; -.
SOURCE DNMT3A; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative promoter usage; Cytoplasm; DNA-binding; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; S-adenosyl-L-methionine; Transferase; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   912  912     DNA (cytosine-5)-methyltransferase 3A. PRO_0000088043
DOMAIN   292   350  59     PWWP. 
ZN_FING   494   586  93     ADD-type. 
REGION   199   403  205     Interaction with DNMT1 and DNMT3B. 
REGION   494   586  93     Interaction with the PRC2/EED-EZH2 complex (By similarity). 
ACT_SITE   710   710        By similarity. 
MOD_RES   105   105        Phosphoserine. 
VAR_SEQ   1   223        Missing (in isoform 2). VSP_029985
STRAND   631   636  6      
TURN   639   641  3      
HELIX   642   649  8      
STRAND   654   660  7      
HELIX   664   673  10      
TURN   674   676  3      
STRAND   678   681  4      
HELIX   684   686  3      
HELIX   689   694  6      
STRAND   699   703  5      
HELIX   708   710  3      
TURN   719   721  3      
TURN   723   726  4      
HELIX   727   738  12      
STRAND   749   758  10      
HELIX   760   770  11      
HELIX   779   781  3      
STRAND   783   785  3      
STRAND   788   793  6      
STRAND   798   800  3      
HELIX   812   814  3      
STRAND   821   827  7      
STRAND   847   849  3      
STRAND   852   854  3      
HELIX   858   865  8      
TURN   869   872  4      
HELIX   879   887  9      
HELIX   892   899  8      
HELIX   900   905  6      
Sequence information
Length: 912 AA [This is the length of the unprocessed precursor] Molecular weight: 101858 Da [This is the MW of the unprocessed precursor] CRC64: BD1FF7C5B4F54A33 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPAMPSSGPG DTSSSAAERE EDRKDGEEQE EPRGKEERQE PSTTARKVGR PGRKRKHPPV 

        70         80         90        100        110        120 
ESGDTPKDPA VISKSPSMAQ DSGASELLPN GDLEKRSEPQ PEEGSPAGGQ KGGAPAEGEG 

       130        140        150        160        170        180 
AAETLPEASR AVENGCCTPK EGRGAPAEAG KEQKETNIES MKMEGSRGRL RGGLGWESSL 

       190        200        210        220        230        240 
RQRPMPRLTF QAGDPYYISK RKRDEWLARW KREAEKKAKV IAGMNAVEEN QGPGESQKVE 

       250        260        270        280        290        300 
EASPPAVQQP TDPASPTVAT TPEPVGSDAG DKNATKAGDD EPEYEDGRGF GIGELVWGKL 

       310        320        330        340        350        360 
RGFSWWPGRI VSWWMTGRSR AAEGTRWVMW FGDGKFSVVC VEKLMPLSSF CSAFHQATYN 

       370        380        390        400        410        420 
KQPMYRKAIY EVLQVASSRA GKLFPVCHDS DESDTAKAVE VQNKPMIEWA LGGFQPSGPK 

       430        440        450        460        470        480 
GLEPPEEEKN PYKEVYTDMW VEPEAAAYAP PPPAKKPRKS TAEKPKVKEI IDERTRERLV 

       490        500        510        520        530        540 
YEVRQKCRNI EDICISCGSL NVTLEHPLFV GGMCQNCKNC FLECAYQYDD DGYQSYCTIC 

       550        560        570        580        590        600 
CGGREVLMCG NNNCCRCFCV ECVDLLVGPG AAQAAIKEDP WNCYMCGHKG TYGLLRRRED 

       610        620        630        640        650        660 
WPSRLQMFFA NNHDQEFDPP KVYPPVPAEK RKPIRVLSLF DGIATGLLVL KDLGIQVDRY 

       670        680        690        700        710        720 
IASEVCEDSI TVGMVRHQGK IMYVGDVRSV TQKHIQEWGP FDLVIGGSPC NDLSIVNPAR 

       730        740        750        760        770        780 
KGLYEGTGRL FFEFYRLLHD ARPKEGDDRP FFWLFENVVA MGVSDKRDIS RFLESNPVMI 

       790        800        810        820        830        840 
DAKEVSAAHR ARYFWGNLPG MNRPLASTVN DKLELQECLE HGRIAKFSKV RTITTRSNSI 

       850        860        870        880        890        900 
KQGKDQHFPV FMNEKEDILW CTEMERVFGF PVHYTDVSNM SRLARQRLLG RSWSVPVIRH 

       910 
LFAPLKEYFA CV 

Q9Y6K1 in FASTA format

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