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Q9Y6K1 (DNM3A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA (cytosine-5)-methyltransferase 3A

Short name=Dnmt3a
EC=2.1.1.37
Alternative name(s):
DNA methyltransferase HsaIIIA
Short name=DNA MTase HsaIIIA
Short name=M.HsaIIIA
Gene names
Name:DNMT3A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length912 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for genome-wide de novo methylation and is essential for the establishment of DNA methylation patterns during development. DNA methylation is coordinated with methylation of histones. It modifies DNA in a non-processive manner and also methylates non-CpG sites. May preferentially methylate DNA linker between 2 nucleosomal cores and is inhibited by histone H1. Plays a role in paternal and maternal imprinting. Required for methylation of most imprinted loci in germ cells. Acts as a transcriptional corepressor for ZBTB18. Recruited to trimethylated 'Lys-36' of histone H3 (H3K36me3) sites. Can actively repress transcription through the recruitment of HDAC activity. Ref.10

Catalytic activity

S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine.

Enzyme regulation

Activated by binding to the regulatory factor DNMT3L By similarity.

Subunit structure

Heterotetramer composed of 1 DNMT3A homodimer and 2 DNMT3L subunits (DNMT3L-DNMT3A-DNMT3A-DNMT3L). Interacts with UBC9, PIAS1 and PIAS2 By similarity. Binds the ZBTB18 transcriptional repressor. Interacts with SETDB1. Associates with HDAC1 through its ADD domain. Interacts with UHRF1 By similarity. Interacts with DNMT1 and DNMT3B. Interacts with the PRC2/EED-EZH2 complex. Interacts with MPHOSPH8. Interacts with histone H3 that is not methylated at 'Lys-4' (H3K4). Ref.3 Ref.9 Ref.10 Ref.14 Ref.17 Ref.18 Ref.19

Subcellular location

Nucleus. Cytoplasm. Note: Accumulates in the major satellite repeats at pericentric heterochromatin By similarity. Ref.3

Tissue specificity

Highly expressed in fetal tissues, skeletal muscle, heart, peripheral blood mononuclear cells, kidney, and at lower levels in placenta, brain, liver, colon, spleen, small intestine and lung. Ref.7

Domain

The PWWP domain is essential for targeting to pericentric heterochromatin. It specifically recognizes and binds trimethylated 'Lys-36' of histone H3 (H3K36me3) By similarity.

Post-translational modification

Sumoylated; sumoylation disrupts the ability to interact with histone deacetylases (HDAC1 and HDAC2) and repress transcription By similarity.

Sequence similarities

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.

Contains 1 ADD domain.

Contains 1 GATA-type zinc finger.

Contains 1 PHD-type zinc finger.

Contains 1 PWWP domain.

Contains 1 SAM-dependent MTase C5-type domain.

Caution

It is uncertain whether Met-1 or Met-4 is the initiator.

Sequence caution

The sequence AAL57039.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAN40037.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Methyltransferase
Repressor
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processC-5 methylation of cytosine

Inferred from direct assay Ref.2. Source: GOC

DNA methylation

Inferred from direct assay Ref.2. Source: UniProtKB

DNA methylation involved in embryo development

Inferred from electronic annotation. Source: Ensembl

DNA methylation involved in gamete generation

Inferred from electronic annotation. Source: Ensembl

DNA methylation on cytosine within a CG sequence

Inferred from electronic annotation. Source: Ensembl

S-adenosylhomocysteine metabolic process

Inferred from electronic annotation. Source: Ensembl

S-adenosylmethioninamine metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

hypermethylation of CpG island

Inferred from electronic annotation. Source: Ensembl

methylation-dependent chromatin silencing

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression by genetic imprinting

Traceable author statement Ref.2. Source: UniProtKB

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentchromosome, centromeric region

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.2. Source: UniProtKB

euchromatin

Inferred from direct assay Ref.2. Source: UniProtKB

nuclear heterochromatin

Inferred from electronic annotation. Source: Ensembl

nuclear matrix

Inferred from direct assay Ref.2. Source: UniProtKB

nucleus

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionDNA (cytosine-5-)-methyltransferase activity

Inferred from direct assay Ref.2. Source: UniProtKB

DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates

Inferred from electronic annotation. Source: Ensembl

DNA binding

Inferred from direct assay Ref.2. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.17. Source: UniProtKB

unmethylated CpG binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y6K1-1)

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.
Isoform 2 (identifier: Q9Y6K1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-213: MPAMPSSGPG...DEWLARWKRE → MGILERVVRRNGRVDRSLKDECDT
Note: It is uncertain whether Met-1 or Met-35 is the initiator.
Isoform 3 (identifier: Q9Y6K1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     151-166: KEQKETNIESMKMEGS → ESSAPGAASSGPTSIP
     167-912: Missing.
Note: Produced by alternative splicing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 912912DNA (cytosine-5)-methyltransferase 3A
PRO_0000088043

Regions

Domain292 – 35059PWWP
Domain482 – 614133ADD
Domain634 – 912279SAM-dependent MTase C5-type
Zinc finger493 – 52331GATA-type; atypical
Zinc finger534 – 59057PHD-type; atypical
Region199 – 403205Interaction with DNMT1 and DNMT3B
Region494 – 58693Interaction with the PRC2/EED-EZH2 complex By similarity
Region641 – 6455S-adenosyl-L-methionine binding Probable
Region686 – 6883S-adenosyl-L-methionine binding Probable
Region891 – 8933S-adenosyl-L-methionine binding Probable

Sites

Active site7101 By similarity
Binding site6641S-adenosyl-L-methionine Probable

Amino acid modifications

Modified residue1051Phosphoserine Ref.8 Ref.13 Ref.16
Modified residue2431Phosphoserine Ref.15 Ref.16
Modified residue2551Phosphoserine Ref.16
Modified residue2611Phosphothreonine Ref.16
Modified residue2671Phosphoserine Ref.16

Natural variations

Alternative sequence1 – 213213MPAMP…RWKRE → MGILERVVRRNGRVDRSLKD ECDT in isoform 2.
VSP_046254
Alternative sequence151 – 16616KEQKE…KMEGS → ESSAPGAASSGPTSIP in isoform 3.
VSP_040998
Alternative sequence167 – 912746Missing in isoform 3.
VSP_040999
Natural variant6991G → D in a patient with chronic myelomonocytic leukemia. Ref.21
VAR_067234
Natural variant7311Missing in a patient with chronic myelomonocytic leukemia. Ref.21
VAR_067235
Natural variant8821R → C in a patient with chronic myelomonocytic leukemia; somatic mutation. Ref.21
VAR_067236
Natural variant8821R → H in a patient with chronic myelomonocytic leukemia; somatic mutation. Ref.21
VAR_067237
Natural variant8821R → P in a patient with chronic myelomonocytic leukemia; somatic mutation. Ref.21
VAR_067238

Experimental info

Mutagenesis7321F → A: Loss of activity du to the incapacity to bind the regulatory subunit DNMT3L. Ref.17

Secondary structure

............................................................................................................... 912
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 15, 2008. Version 4.
Checksum: BD1FF7C5B4F54A33

FASTA912101,858
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 19341BDAE1B71C8B
Show »

FASTA72381,613
Isoform 3 [UniParc].

Checksum: 78756A71196D61B5
Show »

FASTA16616,866

References

« Hide 'large scale' references
[1]"Cloning, expression and chromosome locations of the human DNMT3 gene family."
Xie S., Wang Z., Okano M., Nogami M., Li Y., He W.-W., Okumura K., Li E.
Gene 236:87-95(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal testis.
[2]"A novel Dnmt3a isoform produced from an alternative promoter localizes to euchromatin and its expression correlates with active de novo methylation."
Chen T., Ueda Y., Xie S., Li E.
J. Biol. Chem. 277:38746-38754(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]"Co-operation and communication between the human maintenance and de novo DNA (cytosine-5) methyltransferases."
Kim G.-D., Ni J., Kelesoglu N., Roberts R.J., Pradhan S.
EMBO J. 21:4183-4195(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DNMT1 AND DNMT3B, SUBCELLULAR LOCATION.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 3).
Tissue: Lung, PNS and Skin.
[7]"The human DNA methyltransferases (DNMTs) 1, 3a and 3b: coordinate mRNA expression in normal tissues and overexpression in tumors."
Robertson K.D., Uzvolgyi E., Liang G., Talmadge C., Sumegi J., Gonzales F.A., Jones P.A.
Nucleic Acids Res. 27:2291-2298(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"The histone methyltransferase SETDB1 and the DNA methyltransferase DNMT3A interact directly and localize to promoters silenced in cancer cells."
Li H., Rauch T., Chen Z.-X., Szabo P.E., Riggs A.D., Pfeifer G.P.
J. Biol. Chem. 281:19489-19500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SETDB1.
[10]"The Polycomb group protein EZH2 directly controls DNA methylation."
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 439:871-874(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH THE PRC2/EED-EZH2 COMPLEX.
[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]"Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer."
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.
Nat. Genet. 39:232-236(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: DE NOVO DNA METHYLATION OF TARGET GENES.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, 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]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-243; SER-255; THR-261 AND SER-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA methylation."
Jia D., Jurkowska R.Z., Zhang X., Jeltsch A., Cheng X.
Nature 449:248-251(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 627-909 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, SUBUNIT, MUTAGENESIS OF PHE-732.
[18]"Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX-DNMT3-DNMT3L domain."
Otani J., Nankumo T., Arita K., Inamoto S., Ariyoshi M., Shirakawa M.
EMBO Rep. 10:1235-1241(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 476-614 IN COMPLEXES WITH ZINC AND WITH HISTONE H3 PEPTIDE, SUBUNIT.
[19]"MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a."
Chang Y., Sun L., Kokura K., Horton J.R., Fukuda M., Espejo A., Izumi V., Koomen J.M., Bedford M.T., Zhang X., Shinkai Y., Fang J., Cheng X.
Nat. Commun. 2:533-533(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 40-53 IN COMPLEX WITH MPHOSPH8, INTERACTION WITH MPHOSPH8.
[20]"Structural and histone binding ability characterizations of human PWWP domains."
Wu H., Zeng H., Lam R., Tempel W., Amaya M.F., Xu C., Dombrovski L., Qiu W., Wang Y., Min J.
PLoS ONE 6:E18919-E18919(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 275-427.
[21]"Mutational spectrum analysis of chronic myelomonocytic leukemia includes genes associated with epigenetic regulation: UTX, EZH2, and DNMT3A."
Jankowska A.M., Makishima H., Tiu R.V., Szpurka H., Huang Y., Traina F., Visconte V., Sugimoto Y., Prince C., O'Keefe C., Hsi E.D., List A., Sekeres M.A., Rao A., McDevitt M.A., Maciejewski J.P.
Blood 118:3932-3941(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ASP-699; PHE-731 DEL; CYS-882; HIS-882 AND PRO-882.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF067972 mRNA. Translation: AAD33084.2.
AF480163 mRNA. Translation: AAN40037.1. Different initiation.
AF331856 mRNA. Translation: AAL57039.1. Different initiation.
AC012074 Genomic DNA. Translation: AAY14761.1.
CH471053 Genomic DNA. Translation: EAX00727.1.
BC032392 mRNA. Translation: AAH32392.1.
BC043617 mRNA. Translation: AAH43617.1.
BC051864 mRNA. Translation: AAH51864.1.
CCDSCCDS1718.2. [Q9Y6K1-2]
CCDS33157.1. [Q9Y6K1-1]
CCDS46232.1. [Q9Y6K1-3]
RefSeqNP_072046.2. NM_022552.4. [Q9Y6K1-1]
NP_715640.2. NM_153759.3. [Q9Y6K1-2]
NP_783328.1. NM_175629.2. [Q9Y6K1-1]
NP_783329.1. NM_175630.1. [Q9Y6K1-3]
XP_005264232.1. XM_005264175.2. [Q9Y6K1-1]
XP_005264233.1. XM_005264176.1. [Q9Y6K1-1]
XP_005264234.1. XM_005264177.2.
UniGeneHs.515840.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QRVX-ray2.89A/D/E/H627-912[»]
3A1AX-ray2.30A476-614[»]
3A1BX-ray2.29A476-614[»]
3LLRX-ray2.30A/B/C/D/E275-427[»]
3SVMX-ray2.31P40-53[»]
ProteinModelPortalQ9Y6K1.
SMRQ9Y6K1. Positions 283-425, 475-912.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108125. 53 interactions.
DIPDIP-38004N.
IntActQ9Y6K1. 20 interactions.
STRING9606.ENSP00000264709.

Chemistry

ChEMBLCHEMBL1992.

Protein family/group databases

REBASE4119. M.HsaDnmt3A.

PTM databases

PhosphoSiteQ9Y6K1.

Polymorphism databases

DMDM166215081.

Proteomic databases

MaxQBQ9Y6K1.
PaxDbQ9Y6K1.
PRIDEQ9Y6K1.

Protocols and materials databases

DNASU1788.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264709; ENSP00000264709; ENSG00000119772. [Q9Y6K1-1]
ENST00000321117; ENSP00000324375; ENSG00000119772. [Q9Y6K1-1]
ENST00000380746; ENSP00000370122; ENSG00000119772. [Q9Y6K1-2]
ENST00000402667; ENSP00000384237; ENSG00000119772.
ENST00000406659; ENSP00000384852; ENSG00000119772. [Q9Y6K1-3]
GeneID1788.
KEGGhsa:1788.
UCSCuc002rgc.4. human. [Q9Y6K1-1]
uc002rgf.3. human. [Q9Y6K1-3]

Organism-specific databases

CTD1788.
GeneCardsGC02M025455.
HGNCHGNC:2978. DNMT3A.
HPACAB009469.
HPA026588.
MIM602769. gene.
neXtProtNX_Q9Y6K1.
PharmGKBPA27445.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG70699.
HOGENOMHOG000230875.
HOVERGENHBG051381.
InParanoidQ9Y6K1.
KOK17398.
OMAFVGGMCQ.
OrthoDBEOG7MWGW6.
PhylomeDBQ9Y6K1.
TreeFamTF329039.

Enzyme and pathway databases

BRENDA2.1.1.37. 2681.
ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9Y6K1.
BgeeQ9Y6K1.
CleanExHS_DNMT3A.
GenevestigatorQ9Y6K1.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
InterProIPR025766. ADD.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR025811. C5_MeTrfase_3.
IPR000313. PWWP_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF00145. DNA_methylase. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
SMARTSM00293. PWWP. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
PROSITEPS51533. ADD. 1 hit.
PS00094. C5_MTASE_1. 1 hit.
PS50812. PWWP. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y6K1.
GenomeRNAi1788.
NextBio7279.
PROQ9Y6K1.
SOURCESearch...

Entry information

Entry nameDNM3A_HUMAN
AccessionPrimary (citable) accession number: Q9Y6K1
Secondary accession number(s): E9PEB8 expand/collapse secondary AC list , Q86TE8, Q86XF5, Q8IZV0, Q8WXU9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 15, 2008
Last modified: July 9, 2014
This is version 129 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM