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Q9Y6K1

- DNM3A_HUMAN

UniProt

Q9Y6K1 - DNM3A_HUMAN

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Protein
DNA (cytosine-5)-methyltransferase 3A
Gene
DNMT3A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Enzyme regulationi

Activated by binding to the regulatory factor DNMT3L By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei664 – 6641S-adenosyl-L-methionine Inferred
Active sitei710 – 7101 By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri493 – 52331GATA-type; atypical
Add
BLAST
Zinc fingeri534 – 59057PHD-type; atypical
Add
BLAST

GO - Molecular functioni

  1. DNA (cytosine-5-)-methyltransferase activity Source: UniProtKB
  2. DNA (cytosine-5-)-methyltransferase activity, acting on CpG substrates Source: Ensembl
  3. DNA binding Source: UniProtKB
  4. chromatin binding Source: Ensembl
  5. metal ion binding Source: UniProtKB-KW
  6. protein binding Source: UniProtKB
  7. unmethylated CpG binding Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. C-5 methylation of cytosine Source: GOC
  2. DNA methylation Source: UniProtKB
  3. DNA methylation involved in embryo development Source: Ensembl
  4. DNA methylation involved in gamete generation Source: Ensembl
  5. DNA methylation on cytosine within a CG sequence Source: Ensembl
  6. S-adenosylhomocysteine metabolic process Source: Ensembl
  7. S-adenosylmethioninamine metabolic process Source: Ensembl
  8. cellular response to amino acid stimulus Source: Ensembl
  9. hypermethylation of CpG island Source: Ensembl
  10. methylation-dependent chromatin silencing Source: Ensembl
  11. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  12. regulation of gene expression by genetic imprinting Source: UniProtKB
  13. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BRENDAi2.1.1.37. 2681.
ReactomeiREACT_200808. PRC2 methylates histones and DNA.

Protein family/group databases

REBASEi4119. M.HsaDnmt3A.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA (cytosine-5)-methyltransferase 3A (EC:2.1.1.37)
Short name:
Dnmt3a
Alternative name(s):
DNA methyltransferase HsaIIIA
Short name:
DNA MTase HsaIIIA
Short name:
M.HsaIIIA
Gene namesi
Name:DNMT3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:2978. DNMT3A.

Subcellular locationi

Nucleus. Cytoplasm
Note: Accumulates in the major satellite repeats at pericentric heterochromatin By similarity.1 Publication

GO - Cellular componenti

  1. chromosome, centromeric region Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. euchromatin Source: UniProtKB
  4. nuclear heterochromatin Source: Ensembl
  5. nuclear matrix Source: UniProtKB
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi732 – 7321F → A: Loss of activity du to the incapacity to bind the regulatory subunit DNMT3L. 1 Publication

Organism-specific databases

PharmGKBiPA27445.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 912912DNA (cytosine-5)-methyltransferase 3A
PRO_0000088043Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051Phosphoserine3 Publications
Modified residuei243 – 2431Phosphoserine2 Publications
Modified residuei255 – 2551Phosphoserine1 Publication
Modified residuei261 – 2611Phosphothreonine1 Publication
Modified residuei267 – 2671Phosphoserine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9Y6K1.
PaxDbiQ9Y6K1.
PRIDEiQ9Y6K1.

PTM databases

PhosphoSiteiQ9Y6K1.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

ArrayExpressiQ9Y6K1.
BgeeiQ9Y6K1.
CleanExiHS_DNMT3A.
GenevestigatoriQ9Y6K1.

Organism-specific databases

HPAiCAB009469.
HPA026588.

Interactioni

Subunit structurei

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).7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EEDO755302EBI-923653,EBI-923794
EZH2Q159106EBI-923653,EBI-530054
H3F3BP842437EBI-923653,EBI-120658
SETDB1Q150477EBI-923653,EBI-79691
UHRF1Q96T887EBI-923653,EBI-1548946

Protein-protein interaction databases

BioGridi108125. 53 interactions.
DIPiDIP-38004N.
IntActiQ9Y6K1. 20 interactions.
STRINGi9606.ENSP00000264709.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi295 – 2984
Beta strandi306 – 3116
Helixi313 – 3153
Beta strandi325 – 3306
Turni331 – 3333
Beta strandi336 – 3405
Helixi341 – 3433
Beta strandi344 – 3463
Helixi347 – 3493
Helixi350 – 3534
Helixi356 – 3616
Helixi363 – 38018
Helixi399 – 41113
Turni415 – 4173
Helixi419 – 4224
Helixi476 – 4849
Helixi490 – 4923
Turni495 – 4973
Beta strandi507 – 5137
Helixi515 – 52410
Beta strandi532 – 5365
Turni538 – 5403
Beta strandi544 – 5485
Turni552 – 5543
Beta strandi557 – 5593
Helixi560 – 5667
Helixi571 – 5766
Beta strandi578 – 5803
Turni584 – 5863
Beta strandi595 – 5973
Helixi601 – 6099
Beta strandi634 – 6396
Turni642 – 6443
Helixi645 – 6528
Beta strandi657 – 6637
Helixi667 – 67610
Turni677 – 6793
Beta strandi681 – 6844
Helixi687 – 6893
Helixi692 – 6976
Beta strandi702 – 7065
Helixi711 – 7133
Turni722 – 7243
Turni726 – 7294
Helixi730 – 74112
Beta strandi752 – 76110
Helixi763 – 77311
Helixi782 – 7843
Beta strandi786 – 7883
Beta strandi791 – 7966
Beta strandi801 – 8033
Helixi815 – 8173
Beta strandi824 – 8307
Beta strandi850 – 8523
Beta strandi855 – 8573
Helixi861 – 8688
Turni872 – 8754
Helixi882 – 8909
Helixi895 – 9028
Helixi903 – 9086

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliQ9Y6K1.
SMRiQ9Y6K1. Positions 283-425, 475-912.

Miscellaneous databases

EvolutionaryTraceiQ9Y6K1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini292 – 35059PWWP
Add
BLAST
Domaini482 – 614133ADD
Add
BLAST
Domaini634 – 912279SAM-dependent MTase C5-type
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni199 – 403205Interaction with DNMT1 and DNMT3B
Add
BLAST
Regioni494 – 58693Interaction with the PRC2/EED-EZH2 complex By similarity
Add
BLAST
Regioni641 – 6455S-adenosyl-L-methionine binding Inferred
Regioni686 – 6883S-adenosyl-L-methionine binding Inferred
Regioni891 – 8933S-adenosyl-L-methionine binding Inferred

Domaini

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

Sequence similaritiesi

Contains 1 ADD domain.
Contains 1 PWWP domain.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG70699.
HOGENOMiHOG000230875.
HOVERGENiHBG051381.
InParanoidiQ9Y6K1.
KOiK17398.
OMAiFVGGMCQ.
OrthoDBiEOG7MWGW6.
PhylomeDBiQ9Y6K1.
TreeFamiTF329039.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025766. ADD.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR025811. C5_MeTrfase_3.
IPR000313. PWWP_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF00145. DNA_methylase. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view]
SMARTiSM00293. PWWP. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS51533. ADD. 1 hit.
PS00094. C5_MTASE_1. 1 hit.
PS50812. PWWP. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative promoter usage and alternative splicing. Align

Isoform 1 (identifier: Q9Y6K1-1) [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

MPAMPSSGPG DTSSSAAERE EDRKDGEEQE EPRGKEERQE PSTTARKVGR    50
PGRKRKHPPV ESGDTPKDPA VISKSPSMAQ DSGASELLPN GDLEKRSEPQ 100
PEEGSPAGGQ KGGAPAEGEG AAETLPEASR AVENGCCTPK EGRGAPAEAG 150
KEQKETNIES MKMEGSRGRL RGGLGWESSL RQRPMPRLTF QAGDPYYISK 200
RKRDEWLARW KREAEKKAKV IAGMNAVEEN QGPGESQKVE EASPPAVQQP 250
TDPASPTVAT TPEPVGSDAG DKNATKAGDD EPEYEDGRGF GIGELVWGKL 300
RGFSWWPGRI VSWWMTGRSR AAEGTRWVMW FGDGKFSVVC VEKLMPLSSF 350
CSAFHQATYN KQPMYRKAIY EVLQVASSRA GKLFPVCHDS DESDTAKAVE 400
VQNKPMIEWA LGGFQPSGPK GLEPPEEEKN PYKEVYTDMW VEPEAAAYAP 450
PPPAKKPRKS TAEKPKVKEI IDERTRERLV YEVRQKCRNI EDICISCGSL 500
NVTLEHPLFV GGMCQNCKNC FLECAYQYDD DGYQSYCTIC CGGREVLMCG 550
NNNCCRCFCV ECVDLLVGPG AAQAAIKEDP WNCYMCGHKG TYGLLRRRED 600
WPSRLQMFFA NNHDQEFDPP KVYPPVPAEK RKPIRVLSLF DGIATGLLVL 650
KDLGIQVDRY IASEVCEDSI TVGMVRHQGK IMYVGDVRSV TQKHIQEWGP 700
FDLVIGGSPC NDLSIVNPAR KGLYEGTGRL FFEFYRLLHD ARPKEGDDRP 750
FFWLFENVVA MGVSDKRDIS RFLESNPVMI DAKEVSAAHR ARYFWGNLPG 800
MNRPLASTVN DKLELQECLE HGRIAKFSKV RTITTRSNSI KQGKDQHFPV 850
FMNEKEDILW CTEMERVFGF PVHYTDVSNM SRLARQRLLG RSWSVPVIRH 900
LFAPLKEYFA CV 912
Length:912
Mass (Da):101,858
Last modified:January 15, 2008 - v4
Checksum:iBD1FF7C5B4F54A33
GO
Isoform 2 (identifier: Q9Y6K1-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:723
Mass (Da):81,613
Checksum:i19341BDAE1B71C8B
GO
Isoform 3 (identifier: Q9Y6K1-3) [UniParc]FASTAAdd to Basket

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

Note: Produced by alternative splicing.

Show »
Length:166
Mass (Da):16,866
Checksum:i78756A71196D61B5
GO

Sequence cautioni

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti699 – 6991G → D in a patient with chronic myelomonocytic leukemia. 1 Publication
VAR_067234
Natural varianti731 – 7311Missing in a patient with chronic myelomonocytic leukemia. 1 Publication
VAR_067235
Natural varianti882 – 8821R → C in a patient with chronic myelomonocytic leukemia; somatic mutation. 1 Publication
VAR_067236
Natural varianti882 – 8821R → H in a patient with chronic myelomonocytic leukemia; somatic mutation. 1 Publication
VAR_067237
Natural varianti882 – 8821R → P in a patient with chronic myelomonocytic leukemia; somatic mutation. 1 Publication
VAR_067238

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 213213MPAMP…RWKRE → MGILERVVRRNGRVDRSLKD ECDT in isoform 2.
VSP_046254Add
BLAST
Alternative sequencei151 – 16616KEQKE…KMEGS → ESSAPGAASSGPTSIP in isoform 3.
VSP_040998Add
BLAST
Alternative sequencei167 – 912746Missing in isoform 3.
VSP_040999Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1718.2. [Q9Y6K1-2]
CCDS33157.1. [Q9Y6K1-1]
CCDS46232.1. [Q9Y6K1-3]
RefSeqiNP_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.
UniGeneiHs.515840.

Genome annotation databases

EnsembliENST00000264709; ENSP00000264709; ENSG00000119772. [Q9Y6K1-1]
ENST00000321117; ENSP00000324375; ENSG00000119772. [Q9Y6K1-1]
ENST00000380746; ENSP00000370122; ENSG00000119772. [Q9Y6K1-2]
ENST00000402667; ENSP00000384237; ENSG00000119772.
ENST00000406659; ENSP00000384852; ENSG00000119772. [Q9Y6K1-3]
GeneIDi1788.
KEGGihsa:1788.
UCSCiuc002rgc.4. human. [Q9Y6K1-1]
uc002rgf.3. human. [Q9Y6K1-3]

Polymorphism databases

DMDMi166215081.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1718.2. [Q9Y6K1-2 ]
CCDS33157.1. [Q9Y6K1-1 ]
CCDS46232.1. [Q9Y6K1-3 ]
RefSeqi NP_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.
UniGenei Hs.515840.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QRV X-ray 2.89 A/D/E/H 627-912 [» ]
3A1A X-ray 2.30 A 476-614 [» ]
3A1B X-ray 2.29 A 476-614 [» ]
3LLR X-ray 2.30 A/B/C/D/E 275-427 [» ]
3SVM X-ray 2.31 P 40-53 [» ]
ProteinModelPortali Q9Y6K1.
SMRi Q9Y6K1. Positions 283-425, 475-912.
ModBasei Search...

Protein-protein interaction databases

BioGridi 108125. 53 interactions.
DIPi DIP-38004N.
IntActi Q9Y6K1. 20 interactions.
STRINGi 9606.ENSP00000264709.

Chemistry

ChEMBLi CHEMBL1992.

Protein family/group databases

REBASEi 4119. M.HsaDnmt3A.

PTM databases

PhosphoSitei Q9Y6K1.

Polymorphism databases

DMDMi 166215081.

Proteomic databases

MaxQBi Q9Y6K1.
PaxDbi Q9Y6K1.
PRIDEi Q9Y6K1.

Protocols and materials databases

DNASUi 1788.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264709 ; ENSP00000264709 ; ENSG00000119772 . [Q9Y6K1-1 ]
ENST00000321117 ; ENSP00000324375 ; ENSG00000119772 . [Q9Y6K1-1 ]
ENST00000380746 ; ENSP00000370122 ; ENSG00000119772 . [Q9Y6K1-2 ]
ENST00000402667 ; ENSP00000384237 ; ENSG00000119772 .
ENST00000406659 ; ENSP00000384852 ; ENSG00000119772 . [Q9Y6K1-3 ]
GeneIDi 1788.
KEGGi hsa:1788.
UCSCi uc002rgc.4. human. [Q9Y6K1-1 ]
uc002rgf.3. human. [Q9Y6K1-3 ]

Organism-specific databases

CTDi 1788.
GeneCardsi GC02M025455.
HGNCi HGNC:2978. DNMT3A.
HPAi CAB009469.
HPA026588.
MIMi 602769. gene.
neXtProti NX_Q9Y6K1.
PharmGKBi PA27445.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG70699.
HOGENOMi HOG000230875.
HOVERGENi HBG051381.
InParanoidi Q9Y6K1.
KOi K17398.
OMAi FVGGMCQ.
OrthoDBi EOG7MWGW6.
PhylomeDBi Q9Y6K1.
TreeFami TF329039.

Enzyme and pathway databases

BRENDAi 2.1.1.37. 2681.
Reactomei REACT_200808. PRC2 methylates histones and DNA.

Miscellaneous databases

EvolutionaryTracei Q9Y6K1.
GenomeRNAii 1788.
NextBioi 7279.
PROi Q9Y6K1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y6K1.
Bgeei Q9Y6K1.
CleanExi HS_DNMT3A.
Genevestigatori Q9Y6K1.

Family and domain databases

Gene3Di 3.40.50.150. 1 hit.
InterProi IPR025766. ADD.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR025811. C5_MeTrfase_3.
IPR000313. PWWP_dom.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF00145. DNA_methylase. 1 hit.
PF00855. PWWP. 1 hit.
[Graphical view ]
SMARTi SM00293. PWWP. 1 hit.
[Graphical view ]
SUPFAMi SSF53335. SSF53335. 1 hit.
PROSITEi PS51533. ADD. 1 hit.
PS00094. C5_MTASE_1. 1 hit.
PS50812. PWWP. 1 hit.
PS51679. SAM_MT_C5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: FUNCTION, INTERACTION WITH THE PRC2/EED-EZH2 COMPLEX.
  11. "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.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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.
  14. "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.
  15. "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].
  16. "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.
  17. "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.
  18. "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.
  19. "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.
  20. "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.

Entry informationi

Entry nameiDNM3A_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6K1
Secondary accession number(s): E9PEB8
, Q86TE8, Q86XF5, Q8IZV0, Q8WXU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 15, 2008
Last modified: September 3, 2014
This is version 130 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 2
    Human chromosome 2: 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

External Data

Dasty 3

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