Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA (cytosine-5)-methyltransferase 3A

Gene

DNMT3A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation

Enzyme regulationi

Activated by binding to the regulatory factor DNMT3L.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei664S-adenosyl-L-methionineCurated1
Active sitei710PROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri493 – 523GATA-type; atypicalPROSITE-ProRule annotationAdd BLAST31
Zinc fingeri534 – 590PHD-type; atypicalPROSITE-ProRule annotationAdd BLAST57

GO - Molecular functioni

GO - Biological processi

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

BioCyciZFISH:HS04338-MONOMER.
BRENDAi2.1.1.37. 2681.
ReactomeiR-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-5334118. DNA methylation.
SIGNORiQ9Y6K1.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:2978. DNMT3A.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication

  • Note: Accumulates in the major satellite repeats at pericentric heterochromatin.By similarity

GO - Cellular componenti

  • chromosome, centromeric region Source: Ensembl
  • cytoplasm Source: UniProtKB
  • euchromatin Source: UniProtKB
  • nuclear heterochromatin Source: Ensembl
  • nuclear matrix Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • XY body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Tatton-Brown-Rahman syndrome (TBRS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn overgrowth syndrome characterized by a distinctive facial appearance, tall stature and intellectual disability. Facial gestalt is characterized by a round face, heavy horizontal eyebrows and narrow palpebral fissures. Less common features include atrial septal defects, seizures, umbilical hernia, and scoliosis.
See also OMIM:615879
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071463310I → N in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs587777508dbSNPEnsembl.1
Natural variantiVAR_071464532G → S in TBRS; somatic mutation. 1 Publication1
Natural variantiVAR_071465548M → K in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs587777509dbSNPEnsembl.1
Natural variantiVAR_071466549C → R in TBRS; somatic mutation. 1 Publication1
Natural variantiVAR_071467648L → P in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs587777507dbSNPEnsembl.1
Natural variantiVAR_071468700P → L in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs772368909dbSNPEnsembl.1
Natural variantiVAR_071469749R → C in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs754613602dbSNPEnsembl.1
Natural variantiVAR_071470838N → D in TBRS; somatic mutation. 1 Publication1
Natural variantiVAR_071471902F → S in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs587777510dbSNPEnsembl.1
Natural variantiVAR_071472904P → L in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs149095705dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi732F → A: Loss of activity du to the incapacity to bind the regulatory subunit DNMT3L. 1 Publication1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNETi1788.
MalaCardsiDNMT3A.
MIMi615879. phenotype.
OpenTargetsiENSG00000119772.
Orphaneti404443. Tall stature-intellectual disability-facial dysmorphism syndrome.
PharmGKBiPA27445.

Chemistry databases

ChEMBLiCHEMBL1992.

Polymorphism and mutation databases

BioMutaiDNMT3A.
DMDMi166215081.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000880431 – 912DNA (cytosine-5)-methyltransferase 3AAdd BLAST912

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei105PhosphoserineCombined sources1
Modified residuei124PhosphothreonineBy similarity1
Modified residuei171Omega-N-methylarginineBy similarity1
Modified residuei243PhosphoserineCombined sources1
Modified residuei255PhosphoserineCombined sources1
Modified residuei261PhosphothreonineCombined sources1
Modified residuei267PhosphoserineCombined sources1
Modified residuei390PhosphoserineBy similarity1
Modified residuei393PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y6K1.
PaxDbiQ9Y6K1.
PeptideAtlasiQ9Y6K1.
PRIDEiQ9Y6K1.

PTM databases

iPTMnetiQ9Y6K1.
PhosphoSitePlusiQ9Y6K1.

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

BgeeiENSG00000119772.
CleanExiHS_DNMT3A.
ExpressionAtlasiQ9Y6K1. baseline and differential.
GenevisibleiQ9Y6K1. HS.

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).By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-923653,EBI-923653
CREMQ030602EBI-923653,EBI-3907794
EEDO755302EBI-923653,EBI-923794
EZH2Q159106EBI-923653,EBI-530054
H3F3BP842437EBI-923653,EBI-120658
SETDB1Q150477EBI-923653,EBI-79691
SP100P234973EBI-923653,EBI-751145
TCL1AP562793EBI-923653,EBI-749995
UHRF1Q96T887EBI-923653,EBI-1548946

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi108125. 53 interactors.
DIPiDIP-38004N.
IntActiQ9Y6K1. 27 interactors.
STRINGi9606.ENSP00000264709.

Chemistry databases

BindingDBiQ9Y6K1.

Structurei

Secondary structure

1912
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi295 – 298Combined sources4
Beta strandi306 – 311Combined sources6
Helixi313 – 315Combined sources3
Beta strandi325 – 330Combined sources6
Turni331 – 333Combined sources3
Beta strandi336 – 340Combined sources5
Helixi341 – 343Combined sources3
Beta strandi344 – 346Combined sources3
Helixi347 – 349Combined sources3
Helixi350 – 353Combined sources4
Helixi356 – 361Combined sources6
Helixi363 – 380Combined sources18
Helixi393 – 395Combined sources3
Helixi399 – 411Combined sources13
Turni415 – 417Combined sources3
Helixi419 – 422Combined sources4
Helixi476 – 484Combined sources9
Helixi490 – 492Combined sources3
Turni495 – 497Combined sources3
Beta strandi502 – 505Combined sources4
Beta strandi507 – 514Combined sources8
Helixi515 – 524Combined sources10
Beta strandi532 – 536Combined sources5
Turni538 – 540Combined sources3
Beta strandi544 – 548Combined sources5
Turni552 – 554Combined sources3
Beta strandi557 – 559Combined sources3
Helixi560 – 566Combined sources7
Helixi571 – 577Combined sources7
Beta strandi578 – 580Combined sources3
Turni584 – 586Combined sources3
Beta strandi587 – 589Combined sources3
Beta strandi595 – 597Combined sources3
Helixi601 – 608Combined sources8
Helixi628 – 630Combined sources3
Beta strandi634 – 639Combined sources6
Turni642 – 644Combined sources3
Helixi645 – 652Combined sources8
Beta strandi657 – 663Combined sources7
Helixi667 – 676Combined sources10
Turni677 – 679Combined sources3
Beta strandi681 – 684Combined sources4
Helixi687 – 689Combined sources3
Helixi692 – 697Combined sources6
Beta strandi702 – 706Combined sources5
Helixi711 – 713Combined sources3
Turni722 – 724Combined sources3
Turni726 – 729Combined sources4
Helixi730 – 741Combined sources12
Beta strandi752 – 761Combined sources10
Helixi763 – 773Combined sources11
Beta strandi778 – 781Combined sources4
Helixi782 – 784Combined sources3
Beta strandi786 – 788Combined sources3
Beta strandi791 – 796Combined sources6
Beta strandi801 – 803Combined sources3
Helixi815 – 817Combined sources3
Beta strandi824 – 830Combined sources7
Beta strandi850 – 852Combined sources3
Beta strandi855 – 857Combined sources3
Helixi861 – 868Combined sources8
Turni872 – 875Combined sources4
Helixi882 – 890Combined sources9
Helixi895 – 902Combined sources8
Helixi903 – 908Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4QBQX-ray2.41A/C479-610[»]
4QBRX-ray1.90A/C476-611[»]
4QBSX-ray1.80A476-611[»]
4U7PX-ray3.82A455-912[»]
4U7TX-ray2.90A/C476-912[»]
ProteinModelPortaliQ9Y6K1.
SMRiQ9Y6K1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6K1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini292 – 350PWWPPROSITE-ProRule annotationAdd BLAST59
Domaini482 – 614ADDPROSITE-ProRule annotationAdd BLAST133
Domaini634 – 912SAM-dependent MTase C5-typePROSITE-ProRule annotationAdd BLAST279

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni199 – 403Interaction with DNMT1 and DNMT3B1 PublicationAdd BLAST205
Regioni494 – 586Interaction with the PRC2/EED-EZH2 complexBy similarityAdd BLAST93
Regioni641 – 645S-adenosyl-L-methionine bindingCurated5
Regioni686 – 688S-adenosyl-L-methionine bindingCurated3
Regioni891 – 893S-adenosyl-L-methionine bindingCurated3

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).By similarity

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. C5-methyltransferase family.PROSITE-ProRule annotation
Contains 1 ADD domain.PROSITE-ProRule annotation
Contains 1 GATA-type zinc finger.PROSITE-ProRule annotation
Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
Contains 1 PWWP domain.PROSITE-ProRule annotation
Contains 1 SAM-dependent MTase C5-type domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri493 – 523GATA-type; atypicalPROSITE-ProRule annotationAdd BLAST31
Zinc fingeri534 – 590PHD-type; atypicalPROSITE-ProRule annotationAdd BLAST57

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG410IGHW. Eukaryota.
ENOG410XQ4Y. LUCA.
GeneTreeiENSGT00390000008341.
HOGENOMiHOG000230875.
HOVERGENiHBG051381.
InParanoidiQ9Y6K1.
KOiK17398.
OMAiYTEMWVE.
OrthoDBiEOG091G01TP.
PhylomeDBiQ9Y6K1.
TreeFamiTF329039.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025766. ADD.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR030487. DNMT3A.
IPR000313. PWWP_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR23068:SF10. PTHR23068:SF10. 1 hit.
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. AlignAdd to basket

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

        10         20         30         40         50
MPAMPSSGPG DTSSSAAERE EDRKDGEEQE EPRGKEERQE PSTTARKVGR
60 70 80 90 100
PGRKRKHPPV ESGDTPKDPA VISKSPSMAQ DSGASELLPN GDLEKRSEPQ
110 120 130 140 150
PEEGSPAGGQ KGGAPAEGEG AAETLPEASR AVENGCCTPK EGRGAPAEAG
160 170 180 190 200
KEQKETNIES MKMEGSRGRL RGGLGWESSL RQRPMPRLTF QAGDPYYISK
210 220 230 240 250
RKRDEWLARW KREAEKKAKV IAGMNAVEEN QGPGESQKVE EASPPAVQQP
260 270 280 290 300
TDPASPTVAT TPEPVGSDAG DKNATKAGDD EPEYEDGRGF GIGELVWGKL
310 320 330 340 350
RGFSWWPGRI VSWWMTGRSR AAEGTRWVMW FGDGKFSVVC VEKLMPLSSF
360 370 380 390 400
CSAFHQATYN KQPMYRKAIY EVLQVASSRA GKLFPVCHDS DESDTAKAVE
410 420 430 440 450
VQNKPMIEWA LGGFQPSGPK GLEPPEEEKN PYKEVYTDMW VEPEAAAYAP
460 470 480 490 500
PPPAKKPRKS TAEKPKVKEI IDERTRERLV YEVRQKCRNI EDICISCGSL
510 520 530 540 550
NVTLEHPLFV GGMCQNCKNC FLECAYQYDD DGYQSYCTIC CGGREVLMCG
560 570 580 590 600
NNNCCRCFCV ECVDLLVGPG AAQAAIKEDP WNCYMCGHKG TYGLLRRRED
610 620 630 640 650
WPSRLQMFFA NNHDQEFDPP KVYPPVPAEK RKPIRVLSLF DGIATGLLVL
660 670 680 690 700
KDLGIQVDRY IASEVCEDSI TVGMVRHQGK IMYVGDVRSV TQKHIQEWGP
710 720 730 740 750
FDLVIGGSPC NDLSIVNPAR KGLYEGTGRL FFEFYRLLHD ARPKEGDDRP
760 770 780 790 800
FFWLFENVVA MGVSDKRDIS RFLESNPVMI DAKEVSAAHR ARYFWGNLPG
810 820 830 840 850
MNRPLASTVN DKLELQECLE HGRIAKFSKV RTITTRSNSI KQGKDQHFPV
860 870 880 890 900
FMNEKEDILW CTEMERVFGF PVHYTDVSNM SRLARQRLLG RSWSVPVIRH
910
LFAPLKEYFA CV
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAN40037 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_071463310I → N in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs587777508dbSNPEnsembl.1
Natural variantiVAR_071464532G → S in TBRS; somatic mutation. 1 Publication1
Natural variantiVAR_071465548M → K in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs587777509dbSNPEnsembl.1
Natural variantiVAR_071466549C → R in TBRS; somatic mutation. 1 Publication1
Natural variantiVAR_071467648L → P in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs587777507dbSNPEnsembl.1
Natural variantiVAR_067234699G → D in a patient with chronic myelomonocytic leukemia. 1 PublicationCorresponds to variant rs761064473dbSNPEnsembl.1
Natural variantiVAR_071468700P → L in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs772368909dbSNPEnsembl.1
Natural variantiVAR_067235731Missing in a patient with chronic myelomonocytic leukemia. 1 Publication1
Natural variantiVAR_071469749R → C in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs754613602dbSNPEnsembl.1
Natural variantiVAR_071470838N → D in TBRS; somatic mutation. 1 Publication1
Natural variantiVAR_067236882R → C in a patient with chronic myelomonocytic leukemia; somatic mutation. 1 PublicationCorresponds to variant rs377577594dbSNPEnsembl.1
Natural variantiVAR_067237882R → H in a patient with chronic myelomonocytic leukemia; somatic mutation. 1 PublicationCorresponds to variant rs147001633dbSNPEnsembl.1
Natural variantiVAR_067238882R → P in a patient with chronic myelomonocytic leukemia; somatic mutation. 1 PublicationCorresponds to variant rs147001633dbSNPEnsembl.1
Natural variantiVAR_071471902F → S in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs587777510dbSNPEnsembl.1
Natural variantiVAR_071472904P → L in TBRS; somatic mutation. 1 PublicationCorresponds to variant rs149095705dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0462541 – 213MPAMP…RWKRE → MGILERVVRRNGRVDRSLKD ECDT in isoform 2. 1 PublicationAdd BLAST213
Alternative sequenceiVSP_040998151 – 166KEQKE…KMEGS → ESSAPGAASSGPTSIP in isoform 3. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_040999167 – 912Missing in isoform 3. 1 PublicationAdd BLAST746

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001307821.1. NM_001320892.1. [Q9Y6K1-3]
NP_001307822.1. NM_001320893.1.
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_005264175.4. [Q9Y6K1-1]
XP_005264234.1. XM_005264177.4.
XP_011530969.1. XM_011532667.2.
XP_016859015.1. XM_017003526.1. [Q9Y6K1-1]
XP_016859016.1. XM_017003527.1.
UniGeneiHs.515840.

Genome annotation databases

EnsembliENST00000264709; ENSP00000264709; ENSG00000119772. [Q9Y6K1-1]
ENST00000321117; ENSP00000324375; ENSG00000119772. [Q9Y6K1-1]
ENST00000380746; ENSP00000370122; ENSG00000119772. [Q9Y6K1-2]
ENST00000406659; ENSP00000384852; ENSG00000119772. [Q9Y6K1-3]
GeneIDi1788.
KEGGihsa:1788.
UCSCiuc002rgb.5. human. [Q9Y6K1-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_001307821.1. NM_001320892.1. [Q9Y6K1-3]
NP_001307822.1. NM_001320893.1.
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_005264175.4. [Q9Y6K1-1]
XP_005264234.1. XM_005264177.4.
XP_011530969.1. XM_011532667.2.
XP_016859015.1. XM_017003526.1. [Q9Y6K1-1]
XP_016859016.1. XM_017003527.1.
UniGeneiHs.515840.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4QBQX-ray2.41A/C479-610[»]
4QBRX-ray1.90A/C476-611[»]
4QBSX-ray1.80A476-611[»]
4U7PX-ray3.82A455-912[»]
4U7TX-ray2.90A/C476-912[»]
ProteinModelPortaliQ9Y6K1.
SMRiQ9Y6K1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108125. 53 interactors.
DIPiDIP-38004N.
IntActiQ9Y6K1. 27 interactors.
STRINGi9606.ENSP00000264709.

Chemistry databases

BindingDBiQ9Y6K1.
ChEMBLiCHEMBL1992.

Protein family/group databases

REBASEi4119. M.HsaDnmt3A.

PTM databases

iPTMnetiQ9Y6K1.
PhosphoSitePlusiQ9Y6K1.

Polymorphism and mutation databases

BioMutaiDNMT3A.
DMDMi166215081.

Proteomic databases

EPDiQ9Y6K1.
PaxDbiQ9Y6K1.
PeptideAtlasiQ9Y6K1.
PRIDEiQ9Y6K1.

Protocols and materials databases

DNASUi1788.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264709; ENSP00000264709; ENSG00000119772. [Q9Y6K1-1]
ENST00000321117; ENSP00000324375; ENSG00000119772. [Q9Y6K1-1]
ENST00000380746; ENSP00000370122; ENSG00000119772. [Q9Y6K1-2]
ENST00000406659; ENSP00000384852; ENSG00000119772. [Q9Y6K1-3]
GeneIDi1788.
KEGGihsa:1788.
UCSCiuc002rgb.5. human. [Q9Y6K1-1]

Organism-specific databases

CTDi1788.
DisGeNETi1788.
GeneCardsiDNMT3A.
HGNCiHGNC:2978. DNMT3A.
HPAiCAB009469.
HPA026588.
MalaCardsiDNMT3A.
MIMi602769. gene.
615879. phenotype.
neXtProtiNX_Q9Y6K1.
OpenTargetsiENSG00000119772.
Orphaneti404443. Tall stature-intellectual disability-facial dysmorphism syndrome.
PharmGKBiPA27445.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IGHW. Eukaryota.
ENOG410XQ4Y. LUCA.
GeneTreeiENSGT00390000008341.
HOGENOMiHOG000230875.
HOVERGENiHBG051381.
InParanoidiQ9Y6K1.
KOiK17398.
OMAiYTEMWVE.
OrthoDBiEOG091G01TP.
PhylomeDBiQ9Y6K1.
TreeFamiTF329039.

Enzyme and pathway databases

BioCyciZFISH:HS04338-MONOMER.
BRENDAi2.1.1.37. 2681.
ReactomeiR-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-3214858. RMTs methylate histone arginines.
R-HSA-5334118. DNA methylation.
SIGNORiQ9Y6K1.

Miscellaneous databases

ChiTaRSiDNMT3A. human.
EvolutionaryTraceiQ9Y6K1.
GenomeRNAii1788.
PROiQ9Y6K1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000119772.
CleanExiHS_DNMT3A.
ExpressionAtlasiQ9Y6K1. baseline and differential.
GenevisibleiQ9Y6K1. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025766. ADD.
IPR018117. C5_DNA_meth_AS.
IPR001525. C5_MeTfrase.
IPR030487. DNMT3A.
IPR000313. PWWP_dom.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR23068:SF10. PTHR23068:SF10. 1 hit.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 155 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

Caution

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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.