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Protein

DNA (cytosine-5)-methyltransferase 3A

Gene

DNMT3A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Caution

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

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-methionineCombined sources1 Publication1
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

  • chromatin binding Source: Ensembl
  • DNA (cytosine-5-)-methyltransferase activity Source: UniProtKB
  • DNA binding Source: UniProtKB
  • DNA-methyltransferase activity Source: Reactome
  • identical protein binding Source: IntAct
  • metal ion binding Source: UniProtKB-KW
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator, DNA-binding, Methyltransferase, Repressor, Transferase
LigandMetal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000119772.16
HGNCiHGNC:2978 DNMT3A
MIMi602769 gene
neXtProtiNX_Q9Y6K1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Tatton-Brown-Rahman syndrome (TBRS)3 Publications
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 dbSNP:rs587777508EnsemblClinVar.1
Natural variantiVAR_077522365Y → C in TBRS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs144062658Ensembl.1
Natural variantiVAR_077523529D → N in TBRS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs962805778Ensembl.1
Natural variantiVAR_071464532G → S in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs951361433Ensembl.1
Natural variantiVAR_071465548M → K in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587777509EnsemblClinVar.1
Natural variantiVAR_071466549C → R in TBRS; somatic mutation. 1 Publication1
Natural variantiVAR_071467648L → P in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587777507EnsemblClinVar.1
Natural variantiVAR_071468700P → L in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs772368909Ensembl.1
Natural variantiVAR_071469749R → C in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs754613602Ensembl.1
Natural variantiVAR_077524771R → Q in TBRS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs757823678EnsemblClinVar.1
Natural variantiVAR_077525778V → G in TBRS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs979932565Ensembl.1
Natural variantiVAR_071470838N → D in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs961377711Ensembl.1
Natural variantiVAR_071471902F → S in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587777510EnsemblClinVar.1
Natural variantiVAR_071472904P → L in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs149095705EnsemblClinVar.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
Cross-linki162Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
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

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y6K1
PaxDbiQ9Y6K1
PeptideAtlasiQ9Y6K1
PRIDEiQ9Y6K1
ProteomicsDBi86709
86710 [Q9Y6K1-2]
86711 [Q9Y6K1-3]

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

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi108125, 54 interactors
CORUMiQ9Y6K1
DIPiDIP-38004N
IntActiQ9Y6K1, 31 interactors
MINTiQ9Y6K1
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 – 683Combined sources3
Helixi687 – 689Combined sources3
Helixi692 – 698Combined sources7
Beta strandi702 – 706Combined sources5
Turni711 – 713Combined sources3
Turni722 – 724Combined sources3
Helixi728 – 730Combined sources3
Helixi731 – 741Combined sources11
Beta strandi752 – 761Combined sources10
Helixi763 – 773Combined sources11
Beta strandi778 – 781Combined sources4
Helixi782 – 784Combined sources3
Beta strandi786 – 788Combined sources3
Beta strandi791 – 796Combined sources6
Turni799 – 802Combined sources4
Helixi815 – 818Combined sources4
Beta strandi824 – 826Combined sources3
Beta strandi828 – 830Combined sources3
Helixi837 – 840Combined sources4
Turni843 – 846Combined sources4
Beta strandi849 – 852Combined sources4
Beta strandi855 – 857Combined sources3
Helixi861 – 868Combined sources8
Turni872 – 875Combined sources4
Helixi882 – 891Combined sources10
Helixi895 – 902Combined sources8
Helixi903 – 905Combined sources3
Turni906 – 908Combined sources3

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[»]
5YX2X-ray2.65A/D628-912[»]
6BRRX-ray2.97A/D628-912[»]
6F57X-ray3.10A/D628-912[»]
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 bindingCombined sources1 Publication5
Regioni686 – 688S-adenosyl-L-methionine bindingCombined sources1 Publication3
Regioni891 – 893S-adenosyl-L-methionine bindingCombined sources1 Publication3

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

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
OMAiFPVCHDS
OrthoDBiEOG091G01TP
PhylomeDBiQ9Y6K1
TreeFamiTF329039

Family and domain databases

InterProiView protein in InterPro
IPR025766 ADD
IPR018117 C5_DNA_meth_AS
IPR001525 C5_MeTfrase
IPR030487 DNMT3A
IPR000313 PWWP_dom
IPR029063 SAM-dependent_MTases
PANTHERiPTHR23068:SF10 PTHR23068:SF10, 2 hits
PfamiView protein in Pfam
PF00145 DNA_methylase, 1 hit
PF00855 PWWP, 1 hit
SMARTiView protein in SMART
SM00293 PWWP, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51533 ADD, 1 hit
PS00094 C5_MTASE_1, 1 hit
PS50812 PWWP, 1 hit
PS51679 SAM_MT_C5, 1 hit

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 dbSNP:rs587777508EnsemblClinVar.1
Natural variantiVAR_077522365Y → C in TBRS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs144062658Ensembl.1
Natural variantiVAR_077523529D → N in TBRS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs962805778Ensembl.1
Natural variantiVAR_071464532G → S in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs951361433Ensembl.1
Natural variantiVAR_071465548M → K in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587777509EnsemblClinVar.1
Natural variantiVAR_071466549C → R in TBRS; somatic mutation. 1 Publication1
Natural variantiVAR_071467648L → P in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587777507EnsemblClinVar.1
Natural variantiVAR_067234699G → D in a patient with chronic myelomonocytic leukemia. 1 PublicationCorresponds to variant dbSNP:rs761064473Ensembl.1
Natural variantiVAR_071468700P → L in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs772368909Ensembl.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 dbSNP:rs754613602Ensembl.1
Natural variantiVAR_077524771R → Q in TBRS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs757823678EnsemblClinVar.1
Natural variantiVAR_077525778V → G in TBRS; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs979932565Ensembl.1
Natural variantiVAR_071470838N → D in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs961377711Ensembl.1
Natural variantiVAR_067236882R → C in a patient with chronic myelomonocytic leukemia; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs377577594EnsemblClinVar.1
Natural variantiVAR_067237882R → H in a patient with chronic myelomonocytic leukemia; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs147001633EnsemblClinVar.1
Natural variantiVAR_067238882R → P in a patient with chronic myelomonocytic leukemia; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs147001633EnsemblClinVar.1
Natural variantiVAR_071471902F → S in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs587777510EnsemblClinVar.1
Natural variantiVAR_071472904P → L in TBRS; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs149095705EnsemblClinVar.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

Similar proteinsi

Entry informationi

Entry nameiDNM3A_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6K1
Secondary accession number(s): E9PEB8
, Q86TE8, Q86XF5, Q8IZV0, Q8WXU9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 15, 2008
Last modified: June 20, 2018
This is version 168 of the entry and version 4 of the sequence. See 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

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