UniProt Accession

 DNM3B_HUMAN; Q9UBC3; A2A2E2; B4DSM8; B4DSU1; E1P5M6; E1P5M7; E7EN63; E9PBF2; Q9UBD4; Q9UJQ5; Q9UKA6; Q9UNE5; Q9Y5R9; Q9Y5S0 

Genbank Protein ID

 AF156487; AF156488; AF176228; AF331857; AK299821; AK299915; AL035071; AL035071; AL035071; AL035071; CH471077; CH471077; CH471077; CH471077; CH471077; AF129267; AF129268; AF129269 

Genbank Nucleotide ID

 AAD53062.1; AAD53063.1; AAF04015.1; AAL57040.1; BAG61690.1; BAG61753.1; CAB53069.1; CAB53070.1; CAB53071.1; CAM27373.1; EAW76351.1; EAW76352.1; EAW76353.1; EAW76354.1; EAW76356.1; AAD31432.1; AAD31433.1; AAD31434.1 

Protein Name

 DNA (cytosine-5)-methyltransferase 3B 

Protein Synonyms/Alias

 Dnmt3b; DNA methyltransferase HsaIIIB; DNA MTase HsaIIIB; M.HsaIIIB 

Gene Name

 DNMT3B 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
428	ASDVANNKSSLEDGC	ubiquitination	[1, 2]
562	GLEYEAPKLYPAIPA	ubiquitination	[3]
623	VKHEGNIKYVNDVRN	ubiquitination	[3, 4]
662	SNVNPARKGLYEGTG	ubiquitination	[2]
777	KVQTITTKSNSIKQG	ubiquitination	[3]

Reference

 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 

Functional Description

 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. May preferentially methylates nucleosomal DNA within the nucleosome core region. May function as transcriptional co- repressor by associating with CBX4 and independently of DNA methylation. Seems to be involved in gene silencing (By similarity). In association with DNMT1 and via the recruitment of CTCFL/BORIS, involved in activation of BAG1 gene expression by modulating dimethylation of promoter histone H3 at H3K4 and H3K9. Isoforms 4 and 5 are probably not functional due to the deletion of two conserved methyltransferase motifs. Function as transcriptional corepressor by associating with ZHX1. 

Sequence Annotation

 DOMAIN 225 283 PWWP.
 DOMAIN 423 555 ADD.
 ZN_FING 434 464 GATA-type; atypical.
 ZN_FING 475 531 PHD-type; atypical.
 REGION 1 298 Interaction with DNMT1 and DNMT3A.
 REGION 435 527 Interaction with the PRC2/EED-EZH2
 REGION 582 586 S-adenosyl-L-methionine binding (By
 REGION 627 629 S-adenosyl-L-methionine binding (By
 REGION 832 834 S-adenosyl-L-methionine binding (By
 ACT_SITE 651 651 By similarity.
 BINDING 605 605 S-adenosyl-L-methionine (By similarity).
 MOD_RES 82 82 Phosphoserine.
 MOD_RES 96 96 Phosphothreonine.
 MOD_RES 100 100 Phosphoserine.
 MOD_RES 110 110 Phosphoserine.
 MOD_RES 136 136 Phosphoserine.
 MOD_RES 195 195 Phosphoserine.
 MOD_RES 202 202 Phosphoserine.
 MOD_RES 209 209 Phosphoserine.  

Keyword

 3D-structure; Activator; Alternative splicing; Complete proteome; Disease mutation; DNA-binding; Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; S-adenosyl-L-methionine; Transferase; Ubl conjugation; Zinc; Zinc-finger. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 853 AA 

Protein Sequence

Gene Ontology

 GO:0005720; C:nuclear heterochromatin; IEA:Compara.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; NAS:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
 GO:0071230; P:cellular response to amino acid stimulus; IEA:Compara.
 GO:0006346; P:methylation-dependent chromatin silencing; IEA:Compara.
 GO:0051573; P:negative regulation of histone H3-K9 methylation; IMP:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
 GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
 GO:0031503; P:protein complex localization; IEA:Compara.
 GO:0006349; P:regulation of gene expression by genetic imprinting; IEA:Compara. 

Interpro

 IPR025766; ADD.
 IPR018117; C5_DNA_meth_AS.
 IPR001525; C5_MeTfrase.
 IPR025811; C5_MeTrfase_3.
 IPR000313; PWWP.
 IPR011011; Znf_FYVE_PHD. 

Pfam

 PF00145; DNA_methylase
 PF00855; PWWP 

SMART

 SM00293; PWWP 

PROSITE

 PS51533; ADD
 PS00094; C5_MTASE_1
 PS00095; C5_MTASE_2
 PS50812; PWWP 

PRINTS