NSD2
entrez
7468
canonical
uniprot
O96028
canonical
ensembl
ENSG00000109685
resolver
ensp
ENSP00000372344
resolver
ensp
ENSP00000372347
resolver
ensp
ENSP00000372348
resolver
ensp
ENSP00000372351
resolver
ensp
ENSP00000399251
resolver
ensp
ENSP00000423972
resolver
ensp
ENSP00000427516
resolver
ensp
ENSP00000569150
resolver
ensp
ENSP00000569151
resolver
ensp
ENSP00000592203
resolver
ensp
ENSP00000592204
resolver
ensp
ENSP00000592205
resolver
ensp
ENSP00000592206
resolver
ensp
ENSP00000592207
resolver
ensp
ENSP00000592208
resolver
ensp
ENSP00000592209
resolver
ensp
ENSP00000592210
resolver
ensp
ENSP00000671821
resolver
ensp
ENSP00000690273
resolver
genesymbol
NSD2
resolver
genesymbol_syn
KIAA1090
resolver
genesymbol_syn
MMSET
resolver
genesymbol_syn
TRX5
resolver
genesymbol_syn
WHSC1
resolver
hgnc
HGNC:12766
resolver
uniprot
A2A2T2
resolver
uniprot
A2A2T3
resolver
uniprot
A2A2T4
resolver
uniprot
A7MCZ1
resolver
uniprot
D3DVQ2
resolver
uniprot
O96031
resolver
uniprot
Q4VBY8
resolver
uniprot
Q672J1
resolver
uniprot
Q6IS00
resolver
uniprot
Q86V01
resolver
uniprot
Q9BZB4
resolver
uniprot
Q9UI92
resolver
uniprot
Q9UPR2
resolver
uniprot_entry
NSD2_HUMAN
resolver
uniprot_sec
A2A2T2
resolver
uniprot_sec
A2A2T3
resolver
uniprot_sec
A2A2T4
resolver
uniprot_sec
A7MCZ1
resolver
uniprot_sec
D3DVQ2
resolver
uniprot_sec
O96031
resolver
uniprot_sec
Q4VBY8
resolver
uniprot_sec
Q672J1
resolver
uniprot_sec
Q6IS00
resolver
uniprot_sec
Q86V01
resolver
uniprot_sec
Q9BZB4
resolver
uniprot_sec
Q9UI92
resolver
uniprot_sec
Q9UPR2
resolver
amino_acid_sequence
MEFSIKQSPLSVQSVVKCIKMKQAPEILGSANGKTPSCEVNRECSVFLSKAQLSSSLQEGVMQKFNGHDALPFIPADKLKDLTSRVFNGEPGAHDAKLRFESQEMKGIGTPPNTTPIKNGSPEIKLKITKTYMNGKPLFESSICGDSAADVSQSEENGQKPENKARRNRKRSIKYDSLLEQGLVEAALVSKISSPSDKKIPAKKESCPNTGRDKDHLLKYNVGDLVWSKVSGYPWWPCMVSADPLLHSYTKLKGQKKSARQYHVQFFGDAPERAWIFEKSLVAFEGEGQFEKLCQESAKQAPTKAEKIKLLKPISGKLRAQWEMGIVQAEEAASMSVEERKAKFTFLYVGDQLHLNPQVAKEAGIAAESLGEMAESSGVSEEAAENPKSVREECIPMKRRRRAKLCSSAETLESHPDIGKSTPQKTAEADPRRGVGSPPGRKKTTVSMPRSRKGDAASQFLVFCQKHRDEVVAEHPDASGEEIEELLRSQWSLLSEKQRARYNTKFALVAPVQAEEDSGNVNGKKRNHTKRIQDPTEDAEAEDTPRKRLRTDKHSLRKRDTITDKTARTSSYKAMEAASSLKSQAATKNLSDACKPLKKRNRASTAASSALGFSKSSSPSASLTENEVSDSPGDEPSESPYESADETQTEVSVSSKKSERGVTAKKEYVCQLCEKPGSLLLCEGPCCGAFHLACLGLSRRPEGRFTCSECASGIHSCFVCKESKTDVKRCVVTQCGKFYHEACVKKYPLTVFESRGFRCPLHSCVSCHASNPSNPRPSKGKMMRCVRCPVAYHSGDACLAAGCSVIASNSIICTAHFTARKGKRHHAHVNVSWCFVCSKGGSLLCCESCPAAFHPDCLNIEMPDGSWFCNDCRAGKKLHFQDIIWVKLGNYRWWPAEVCHPKNVPPNIQKMKHEIGEFPVFFFGSKDYYWTHQARVFPYMEGDRGSRYQGVRGIGRVFKNALQEAEARFREIKLQREARETQESERKPPPYKHIKVNKPYGKVQIYTADISEIPKCNCKPTDENPCGFDSECLNRMLMFECHPQVCPAGEFCQNQCFTKRQYPETKIIKTDGKGWGLVAKRDIRKGEFVNEYVGELIDEEECMARIKHAHENDITHFYMLTIDKDRIIDAGPKGNYSRFMNHSCQPNCETLKWTVNGDTRVGLFAVCDIPAGTELTFNYNLDCLGNEKTVCRCGASNCSGFLGDRPKTSTTLSSEEKGKKTKKKTRRRRAKGEGKRQSEDECFRCGDGGQLVLCDRKFCTKAYHLSCLGLGKRPFGKWECPWHHCDVCGKPSTSFCHLCPNSFCKEHQDGTAFSCTPDGRSYCCEHDLGAASVRSTKTEKPPPEPGKPKGKRRRRRGWRRVTEGK
uniprot
proteins
disease_involvement
DISEASE: Rauch-Steindl syndrome (RAUST) [MIM:619695]: An autosomal dominant disorder characterized by poor pre- and postnatal growth, facial dysmorphism, and variable developmental delay with delayed motor and speech acquisition and impaired intellectual. Other features may include hypotonia and behavioral abnormalities. {ECO:0000269|PubMed:29760529, ECO:0000269|PubMed:29892088, ECO:0000269|PubMed:33941880}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=A chromosomal aberration involving NSD2 is a cause of multiple myeloma tumors. Translocation t(4;14)(p16.3;q32.3) with IgH. {ECO:0000269|PubMed:10945609, ECO:0000269|PubMed:11337357, ECO:0000269|PubMed:12433679, ECO:0000269|PubMed:15257719, ECO:0000269|PubMed:9618163, ECO:0000269|PubMed:9787135}.; DISEASE: Note=NSD2 is located in the Wolf-Hirschhorn syndrome (WHS) critical region. WHS results from by sub-telomeric deletions in the short arm of chromosome 4. NSD2 is deleted in every case, however deletion of linked genes contributes to both the severity of the core characteristics and the presence of the additional syndromic problems. {ECO:0000269|PubMed:15734578}.
uniprot
proteins
ec_number
2.1.1.357
uniprot
proteins
function
FUNCTION: Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2) (PubMed:19808676, PubMed:22099308, PubMed:27571355, PubMed:29728617, PubMed:33941880). Also monomethylates nucleosomal histone H3 at 'Lys-36' (H3K36me) in vitro (PubMed:22099308). Does not trimethylate nucleosomal histone H3 at 'Lys-36' (H3K36me3) (PubMed:22099308). However, specifically trimethylates histone H3 at 'Lys-36' (H3K36me3) at euchromatic regions in embryonic stem (ES) cells (By similarity). By methylating histone H3 at 'Lys-36', involved in the regulation of gene transcription during various biological processes (PubMed:16115125, PubMed:22099308, PubMed:29728617). In ES cells, associates with developmental transcription factors such as SALL1 and represses inappropriate gene transcription mediated by histone deacetylation (By similarity). During heart development, associates with transcription factor NKX2-5 to repress transcription of NKX2-5 target genes (By similarity). Plays an essential role in adipogenesis, by regulating expression of genes involved in pre-adipocyte differentiation (PubMed:29728617). During T-cell receptor (TCR) and CD28-mediated T-cell activation, promotes the transcription of transcription factor BCL6 which is required for follicular helper T (Tfh) cell differentiation (By similarity). During B-cell development, required for the generation of the B1 lineage (By similarity). During B2 cell activation, may contribute to the control of isotype class switch recombination (CRS), splenic germinal center formation, and the humoral immune response (By similarity). Plays a role in class switch recombination of the immunoglobulin heavy chain (IgH) locus during B-cell activation (By similarity). By regulating the methylation of histone H3 at 'Lys-36' and histone H4 at 'Lys-20' at the IgH locus, involved in TP53BP1 recruitment to the IgH switch region and promotes the transcription of IgA (By similarity). {ECO:0000250|UniProtKB:Q8BVE8, ECO:0000269|PubMed:16115125, ECO:0000269|PubMed:19808676, ECO:0000269|PubMed:22099308, ECO:0000269|PubMed:27571355, ECO:0000269|PubMed:29728617, ECO:0000269|PubMed:33941880}.; FUNCTION: [Isoform 1]: Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2). {ECO:0000269|PubMed:22099308}.; FUNCTION: [Isoform 4]: Histone methyltransferase which specifically dimethylates nucleosomal histone H3 at 'Lys-36' (H3K36me2) (PubMed:22099308). Methylation of histone H3 at 'Lys-27' is controversial (PubMed:18172012, PubMed:22099308). Mono-, di- or tri-methylates histone H3 at 'Lys-27' (H3K27me, H3K27me2 and H3K27me3) (PubMed:18172012). Does not methylate histone H3 at 'Lys-27' (PubMed:22099308). May act as a transcription regulator that binds DNA and suppresses IL5 transcription through HDAC recruitment (PubMed:11152655, PubMed:18172012). {ECO:0000269|PubMed:11152655, ECO:0000269|PubMed:18172012, ECO:0000269|PubMed:22099308}.
uniprot
proteins
mass_dalton
152258
uniprot
proteins
mutagenesis
MUTAGEN 1092; /note="Y->A: Loss of methyltransferase activity. Reduces levels of H3K36me2 in preadipocytes; when associated with A-1179."; /evidence="ECO:0000269|PubMed:22099308, ECO:0000269|PubMed:29728617"; MUTAGEN 1142; /note="H->G: Reduces levels of H3K36me2 in preadipocytes; when associated with A-1179."; /evidence="ECO:0000269|PubMed:29728617"; MUTAGEN 1179; /note="Y->A: Loss of methyltransferase activity. Reduces levels of H3K36me2 in preadipocytes; when associated with A-1092 or G-1142."; /evidence="ECO:0000269|PubMed:22099308, ECO:0000269|PubMed:29728617
uniprot
proteins
protein_family
Class V-like SAM-binding methyltransferase superfamily
uniprot
proteins
protein_family
Histone-lysine methyltransferase family
uniprot
proteins
protein_family
SET2 subfamily
uniprot
proteins
pubmed
10470851
uniprot
proteins
pubmed
10945609
uniprot
proteins
pubmed
11152655
uniprot
proteins
pubmed
11337357
uniprot
proteins
pubmed
12433679
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15257719
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15677557
uniprot
proteins
pubmed
15734578
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16115125
uniprot
proteins
pubmed
16197452
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18172012
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19808676
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
22099308
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
27571355
uniprot
proteins
pubmed
29728617
uniprot
proteins
pubmed
29760529
uniprot
proteins
pubmed
29892088
uniprot
proteins
pubmed
33941880
uniprot
proteins
pubmed
9618163
uniprot
proteins
pubmed
9787135
uniprot
proteins
sequence_length
1365
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15677557, ECO:0000269|PubMed:16197452}. Chromosome {ECO:0000250|UniProtKB:Q8BVE8}. Note=In embryonic stem (ES) cells, localizes to small foci, probably corresponding to euchromatin (By similarity). In B-cells, localizes to Ig heavy chain switch region during class switch recombination (By similarity). {ECO:0000250|UniProtKB:Q8BVE8}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:15677557, ECO:0000269|PubMed:16197452}. Chromosome {ECO:0000269|PubMed:15677557}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:15677557, ECO:0000269|PubMed:16197452}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:15677557, ECO:0000269|PubMed:16197452}. Nucleus, nucleolus {ECO:0000269|PubMed:15677557, ECO:0000269|PubMed:16197452}.
uniprot
proteins