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SETD2 (SET domain containing 2, histone lysine methyltransferase)

Written2020-07Vivian Wang, Assunta De Rienzo
Division of Thoracic Surgery, Brigham and Women's Hospital and Harvard Medical School, Boston, USA;;

Abstract Review of SETD2 and its role in cancer

Keywords SETD2 gene; methyltransferase; cancer

(Note : for Links provided by Atlas : click)


Alias (NCBI)HBP231
HGNC Alias symbHYPB
HGNC Previous nameSET domain containing 2
LocusID (NCBI) 29072
Atlas_Id 51302
Location 3p21.31  [Link to chromosome band 3p21]
Location_base_pair Starts at 47016408 and ends at 47163977 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping SETD2.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)


Description SETD2 gene spans 147 kb. It is composed of 26 exons encoding three mRNA transcript variants ranging from 8,452 to 8,737 nucleotides in length.
Transcription Transcription start is 189 bp for variant 1 and 305 bp for variant 2 upstream of the first ATG of the SETD2 ORF. Variant 2 differs in the 5' UTR and coding sequence compared with variant 1, resulting in a shorter isoform of the SETD2 protein. A third non-coding variant contains an alternate exon compared with variant 1.
Pseudogene No SETD2 pseudogene has been reported.


  Graphic representation of SETD2 protein. SETD2 (isoform 1) is a 2564 aa protein. AWS, associated with SET; SET, Su(var)3-9, enhancer-of-zeste, trithorax; PS, post-SET; WW, rsp5-domain; CC, coiled-coil; LCR, low-charged region; SRI, Set2 Rpb1 Interacting.
Description Human SETD2 is a methyltransferase with 2 main isoforms. Isoform 1 is 2,564 amino acids with a molecular weight of 287.5 kDa. Isoform 2 is 44 residues shorter than isoform 1 at the N-terminus, and is 2520 amino acids with a molecular weight of 282.6 kDa. Three conserved functional domains have been identified in the SETD2: the triplicate AWS-SET-PostSET domains, a WW domain, and a Set2 Rpb1 Interacting (SRI) domain (Li et al., 2016).
The triplicate AWS-SET-PostSET domain mediates methyltransferase activity specific for histone H3 lysine 36 (H3K36) (Edmunds et al., 2008), and a few other non-histone targets (Park et al., 2016). The SET (Suppressor of Variegation, Enhancer of zeste and Trithorax) domain is an evolutionarily conserved motif of 130 amino acids (Rea et al., 2000; Tschiersch et al., 1994), usually present as part of a multi-domain where it is flanked by an AWS (Associated with SET domain) and a PostSET domain. It includes a beta-sheet structure that facilitates multiple rounds of methylation without substrate disassociation (Zhang et al., 2003).
The WW domain, located in the C-terminal region of SETD2, contains two conserved tryptophan (W) residues (Sudol et al., 1995). The WW domain preferentially binds proline-rich segments of other proteins, mediating protein-protein interactions, such as the proline-rich motifs in the Huntingtin protein in Huntington's disease (Gao et al., 2014).
The SRI domain encompasses a 79 amino acid region towards the C-terminal end of SETD2 and is the primary docking site of RNA Pol II (Li et al., 2005; Kizer et al., 2005). It is composed of a low charged region rich in glutamine and proline. Human SETD2 associates with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase II (RNAPII), linking SETD2 to the transcription elongation process (Li et al., 2002). In yeast, deletion of the CTD region on RNA polymerase II defects trimethylation of H3K36, suggesting that H3K36 trimethylation and transcription elongation are coupled processes (Krogan et al., 2003).
Expression SETD2 is ubiquitously expressed in all human tissues and cell lines tested, including many cancer-derived cell lines. Expression is relatively high in bone marrow, lymph node, testis and thyroid tissue, and it is relatively low in pancreas, heart and salivary gland tissue (Fagerberg et al., 2014).
Localisation SETD2 localizes as nuclear speckles and additionally in cytosol.
Function SETD2 is a lysine methyltransferase and transcriptional regulator involved in histone modification, DNA repair, mRNA regulation, genomic stability, alternative splicing, and interferon-α signaling (Aymard et al., 2014; Skucha, et al., 2019; Luco et al., 2010; de Almeida et al., 2011). The C-terminal end of SETD2 complexes with Heterogeneous Nuclear Ribonucleoprotein L ( HNRNPL) and mediates a non-redundant, co-transcriptional trimethylation to histone H3 at lysine 36 (H3K36me). (Yuan et al., 2009) It was demonstrated that Setd2, the mouse homologue of human Huntingtin-interacting protein HYPB, can modulate all detectable K36me3, but not K36me2 or K36me1, throughout the nucleus using siRNA experiments (Edmunds et al., 2008). Similarly, in yeast, knockdown of Setd2 results in complete absence of H3Kme3 without affecting H3Kme1 or H3Kme2. Loss of SETD2 is associated with greater chromatin accessibility (Carvalho et al., 2014; Simon et al., 2014).
In addition to H3K36, SETD2 methylates two other non-histone targets: the α-tubulin on lysine 40 of mitotic microtubules (Park et al., 2016) and the signal transducer and transcription activator ( STAT1) on lysine 525 (Chen et al., 2017).
SETD2 is also a critical amplifier of interferon-α signaling as STAT1 methylation on lysine 525 catalyzed by SETD2 is an essential signaling event on the induction of interferon stimulating genes, such as ISG15 and MX2 (Chen et al., 2017).
The C-terminal domain of SETD2 has been shown to interact with the tumor suppressor TP53, and modulate the expression of its downstream target genes (Xie et al., 2008; Carvalho et al., 2019).
Homology The AWS-SET-postSET domains in human SETD2 share sequence homology and functional similarity with those in yeast Setd2. The SET domain that mediates methyltransferase activity is a ~130 amino acid sequence motif that is evolutionarily conserved from mammals to yeast and even in some bacteria and viruses (Rea et al., 2000; Tschiersch et al., 1994).


Note Inactivating SETD2 mutations are common in clear cell renal cell cancer but have been identified also in other cancers including lung cancer, acute lymphoblastic leukemia, and glioma (Fahey and Davis, 2017). The majority of somatic SETD2 mutations are missense mutations (Li et al., 2016). SETD2-deficient cancers exhibit a wide range of mutations, including insertions, deletions, and chromosomal aberrations, suggesting an additional role for SETD2 in genome stability (Li et al., 2016). Homozygous deletion of Setd2 in mice has been shown to result in embryonic lethality (Hu et al., 2010).

Implicated in

Entity Clear cell renal cell carcinoma (ccRCC)
Note The overall frequency of SETD2 mutations in ccRCC is approximately 15.6% (Cancer Genome Atlas Research Network, 2013). SETD2 mutations were found to be associated with shorter cancer-specific survival (P = 0.036; HR 1.68; 95% CI 1.04-2.73) (Hakimi et al., 2013). The presence of SETD2 mutations was a predictor of ccRCC recurrence. The fraction of truncating SETD2 mutations in ccRCC (57%) was significantly higher than the fraction of truncating SETD2 mutations in non-ccRCC tumors (32%).
Entity Pancreatic adenocarcinoma
Note Low SETD2 expression was correlated with poor prognosis in patients with pancreatic adenocarcinoma. In vivo, Setd2 loss in murine pancreatic acinar cells facilitated Kras-induced acinar-to-ductal reprogramming, mainly through epigenetic dysregulation of Fbxw7. This suggests that Setd2 may act as a putative tumor suppressor in Kras-driven pancreatic carcinogenesis. A Setd2 ablation in murine pancreatic cancer cells enhanced epithelial-mesenchymal transition (EMT) through impaired epigenetic regulation of a-catenin (Ctnna1). Setd2 deficiency in murine pancreatic cancer cell lines also led to sustained Akt activation (Niu et al., 2020).
Entity Malignant Mesothelioma (MM):
Note SETD2 is located in a region frequently lost in malignant pleural mesothelioma (MPM). In 2016, a comprehensive genomic analysis of 212 MPM patients identified SETD2 to be frequently mutated in this disease. In addition, gene fusions and splice-site alterations were also frequent mechanisms for inactivation of SETD2 in MPM (Bueno et al., 2016). In a cohort of 33 malignant mesotheliomas, 27% showed minute biallelic deletions or loss of heterozygosity combined with point mutations in SETD2 by using combined high-density comparative genomic hybridization array and whole exome sequencing analyses (Yoshikawa et al., 2015).
Entity Acute Leukemia
Note SETD2 mutations have been found to be frequent (22%) in acute lymphoid and myeloid leukemias (ALL and AML) carrying a mixed lineage leukemia (MLL)-rearrangement. Knockdown of SETD2 in pre-leukemic cells carrying a KMT2A (MLL) fusion-gene increased both clonogenicity and proliferation of these cells, suggesting that loss of function of SETD2 may promote progression of the disease. In acute leukemia, SETD2 was found mutated in 6% of cases (Zhu et al., 2014). These mutations were commonly nonsense or frameshift, mostly affecting the SRI domain, and approximately a quarter of samples carried bi-allelic SETD2 mutations. A comparison of matched primary and relapsed ALL samples suggested that mutations in epigenetic regulators as a class, including SETD2 mutations, were more common at relapse (Mar et al., 2014).
Entity Gastrointestinal Stromal Tumors
Note SETD2 loss has been associated with more aggressive gastrointestinal stromal tumors (Huang et al., 2016).
Entity Lung Adenocarcinoma
Note SETD2 mutations were found to occur in 9% of lung adenocarcinomas (Cancer Genome Atlas Research Network, 2015). SETD2 fusion mutations are more common than point mutations in lung adenocarcinoma (Lee et al., 2019; Rosell et al., 2020). It has been also shown that suppression of SETD2 or CREB1 confers resistance to cisplatin through inhibition of H3K36me3 and ERK activation in non-small cell lung cancer cell lines (Kim et al., 2019).
Entity Lung Neuroendocrine Tumors
Note Genome wide SNP array analysis of 11 well-differentiated pulmonary carcinoid tumors has revealed loss of heterozygosity of SETD2 in these tumors (Cros et al., 2020).
Entity Primary Central Nervous System Tumors
Note A study published in 2013 showed that 15-28% of pediatric high-grade gliomas (HGGs) and 8% of adult HGGs displayed SETD2 mutations (Fontebasso et al., 2013).
Entity Bladder Carcinoma
Note SETD2 mutations have been observed in 6-10% of bladder urothelial carcinomas (Van Allen et al., 2014).
Entity Huntington's Disease
Note SETD2 was first identified as a huntingtin-interacting protein, implicated in the pathogenesis of Huntington's disease (Faber et al., 1998). The WW domain of SETD2 was found to interact with the N-terminal PRR region of huntingtin protein. (Passani et al., 2000). A stretch of polyproline residues preceding the WW domain was found to modulate the interaction between the SETD2 and huntingtin proteins (Gao et al., 2014).


Comprehensive molecular profiling of lung adenocarcinoma
Nature 2014 Jul 31;511(7511):543-50.
PMID 25079552
Transcriptionally active chromatin recruits homologous recombination at DNA double-strand breaks
Aymard F, Bugler B, Schmidt CK, Guillou E, Caron P, Briois S, Iacovoni JS, Daburon V, Miller KM, Jackson SP, Legube G
Nat Struct Mol Biol 2014 Apr;21(4):366-74.
PMID 24658350
Comprehensive genomic analysis of malignant pleural mesothelioma identifies recurrent mutations, gene fusions and splicing alterations
Bueno R, Stawiski EW, Goldstein LD, Durinck S, De Rienzo A, Modrusan Z, Gnad F, Nguyen TT, Jaiswal BS, Chirieac LR, Sciaranghella D, Dao N, Gustafson CE, Munir KJ, Hackney JA, Chaudhuri A, Gupta R, Guillory J, Toy K, Ha C, Chen YJ, Stinson J, Chaudhuri S, Zhang N, Wu TD, Sugarbaker DJ, de Sauvage FJ, Richards WG, Seshagiri S
Nat Genet 2016 Apr;48(4):407-16.
PMID 26928227
SETD2 is required for DNA double-strand break repair and activation of the p53-mediated checkpoint
Carvalho S, Vítor AC, Sridhara SC, Martins FB, Raposo AC, Desterro JM, Ferreira J, de Almeida SF
Elife 2014 May 6;3:e02482.
PMID 24843002
Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity
Chen K, Liu J, Liu S, Xia M, Zhang X, Han D, Jiang Y, Wang C, Cao X
Cell 2017 Jul 27;170(3):492-506.e14.
PMID 28753426
Specific genomic alterations in high grade pulmonary neuroendocrine tumours with carcinoid morphology
Cros J, Théou-Anton N, Gounant V, Nicolle R, Reyes C, Humez S, Hescot S, Thomas de Montpréville V, Guyétant S, Scoazec JY, Guyard A, de Mestier L, Brosseau S, Mordant P, Castier Y, Gentien D, Ruszniewski P, Zalcman G, Couvelard A, Cazes A
Neuroendocrinology 2020 Feb 3.
PMID 32015233
Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation
Edmunds JW, Mahadevan LC, Clayton AL
EMBO J 2008 Jan 23;27(2):406-20.
PMID 18157086
Huntingtin interacts with a family of WW domain proteins
Faber PW, Barnes GT, Srinidhi J, Chen J, Gusella JF, MacDonald ME
Hum Mol Genet 1998 Sep;7(9):1463-74.
PMID 9700202
SETting the Stage for Cancer Development: SETD2 and the Consequences of Lost Methylation
Fahey CC, Davis IJ
Cold Spring Harb Perspect Med 2017 May 1;7(5):a026468.
PMID 28159833
Mutations in SETD2 and genes affecting histone H3K36 methylation target hemispheric high-grade gliomas
Fontebasso AM, Schwartzentruber J, Khuong-Quang DA, Liu XY, Sturm D, Korshunov A, Jones DT, Witt H, Kool M, Albrecht S, Fleming A, Hadjadj D, Busche S, Lepage P, Montpetit A, Staffa A, Gerges N, Zakrzewska M, Zakrzewski K, Liberski PP, Hauser P, Garami M, Klekner A, Bognar L, Zadeh G, Faury D, Pfister SM, Jabado N, Majewski J
Acta Neuropathol 2013 May;125(5):659-69.
PMID 23417712
Autoinhibitory structure of the WW domain of HYPB/SETD2 regulates its interaction with the proline-rich region of huntingtin
Gao YG, Yang H, Zhao J, Jiang YJ, Hu HY
Structure 2014 Mar 4;22(3):378-86.
PMID 24412394
Adverse outcomes in clear cell renal cell carcinoma with mutations of 3p21 epigenetic regulators BAP1 and SETD2: a report by MSKCC and the KIRC TCGA research network
Hakimi AA, Ostrovnaya I, Reva B, Schultz N, Chen YB, Gonen M, Liu H, Takeda S, Voss MH, Tickoo SK, Reuter VE, Russo P, Cheng EH, Sander C, Motzer RJ, Hsieh JJ,
Clin Cancer Res 2013 Jun 15;19(12):3259-67.
PMID 23620406
Histone H3 lysine 36 methyltransferase Hypb/Setd2 is required for embryonic vascular remodeling
Hu M, Sun XJ, Zhang YL, Kuang Y, Hu CQ, Wu WL, Shen SH, Du TT, Li H, He F, Xiao HS, Wang ZG, Liu TX, Lu H, Huang QH, Chen SJ, Chen Z
Proc Natl Acad Sci U S A 2010 Feb 16;107(7):2956-61.
PMID 20133625
SETD2 histone modifier loss in aggressive GI stromal tumours
Huang KK, McPherson JR, Tay ST, Das K, Tan IB, Ng CC, Chia NY, Zhang SL, Myint SS, Hu L, Rajasegaran V, Huang D, Loh JL, Gan A, Sairi AN, Sam XX, Dominguez LT, Lee M, Soo KC, Ooi LL, Ong HS, Chung A, Chow PK, Wong WK, Selvarajan S, Ong CK, Lim KH, Nandi T, Rozen S, Teh BT, Quek R, Tan P
Gut 2016 Dec;65(12):1960-1972.
PMID 26338826
Acquired SETD2 mutation and impaired CREB1 activation confer cisplatin resistance in metastatic non-small cell lung cancer
Kim IK, McCutcheon JN, Rao G, Liu SV, Pommier Y, Skrzypski M, Zhang YW, Giaccone G
Oncogene 2019 Jan;38(2):180-193.
PMID 30093630
A novel domain in Set2 mediates RNA polymerase II interaction and couples histone H3 K36 methylation with transcript elongation
Kizer KO, Phatnani HP, Shibata Y, Hall H, Greenleaf AL, Strahl BD
Mol Cell Biol 2005 Apr;25(8):3305-16.
PMID 15798214
Methylation of histone H3 by Set2 in Saccharomyces cerevisiae is linked to transcriptional elongation by RNA polymerase II
Krogan NJ, Kim M, Tong A, Golshani A, Cagney G, Canadien V, Richards DP, Beattie BK, Emili A, Boone C, Shilatifard A, Buratowski S, Greenblatt J
Mol Cell Biol 2003 Jun;23(12):4207-18.
PMID 12773564
Tracing Oncogene Rearrangements in the Mutational History of Lung Adenocarcinoma
Lee JJ, Park S, Park H, Kim S, Lee J, Lee J, Youk J, Yi K, An Y, Park IK, Kang CH, Chung DH, Kim TM, Jeon YK, Hong D, Park PJ, Ju YS, Kim YT
Cell 2019 Jun 13;177(7):1842-1857.e21.
PMID 31155235
The histone mark H3K36me3 regulates human DNA mismatch repair through its interaction with MutSα
Li F, Mao G, Tong D, Huang J, Gu L, Yang W, Li GM
Cell 2013 Apr 25;153(3):590-600.
PMID 23622243
SETD2: an epigenetic modifier with tumor suppressor functionality
Li J, Duns G, Westers H, Sijmons R, van den Berg A, Kok K
Oncotarget 2016 Aug 2;7(31):50719-50734.
PMID 27191891
Association of the histone methyltransferase Set2 with RNA polymerase II plays a role in transcription elongation
Li J, Moazed D, Gygi SP
J Biol Chem 2002 Dec 20;277(51):49383-8.
PMID 12381723
Regulation of alternative splicing by histone modifications
Luco RF, Pan Q, Tominaga K, Blencowe BJ, Pereira-Smith OM, Misteli T
Science 2010 Feb 19;327(5968):996-1000.
PMID 20133523
Mutations in epigenetic regulators including SETD2 are gained during relapse in paediatric acute lymphoblastic leukaemia
Mar BG, Bullinger LB, McLean KM, Grauman PV, Harris MH, Stevenson K, Neuberg DS, Sinha AU, Sallan SE, Silverman LB, Kung AL, Lo Nigro L, Ebert BL, Armstrong SA
Nat Commun 2014 Mar 24;5:3469.
PMID 24662245
Loss of Setd2 promotes Kras-induced acinar-to-ductal metaplasia and epithelia-mesenchymal transition during pancreatic carcinogenesis
Niu N, Lu P, Yang Y, He R, Zhang L, Shi J, Wu J, Yang M, Zhang ZG, Wang LW, Gao WQ, Habtezion A, Xiao GG, Sun Y, Li L, Xue J
Gut 2020 Apr;69(4):715-726.
PMID 31300513
Dual Chromatin and Cytoskeletal Remodeling by SETD2
Park IY, Powell RT, Tripathi DN, Dere R, Ho TH, Blasius TL, Chiang YC, Davis IJ, Fahey CC, Hacker KE, Verhey KJ, Bedford MT, Jonasch E, Rathmell WK, Walker CL
Cell 2016 Aug 11;166(4):950-962.
PMID 27518565
Huntingtin's WW domain partners in Huntington's disease post-mortem brain fulfill genetic criteria for direct involvement in Huntington's disease pathogenesis
Passani LA, Bedford MT, Faber PW, McGinnis KM, Sharp AH, Gusella JF, Vonsattel JP, MacDonald ME
Hum Mol Genet 2000 Sep 1;9(14):2175-82.
PMID 10958656
Regulation of chromatin structure by site-specific histone H3 methyltransferases
Rea S, Eisenhaber F, O', Carroll D, Strahl BD, Sun ZW, Schmid M, Opravil S, Mechtler K, Ponting CP, Allis CD, Jenuwein T
Nature 2000 Aug 10;406(6796):593-9.
PMID 10949293
Novel molecular targets for the treatment of lung cancer
Rosell R, Karachaliou N, Arrieta O
Curr Opin Oncol 2020 Jan;32(1):37-43.
PMID 31599770
Variation in chromatin accessibility in human kidney cancer links H3K36 methyltransferase loss with widespread RNA processing defects
Simon JM, Hacker KE, Singh D, Brannon AR, Parker JS, Weiser M, Ho TH, Kuan PF, Jonasch E, Furey TS, Prins JF, Lieb JD, Rathmell WK, Davis IJ
Genome Res 2014 Feb;24(2):241-50.
PMID 24158655
Roles of SETD2 in Leukemia-Transcription, DNA-Damage, and Beyond
Skucha A, Ebner J, Grebien F
Int J Mol Sci 2019 Feb 27;20(5):1029.
PMID 30818762
Characterization of a novel protein-binding module--the WW domain
Sudol M, Chen HI, Bougeret C, Einbond A, Bork P
FEBS Lett 1995 Aug 1;369(1):67-71.
PMID 7641887
The protein encoded by the Drosophila position-effect variegation suppressor gene Su(var)3-9 combines domains of antagonistic regulators of homeotic gene complexes
Tschiersch B, Hofmann A, Krauss V, Dorn R, Korge G, Reuter G
EMBO J 1994 Aug 15;13(16):3822-31.
PMID 7915232
Somatic ERCC2 mutations correlate with cisplatin sensitivity in muscle-invasive urothelial carcinoma
Van Allen EM, Mouw KW, Kim P, Iyer G, Wagle N, Al-Ahmadie H, Zhu C, Ostrovnaya I, Kryukov GV, O', Connor KW, Sfakianos J, Garcia-Grossman I, Kim J, Guancial EA, Bambury R, Bahl S, Gupta N, Farlow D, Qu A, Signoretti S, Barletta JA, Reuter V, Boehm J, Lawrence M, Getz G, Kantoff P, Bochner BH, Choueiri TK, Bajorin DF, Solit DB, Gabriel S, D', Andrea A, Garraway LA, Rosenberg JE
Cancer Discov 2014 Oct;4(10):1140-53.
PMID 25096233
Histone methyltransferase protein SETD2 interacts with p53 and selectively regulates its downstream genes
Xie P, Tian C, An L, Nie J, Lu K, Xing G, Zhang L, He F
Cell Signal 2008 Sep;20(9):1671-8.
PMID 18585004
Biallelic germline and somatic mutations in malignant mesothelioma: multiple mutations in transcription regulators including mSWI/SNF genes
Yoshikawa Y, Sato A, Tsujimura T, Otsuki T, Fukuoka K, Hasegawa S, Nakano T, Hashimoto-Tamaoki T
Int J Cancer 2015 Feb 1;136(3):560-71.
PMID 24916674
Structural basis for the product specificity of histone lysine methyltransferases
Zhang X, Yang Z, Khan SI, Horton JR, Tamaru H, Selker EU, Cheng X
Mol Cell 2003 Jul;12(1):177-85.
PMID 12887903
Identification of functional cooperative mutations of SETD2 in human acute leukemia
Zhu X, He F, Zeng H, Ling S, Chen A, Wang Y, Yan X, Wei W, Pang Y, Cheng H, Hua C, Zhang Y, Yang X, Lu X, Cao L, Hao L, Dong L, Zou W, Wu J, Li X, Zheng S, Yan J, Zhou J, Zhang L, Mi S, Wang X, Zhang L, Zou Y, Chen Y, Geng Z, Wang J, Zhou J, Liu X, Wang J, Yuan W, Huang G, Cheng T, Wang QF
Nat Genet 2014 Mar;46(3):287-93.
PMID 24509477
Splicing enhances recruitment of methyltransferase HYPB/Setd2 and methylation of histone H3 Lys36
de Almeida SF, Grosso AR, Koch F, Fenouil R, Carvalho S, Andrade J, Levezinho H, Gut M, Eick D, Gut I, Andrau JC, Ferrier P, Carmo-Fonseca M
Nat Struct Mol Biol 2011 Jul 26;18(9):977-83.
PMID 21792193


This paper should be referenced as such :
Wang V, De Rienzo A
SETD2 (SET domain containing 2, histone lysine methyltransferase)
Atlas Genet Cytogenet Oncol Haematol. 2021;25(2):68-72
Free journal version : [ pdf ]   [ DOI ]

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 3 ]
  B-cell Prolymphocytic Leukemia
Early T-cell precursor acute lymphoblastic leukemia
t(3;3)(p21;p21) SETD2::CCDC12

External links

HGNC (Hugo)SETD2   18420
LRG (Locus Reference Genomic)LRG_775
Entrez_Gene (NCBI)SETD2    SET domain containing 2, histone lysine methyltransferase
AliasesHBP231; HIF-1; HIP-1; HSPC069; 
GeneCards (Weizmann)SETD2
Ensembl hg19 (Hinxton)ENSG00000181555 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000181555 [Gene_View]  ENSG00000181555 [Sequence]  chr3:47016408-47163977 [Contig_View]  SETD2 [Vega]
ICGC DataPortalENSG00000181555
TCGA cBioPortalSETD2
Genatlas (Paris)SETD2
SOURCE (Princeton)SETD2
Genetics Home Reference (NIH)SETD2
Genomic and cartography
GoldenPath hg38 (UCSC)SETD2  -     chr3:47016408-47163977 -  3p21.31   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)SETD2  -     3p21.31   [Description]    (hg19-Feb_2009)
GoldenPathSETD2 - 3p21.31 [CytoView hg19]  SETD2 - 3p21.31 [CytoView hg38]
Genome Data Viewer NCBISETD2 [Mapview hg19]  
OMIM612778   616831   
Gene and transcription
Genbank (Entrez)AB051519 AF049103 AF049610 AF161554 AI671342
RefSeq transcript (Entrez)NM_001349370 NM_012271 NM_014159
Consensus coding sequences : CCDS (NCBI)SETD2
Gene ExpressionSETD2 [ NCBI-GEO ]   SETD2 [ EBI - ARRAY_EXPRESS ]   SETD2 [ SEEK ]   SETD2 [ MEM ]
Gene Expression Viewer (FireBrowse)SETD2 [ Firebrowse - Broad ]
GenevisibleExpression of SETD2 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)29072
GTEX Portal (Tissue expression)SETD2
Human Protein AtlasENSG00000181555-SETD2 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
Domain families : Pfam (Sanger)
Domain families : Pfam (NCBI)
Conserved Domain (NCBI)SETD2
Human Protein Atlas [tissue]ENSG00000181555-SETD2 [tissue]
Protein Interaction databases
Ontologies - Pathways
PubMed137 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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