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Histone-lysine N-methyltransferase SETD2 (EC 2.1.1.43) (HIF-1) (Huntingtin yeast partner B) (Huntingtin-interacting protein 1) (HIP-1) (Huntingtin-interacting protein B) (Lysine N-methyltransferase 3A) (Protein-lysine N-methyltransferase SETD2) (EC 2.1.1.-) (SET domain-containing protein 2) (hSET2) (p231HBP)

 SETD2_HUMAN             Reviewed;        2564 AA.
Q9BYW2; O75397; O75405; Q17RW8; Q5BKS9; Q5QGN2; Q69YI5; Q6IN64; Q6ZN53;
Q6ZS25; Q8N3R0; Q8TCN0; Q9C0D1; Q9H696; Q9NZW9;
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
11-DEC-2019, entry version 170.
RecName: Full=Histone-lysine N-methyltransferase SETD2 {ECO:0000305};
EC=2.1.1.- {ECO:0000269|PubMed:23043551, ECO:0000269|PubMed:27474439};
AltName: Full=HIF-1;
AltName: Full=Huntingtin yeast partner B {ECO:0000303|PubMed:16118227};
AltName: Full=Huntingtin-interacting protein 1;
Short=HIP-1;
AltName: Full=Huntingtin-interacting protein B {ECO:0000303|PubMed:16118227};
AltName: Full=Lysine N-methyltransferase 3A {ECO:0000303|PubMed:19332550};
AltName: Full=Protein-lysine N-methyltransferase SETD2 {ECO:0000305};
EC=2.1.1.- {ECO:0000269|PubMed:27518565, ECO:0000269|PubMed:28753426};
AltName: Full=SET domain-containing protein 2 {ECO:0000303|PubMed:19332550};
Short=hSET2 {ECO:0000303|PubMed:19332550};
AltName: Full=p231HBP {ECO:0000303|PubMed:11461154};
Name=SETD2;
Synonyms=HIF1, HYPB {ECO:0000303|PubMed:16118227},
KIAA1732 {ECO:0000303|PubMed:11214970},
KMT3A {ECO:0000303|PubMed:19332550}, SET2 {ECO:0000303|PubMed:19332550,
ECO:0000303|Ref.7}; ORFNames=HSPC069;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1390.
TISSUE=Brain, and Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-2564 (ISOFORM 3), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 927-1482 (ISOFORMS 1/2/3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 2228-2564 (ISOFORM 1).
TISSUE=Adipose tissue;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 368-2564 (ISOFORM 1), FUNCTION (MICROBIAL
INFECTION), DNA-BINDING, TISSUE SPECIFICITY, AND INTERACTION WITH HTT.
PubMed=11461154; DOI=10.1006/mcne.2001.1004;
Rega S., Stiewe T., Chang D.-I., Pollmeier B., Esche H., Bardenheuer W.,
Marquitan G., Puetzer B.M.;
"Identification of the full-length huntingtin-interacting protein
p231HBP/HYPB as a DNA-binding factor.";
Mol. Cell. Neurosci. 18:68-79(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 388-2564 (ISOFORM 1), AND VARIANT
LEU-1962.
TISSUE=Cerebellum, Duodenum, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 481-2564 (ISOFORM 1), FUNCTION,
AUTOMETHYLATION, MUTAGENESIS OF ARG-1625, AND INTERACTION WITH POLR2A.
PubMed=16118227; DOI=10.1074/jbc.m504012200;
Sun X.-J., Wei J., Wu X.-Y., Hu M., Wang L., Wang H.-H., Zhang Q.-H.,
Chen S.-J., Huang Q.-H., Chen Z.;
"Identification and characterization of a novel human histone H3 lysine 36
specific methyltransferase.";
J. Biol. Chem. 280:35261-35271(2005).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 481-2564 (ISOFORM 2).
Sun X.J., Wei J., Wu X.Y., Hu M., Wang H.H., Zhang Q.H., Huang Q.H.,
Chen Z.;
"Identification of a human histone H3-K36-specific methyltransferase that
is orthologous to Saccharomyces cerevisiae SET2 protein.";
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 650-2564 (ISOFORM 1), AND VARIANT
LEU-1962.
TISSUE=Brain;
PubMed=11214970; DOI=10.1093/dnares/7.6.347;
Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIX. The
complete sequences of 100 new cDNA clones from brain which code for large
proteins in vitro.";
DNA Res. 7:347-355(2000).
[9]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1402-2069.
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for 300
previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
cells.";
Genome Res. 10:1546-1560(2000).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 2378-2564, AND INTERACTION WITH HTT.
TISSUE=Frontal cortex;
PubMed=9700202; DOI=10.1093/hmg/7.9.1463;
Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F.,
MacDonald M.E.;
"Huntingtin interacts with a family of WW domain proteins.";
Hum. Mol. Genet. 7:1463-1474(1998).
[12]
INTERACTION WITH HTT.
PubMed=10958656; DOI=10.1093/hmg/9.14.2175;
Passani L.A., Bedford M.T., Faber P.W., McGinnis K.M., Sharp A.H.,
Gusella J.F., Vonsattel J.-P., MacDonald M.E.;
"Huntingtin's WW domain partners in Huntington's disease post-mortem brain
fulfill genetic criteria for direct involvement in Huntington's disease
pathogenesis.";
Hum. Mol. Genet. 9:2175-2182(2000).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[14]
INTERACTION WITH TP53.
PubMed=18585004; DOI=10.1016/j.cellsig.2008.05.012;
Xie P., Tian C., An L., Nie J., Lu K., Xing G., Zhang L., He F.;
"Histone methyltransferase protein SETD2 interacts with p53 and selectively
regulates its downstream genes.";
Cell. Signal. 20:1671-1678(2008).
[15]
FUNCTION, AND INTERACTION WITH IWS1.
PubMed=19141475; DOI=10.1101/gad.1720008;
Yoh S.M., Lucas J.S., Jones K.A.;
"The Iws1:Spt6:CTD complex controls cotranscriptional mRNA biosynthesis and
HYPB/Setd2-mediated histone H3K36 methylation.";
Genes Dev. 22:3422-3434(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1228, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-323; SER-624;
SER-754; SER-1228; THR-1872; SER-2080 AND SER-2082, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
INTERACTION WITH HNRNPL.
PubMed=19332550; DOI=10.1074/jbc.m808431200;
Yuan W., Xie J., Long C., Erdjument-Bromage H., Ding X., Zheng Y.,
Tempst P., Chen S., Zhu B., Reinberg D.;
"Heterogeneous nuclear ribonucleoprotein L is a subunit of human KMT3a/Set2
complex required for H3 Lys-36 trimethylation activity in vivo.";
J. Biol. Chem. 284:15701-15707(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-321; SER-323;
SER-708; SER-744 AND SER-754, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
INVOLVEMENT IN RCC.
PubMed=20054297; DOI=10.1038/nature08672;
Dalgliesh G.L., Furge K., Greenman C., Chen L., Bignell G., Butler A.,
Davies H., Edkins S., Hardy C., Latimer C., Teague J., Andrews J.,
Barthorpe S., Beare D., Buck G., Campbell P.J., Forbes S., Jia M.,
Jones D., Knott H., Kok C.Y., Lau K.W., Leroy C., Lin M.L., McBride D.J.,
Maddison M., Maguire S., McLay K., Menzies A., Mironenko T., Mulderrig L.,
Mudie L., O'Meara S., Pleasance E., Rajasingham A., Shepherd R., Smith R.,
Stebbings L., Stephens P., Tang G., Tarpey P.S., Turrell K., Dykema K.J.,
Khoo S.K., Petillo D., Wondergem B., Anema J., Kahnoski R.J., Teh B.T.,
Stratton M.R., Futreal P.A.;
"Systematic sequencing of renal carcinoma reveals inactivation of histone
modifying genes.";
Nature 463:360-363(2010).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-323; SER-624 AND
THR-1872, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[23]
FUNCTION.
PubMed=21792193; DOI=10.1038/nsmb.2123;
de Almeida S.F., Grosso A.R., Koch F., Fenouil R., Carvalho S., Andrade J.,
Levezinho H., Gut M., Eick D., Gut I., Andrau J.C., Ferrier P.,
Carmo-Fonseca M.;
"Splicing enhances recruitment of methyltransferase HYPB/Setd2 and
methylation of histone H3 Lys36.";
Nat. Struct. Mol. Biol. 18:977-983(2011).
[24]
FUNCTION.
PubMed=21526191; DOI=10.1371/journal.pone.0018844;
Hahn M.A., Wu X., Li A.X., Hahn T., Pfeifer G.P.;
"Relationship between gene body DNA methylation and intragenic H3K9me3 and
H3K36me3 chromatin marks.";
PLoS ONE 6:E18844-E18844(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-323; SER-624;
SER-754 AND SER-2082, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[26]
INVOLVEMENT IN LLS.
PubMed=23160955; DOI=10.1126/science.1227764;
O'Roak B.J., Vives L., Fu W., Egertson J.D., Stanaway I.B., Phelps I.G.,
Carvill G., Kumar A., Lee C., Ankenman K., Munson J., Hiatt J.B.,
Turner E.H., Levy R., O'Day D.R., Krumm N., Coe B.P., Martin B.K.,
Borenstein E., Nickerson D.A., Mefford H.C., Doherty D., Akey J.M.,
Bernier R., Eichler E.E., Shendure J.;
"Multiplex targeted sequencing identifies recurrently mutated genes in
autism spectrum disorders.";
Science 338:1619-1622(2012).
[27]
FUNCTION, INVOLVEMENT IN RCC, VARIANTS RCC ASP-1733 AND PRO-1769, AND
CHARACTERIZATION OF VARIANTS RCC ASP-1733 AND PRO-1769.
PubMed=23622243; DOI=10.1016/j.cell.2013.03.025;
Li F., Mao G., Tong D., Huang J., Gu L., Yang W., Li G.M.;
"The histone mark H3K36me3 regulates human DNA mismatch repair through its
interaction with MutSalpha.";
Cell 153:590-600(2013).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-344; SER-422;
SER-532; SER-614; SER-624; THR-626; SER-744; SER-754; SER-1098; SER-1228;
SER-1696; THR-1853; THR-1872; SER-1888; SER-1952; SER-2080 AND SER-2082,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[29]
INVOLVEMENT IN RCC.
PubMed=23792563; DOI=10.1038/nature12222;
Creighton C.J., Morgan M., Gunaratne P.H., Wheeler D.A., Gibbs R.A.,
Gordon Robertson A., Chu A., Beroukhim R., Cibulskis K., Signoretti S.,
Vandin Hsin-Ta Wu F., Raphael B.J., Verhaak R.G., Tamboli P.,
Torres-Garcia W., Akbani R., Weinstein J.N., Reuter V., Hsieh J.J.,
Rose Brannon A., Ari Hakimi A., Jacobsen A., Ciriello G., Reva B.,
Ricketts C.J., Marston Linehan W., Stuart J.M., Kimryn Rathmell W.,
Shen H., Laird P.W., Muzny D., Davis C., Morgan M., Xi L., Chang K.,
Kakkar N., Trevino L.R., Benton S., Reid J.G., Morton D., Doddapaneni H.,
Han Y., Lewis L., Dinh H., Kovar C., Zhu Y., Santibanez J., Wang M.,
Hale W., Kalra D., Creighton C.J., Wheeler D.A., Gibbs R.A., Getz G.,
Cibulskis K., Lawrence M.S., Sougnez C., Carter S.L., Sivachenko A.,
Lichtenstein L., Stewart C., Voet D., Fisher S., Gabriel S.B., Lander E.,
Beroukhim R., Schumacher S.E., Tabak B., Saksena G., Onofrio R.C.,
Carter S.L., Cherniack A.D., Gentry J., Ardlie K., Sougnez C., Getz G.,
Gabriel S.B., Meyerson M., Gordon Robertson A., Chu A., Chun H.J.,
Mungall A.J., Sipahimalani P., Stoll D., Ally A., Balasundaram M.,
Butterfield Y.S., Carlsen R., Carter C., Chuah E., Coope R.J., Dhalla N.,
Gorski S., Guin R., Hirst C., Hirst M., Holt R.A., Lebovitz C., Lee D.,
Li H.I., Mayo M., Moore R.A., Pleasance E., Plettner P., Schein J.E.,
Shafiei A., Slobodan J.R., Tam A., Thiessen N., Varhol R.J., Wye N.,
Zhao Y., Birol I., Jones S.J., Marra M.A., Auman J.T., Tan D., Jones C.D.,
Hoadley K.A., Mieczkowski P.A., Mose L.E., Jefferys S.R., Topal M.D.,
Liquori C., Turman Y.J., Shi Y., Waring S., Buda E., Walsh J., Wu J.,
Bodenheimer T., Hoyle A.P., Simons J.V., Soloway M.G., Balu S.,
Parker J.S., Neil Hayes D., Perou C.M., Kucherlapati R., Park P., Shen H.,
Triche T. Jr., Weisenberger D.J., Lai P.H., Bootwalla M.S., Maglinte D.T.,
Mahurkar S., Berman B.P., Van Den Berg D.J., Cope L., Baylin S.B.,
Laird P.W., Creighton C.J., Wheeler D.A., Getz G., Noble M.S., Dicara D.,
Zhang H., Cho J., Heiman D.I., Gehlenborg N., Voet D., Mallard W., Lin P.,
Frazer S., Stojanov P., Liu Y., Zhou L., Kim J., Lawrence M.S., Chin L.,
Vandin F., Wu H.T., Raphael B.J., Benz C., Yau C., Reynolds S.M.,
Shmulevich I., Verhaak R.G., Torres-Garcia W., Vegesna R., Kim H.,
Zhang W., Cogdell D., Jonasch E., Ding Z., Lu Y., Akbani R., Zhang N.,
Unruh A.K., Casasent T.D., Wakefield C., Tsavachidou D., Chin L.,
Mills G.B., Weinstein J.N., Jacobsen A., Rose Brannon A., Ciriello G.,
Schultz N., Ari Hakimi A., Reva B., Antipin Y., Gao J., Cerami E.,
Gross B., Arman Aksoy B., Sinha R., Weinhold N., Onur Sumer S.,
Taylor B.S., Shen R., Ostrovnaya I., Hsieh J.J., Berger M.F., Ladanyi M.,
Sander C., Fei S.S., Stout A., Spellman P.T., Rubin D.L., Liu T.T.,
Stuart J.M., Ng S., Paull E.O., Carlin D., Goldstein T., Waltman P.,
Ellrott K., Zhu J., Haussler D., Gunaratne P.H., Xiao W., Shelton C.,
Gardner J., Penny R., Sherman M., Mallery D., Morris S., Paulauskis J.,
Burnett K., Shelton T., Signoretti S., Kaelin W.G., Choueiri T.,
Atkins M.B., Penny R., Burnett K., Mallery D., Curley E., Tickoo S.,
Reuter V., Kimryn Rathmell W., Thorne L., Boice L., Huang M., Fisher J.C.,
Marston Linehan W., Vocke C.D., Peterson J., Worrell R., Merino M.J.,
Schmidt L.S., Tamboli P., Czerniak B.A., Aldape K.D., Wood C.G., Boyd J.,
Weaver J., Iacocca M.V., Petrelli N., Witkin G., Brown J., Czerwinski C.,
Huelsenbeck-Dill L., Rabeno B., Myers J., Morrison C., Bergsten J.,
Eckman J., Harr J., Smith C., Tucker K., Anne Zach L., Bshara W.,
Gaudioso C., Morrison C., Dhir R., Maranchie J., Nelson J., Parwani A.,
Potapova O., Fedosenko K., Cheville J.C., Houston Thompson R.,
Signoretti S., Kaelin W.G., Atkins M.B., Tickoo S., Reuter V.,
Marston Linehan W., Vocke C.D., Peterson J., Merino M.J., Schmidt L.S.,
Tamboli P., Mosquera J.M., Rubin M.A., Blute M.L., Kimryn Rathmell W.,
Pihl T., Jensen M., Sfeir R., Kahn A., Chu A., Kothiyal P., Snyder E.,
Pontius J., Ayala B., Backus M., Walton J., Baboud J., Berton D.,
Nicholls M., Srinivasan D., Raman R., Girshik S., Kigonya P., Alonso S.,
Sanbhadti R., Barletta S., Pot D., Sheth M., Demchok J.A., Davidsen T.,
Wang Z., Yang L., Tarnuzzer R.W., Zhang J., Eley G., Ferguson M.L.,
Mills Shaw K.R., Guyer M.S., Ozenberger B.A., Sofia H.J.;
"Comprehensive molecular characterization of clear cell renal cell
carcinoma.";
Nature 499:43-49(2013).
[30]
FUNCTION.
PubMed=23325844; DOI=10.1093/nar/gks1472;
Carvalho S., Raposo A.C., Martins F.B., Grosso A.R., Sridhara S.C.,
Rino J., Carmo-Fonseca M., de Almeida S.F.;
"Histone methyltransferase SETD2 coordinates FACT recruitment with
nucleosome dynamics during transcription.";
Nucleic Acids Res. 41:2881-2893(2013).
[31]
FUNCTION.
PubMed=24843002; DOI=10.7554/elife.02482;
Carvalho S., Vitor A.C., Sridhara S.C., Martins F.B., Raposo A.C.,
Desterro J.M., Ferreira J., de Almeida S.F.;
"SETD2 is required for DNA double-strand break repair and activation of the
p53-mediated checkpoint.";
Elife 3:E02482-E02482(2014).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-614 AND THR-1853,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[33]
INVOLVEMENT IN ALL, AND VARIANTS ALL ARG-2; GLY-19; ILE-267; PRO-470;
ALA-499; 794-TYR--GLU-2564 DEL; PRO-1076; GLY-1093; ALA-1171; GLY-1351;
GLU-1365; 1416-GLU--GLU-2564 DEL; ASN-1453; PRO-1609; MET-1663; PRO-1821;
ALA-1915; VAL-1920; SER-2361 AND 2546-LYS--GLU-2564 DEL.
PubMed=24662245; DOI=10.1038/ncomms4469;
Mar B.G., Bullinger L.B., McLean K.M., Grauman P.V., Harris M.H.,
Stevenson K., Neuberg D.S., Sinha A.U., Sallan S.E., Silverman L.B.,
Kung A.L., Lo Nigro L., Ebert B.L., Armstrong S.A.;
"Mutations in epigenetic regulators including SETD2 are gained during
relapse in paediatric acute lymphoblastic leukaemia.";
Nat. Commun. 5:3469-3469(2014).
[34]
INVOLVEMENT IN AML, INVOLVEMENT IN ALL, VARIANTS AML 70-ARG--GLU-2564 DEL;
ASN-800; GLY-1397; SER-1804; TRP-2122; 2325-GLN--GLU-2564 DEL AND LEU-2505,
AND VARIANTS ALL SER-226; ILE-761; ASN-1493; 1496-ARG--GLU-2564 DEL;
GLN-1654; 2077-ARG--GLU-2564 DEL; ALA-2214 AND 2524-CYS--GLU-2564 DEL.
PubMed=24509477; DOI=10.1038/ng.2894;
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 Q.F.;
"Identification of functional cooperative mutations of SETD2 in human acute
leukemia.";
Nat. Genet. 46:287-293(2014).
[35]
INVOLVEMENT IN LLS.
PubMed=26084711; DOI=10.1007/s10803-015-2484-8;
Lumish H.S., Wynn J., Devinsky O., Chung W.K.;
"SETD2 mutation in a child with autism, intellectual disabilities and
epilepsy.";
J. Autism Dev. Disord. 45:3764-3770(2015).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-637, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.o114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to replication
stress reveals novel small ubiquitin-like modified target proteins and
acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[37]
INVOLVEMENT IN RCC.
PubMed=25728682; DOI=10.1038/onc.2015.24;
Kanu N., Groenroos E., Martinez P., Burrell R.A., Yi Goh X., Bartkova J.,
Maya-Mendoza A., Mistrik M., Rowan A.J., Patel H., Rabinowitz A., East P.,
Wilson G., Santos C.R., McGranahan N., Gulati S., Gerlinger M.,
Birkbak N.J., Joshi T., Alexandrov L.B., Stratton M.R., Powles T.,
Matthews N., Bates P.A., Stewart A., Szallasi Z., Larkin J., Bartek J.,
Swanton C.;
"SETD2 loss-of-function promotes renal cancer branched evolution through
replication stress and impaired DNA repair.";
Oncogene 34:5699-5708(2015).
[38]
FUNCTION AS ALPHA-TUBULIN METHYLTRANSFERASE, CATALYTIC ACTIVITY, AND
INTERACTION WITH TUBA1A.
PubMed=27518565; DOI=10.1016/j.cell.2016.07.005;
Park I.Y., Powell R.T., Tripathi D.N., Dere R., Ho T.H., Blasius T.L.,
Chiang Y.C., Davis I.J., Fahey C.C., Hacker K.E., Verhey K.J.,
Bedford M.T., Jonasch E., Rathmell W.K., Walker C.L.;
"Dual chromatin and cytoskeletal remodeling by SETD2.";
Cell 166:950-962(2016).
[39]
POSSIBLE INVOLVEMENT IN LLS, AND FUNCTION.
PubMed=27317772; DOI=10.1136/jmedgenet-2015-103638;
Tlemsani C., Luscan A., Leulliot N., Bieth E., Afenjar A., Baujat G.,
Doco-Fenzy M., Goldenberg A., Lacombe D., Lambert L., Odent S., Pasche J.,
Sigaudy S., Buffet A., Violle-Poirsier C., Briand-Suleau A., Laurendeau I.,
Chin M., Saugier-Veber P., Vidaud D., Cormier-Daire V., Vidaud M.,
Pasmant E., Burglen L.;
"SETD2 and DNMT3A screen in the Sotos-like syndrome French cohort.";
J. Med. Genet. 53:743-751(2016).
[40]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH STAT1, AND MUTAGENESIS OF
ARG-1625 AND CYS-1631.
PubMed=28753426; DOI=10.1016/j.cell.2017.06.042;
Chen K., Liu J., Liu S., Xia M., Zhang X., Han D., Jiang Y., Wang C.,
Cao X.;
"Methyltransferase SETD2-mediated methylation of STAT1 is critical for
interferon antiviral activity.";
Cell 170:492-506(2017).
[41]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-359; LYS-637 AND LYS-776, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[42]
STRUCTURE BY NMR OF 2457-2564, INTERACTION WITH POLR2A, MUTAGENESIS OF
ARG-2475; LYS-2476; GLN-2480; PHE-2481; VAL-2483; LYS-2506; ARG-2510;
HIS-2514; GLY-2515; GLU-2528 AND GLU-2531, AND CHARACTERIZATION OF VARIANT
AML LEU-2505.
PubMed=16314571; DOI=10.1073/pnas.0506350102;
Li M., Phatnani H.P., Guan Z., Sage H., Greenleaf A.L., Zhou P.;
"Solution structure of the Set2-Rpb1 interacting domain of human Set2 and
its interaction with the hyperphosphorylated C-terminal domain of Rpb1.";
Proc. Natl. Acad. Sci. U.S.A. 102:17636-17641(2005).
[43]
X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 1434-1711 IN COMPLEX WITH
S-ADENOSYL-L-METHIONINE OR N-PROPYL SINEFUNGIN AND ZINC, FUNCTION,
BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
MUTAGENESIS OF PHE-1668; GLN-1669; ARG-1670 AND TYR-1671.
PubMed=23043551; DOI=10.1021/ja307060p;
Zheng W., Ibanez G., Wu H., Blum G., Zeng H., Dong A., Li F., Hajian T.,
Allali-Hassani A., Amaya M.F., Siarheyeva A., Yu W., Brown P.J.,
Schapira M., Vedadi M., Min J., Luo M.;
"Sinefungin derivatives as inhibitors and structure probes of protein
lysine methyltransferase SETD2.";
J. Am. Chem. Soc. 134:18004-18014(2012).
[44]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 1434-1711 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE AND ZINC, FUNCTION, CATALYTIC ACTIVITY, DOMAIN,
AND MUTAGENESIS OF PHE-1589; TYR-1604; GLU-1636; THR-1637; PHE-1668 AND
TYR-1671.
PubMed=27474439; DOI=10.1101/gad.284323.116;
Yang S., Zheng X., Lu C., Li G.M., Allis C.D., Li H.;
"Molecular basis for oncohistone H3 recognition by SETD2
methyltransferase.";
Genes Dev. 30:1611-1616(2016).
[45]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1435-1711 IN COMPLEX WITH
S-ADENOSYL-L-HOMOCYSTEINE AND ZINC, AND DOMAIN.
PubMed=28256625; DOI=10.1038/srep43906;
Zhang Y., Shan C.M., Wang J., Bao K., Tong L., Jia S.;
"Molecular basis for the role of oncogenic histone mutations in modulating
H3K36 methylation.";
Sci. Rep. 7:43906-43906(2017).
[46]
VARIANT LLS TRP-1815.
PubMed=24852293; DOI=10.1136/jmedgenet-2014-102402;
Luscan A., Laurendeau I., Malan V., Francannet C., Odent S., Giuliano F.,
Lacombe D., Touraine R., Vidaud M., Pasmant E., Cormier-Daire V.;
"Mutations in SETD2 cause a novel overgrowth condition.";
J. Med. Genet. 51:512-517(2014).
[47]
VARIANT CYS-488.
PubMed=26637798; DOI=10.1016/j.neuron.2015.11.009;
D'Gama A.M., Pochareddy S., Li M., Jamuar S.S., Reiff R.E., Lam A.T.,
Sestan N., Walsh C.A.;
"Targeted DNA Sequencing from Autism Spectrum Disorder Brains Implicates
Multiple Genetic Mechanisms.";
Neuron 88:910-917(2015).
-!- FUNCTION: Histone methyltransferase that specifically trimethylates
'Lys-36' of histone H3 (H3K36me3) using dimethylated 'Lys-36'
(H3K36me2) as substrate (PubMed:16118227, PubMed:19141475,
PubMed:21526191, PubMed:21792193, PubMed:23043551, PubMed:27474439).
Represents the main enzyme generating H3K36me3, a specific tag for
epigenetic transcriptional activation (By similarity). Plays a role in
chromatin structure modulation during elongation by coordinating
recruitment of the FACT complex and by interacting with
hyperphosphorylated POLR2A (PubMed:23325844). Acts as a key regulator
of DNA mismatch repair in G1 and early S phase by generating H3K36me3,
a mark required to recruit MSH6 subunit of the MutS alpha complex:
early recruitment of the MutS alpha complex to chromatin to be
replicated allows a quick identification of mismatch DNA to initiate
the mismatch repair reaction (PubMed:23622243). Required for DNA
double-strand break repair in response to DNA damage: acts by mediating
formation of H3K36me3, promoting recruitment of RAD51 and DNA repair
via homologous recombination (HR) (PubMed:24843002). Acts as a tumor
suppressor (PubMed:24509477). H3K36me3 also plays an essential role in
the maintenance of a heterochromatic state, by recruiting DNA
methyltransferase DNMT3A (PubMed:27317772). H3K36me3 is also enhanced
in intron-containing genes, suggesting that SETD2 recruitment is
enhanced by splicing and that splicing is coupled to recruitment of
elongating RNA polymerase (PubMed:21792193). Required during
angiogenesis (By similarity). Required for endoderm development by
promoting embryonic stem cell differentiation toward endoderm: acts by
mediating formation of H3K36me3 in distal promoter regions of FGFR3,
leading to regulate transcription initiation of FGFR3 (By similarity).
In addition to histones, also mediates methylation of other proteins,
such as tubulins and STAT1 (PubMed:27518565, PubMed:28753426).
Trimethylates 'Lys-40' of alpha-tubulins such as TUBA1B (alpha-
TubK40me3); alpha-TubK40me3 is required for normal mitosis and
cytokinesis and may be a specific tag in cytoskeletal remodeling
(PubMed:27518565). Involved in interferon-alpha-induced antiviral
defense by mediating both monomethylation of STAT1 at 'Lys-525' and
catalyzing H3K36me3 on promoters of some interferon-stimulated genes
(ISGs) to activate gene transcription (PubMed:28753426).
{ECO:0000250|UniProtKB:E9Q5F9, ECO:0000269|PubMed:16118227,
ECO:0000269|PubMed:19141475, ECO:0000269|PubMed:21526191,
ECO:0000269|PubMed:21792193, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:23325844, ECO:0000269|PubMed:23622243,
ECO:0000269|PubMed:24509477, ECO:0000269|PubMed:24843002,
ECO:0000269|PubMed:27317772, ECO:0000269|PubMed:27474439,
ECO:0000269|PubMed:27518565, ECO:0000269|PubMed:28753426}.
-!- FUNCTION: (Microbial infection) Recruited to the promoters of
adenovirus 12 E1A gene in case of infection, possibly leading to
regulate its expression. {ECO:0000269|PubMed:11461154}.
-!- CATALYTIC ACTIVITY:
Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-
methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
Evidence={ECO:0000269|PubMed:23043551, ECO:0000269|PubMed:27474439};
-!- CATALYTIC ACTIVITY:
Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
Evidence={ECO:0000269|PubMed:28753426};
-!- CATALYTIC ACTIVITY:
Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
Evidence={ECO:0000269|PubMed:27518565};
-!- ACTIVITY REGULATION: Specifically inhibited by sinefungin derivatives.
N-propyl sinefungin (Pr-SNF) interacts preferentially with SETD2.
{ECO:0000269|PubMed:23043551}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.21 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:23043551};
KM=0.42 uM for histone H3 {ECO:0000269|PubMed:23043551};
Note=Kcat is 0.14 min(-1). {ECO:0000269|PubMed:23043551};
-!- SUBUNIT: Specifically interacts with hyperphosphorylated C-terminal
domain (CTD) of RNA polymerase II large subunit (POLR2A): binds to CTD
heptad repeats doubly phosphorylated on 'Ser-2' and 'Ser-5' of each
heptad (PubMed:16118227, PubMed:16314571). Interacts with HTT
(PubMed:11461154, PubMed:9700202, PubMed:10958656). Interacts with IWS1
(PubMed:19141475). Interacts with p53/TP53; leading to regulate
p53/TP53 target genes (PubMed:18585004). Component of a complex with
HNRNPL (PubMed:19332550). Interacts with TUBA1A; the interaction is
independent on alpha-tubulin acetylation on 'Lys-40' (PubMed:27518565).
Interacts with STAT1 (PubMed:28753426). {ECO:0000269|PubMed:10958656,
ECO:0000269|PubMed:11461154, ECO:0000269|PubMed:16118227,
ECO:0000269|PubMed:16314571, ECO:0000269|PubMed:18585004,
ECO:0000269|PubMed:19141475, ECO:0000269|PubMed:19332550,
ECO:0000269|PubMed:27518565, ECO:0000269|PubMed:28753426,
ECO:0000269|PubMed:9700202}.
-!- INTERACTION:
P42858:HTT; NbExp=4; IntAct=EBI-945869, EBI-466029;
P84022:SMAD3; NbExp=2; IntAct=EBI-945869, EBI-347161;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:E9Q5F9}.
Chromosome {ECO:0000250|UniProtKB:E9Q5F9}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9BYW2-1; Sequence=Displayed;
Name=2;
IsoId=Q9BYW2-2; Sequence=VSP_020915;
Name=3;
IsoId=Q9BYW2-3; Sequence=VSP_020914;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:11461154}.
-!- DOMAIN: The low charge region mediates the transcriptional activation
activity. {ECO:0000269|PubMed:16118227}.
-!- DOMAIN: The catalytic SET domain binds histone H3 (PubMed:27474439,
PubMed:28256625). It is also able to bind oncogenic histone H3 K36M/I
found in a number of cancer types, in which histone H3 'Lys-36' is
replaced by a Met or an Ile residue. When binding the oncogenic variant
histone H3 K36M/I, the SET domain undergoes dramatic conformational
change to accommodate the histone H3 peptide, leading to sequester and
inhibit SETD2 activity and block global H3K36 methylation
(PubMed:27474439, PubMed:28256625). {ECO:0000269|PubMed:27474439,
ECO:0000269|PubMed:28256625}.
-!- PTM: May be automethylated. {ECO:0000269|PubMed:16118227}.
-!- DISEASE: Renal cell carcinoma (RCC) [MIM:144700]: Renal cell carcinoma
is a heterogeneous group of sporadic or hereditary carcinoma derived
from cells of the proximal renal tubular epithelium. It is
subclassified into clear cell renal carcinoma (non-papillary
carcinoma), papillary renal cell carcinoma, chromophobe renal cell
carcinoma, collecting duct carcinoma with medullary carcinoma of the
kidney, and unclassified renal cell carcinoma. Clear cell renal cell
carcinoma is the most common subtype. {ECO:0000269|PubMed:20054297,
ECO:0000269|PubMed:23622243, ECO:0000269|PubMed:23792563,
ECO:0000269|PubMed:25728682}. Note=The disease may be caused by
mutations affecting the gene represented in this entry. Defects of
SETD2 are associated with loss of DNA methylation at non-promoter
regions (PubMed:23792563). SETD2 defects lead to aberrant and reduced
nucleosome compaction and chromatin association of key replication
proteins, such as MCM7 and DNA polymerase delta, leading to hinder
replication fork progression and prevent loading of RAD51 homologous
recombination repair factor at DNA breaks (PubMed:25728682).
{ECO:0000269|PubMed:23792563, ECO:0000269|PubMed:25728682}.
-!- DISEASE: Luscan-Lumish syndrome (LLS) [MIM:616831]: An autosomal
dominant syndrome with a variable phenotype. Clinical features include
macrocephaly, distinctive facial appearance, postnatal overgrowth,
various degrees of learning difficulties, autism spectrum disorder, and
intellectual disability. {ECO:0000269|PubMed:23160955,
ECO:0000269|PubMed:24852293, ECO:0000269|PubMed:26084711,
ECO:0000269|PubMed:27317772}. Note=The disease may be caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Leukemia, acute lymphoblastic (ALL) [MIM:613065]: A subtype of
acute leukemia, a cancer of the white blood cells. ALL is a malignant
disease of bone marrow and the most common malignancy diagnosed in
children. The malignant cells are lymphoid precursor cells
(lymphoblasts) that are arrested in an early stage of development. The
lymphoblasts replace the normal marrow elements, resulting in a marked
decrease in the production of normal blood cells. Consequently, anemia,
thrombocytopenia, and neutropenia occur to varying degrees. The
lymphoblasts also proliferate in organs other than the marrow,
particularly the liver, spleen, and lymphnodes.
{ECO:0000269|PubMed:24509477, ECO:0000269|PubMed:24662245}. Note=The
disease may be caused by mutations affecting distinct genetic loci,
including the gene represented in this entry.
-!- DISEASE: Leukemia, acute myelogenous (AML) [MIM:601626]: A subtype of
acute leukemia, a cancer of the white blood cells. AML is a malignant
disease of bone marrow characterized by maturational arrest of
hematopoietic precursors at an early stage of development. Clonal
expansion of myeloid blasts occurs in bone marrow, blood, and other
tissue. Myelogenous leukemias develop from changes in cells that
normally produce neutrophils, basophils, eosinophils and monocytes.
{ECO:0000269|PubMed:16314571, ECO:0000269|PubMed:24509477}. Note=The
disease may be caused by mutations affecting distinct genetic loci,
including the gene represented in this entry.
-!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00190}.
-!- SEQUENCE CAUTION:
Sequence=AAF29041.1; Type=Frameshift; Evidence={ECO:0000305};
Sequence=AAH72440.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
Sequence=AAI17163.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=AAI17165.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=AAT77612.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=AAT77613.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=BAB15367.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=BAB15367.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAC87131.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
Sequence=CAC28349.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
Sequence=CAD38601.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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EMBL; AC094020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC127430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AK026125; BAB15367.1; ALT_SEQ; mRNA.
EMBL; AK127782; BAC87131.1; ALT_INIT; mRNA.
EMBL; AK131371; BAD18522.1; -; mRNA.
EMBL; AL713692; CAD28492.1; -; mRNA.
EMBL; AL831959; CAD38601.2; ALT_INIT; mRNA.
EMBL; AL833394; CAH10589.1; -; mRNA.
EMBL; AJ238403; CAC28349.1; ALT_SEQ; mRNA.
EMBL; BC072440; AAH72440.1; ALT_SEQ; mRNA.
EMBL; BC090954; AAH90954.1; -; mRNA.
EMBL; BC117162; AAI17163.1; ALT_INIT; mRNA.
EMBL; BC117164; AAI17165.1; ALT_INIT; mRNA.
EMBL; AY576987; AAT77612.1; ALT_INIT; mRNA.
EMBL; AY576988; AAT77613.1; ALT_INIT; mRNA.
EMBL; AB051519; BAB21823.2; -; mRNA.
EMBL; AF161554; AAF29041.1; ALT_FRAME; mRNA.
EMBL; AF049103; AAC26194.1; -; mRNA.
EMBL; AF049610; AAC26846.1; -; mRNA.
CCDS; CCDS2749.2; -. [Q9BYW2-1]
RefSeq; NP_054878.5; NM_014159.6. [Q9BYW2-1]
PDB; 2A7O; NMR; -; A=2457-2564.
PDB; 2MDC; NMR; -; A=2385-2430.
PDB; 2MDI; NMR; -; A=2377-2430.
PDB; 2MDJ; NMR; -; A=2377-2430.
PDB; 4FMU; X-ray; 2.10 A; A=1434-1711.
PDB; 4H12; X-ray; 1.99 A; A=1434-1711.
PDB; 5JJY; X-ray; 2.05 A; A=1434-1711.
PDB; 5JLB; X-ray; 1.50 A; A=1434-1711.
PDB; 5JLE; X-ray; 2.40 A; A=1434-1711.
PDB; 5LSS; X-ray; 1.79 A; A=1433-1711.
PDB; 5LSX; X-ray; 2.90 A; A=1433-1711.
PDB; 5LSY; X-ray; 1.62 A; A=1433-1711.
PDB; 5LSZ; X-ray; 1.62 A; A=1433-1711.
PDB; 5LT6; X-ray; 2.05 A; A/B=1433-1711.
PDB; 5LT7; X-ray; 1.51 A; A=1433-1711.
PDB; 5LT8; X-ray; 1.57 A; A=1433-1711.
PDB; 5V21; X-ray; 2.42 A; A=1435-1711.
PDB; 5V22; X-ray; 2.40 A; A=1435-1711.
PDBsum; 2A7O; -.
PDBsum; 2MDC; -.
PDBsum; 2MDI; -.
PDBsum; 2MDJ; -.
PDBsum; 4FMU; -.
PDBsum; 4H12; -.
PDBsum; 5JJY; -.
PDBsum; 5JLB; -.
PDBsum; 5JLE; -.
PDBsum; 5LSS; -.
PDBsum; 5LSX; -.
PDBsum; 5LSY; -.
PDBsum; 5LSZ; -.
PDBsum; 5LT6; -.
PDBsum; 5LT7; -.
PDBsum; 5LT8; -.
PDBsum; 5V21; -.
PDBsum; 5V22; -.
SMR; Q9BYW2; -.
BioGrid; 118845; 57.
IntAct; Q9BYW2; 32.
STRING; 9606.ENSP00000386759; -.
BindingDB; Q9BYW2; -.
ChEMBL; CHEMBL3108647; -.
iPTMnet; Q9BYW2; -.
PhosphoSitePlus; Q9BYW2; -.
BioMuta; SETD2; -.
DMDM; 296452963; -.
OGP; Q9BYW2; -.
EPD; Q9BYW2; -.
jPOST; Q9BYW2; -.
MassIVE; Q9BYW2; -.
MaxQB; Q9BYW2; -.
PaxDb; Q9BYW2; -.
PeptideAtlas; Q9BYW2; -.
PRIDE; Q9BYW2; -.
ProteomicsDB; 79730; -. [Q9BYW2-1]
ProteomicsDB; 79731; -. [Q9BYW2-2]
ProteomicsDB; 79732; -. [Q9BYW2-3]
Ensembl; ENST00000409792; ENSP00000386759; ENSG00000181555. [Q9BYW2-1]
GeneID; 29072; -.
KEGG; hsa:29072; -.
UCSC; uc003cqs.4; human. [Q9BYW2-1]
CTD; 29072; -.
DisGeNET; 29072; -.
EuPathDB; HostDB:ENSG00000181555.19; -.
GeneCards; SETD2; -.
HGNC; HGNC:18420; SETD2.
HPA; HPA042451; -.
MalaCards; SETD2; -.
MIM; 144700; phenotype.
MIM; 601626; phenotype.
MIM; 612778; gene.
MIM; 613065; phenotype.
MIM; 616831; phenotype.
neXtProt; NX_Q9BYW2; -.
OpenTargets; ENSG00000181555; -.
Orphanet; 821; Sotos syndrome.
PharmGKB; PA143485612; -.
eggNOG; KOG4442; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00940000160086; -.
InParanoid; Q9BYW2; -.
KO; K11423; -.
OMA; FKSSFCC; -.
OrthoDB; 507784at2759; -.
PhylomeDB; Q9BYW2; -.
TreeFam; TF106477; -.
BRENDA; 2.1.1.43; 2681.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
SignaLink; Q9BYW2; -.
SIGNOR; Q9BYW2; -.
ChiTaRS; SETD2; human.
EvolutionaryTrace; Q9BYW2; -.
GeneWiki; SETD2; -.
GenomeRNAi; 29072; -.
Pharos; Q9BYW2; Tchem.
PRO; PR:Q9BYW2; -.
Proteomes; UP000005640; Chromosome 3.
RNAct; Q9BYW2; protein.
Bgee; ENSG00000181555; Expressed in 229 organ(s), highest expression level in oviduct epithelium.
ExpressionAtlas; Q9BYW2; baseline and differential.
Genevisible; Q9BYW2; HS.
GO; GO:0005694; C:chromosome; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0043014; F:alpha-tubulin binding; IDA:UniProtKB.
GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:UniProtKB.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0035441; P:cell migration involved in vasculogenesis; IEA:Ensembl.
GO; GO:0060977; P:coronary vasculature morphogenesis; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
GO; GO:0060669; P:embryonic placenta morphogenesis; IEA:Ensembl.
GO; GO:0035987; P:endodermal cell differentiation; ISS:UniProtKB.
GO; GO:0030900; P:forebrain development; IEA:Ensembl.
GO; GO:0097676; P:histone H3-K36 dimethylation; IDA:HGNC.
GO; GO:0097198; P:histone H3-K36 trimethylation; IDA:UniProtKB.
GO; GO:0048332; P:mesoderm morphogenesis; IEA:Ensembl.
GO; GO:1902850; P:microtubule cytoskeleton organization involved in mitosis; IDA:UniProtKB.
GO; GO:0006298; P:mismatch repair; IMP:UniProtKB.
GO; GO:0001763; P:morphogenesis of a branching structure; IEA:Ensembl.
GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
GO; GO:0034728; P:nucleosome organization; IMP:UniProtKB.
GO; GO:0018026; P:peptidyl-lysine monomethylation; IDA:UniProtKB.
GO; GO:0018023; P:peptidyl-lysine trimethylation; IDA:UniProtKB.
GO; GO:0060039; P:pericardium development; IEA:Ensembl.
GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:UniProtKB.
GO; GO:0032465; P:regulation of cytokinesis; IDA:UniProtKB.
GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IDA:UniProtKB.
GO; GO:0010793; P:regulation of mRNA export from nucleus; IMP:UniProtKB.
GO; GO:1905634; P:regulation of protein localization to chromatin; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
GO; GO:0034340; P:response to type I interferon; IDA:UniProtKB.
GO; GO:0048864; P:stem cell development; IEA:Ensembl.
GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:UniProtKB.
CDD; cd00201; WW; 1.
Gene3D; 1.10.1740.100; -; 1.
Gene3D; 1.20.930.10; -; 1.
InterPro; IPR006560; AWS_dom.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR042294; SETD2.
InterPro; IPR013257; SRI.
InterPro; IPR038190; SRI_sf.
InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
PANTHER; PTHR46711; PTHR46711; 1.
Pfam; PF17907; AWS; 1.
Pfam; PF00856; SET; 1.
Pfam; PF08236; SRI; 1.
Pfam; PF00397; WW; 1.
SMART; SM00570; AWS; 1.
SMART; SM00508; PostSET; 1.
SMART; SM00317; SET; 1.
SMART; SM00456; WW; 1.
SUPFAM; SSF51045; SSF51045; 1.
PROSITE; PS51215; AWS; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50280; SET; 1.
PROSITE; PS01159; WW_DOMAIN_1; 1.
PROSITE; PS50020; WW_DOMAIN_2; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Antiviral defense;
Autism spectrum disorder; Chromatin regulator; Chromosome; Coiled coil;
Developmental protein; Differentiation; Disease mutation; DNA damage;
DNA repair; Host-virus interaction; Immunity; Innate immunity;
Isopeptide bond; Mental retardation; Metal-binding; Methyltransferase;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
S-adenosyl-L-methionine; Transcription; Transcription regulation;
Transferase; Tumor suppressor; Ubl conjugation; Zinc.
CHAIN 1..2564
/note="Histone-lysine N-methyltransferase SETD2"
/id="PRO_0000252367"
DOMAIN 1494..1548
/note="AWS"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
DOMAIN 1550..1667
/note="SET"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
DOMAIN 1674..1690
/note="Post-SET"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
DOMAIN 2389..2422
/note="WW"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
REGION 1418..1714
/note="Interaction with TUBA1A"
/evidence="ECO:0000269|PubMed:27518565"
REGION 1560..1562
/note="Inhibitor binding"
/evidence="ECO:0000269|PubMed:23043551"
REGION 1560..1562
/note="S-adenosyl-L-methionine binding"
/evidence="ECO:0000244|PDB:4H12, ECO:0000244|PDB:5JJY,
ECO:0000244|PDB:5JLB, ECO:0000244|PDB:5JLE,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
REGION 1603..1605
/note="Inhibitor binding"
/evidence="ECO:0000269|PubMed:23043551"
REGION 1603..1605
/note="S-adenosyl-L-methionine binding"
/evidence="ECO:0000244|PDB:4H12, ECO:0000244|PDB:5JJY,
ECO:0000244|PDB:5JLB, ECO:0000244|PDB:5JLE,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
REGION 1628..1629
/note="Inhibitor binding"
/evidence="ECO:0000269|PubMed:23043551"
REGION 1628..1629
/note="S-adenosyl-L-methionine binding"
/evidence="ECO:0000244|PDB:4H12, ECO:0000244|PDB:5JJY,
ECO:0000244|PDB:5JLB, ECO:0000244|PDB:5JLE,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
REGION 2137..2366
/note="Low charge region"
/evidence="ECO:0000269|PubMed:16118227"
REGION 2457..2564
/note="Interaction with POLR2A"
/evidence="ECO:0000269|PubMed:16314571"
COILED 2117..2146
/evidence="ECO:0000255"
COMPBIAS 166..247
/note="Pro-rich"
COMPBIAS 385..456
/note="Arg-rich"
COMPBIAS 2149..2232
/note="Pro-rich"
COMPBIAS 2266..2365
/note="Gln-rich"
METAL 1499
/note="Zinc 1"
/evidence="ECO:0000244|PDB:4FMU, ECO:0000244|PDB:4H12,
ECO:0000244|PDB:5JJY, ECO:0000244|PDB:5JLB,
ECO:0000244|PDB:5JLE, ECO:0000244|PDB:5V21,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
METAL 1501
/note="Zinc 1"
/evidence="ECO:0000244|PDB:4FMU, ECO:0000244|PDB:4H12,
ECO:0000244|PDB:5JJY, ECO:0000244|PDB:5JLB,
ECO:0000244|PDB:5JLE, ECO:0000244|PDB:5V21,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
METAL 1516
/note="Zinc 1"
/evidence="ECO:0000244|PDB:4FMU, ECO:0000244|PDB:4H12,
ECO:0000244|PDB:5JJY, ECO:0000244|PDB:5JLB,
ECO:0000244|PDB:5JLE, ECO:0000244|PDB:5V21,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
METAL 1516
/note="Zinc 2"
/evidence="ECO:0000244|PDB:4FMU, ECO:0000244|PDB:4H12,
ECO:0000244|PDB:5JJY, ECO:0000244|PDB:5JLB,
ECO:0000244|PDB:5JLE, ECO:0000244|PDB:5V21,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
METAL 1520
/note="Zinc 1"
/evidence="ECO:0000244|PDB:4FMU, ECO:0000244|PDB:4H12,
ECO:0000244|PDB:5JJY, ECO:0000244|PDB:5JLB,
ECO:0000244|PDB:5JLE, ECO:0000244|PDB:5V21,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
METAL 1529
/note="Zinc 2"
/evidence="ECO:0000244|PDB:4FMU, ECO:0000244|PDB:4H12,
ECO:0000244|PDB:5JJY, ECO:0000244|PDB:5JLB,
ECO:0000244|PDB:5JLE, ECO:0000244|PDB:5V21,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
METAL 1533
/note="Zinc 2"
/evidence="ECO:0000244|PDB:4FMU, ECO:0000244|PDB:4H12,
ECO:0000244|PDB:5JJY, ECO:0000244|PDB:5JLB,
ECO:0000244|PDB:5JLE, ECO:0000244|PDB:5V21,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
METAL 1539
/note="Zinc 2"
/evidence="ECO:0000244|PDB:4FMU, ECO:0000244|PDB:4H12,
ECO:0000244|PDB:5JJY, ECO:0000244|PDB:5JLB,
ECO:0000244|PDB:5JLE, ECO:0000244|PDB:5V21,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
METAL 1631
/note="Zinc 3"
/evidence="ECO:0000244|PDB:4FMU, ECO:0000244|PDB:4H12,
ECO:0000244|PDB:5JJY, ECO:0000244|PDB:5JLB,
ECO:0000244|PDB:5JLE, ECO:0000244|PDB:5V21,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
METAL 1678
/note="Zinc 3"
/evidence="ECO:0000244|PDB:4FMU, ECO:0000244|PDB:4H12,
ECO:0000244|PDB:5JJY, ECO:0000244|PDB:5JLB,
ECO:0000244|PDB:5JLE, ECO:0000244|PDB:5V21,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
METAL 1680
/note="Zinc 3"
/evidence="ECO:0000244|PDB:4FMU, ECO:0000244|PDB:4H12,
ECO:0000244|PDB:5JJY, ECO:0000244|PDB:5JLB,
ECO:0000244|PDB:5JLE, ECO:0000244|PDB:5V21,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
METAL 1685
/note="Zinc 3"
/evidence="ECO:0000244|PDB:4FMU, ECO:0000244|PDB:4H12,
ECO:0000244|PDB:5JJY, ECO:0000244|PDB:5JLB,
ECO:0000244|PDB:5JLE, ECO:0000244|PDB:5V21,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
BINDING 1625
/note="Inhibitor"
/evidence="ECO:0000269|PubMed:23043551"
BINDING 1676
/note="Inhibitor; alternate"
/evidence="ECO:0000269|PubMed:23043551"
BINDING 1676
/note="S-adenosyl-L-methionine; alternate"
/evidence="ECO:0000244|PDB:4H12, ECO:0000244|PDB:5JJY,
ECO:0000244|PDB:5JLB, ECO:0000244|PDB:5JLE,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
BINDING 1679
/note="Inhibitor; via amide nitrogen; alternate"
/evidence="ECO:0000244|PDB:5V22,
ECO:0000269|PubMed:23043551, ECO:0000269|PubMed:28256625"
BINDING 1679
/note="S-adenosyl-L-methionine; via amide nitrogen;
alternate"
/evidence="ECO:0000244|PDB:4H12, ECO:0000244|PDB:5JJY,
ECO:0000244|PDB:5JLB, ECO:0000244|PDB:5JLE,
ECO:0000244|PDB:5V22, ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439, ECO:0000269|PubMed:28256625"
MOD_RES 131
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163"
MOD_RES 321
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:24275569"
MOD_RES 323
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692"
MOD_RES 344
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 422
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 532
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 614
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
MOD_RES 624
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163"
MOD_RES 626
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 698
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:E9Q5F9"
MOD_RES 708
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332"
MOD_RES 744
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163"
MOD_RES 754
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332, ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163"
MOD_RES 1098
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 1228
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:23186163"
MOD_RES 1413
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:E9Q5F9"
MOD_RES 1415
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:E9Q5F9"
MOD_RES 1417
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:E9Q5F9"
MOD_RES 1696
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 1844
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:E9Q5F9"
MOD_RES 1845
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:E9Q5F9"
MOD_RES 1853
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569"
MOD_RES 1872
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163"
MOD_RES 1888
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 1952
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 1980
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:E9Q5F9"
MOD_RES 1988
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:E9Q5F9"
MOD_RES 1995
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:E9Q5F9"
MOD_RES 2080
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163"
MOD_RES 2082
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163"
CROSSLNK 359
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
CROSSLNK 637
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733"
CROSSLNK 776
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0000244|PubMed:28112733"
VAR_SEQ 1573..2564
/note="Missing (in isoform 3)"
/evidence="ECO:0000303|PubMed:17974005"
/id="VSP_020914"
VAR_SEQ 1715..2564
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|Ref.7"
/id="VSP_020915"
VARIANT 2
/note="K -> R (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079054"
VARIANT 19
/note="E -> G (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079055"
VARIANT 70..2564
/note="Missing (in AML; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079056"
VARIANT 226
/note="P -> S (in ALL; unknown pathological significance;
somatic mutation; dbSNP:rs780963440)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079057"
VARIANT 267
/note="V -> I (in ALL; unknown pathological significance;
somatic mutation; dbSNP:rs186148199)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079058"
VARIANT 470
/note="S -> P (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079059"
VARIANT 488
/note="Y -> C (found in a patient with autism; unknown
pathological significance; dbSNP:rs757781388)"
/evidence="ECO:0000269|PubMed:26637798"
/id="VAR_078707"
VARIANT 499
/note="T -> A (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079060"
VARIANT 761
/note="M -> I (in ALL; unknown pathological significance;
somatic mutation; dbSNP:rs188887061)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079061"
VARIANT 768
/note="V -> L (in dbSNP:rs9311404)"
/id="VAR_027839"
VARIANT 794..2564
/note="Missing (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079062"
VARIANT 800
/note="S -> N (in AML; unknown pathological significance;
somatic mutation; dbSNP:rs1169288572)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079063"
VARIANT 902
/note="E -> Q (in dbSNP:rs58906143)"
/id="VAR_061216"
VARIANT 1076
/note="S -> P (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079064"
VARIANT 1093
/note="S -> G (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079065"
VARIANT 1171
/note="T -> A (in ALL; unknown pathological significance;
somatic mutation; dbSNP:rs540476365)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079066"
VARIANT 1351
/note="D -> G (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079067"
VARIANT 1365
/note="G -> E (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079068"
VARIANT 1397
/note="D -> G (in AML; unknown pathological significance;
somatic mutation; dbSNP:rs754921650)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079069"
VARIANT 1416..2564
/note="Missing (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079070"
VARIANT 1453
/note="D -> N (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079071"
VARIANT 1493
/note="D -> N (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079072"
VARIANT 1496..2564
/note="Missing (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079073"
VARIANT 1609
/note="L -> P (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079074"
VARIANT 1654
/note="K -> Q (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079075"
VARIANT 1663
/note="T -> M (in ALL; unknown pathological significance;
somatic mutation; dbSNP:rs1478147351)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079076"
VARIANT 1733
/note="N -> D (in RCC; defects in recruitment of the MutS
alpha complex)"
/evidence="ECO:0000269|PubMed:23622243"
/id="VAR_069812"
VARIANT 1769
/note="S -> P (in RCC; defects in recruitment of the MutS
alpha complex)"
/evidence="ECO:0000269|PubMed:23622243"
/id="VAR_069813"
VARIANT 1804
/note="L -> S (in AML; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079077"
VARIANT 1815
/note="L -> W (in LLS; unknown pathological significance;
dbSNP:rs869025570)"
/evidence="ECO:0000269|PubMed:24852293"
/id="VAR_076536"
VARIANT 1821
/note="L -> P (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079078"
VARIANT 1868
/note="A -> D (in dbSNP:rs11721074)"
/id="VAR_027840"
VARIANT 1915
/note="V -> A (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079079"
VARIANT 1920
/note="E -> V (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079080"
VARIANT 1962
/note="P -> L (in dbSNP:rs4082155)"
/evidence="ECO:0000269|PubMed:11214970,
ECO:0000269|PubMed:15489334"
/id="VAR_027841"
VARIANT 2077..2564
/note="Missing (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079081"
VARIANT 2122
/note="R -> W (in AML; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079082"
VARIANT 2214
/note="T -> A (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079083"
VARIANT 2325..2564
/note="Missing (in AML; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079084"
VARIANT 2361
/note="P -> S (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079085"
VARIANT 2505
/note="F -> L (in AML; Impairs interaction with
hyperphosphorylated POLR2A; unknown pathological
significance; somatic mutation)"
/evidence="ECO:0000269|PubMed:16314571,
ECO:0000269|PubMed:24509477"
/id="VAR_079086"
VARIANT 2524..2564
/note="Missing (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24509477"
/id="VAR_079087"
VARIANT 2546..2564
/note="Missing (in ALL; unknown pathological significance;
somatic mutation)"
/evidence="ECO:0000269|PubMed:24662245"
/id="VAR_079088"
MUTAGEN 1589
/note="F->A: Strongly reduced methyltransferase activity."
/evidence="ECO:0000269|PubMed:27474439"
MUTAGEN 1604
/note="Y->A: Increased methyltransferase activity."
/evidence="ECO:0000269|PubMed:27474439"
MUTAGEN 1625
/note="R->H,G: Loss of methyltransferase activity.
Abolishes ability to monomethylate STAT1."
/evidence="ECO:0000269|PubMed:16118227,
ECO:0000269|PubMed:28753426"
MUTAGEN 1631
/note="C->A: Does not affect methyltransferase activity."
/evidence="ECO:0000269|PubMed:28753426"
MUTAGEN 1636
/note="E->A: Increased methyltransferase activity."
/evidence="ECO:0000269|PubMed:27474439"
MUTAGEN 1637
/note="T->A: Increased methyltransferase activity."
/evidence="ECO:0000269|PubMed:27474439"
MUTAGEN 1668
/note="F->A: Strongly reduced methyltransferase activity."
/evidence="ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439"
MUTAGEN 1669
/note="Q->A: Loss of methyltransferase activity."
/evidence="ECO:0000269|PubMed:23043551"
MUTAGEN 1670
/note="R->A,V,L,I,F: Impaired methyltransferase activity."
/evidence="ECO:0000269|PubMed:23043551"
MUTAGEN 1670
/note="R->P,W,K,Q: Loss of methyltransferase activity."
/evidence="ECO:0000269|PubMed:23043551"
MUTAGEN 1671
/note="Y->A: Strongly reduced methyltransferase activity."
/evidence="ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439"
MUTAGEN 2475
/note="R->A: Does not affect interaction with
hyperphosphorylated POLR2A."
/evidence="ECO:0000269|PubMed:16314571"
MUTAGEN 2476
/note="K->A: Does not affect interaction with
hyperphosphorylated POLR2A."
/evidence="ECO:0000269|PubMed:16314571"
MUTAGEN 2480
/note="Q->A: Does not affect interaction with
hyperphosphorylated POLR2A."
/evidence="ECO:0000269|PubMed:16314571"
MUTAGEN 2481
/note="F->A: Does not affect interaction with
hyperphosphorylated POLR2A."
/evidence="ECO:0000269|PubMed:16314571"
MUTAGEN 2483
/note="V->A: Impairs interaction with hyperphosphorylated
POLR2A."
/evidence="ECO:0000269|PubMed:16314571"
MUTAGEN 2506
/note="K->A: Impairs interaction with hyperphosphorylated
POLR2A."
/evidence="ECO:0000269|PubMed:16314571"
MUTAGEN 2510
/note="R->A: Impairs interaction with hyperphosphorylated
POLR2A."
/evidence="ECO:0000269|PubMed:16314571"
MUTAGEN 2514
/note="H->A: Impairs interaction with hyperphosphorylated
POLR2A."
/evidence="ECO:0000269|PubMed:16314571"
MUTAGEN 2515
/note="G->A,T: Does not affect interaction with
hyperphosphorylated POLR2A."
/evidence="ECO:0000269|PubMed:16314571"
MUTAGEN 2528
/note="E->A: Increases interaction with hyperphosphorylated
POLR2A; when associated with A-2531."
/evidence="ECO:0000269|PubMed:16314571"
MUTAGEN 2531
/note="E->A: Increases interaction with hyperphosphorylated
POLR2A; when associated with A-2528."
/evidence="ECO:0000269|PubMed:16314571"
CONFLICT 448
/note="R -> Q (in Ref. 2; BAD18522)"
/evidence="ECO:0000305"
CONFLICT 455
/note="A -> V (in Ref. 3; CAD38601)"
/evidence="ECO:0000305"
CONFLICT 912
/note="L -> P (in Ref. 2; BAB15367)"
/evidence="ECO:0000305"
CONFLICT 964
/note="E -> K (in Ref. 4; CAC28349, 6; AAT77612 and 7;
AAT77613)"
/evidence="ECO:0000305"
CONFLICT 1080
/note="M -> I (in Ref. 2; BAC87131)"
/evidence="ECO:0000305"
CONFLICT 1080
/note="M -> T (in Ref. 3; CAD38601)"
/evidence="ECO:0000305"
CONFLICT 1212
/note="V -> F (in Ref. 2; BAD18522)"
/evidence="ECO:0000305"
CONFLICT 1269
/note="T -> A (in Ref. 4; CAC28349, 6; AAT77612 and 7;
AAT77613)"
/evidence="ECO:0000305"
CONFLICT 1338
/note="E -> G (in Ref. 2; BAB15367)"
/evidence="ECO:0000305"
CONFLICT 1498
/note="Q -> R (in Ref. 3; CAD38601)"
/evidence="ECO:0000305"
CONFLICT 1706
/note="K -> N (in Ref. 10; AAF29041)"
/evidence="ECO:0000305"
CONFLICT 1736
/note="L -> P (in Ref. 4; CAC28349 and 6; AAT77612)"
/evidence="ECO:0000305"
STRAND 1448..1450
/evidence="ECO:0000244|PDB:5JLB"
HELIX 1451..1455
/evidence="ECO:0000244|PDB:5JLB"
HELIX 1457..1465
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1480..1483
/evidence="ECO:0000244|PDB:5JLB"
HELIX 1506..1511
/evidence="ECO:0000244|PDB:5JLB"
HELIX 1521..1524
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1531..1533
/evidence="ECO:0000244|PDB:5LSX"
HELIX 1536..1538
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1539..1541
/evidence="ECO:0000244|PDB:5JLE"
TURN 1543..1547
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1552..1556
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1558..1560
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1562..1568
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1575..1578
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1582..1584
/evidence="ECO:0000244|PDB:5JLB"
HELIX 1586..1598
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1606..1610
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1613..1616
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1618..1621
/evidence="ECO:0000244|PDB:5JLB"
HELIX 1623..1626
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1634..1642
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1645..1654
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1661..1664
/evidence="ECO:0000244|PDB:5JLB"
HELIX 1667..1670
/evidence="ECO:0000244|PDB:5LT7"
STRAND 1672..1674
/evidence="ECO:0000244|PDB:5JLB"
STRAND 1675..1677
/evidence="ECO:0000244|PDB:5LT7"
STRAND 1687..1691
/evidence="ECO:0000244|PDB:5LT7"
HELIX 1697..1700
/evidence="ECO:0000244|PDB:5JLB"
STRAND 2377..2379
/evidence="ECO:0000244|PDB:2MDJ"
HELIX 2386..2388
/evidence="ECO:0000244|PDB:2MDI"
STRAND 2392..2399
/evidence="ECO:0000244|PDB:2MDC"
TURN 2401..2403
/evidence="ECO:0000244|PDB:2MDJ"
STRAND 2405..2409
/evidence="ECO:0000244|PDB:2MDC"
TURN 2410..2413
/evidence="ECO:0000244|PDB:2MDC"
STRAND 2414..2419
/evidence="ECO:0000244|PDB:2MDI"
STRAND 2424..2428
/evidence="ECO:0000244|PDB:2MDC"
HELIX 2463..2486
/evidence="ECO:0000244|PDB:2A7O"
TURN 2487..2489
/evidence="ECO:0000244|PDB:2A7O"
STRAND 2495..2498
/evidence="ECO:0000244|PDB:2A7O"
HELIX 2502..2524
/evidence="ECO:0000244|PDB:2A7O"
HELIX 2527..2529
/evidence="ECO:0000244|PDB:2A7O"
HELIX 2534..2548
/evidence="ECO:0000244|PDB:2A7O"
TURN 2549..2551
/evidence="ECO:0000244|PDB:2A7O"
HELIX 2557..2559
/evidence="ECO:0000244|PDB:2A7O"
SEQUENCE 2564 AA; 287597 MW; 2B1BAE5867AB8EAB CRC64;
MKQLQPQPPP KMGDFYDPEH PTPEEEENEA KIENVQKTGF IKGPMFKGVA SSRFLPKGTK
TKVNLEEQGR QKVSFSFSLT KKTLQNRFLT ALGNEKQSDT PNPPAVPLQV DSTPKMKMEI
GDTLSTAEES SPPKSRVELG KIHFKKHLLH VTSRPLLATT TAVASPPTHA APLPAVIAES
TTVDSPPSSP PPPPPPAQAT TLSSPAPVTE PVALPHTPIT VLMAAPVPLP VDVAVRSLKE
PPIIIVPESL EADTKQDTIS NSLEEHVTQI LNEQADISSK KEDSHIGKDE EIPDSSKISL
SCKKTGSKKK SSQSEGIFLG SESDEDSVRT SSSQRSHDLK FSASIEKERD FKKSSAPLKS
EDLGKPSRSK TDRDDKYFSY SKLERDTRYV SSRCRSERER RRSRSHSRSE RGSRTNLSYS
RSERSHYYDS DRRYHRSSPY RERTRYSRPY TDNRARESSD SEEEYKKTYS RRTSSHSSSY
RDLRTSSYSK SDRDCKTETS YLEMERRGKY SSKLERESKR TSENEAIKRC CSPPNELGFR
RGSSYSKHDS SASRYKSTLS KPIPKSDKFK NSFCCTELNE EIKQSHSFSL QTPCSKGSEL
RMINKNPERE KAGSPAPSNR LNDSPTLKKL DELPIFKSEF ITHDSHDSIK ELDSLSKVKN
DQLRSFCPIE LNINGSPGAE SDLATFCTSK TDAVLMTSDD SVTGSELSPL VKACMLSSNG
FQNISRCKEK DLDDTCMLHK KSESPFRETE PLVSPHQDKL MSMPVMTVDY SKTVVKEPVD
TRVSCCKTKD SDIYCTLNDS NPSLCNSEAE NIEPSVMKIS SNSFMNVHLE SKPVICDSRN
LTDHSKFACE EYKQSIGSTS SASVNHFDDL YQPIGSSGIA SSLQSLPPGI KVDSLTLLKC
GENTSPVLDA VLKSKKSSEF LKHAGKETIV EVGSDLPDSG KGFASRENRR NNGLSGKCLQ
EAQEEGNSIL PERRGRPEIS LDERGEGGHV HTSDDSEVVF SSCDLNLTME DSDGVTYALK
CDSSGHAPEI VSTVHEDYSG SSESSNDESD SEDTDSDDSS IPRNRLQSVV VVPKNSTLPM
EETSPCSSRS SQSYRHYSDH WEDERLESRR HLYEEKFESI ASKACPQTDK FFLHKGTEKN
PEISFTQSSR KQIDNRLPEL SHPQSDGVDS TSHTDVKSDP LGHPNSEETV KAKIPSRQQE
ELPIYSSDFE DVPNKSWQQT TFQNRPDSRL GKTELSFSSS CEIPHVDGLH SSEELRNLGW
DFSQEKPSTT YQQPDSSYGA CGGHKYQQNA EQYGGTRDYW QGNGYWDPRS GRPPGTGVVY
DRTQGQVPDS LTDDREEEEN WDQQDGSHFS DQSDKFLLSL QKDKGSVQAP EISSNSIKDT
LAVNEKKDFS KNLEKNDIKD RGPLKKRRQE IESDSESDGE LQDRKKVRVE VEQGETSVPP
GSALVGPSCV MDDFRDPQRW KECAKQGKMP CYFDLIEENV YLTERKKNKS HRDIKRMQCE
CTPLSKDERA QGEIACGEDC LNRLLMIECS SRCPNGDYCS NRRFQRKQHA DVEVILTEKK
GWGLRAAKDL PSNTFVLEYC GEVLDHKEFK ARVKEYARNK NIHYYFMALK NDEIIDATQK
GNCSRFMNHS CEPNCETQKW TVNGQLRVGF FTTKLVPSGS ELTFDYQFQR YGKEAQKCFC
GSANCRGYLG GENRVSIRAA GGKMKKERSR KKDSVDGELE ALMENGEGLS DKNQVLSLSR
LMVRIETLEQ KLTCLELIQN THSQSCLKSF LERHGLSLLW IWMAELGDGR ESNQKLQEEI
IKTLEHLPIP TKNMLEESKV LPIIQRWSQT KTAVPPLSEG DGYSSENTSR AHTPLNTPDP
STKLSTEADT DTPKKLMFRR LKIISENSMD SAISDATSEL EGKDGKEDLD QLENVPVEEE
EELQSQQLLP QQLPECKVDS ETNIEASKLP TSEPEADAEI EPKESNGTKL EEPINEETPS
QDEEEGVSDV ESERSQEQPD KTVDISDLAT KLLDSWKDLK EVYRIPKKSQ TEKENTTTER
GRDAVGFRDQ TPAPKTPNRS RERDPDKQTQ NKEKRKRRSS LSPPSSAYER GTKRPDDRYD
TPTSKKKVRI KDRNKLSTEE RRKLFEQEVA QREAQKQQQQ MQNLGMTSPL PYDSLGYNAP
HHPFAGYPPG YPMQAYVDPS NPNAGKVLLP TPSMDPVCSP APYDHAQPLV GHSTEPLSAP
PPVPVVPHVA APVEVSSSQY VAQSDGVVHQ DSSVAVLPVP APGPVQGQNY SVWDSNQQSV
SVQQQYSPAQ SQATIYYQGQ TCPTVYGVTS PYSQTTPPIV QSYAQPSLQY IQGQQIFTAH
PQGVVVQPAA AVTTIVAPGQ PQPLQPSEMV VTNNLLDLPP PSPPKPKTIV LPPNWKTARD
PEGKIYYYHV ITRQTQWDPP TWESPGDDAS LEHEAEMDLG TPTYDENPMK ASKKPKTAEA
DTSSELAKKS KEVFRKEMSQ FIVQCLNPYR KPDCKVGRIT TTEDFKHLAR KLTHGVMNKE
LKYCKNPEDL ECNENVKHKT KEYIKKYMQK FGAVYKPKED TELE


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EIAAB37975 H3-K4-HMTase SETD7,Histone H3-K4 methyltransferase SETD7,Histone-lysine N-methyltransferase SETD7,Homo sapiens,Human,KIAA1717,KMT7,Lysine N-methyltransferase 7,SET domain-containing protein 7,SET7,SET
EIAAB38899 Histone methyltransferase SMYD2,Homo sapiens,HSKM-B,Human,KMT3C,Lysine N-methyltransferase 3C,N-lysine methyltransferase SMYD2,SET and MYND domain-containing protein 2,SMYD2
CSB-EL021103HU Human Histone-lysine N-methyltransferase SETD2(SETD2) ELISA kit SpeciesHuman 96T
CSB-EL021103HU Human Histone-lysine N-methyltransferase SETD2(SETD2) ELISA kit 96T
EIAAB27934 DC28,Histone-lysine N-methyltransferase NSD3,Homo sapiens,Human,NSD3,Nuclear SET domain-containing protein 3,Protein whistle,WHSC1L1,WHSC1-like 1 isoform 9 with methyltransferase activity to lysine,WH
EIAAB37958 C13orf4,Chronic lymphocytic leukemia deletion region gene 8 protein,CLLD8,Histone-lysine N-methyltransferase SETDB2,Homo sapiens,Human,KMT1F,Lysine N-methyltransferase 1F,SET domain bifurcated 2,SETDB
EIAAB37954 Histone-lysine N-methyltransferase SETD1B,Homo sapiens,hSET1B,Human,KIAA1076,KMT2G,Lysine N-methyltransferase 2G,SET domain-containing protein 1B,SET1B,SETD1B
EIAAB32202 Huntingtin yeast partner C,Huntingtin-interacting protein C,Hypc,Mouse,Mus musculus,Pre-mRNA-processing factor 40 homolog B,Prpf40b
EIAAB12653 EHMT1,Euchromatic histone-lysine N-methyltransferase 1,EUHMTASE1,Eu-HMTase1,G9a-like protein 1,GLP,GLP,GLP1,H3-K9-HMTase 5,Histone H3-K9 methyltransferase 5,Histone-lysine N-methyltransferase EHMT1,Ho
EIAAB37978 H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,Mouse,Mus musculus,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PR-Set7,SET domain-containing protein 8,Se
EIAAB37979 Bos taurus,Bovine,H4-K20-HMTase SETD8,Histone-lysine N-methyltransferase SETD8,N-lysine methyltransferase SETD8,PR_SET domain-containing protein 07,PR_SET07,PR-Set7,SET domain-containing protein 8,SET
EIAAB32201 Homo sapiens,Human,Huntingtin yeast partner C,Huntingtin-interacting protein C,HYPC,Pre-mRNA-processing factor 40 homolog B,PRPF40B
EIAAB32199 Fas ligand-associated factor 1,FBP11,FLAF1,FNBP3,Formin-binding protein 11,Formin-binding protein 3,HIP10,HIP-10,Homo sapiens,HSPC225,Human,Huntingtin yeast partner A,Huntingtin-interacting protein 10
EIAAB40615 H3-K9-HMTase 1,Histone H3-K9 methyltransferase 1,Histone-lysine N-methyltransferase SUV39H1,Homo sapiens,Human,KMT1A,Lysine N-methyltransferase 1A,Position-effect variegation 3-9 homolog,Su(var)3-9 ho
EIAAB40618 H3-K9-HMTase 2,Histone H3-K9 methyltransferase 2,Histone-lysine N-methyltransferase SUV39H2,Homo sapiens,Human,KMT1B,Lysine N-methyltransferase 1B,Su(var)3-9 homolog 2,Suppressor of variegation 3-9 ho
EIAAB24941 HALR,Histone-lysine N-methyltransferase MLL3,Homo sapiens,Homologous to ALR protein,Human,KIAA1506,KMT2C,KMT2C,Lysine N-methyltransferase 2C,MLL3,Myeloid_lymphoid or mixed-lineage leukemia protein 3
EIAAB24940 ALL1-related protein,ALR,Histone-lysine N-methyltransferase MLL2,Homo sapiens,Human,KMT2B,KMT2B,Lysine N-methyltransferase 2B,MLL2,Myeloid_lymphoid or mixed-lineage leukemia protein 2