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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) (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.
27-SEP-2017, entry version 151.
RecName: Full=Histone-lysine N-methyltransferase SETD2;
EC=2.1.1.43;
AltName: Full=HIF-1;
AltName: Full=Huntingtin yeast partner B;
AltName: Full=Huntingtin-interacting protein 1;
Short=HIP-1;
AltName: Full=Huntingtin-interacting protein B;
AltName: Full=Lysine N-methyltransferase 3A;
AltName: Full=SET domain-containing protein 2;
Short=hSET2;
AltName: Full=p231HBP;
Name=SETD2; Synonyms=HIF1, HYPB, KIAA1732, KMT3A, SET2;
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), 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 ASP-1733 AND PRO-1769, AND
CHARACTERIZATION OF VARIANTS 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]
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).
[32]
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).
[33]
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).
[34]
FUNCTION AS ALPHA-TUBULIN METHYLTRANSFERASE, 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).
[35]
POSSIBLE INVOLVEMENT IN LLS.
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. 0:0-0(2016).
[36]
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).
[37]
STRUCTURE BY NMR OF 2457-2564, INTERACTION WITH POLR2A, AND
MUTAGENESIS OF ARG-2475; LYS-2476; GLN-2480; PHE-2481; VAL-2483;
PHE-2505; LYS-2506; ARG-2510; HIS-2514; GLY-2515; GLU-2528 AND
GLU-2531.
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).
[38]
X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 1434-1711 IN COMPLEX WITH
S-ADENOSYL-L-METHIONINE OR N-PROPYL SINEFUNGIN, FUNCTION,
BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, ENZYME 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).
[39]
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).
[40]
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. Represents the main enzyme
generating H3K36me3, a specific tag for epigenetic transcriptional
activation. Plays a role in chromatin structure modulation during
elongation by coordinating recruitment of the FACT complex and by
interacting with hyperphosphorylated POLR2A. 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. H3K36me3 also plays an essential role in the maintenance
of a heterochromatic state, by recruiting DNA methyltransferase
DNMT3A. 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.
Required during angiogenesis. Recruited to the promoters of
adenovirus 12 E1A gene in case of infection, possibly leading to
regulate its expression. Trimethylates 'Lys-40' of alpha-tubulins
such as TUBA1B (alpha-TubK40me3) (PubMed:27518565). Alpha-
TubK40me3 is required for normal mitosis and cytokinesis and is
proposed to be a specific tag in cytoskeletal remodeling
(PubMed:27518565). {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:27518565}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:23043551}.
-!- ENZYME 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).;
-!- 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. Interacts with HTT and IWS1. Interacts
with p53/TP53; leading to regulate p53/TP53 target genes.
Component of a complex with HNRNPL. Interacts with TUBA1A; the
interaction is independent on alpha-tubulin acetylation on 'Lys-
40'. {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:23043551,
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:0000305}. Chromosome
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9BYW2-1; Sequence=Displayed;
Name=2;
IsoId=Q9BYW2-2; Sequence=VSP_020915;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9BYW2-3; Sequence=VSP_020914;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:11461154}.
-!- DOMAIN: The low charge region mediates the transcriptional
activation activity. {ECO:0000269|PubMed:16118227}.
-!- PTM: May be automethylated.
-!- 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}.
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).
{ECO:0000269|PubMed:23792563}.
-!- 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.
-!- 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; Positions=Several; Evidence={ECO:0000305};
Sequence=AAH72440.1; Type=Erroneous termination; Positions=463; Note=Translated as Glu.; Evidence={ECO:0000305};
Sequence=AAI17163.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAI17165.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT77612.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAT77613.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAB15367.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAC28349.1; Type=Erroneous termination; Positions=385; Note=Translated as Arg.; Evidence={ECO:0000305};
Sequence=CAD38601.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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]
UniGene; Hs.517941; -.
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; -.
ProteinModelPortal; Q9BYW2; -.
SMR; Q9BYW2; -.
BioGrid; 118845; 48.
IntAct; Q9BYW2; 15.
MINT; MINT-1537591; -.
STRING; 9606.ENSP00000386759; -.
BindingDB; Q9BYW2; -.
ChEMBL; CHEMBL3108647; -.
iPTMnet; Q9BYW2; -.
PhosphoSitePlus; Q9BYW2; -.
BioMuta; SETD2; -.
DMDM; 296452963; -.
OGP; Q9BYW2; -.
EPD; Q9BYW2; -.
MaxQB; Q9BYW2; -.
PaxDb; Q9BYW2; -.
PeptideAtlas; Q9BYW2; -.
PRIDE; Q9BYW2; -.
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; -.
H-InvDB; HIX0021942; -.
H-InvDB; HIX0163343; -.
HGNC; HGNC:18420; SETD2.
HPA; HPA042451; -.
MalaCards; SETD2; -.
MIM; 144700; phenotype.
MIM; 612778; gene.
MIM; 616831; phenotype.
neXtProt; NX_Q9BYW2; -.
OpenTargets; ENSG00000181555; -.
Orphanet; 821; Sotos syndrome.
PharmGKB; PA143485612; -.
eggNOG; KOG4442; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00780000121845; -.
HOVERGEN; HBG093939; -.
InParanoid; Q9BYW2; -.
KO; K11423; -.
OMA; FIGHDSH; -.
OrthoDB; EOG091G040P; -.
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; -.
PRO; PR:Q9BYW2; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000181555; -.
CleanEx; HS_SETD2; -.
ExpressionAtlas; Q9BYW2; baseline and differential.
Genevisible; Q9BYW2; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:HGNC.
GO; GO:0018024; F:histone-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:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
GO; GO:0060669; P:embryonic placenta morphogenesis; IEA:Ensembl.
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: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:0060039; P:pericardium development; IEA:Ensembl.
GO; GO:0010793; P:regulation of mRNA export from nucleus; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0048864; P:stem cell development; IEA:Ensembl.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IMP:UniProtKB.
CDD; cd00201; WW; 1.
InterPro; IPR006560; AWS_dom.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR013257; SRI.
InterPro; IPR001202; WW_dom.
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;
Autism spectrum disorder; Chromatin regulator; Chromosome;
Coiled coil; Complete proteome; Disease mutation; Isopeptide bond;
Mental retardation; Methyltransferase; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; S-adenosyl-L-methionine;
Transcription; Transcription regulation; Transferase; Ubl conjugation.
CHAIN 1 2564 Histone-lysine N-methyltransferase SETD2.
/FTId=PRO_0000252367.
DOMAIN 1494 1548 AWS. {ECO:0000255|PROSITE-
ProRule:PRU00562}.
DOMAIN 1550 1667 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 1674 1690 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
DOMAIN 2389 2422 WW. {ECO:0000255|PROSITE-
ProRule:PRU00224}.
REGION 1418 1714 Interaction with TUBA1A.
{ECO:0000269|PubMed:27518565}.
REGION 1560 1562 Inhibitor binding.
REGION 1560 1562 S-adenosyl-L-methionine binding.
REGION 1603 1605 Inhibitor binding.
REGION 1603 1605 S-adenosyl-L-methionine binding.
REGION 1628 1629 Inhibitor binding.
REGION 1628 1629 S-adenosyl-L-methionine binding.
REGION 2137 2366 Low charge region.
REGION 2457 2564 Interaction with POLR2A.
COILED 2117 2146 {ECO:0000255}.
COMPBIAS 166 247 Pro-rich.
COMPBIAS 385 456 Arg-rich.
COMPBIAS 2149 2232 Pro-rich.
COMPBIAS 2266 2365 Gln-rich.
BINDING 1625 1625 Inhibitor.
BINDING 1676 1676 Inhibitor; alternate.
BINDING 1676 1676 S-adenosyl-L-methionine; alternate.
BINDING 1679 1679 Inhibitor; via amide nitrogen; alternate.
BINDING 1679 1679 S-adenosyl-L-methionine; via amide
nitrogen; alternate.
MOD_RES 131 131 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 323 323 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 532 532 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 614 614 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 624 624 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 626 626 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 698 698 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q5F9}.
MOD_RES 708 708 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 744 744 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 754 754 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1098 1098 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1228 1228 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1413 1413 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q5F9}.
MOD_RES 1415 1415 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q5F9}.
MOD_RES 1417 1417 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q5F9}.
MOD_RES 1696 1696 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1844 1844 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q5F9}.
MOD_RES 1845 1845 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q5F9}.
MOD_RES 1853 1853 Phosphothreonine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1872 1872 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1888 1888 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1952 1952 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1980 1980 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q5F9}.
MOD_RES 1988 1988 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q5F9}.
MOD_RES 1995 1995 Phosphoserine.
{ECO:0000250|UniProtKB:E9Q5F9}.
MOD_RES 2080 2080 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 2082 2082 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 359 359 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 637 637 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 776 776 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1573 2564 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_020914.
VAR_SEQ 1715 2564 Missing (in isoform 2).
{ECO:0000303|Ref.7}.
/FTId=VSP_020915.
VARIANT 488 488 Y -> C (found in a patient with autism;
unknown pathological significance;
dbSNP:rs757781388).
{ECO:0000269|PubMed:26637798}.
/FTId=VAR_078707.
VARIANT 768 768 V -> L (in dbSNP:rs9311404).
/FTId=VAR_027839.
VARIANT 902 902 E -> Q (in dbSNP:rs58906143).
/FTId=VAR_061216.
VARIANT 1733 1733 N -> D (in RCC cell line; defects in
recruitment of the MutS alpha complex).
{ECO:0000269|PubMed:23622243}.
/FTId=VAR_069812.
VARIANT 1769 1769 S -> P (in RCC cell line; defects in
recruitment of the MutS alpha complex).
{ECO:0000269|PubMed:23622243}.
/FTId=VAR_069813.
VARIANT 1815 1815 L -> W (in LLS; unknown pathological
significance; dbSNP:rs869025570).
{ECO:0000269|PubMed:24852293}.
/FTId=VAR_076536.
VARIANT 1868 1868 A -> D (in dbSNP:rs11721074).
/FTId=VAR_027840.
VARIANT 1962 1962 P -> L (in dbSNP:rs4082155).
{ECO:0000269|PubMed:11214970,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_027841.
MUTAGEN 1625 1625 R->H: Loss of methyltransferase activity.
{ECO:0000269|PubMed:16118227}.
MUTAGEN 1668 1668 F->A: Loss of methyltransferase activity.
{ECO:0000269|PubMed:23043551}.
MUTAGEN 1669 1669 Q->A: Loss of methyltransferase activity.
{ECO:0000269|PubMed:23043551}.
MUTAGEN 1670 1670 R->A,V,L,I,F: Impaired methyltransferase
activity. {ECO:0000269|PubMed:23043551}.
MUTAGEN 1670 1670 R->P,W,K,Q: Loss of methyltransferase
activity. {ECO:0000269|PubMed:23043551}.
MUTAGEN 1671 1671 Y->A: Loss of methyltransferase activity.
{ECO:0000269|PubMed:23043551}.
MUTAGEN 2475 2475 R->A: Does not affect interaction with
hyperphosphorylated POLR2A.
{ECO:0000269|PubMed:16314571}.
MUTAGEN 2476 2476 K->A: Does not affect interaction with
hyperphosphorylated POLR2A.
{ECO:0000269|PubMed:16314571}.
MUTAGEN 2480 2480 Q->A: Does not affect interaction with
hyperphosphorylated POLR2A.
{ECO:0000269|PubMed:16314571}.
MUTAGEN 2481 2481 F->A: Does not affect interaction with
hyperphosphorylated POLR2A.
{ECO:0000269|PubMed:16314571}.
MUTAGEN 2483 2483 V->A: Impairs interaction with
hyperphosphorylated POLR2A.
{ECO:0000269|PubMed:16314571}.
MUTAGEN 2505 2505 F->L: Impairs interaction with
hyperphosphorylated POLR2A.
{ECO:0000269|PubMed:16314571}.
MUTAGEN 2506 2506 K->A: Impairs interaction with
hyperphosphorylated POLR2A.
{ECO:0000269|PubMed:16314571}.
MUTAGEN 2510 2510 R->A: Impairs interaction with
hyperphosphorylated POLR2A.
{ECO:0000269|PubMed:16314571}.
MUTAGEN 2514 2514 H->A: Impairs interaction with
hyperphosphorylated POLR2A.
{ECO:0000269|PubMed:16314571}.
MUTAGEN 2515 2515 G->A,T: Does not affect interaction with
hyperphosphorylated POLR2A.
{ECO:0000269|PubMed:16314571}.
MUTAGEN 2528 2528 E->A: Increases interaction with
hyperphosphorylated POLR2A; when
associated with A-2531.
{ECO:0000269|PubMed:16314571}.
MUTAGEN 2531 2531 E->A: Increases interaction with
hyperphosphorylated POLR2A; when
associated with A-2528.
{ECO:0000269|PubMed:16314571}.
CONFLICT 448 448 R -> Q (in Ref. 2; BAD18522).
{ECO:0000305}.
CONFLICT 455 455 A -> V (in Ref. 3; CAD38601).
{ECO:0000305}.
CONFLICT 912 912 L -> P (in Ref. 2; BAB15367).
{ECO:0000305}.
CONFLICT 964 964 E -> K (in Ref. 4; CAC28349, 6; AAT77612
and 7; AAT77613). {ECO:0000305}.
CONFLICT 1080 1080 M -> I (in Ref. 2; BAC87131).
{ECO:0000305}.
CONFLICT 1080 1080 M -> T (in Ref. 3; CAD38601).
{ECO:0000305}.
CONFLICT 1212 1212 V -> F (in Ref. 2; BAD18522).
{ECO:0000305}.
CONFLICT 1269 1269 T -> A (in Ref. 4; CAC28349, 6; AAT77612
and 7; AAT77613). {ECO:0000305}.
CONFLICT 1338 1338 E -> G (in Ref. 2; BAB15367).
{ECO:0000305}.
CONFLICT 1498 1498 Q -> R (in Ref. 3; CAD38601).
{ECO:0000305}.
CONFLICT 1706 1706 K -> N (in Ref. 10; AAF29041).
{ECO:0000305}.
CONFLICT 1736 1736 L -> P (in Ref. 4; CAC28349 and 6;
AAT77612). {ECO:0000305}.
STRAND 1448 1450 {ECO:0000244|PDB:5JLB}.
HELIX 1451 1455 {ECO:0000244|PDB:5JLB}.
HELIX 1457 1465 {ECO:0000244|PDB:5JLB}.
STRAND 1480 1483 {ECO:0000244|PDB:5JLB}.
HELIX 1506 1511 {ECO:0000244|PDB:5JLB}.
HELIX 1521 1524 {ECO:0000244|PDB:5JLB}.
STRAND 1531 1533 {ECO:0000244|PDB:5LSX}.
HELIX 1536 1538 {ECO:0000244|PDB:5JLB}.
STRAND 1539 1541 {ECO:0000244|PDB:5JLE}.
TURN 1543 1547 {ECO:0000244|PDB:5JLB}.
STRAND 1552 1556 {ECO:0000244|PDB:5JLB}.
STRAND 1558 1560 {ECO:0000244|PDB:5JLB}.
STRAND 1562 1568 {ECO:0000244|PDB:5JLB}.
STRAND 1575 1578 {ECO:0000244|PDB:5JLB}.
STRAND 1582 1584 {ECO:0000244|PDB:5JLB}.
HELIX 1586 1598 {ECO:0000244|PDB:5JLB}.
STRAND 1606 1610 {ECO:0000244|PDB:5JLB}.
STRAND 1613 1616 {ECO:0000244|PDB:5JLB}.
STRAND 1618 1621 {ECO:0000244|PDB:5JLB}.
HELIX 1623 1626 {ECO:0000244|PDB:5JLB}.
STRAND 1634 1642 {ECO:0000244|PDB:5JLB}.
STRAND 1645 1654 {ECO:0000244|PDB:5JLB}.
STRAND 1661 1664 {ECO:0000244|PDB:5JLB}.
HELIX 1667 1670 {ECO:0000244|PDB:5LT7}.
STRAND 1672 1674 {ECO:0000244|PDB:5JLB}.
STRAND 1675 1677 {ECO:0000244|PDB:5LT7}.
STRAND 1687 1691 {ECO:0000244|PDB:5LT7}.
HELIX 1697 1700 {ECO:0000244|PDB:5JLB}.
STRAND 2377 2379 {ECO:0000244|PDB:2MDJ}.
HELIX 2386 2388 {ECO:0000244|PDB:2MDI}.
STRAND 2392 2399 {ECO:0000244|PDB:2MDC}.
TURN 2401 2403 {ECO:0000244|PDB:2MDJ}.
STRAND 2405 2409 {ECO:0000244|PDB:2MDC}.
TURN 2410 2413 {ECO:0000244|PDB:2MDC}.
STRAND 2414 2419 {ECO:0000244|PDB:2MDI}.
STRAND 2424 2428 {ECO:0000244|PDB:2MDC}.
HELIX 2463 2486 {ECO:0000244|PDB:2A7O}.
TURN 2487 2489 {ECO:0000244|PDB:2A7O}.
STRAND 2495 2498 {ECO:0000244|PDB:2A7O}.
HELIX 2502 2524 {ECO:0000244|PDB:2A7O}.
HELIX 2527 2529 {ECO:0000244|PDB:2A7O}.
HELIX 2534 2548 {ECO:0000244|PDB:2A7O}.
TURN 2549 2551 {ECO:0000244|PDB:2A7O}.
HELIX 2557 2559 {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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