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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.
22-NOV-2017, entry version 153.
RecName: Full=Histone-lysine N-methyltransferase SETD2 {ECO:0000305};
EC=2.1.1.43 {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. 0:0-0(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, 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).
[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: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:23043551, ECO:0000269|PubMed:27474439}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + [protein]-L-lysine =
S-adenosyl-L-homocysteine + [protein]-N(6)-methyl-L-lysine.
{ECO:0000269|PubMed:28753426}.
-!- CATALYTIC ACTIVITY: 3 S-adenosyl-L-methionine + [protein]-L-lysine
= 3 S-adenosyl-L-homocysteine + [protein]-N(6),N(6),N(6)-methyl-L-
lysine. {ECO:0000269|PubMed:27518565}.
-!- 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). {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;
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}.
-!- 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; 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; 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; 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; 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:UniProtKB-KW.
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.
InterPro; IPR006560; AWS_dom.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR013257; SRI.
InterPro; IPR001202; WW_dom.
InterPro; IPR036020; WW_dom_sf.
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; Complete proteome; Developmental protein;
Differentiation; Disease mutation; DNA damage; DNA repair; 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 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.
{ECO:0000269|PubMed:23043551}.
REGION 1560 1562 S-adenosyl-L-methionine binding.
{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 Inhibitor binding.
{ECO:0000269|PubMed:23043551}.
REGION 1603 1605 S-adenosyl-L-methionine binding.
{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 Inhibitor binding.
{ECO:0000269|PubMed:23043551}.
REGION 1628 1629 S-adenosyl-L-methionine binding.
{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 Low charge region.
{ECO:0000269|PubMed:16118227}.
REGION 2457 2564 Interaction with POLR2A.
{ECO:0000269|PubMed:16314571}.
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.
METAL 1499 1499 Zinc 1. {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 1501 Zinc 1. {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 1516 Zinc 1. {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 1516 Zinc 2. {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 1520 Zinc 1. {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 1529 Zinc 2. {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 1533 Zinc 2. {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 1539 Zinc 2. {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 1631 Zinc 3. {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 1678 Zinc 3. {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 1680 Zinc 3. {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 1685 Zinc 3. {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 1625 Inhibitor. {ECO:0000269|PubMed:23043551}.
BINDING 1676 1676 Inhibitor; alternate.
{ECO:0000269|PubMed:23043551}.
BINDING 1676 1676 S-adenosyl-L-methionine; alternate.
{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 1679 Inhibitor; via amide nitrogen; alternate.
{ECO:0000244|PDB:5V22,
ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:28256625}.
BINDING 1679 1679 S-adenosyl-L-methionine; via amide
nitrogen; alternate.
{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 131 131 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 2 2 K -> R (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079054.
VARIANT 19 19 E -> G (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079055.
VARIANT 70 2564 Missing (in AML; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079056.
VARIANT 226 226 P -> S (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079057.
VARIANT 267 267 V -> I (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079058.
VARIANT 470 470 S -> P (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079059.
VARIANT 488 488 Y -> C (found in a patient with autism;
unknown pathological significance;
dbSNP:rs757781388).
{ECO:0000269|PubMed:26637798}.
/FTId=VAR_078707.
VARIANT 499 499 T -> A (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079060.
VARIANT 761 761 M -> I (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079061.
VARIANT 768 768 V -> L (in dbSNP:rs9311404).
/FTId=VAR_027839.
VARIANT 794 2564 Missing (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079062.
VARIANT 800 800 S -> N (in AML; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079063.
VARIANT 902 902 E -> Q (in dbSNP:rs58906143).
/FTId=VAR_061216.
VARIANT 1076 1076 S -> P (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079064.
VARIANT 1093 1093 S -> G (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079065.
VARIANT 1171 1171 T -> A (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079066.
VARIANT 1351 1351 D -> G (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079067.
VARIANT 1365 1365 G -> E (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079068.
VARIANT 1397 1397 D -> G (in AML; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079069.
VARIANT 1416 2564 Missing (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079070.
VARIANT 1453 1453 D -> N (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079071.
VARIANT 1493 1493 D -> N (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079072.
VARIANT 1496 2564 Missing (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079073.
VARIANT 1609 1609 L -> P (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079074.
VARIANT 1654 1654 K -> Q (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079075.
VARIANT 1663 1663 T -> M (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079076.
VARIANT 1733 1733 N -> D (in RCC; defects in recruitment of
the MutS alpha complex).
{ECO:0000269|PubMed:23622243}.
/FTId=VAR_069812.
VARIANT 1769 1769 S -> P (in RCC; defects in recruitment of
the MutS alpha complex).
{ECO:0000269|PubMed:23622243}.
/FTId=VAR_069813.
VARIANT 1804 1804 L -> S (in AML; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079077.
VARIANT 1815 1815 L -> W (in LLS; unknown pathological
significance; dbSNP:rs869025570).
{ECO:0000269|PubMed:24852293}.
/FTId=VAR_076536.
VARIANT 1821 1821 L -> P (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079078.
VARIANT 1868 1868 A -> D (in dbSNP:rs11721074).
/FTId=VAR_027840.
VARIANT 1915 1915 V -> A (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079079.
VARIANT 1920 1920 E -> V (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079080.
VARIANT 1962 1962 P -> L (in dbSNP:rs4082155).
{ECO:0000269|PubMed:11214970,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_027841.
VARIANT 2077 2564 Missing (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079081.
VARIANT 2122 2122 R -> W (in AML; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079082.
VARIANT 2214 2214 T -> A (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079083.
VARIANT 2325 2564 Missing (in AML; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079084.
VARIANT 2361 2361 P -> S (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079085.
VARIANT 2505 2505 F -> L (in AML; Impairs interaction with
hyperphosphorylated POLR2A; unknown
pathological significance; somatic
mutation). {ECO:0000269|PubMed:16314571,
ECO:0000269|PubMed:24509477}.
/FTId=VAR_079086.
VARIANT 2524 2564 Missing (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24509477}.
/FTId=VAR_079087.
VARIANT 2546 2564 Missing (in ALL; unknown pathological
significance; somatic mutation).
{ECO:0000269|PubMed:24662245}.
/FTId=VAR_079088.
MUTAGEN 1589 1589 F->A: Strongly reduced methyltransferase
activity. {ECO:0000269|PubMed:27474439}.
MUTAGEN 1604 1604 Y->A: Increased methyltransferase
activity. {ECO:0000269|PubMed:27474439}.
MUTAGEN 1625 1625 R->H,G: Loss of methyltransferase
activity. Abolishes ability to
monomethylate STAT1.
{ECO:0000269|PubMed:16118227,
ECO:0000269|PubMed:28753426}.
MUTAGEN 1631 1631 C->A: Does not affect methyltransferase
activity. {ECO:0000269|PubMed:28753426}.
MUTAGEN 1636 1636 E->A: Increased methyltransferase
activity. {ECO:0000269|PubMed:27474439}.
MUTAGEN 1637 1637 T->A: Increased methyltransferase
activity. {ECO:0000269|PubMed:27474439}.
MUTAGEN 1668 1668 F->A: Strongly reduced methyltransferase
activity. {ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439}.
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: Strongly reduced methyltransferase
activity. {ECO:0000269|PubMed:23043551,
ECO:0000269|PubMed:27474439}.
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 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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547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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San Jose, CA 95123




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NL850396268B01 KVK nummer 52327027
Kuiper 1
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