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Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific (EC 2.1.1.43) (Androgen receptor coactivator 267 kDa protein) (Androgen receptor-associated protein of 267 kDa) (H3-K36-HMTase) (H4-K20-HMTase) (Lysine N-methyltransferase 3B) (Nuclear receptor-binding SET domain-containing protein 1) (NR-binding SET domain-containing protein)

 NSD1_HUMAN              Reviewed;        2696 AA.
Q96L73; Q96PD8; Q96RN7;
03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
25-OCT-2017, entry version 170.
RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific;
EC=2.1.1.43;
AltName: Full=Androgen receptor coactivator 267 kDa protein;
AltName: Full=Androgen receptor-associated protein of 267 kDa;
AltName: Full=H3-K36-HMTase;
AltName: Full=H4-K20-HMTase;
AltName: Full=Lysine N-methyltransferase 3B;
AltName: Full=Nuclear receptor-binding SET domain-containing protein 1;
Short=NR-binding SET domain-containing protein;
Name=NSD1; Synonyms=ARA267, KMT3B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND INTERACTION WITH
AR.
PubMed=11509567; DOI=10.1074/jbc.M104765200;
Wang X., Yeh S., Wu G., Hsu C.-L., Wang L., Chang T., Yang Y., Guo Y.,
Chang C.;
"Identification and characterization of a novel androgen receptor
coregulator ARA267-alpha in prostate cancer cells.";
J. Biol. Chem. 276:40417-40423(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11733144; DOI=10.1016/S0378-1119(01)00750-8;
Kurotaki N., Harada N., Yoshiura K., Sugano S., Niikawa N.,
Matsumoto N.;
"Molecular characterization of NSD1, a human homologue of the mouse
Nsd1 gene.";
Gene 279:197-204(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND CHROMOSOMAL TRANSLOCATION
WITH NUP98.
PubMed=11493482; DOI=10.1182/blood.V98.4.1264;
Jaju R.J., Fidler C., Haas O.A., Strickson A.J., Watkins F., Clark K.,
Cross N.C., Cheng J.F., Aplan P.D., Kearney L., Boultwood J.,
Wainscoat J.S.;
"A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in de
novo childhood acute myeloid leukemia.";
Blood 98:1264-1267(2001).
[4]
INVOLVEMENT IN SOTOS1.
PubMed=11896389; DOI=10.1038/ng863;
Kurotaki N., Imaizumi K., Harada N., Masuno M., Kondoh T., Nagai T.,
Ohashi H., Naritomi K., Tsukahara M., Makita Y., Sugimoto T.,
Sonoda T., Hasegawa T., Chinen Y., Tomita Ha H.A., Kinoshita A.,
Mizuguchi T., Yoshiura Ki K., Ohta T., Kishino T., Fukushima Y.,
Niikawa N., Matsumoto N.;
"Haploinsufficiency of NSD1 causes Sotos syndrome.";
Nat. Genet. 30:365-366(2002).
[5]
INVOLVEMENT IN SOTOS1 AND BWS.
PubMed=14997421; DOI=10.1086/383093;
Baujat G., Rio M., Rossignol S., Sanlaville D., Lyonnet S.,
Le Merrer M., Munnich A., Gicquel C., Cormier-Daire V., Colleaux L.;
"Paradoxical NSD1 mutations in Beckwith-Wiedemann syndrome and 11p15
anomalies in Sotos syndrome.";
Am. J. Hum. Genet. 74:715-720(2004).
[6]
INVOLVEMENT IN MYELODYSPLASTIC SYNDROME.
PubMed=15382262; DOI=10.1002/gcc.20103;
La Starza R., Gorello P., Rosati R., Riezzo A., Veronese A.,
Ferrazzi E., Martelli M.F., Negrini M., Mecucci C.;
"Cryptic insertion producing two NUP98/NSD1 chimeric transcripts in
adult refractory anemia with an excess of blasts.";
Genes Chromosomes Cancer 41:395-399(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-766, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2471, 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).
[9]
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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2462, 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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483 AND SER-486, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483; SER-486; SER-2369
AND SER-2471, 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).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2616, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-906 AND LYS-1339, 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).
[16]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1852-2082 IN COMPLEX WITH
S-ADENOSYL-L-METHIONINE AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY,
MUTAGENESIS OF ARG-1914 AND ARG-1952, AND CHARACTERIZATION OF SOTOS1
VARIANTS GLN-1984; GLN-2005 AND GLN-2017.
PubMed=21196496; DOI=10.1074/jbc.M110.204115;
Qiao Q., Li Y., Chen Z., Wang M., Reinberg D., Xu R.M.;
"The structure of NSD1 reveals an autoregulatory mechanism underlying
histone H3K36 methylation.";
J. Biol. Chem. 286:8361-8368(2011).
[17]
VARIANTS SOTOS1 LEU-1616; PRO-1637; TRP-1674; VAL-1792; ARG-1925;
GLN-2005; GLN-2017; GLN-2143 AND SER-2183, AND VARIANTS LEU-614;
THR-691; PRO-726; PRO-1036; ILE-1091; ILE-2250 AND THR-2261.
PubMed=12464997; DOI=10.1086/345647;
Douglas J., Hanks S., Temple I.K., Davies S., Murray A., Upadhyaya M.,
Tomkins S., Hughes H.E., Cole T.R.P., Rahman N.;
"NSD1 mutations are the major cause of Sotos syndrome and occur in
some cases of Weaver syndrome but are rare in other overgrowth
phenotypes.";
Am. J. Hum. Genet. 72:132-143(2003).
[18]
VARIANTS SOTOS1 ASN-1687; ASP-1955; GLN-1984; CYS-1997 AND TRP-2017.
PubMed=12807965; DOI=10.1136/jmg.40.6.436;
Rio M., Clech L., Amiel J., Faivre L., Lyonnet S., Le Merrer M.,
Odent S., Lacombe D., Edery P., Brauner R., Raoul O., Gosset P.,
Prieur M., Vekemans M., Munnich A., Colleaux L., Cormier-Daire V.;
"Spectrum of NSD1 mutations in Sotos and Weaver syndromes.";
J. Med. Genet. 40:436-440(2003).
[19]
VARIANT [LARGE SCALE ANALYSIS] PRO-726.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
-!- FUNCTION: Histone methyltransferase. Preferentially methylates
'Lys-36' of histone H3 and 'Lys-20' of histone H4 (in vitro).
Transcriptional intermediary factor capable of both negatively or
positively influencing transcription, depending on the cellular
context. {ECO:0000269|PubMed:21196496}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
{ECO:0000269|PubMed:21196496}.
-!- SUBUNIT: Interacts with the ligand-binding domains of RARA and
THRA in the absence of ligand; in the presence of ligand the
interaction is severely disrupted but some binding still occurs.
Interacts with the ligand-binding domains of RXRA and ESRRA only
in the presence of ligand. Interacts with ZNF496 (By similarity).
Interacts with AR DNA- and ligand-binding domains. {ECO:0000250,
ECO:0000269|PubMed:11509567, ECO:0000269|PubMed:21196496}.
-!- INTERACTION:
Q04206:RELA; NbExp=2; IntAct=EBI-2862434, EBI-73886;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=ARA267-beta;
IsoId=Q96L73-1; Sequence=Displayed;
Name=2; Synonyms=ARA267-alpha;
IsoId=Q96L73-2; Sequence=VSP_007682, VSP_007683;
Name=3;
IsoId=Q96L73-3; Sequence=VSP_007684;
-!- TISSUE SPECIFICITY: Expressed in the fetal/adult brain, kidney,
skeletal muscle, spleen, and the thymus, and faintly in the lung.
-!- DISEASE: Sotos syndrome 1 (SOTOS1) [MIM:117550]: A childhood
overgrowth syndrome characterized by pre- and postnatal
overgrowth, developmental delay, mental retardation, advanced bone
age, and abnormal craniofacial morphology including
macrodolichocephaly with frontal bossing, frontoparietal
sparseness of hair, apparent hypertelorism, downslanting palpebral
fissures, and facial flushing. Common oral findings include:
premature eruption of teeth; high, arched palate; pointed chin
and, more rarely, prognathism. {ECO:0000269|PubMed:11896389,
ECO:0000269|PubMed:12464997, ECO:0000269|PubMed:12807965,
ECO:0000269|PubMed:14997421}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Beckwith-Wiedemann syndrome (BWS) [MIM:130650]: A
disorder characterized by anterior abdominal wall defects
including exomphalos (omphalocele), pre- and postnatal overgrowth,
and macroglossia. Additional less frequent complications include
specific developmental defects and a predisposition to embryonal
tumors. {ECO:0000269|PubMed:14997421}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- DISEASE: Note=A chromosomal aberration involving NSD1 is found in
childhood acute myeloid leukemia. Translocation t(5;11)(q35;p15.5)
with NUP98.
-!- DISEASE: Note=A chromosomal aberration involving NSD1 is found in
an adult form of myelodysplastic syndrome (MDS). Insertion of
NUP98 into NSD1 generates a NUP98-NSD1 fusion product.
{ECO:0000269|PubMed:15382262}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NSD1ID356.html";
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EMBL; AF380302; AAL27991.1; -; mRNA.
EMBL; AY049721; AAL06645.1; -; mRNA.
EMBL; AF395588; AAL40694.1; -; mRNA.
EMBL; AF322907; AAK92049.1; -; mRNA.
CCDS; CCDS4412.1; -. [Q96L73-1]
CCDS; CCDS4413.1; -. [Q96L73-2]
RefSeq; NP_071900.2; NM_022455.4. [Q96L73-1]
RefSeq; NP_758859.1; NM_172349.2. [Q96L73-2]
UniGene; Hs.106861; -.
PDB; 3OOI; X-ray; 1.75 A; A=1852-2082.
PDBsum; 3OOI; -.
ProteinModelPortal; Q96L73; -.
SMR; Q96L73; -.
BioGrid; 122135; 38.
DIP; DIP-58517N; -.
IntAct; Q96L73; 10.
STRING; 9606.ENSP00000395929; -.
BindingDB; Q96L73; -.
ChEMBL; CHEMBL3588738; -.
iPTMnet; Q96L73; -.
PhosphoSitePlus; Q96L73; -.
BioMuta; NSD1; -.
DMDM; 32469769; -.
EPD; Q96L73; -.
MaxQB; Q96L73; -.
PaxDb; Q96L73; -.
PeptideAtlas; Q96L73; -.
PRIDE; Q96L73; -.
Ensembl; ENST00000347982; ENSP00000343209; ENSG00000165671. [Q96L73-2]
Ensembl; ENST00000354179; ENSP00000346111; ENSG00000165671. [Q96L73-2]
Ensembl; ENST00000439151; ENSP00000395929; ENSG00000165671. [Q96L73-1]
GeneID; 64324; -.
KEGG; hsa:64324; -.
UCSC; uc003mfr.5; human. [Q96L73-1]
CTD; 64324; -.
DisGeNET; 64324; -.
EuPathDB; HostDB:ENSG00000165671.18; -.
GeneCards; NSD1; -.
GeneReviews; NSD1; -.
HGNC; HGNC:14234; NSD1.
HPA; HPA048431; -.
HPA; HPA070333; -.
MalaCards; NSD1; -.
MIM; 117550; phenotype.
MIM; 130650; phenotype.
MIM; 606681; gene.
neXtProt; NX_Q96L73; -.
OpenTargets; ENSG00000165671; -.
Orphanet; 228415; 5q35 microduplication syndrome.
Orphanet; 238613; Beckwith-Wiedemann syndrome due to NSD1 mutation.
Orphanet; 821; Sotos syndrome.
Orphanet; 3447; Weaver syndrome.
PharmGKB; PA31790; -.
eggNOG; KOG1081; Eukaryota.
eggNOG; COG2940; LUCA.
GeneTree; ENSGT00780000121845; -.
HOGENOM; HOG000113857; -.
HOVERGEN; HBG007518; -.
InParanoid; Q96L73; -.
KO; K15588; -.
OMA; VQKYPPT; -.
OrthoDB; EOG091G00XD; -.
PhylomeDB; Q96L73; -.
TreeFam; TF329088; -.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
SIGNOR; Q96L73; -.
ChiTaRS; NSD1; human.
GenomeRNAi; 64324; -.
PRO; PR:Q96L73; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000165671; -.
CleanEx; HS_NSD1; -.
ExpressionAtlas; Q96L73; baseline and differential.
Genevisible; Q96L73; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0050681; F:androgen receptor binding; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; ISS:UniProtKB.
GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:UniProtKB.
GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); ISS:UniProtKB.
GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
GO; GO:0042974; F:retinoic acid receptor binding; ISS:UniProtKB.
GO; GO:0046965; F:retinoid X receptor binding; ISS:UniProtKB.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0046966; F:thyroid hormone receptor binding; ISS:UniProtKB.
GO; GO:0003712; F:transcription cofactor activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0016571; P:histone methylation; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0000414; P:regulation of histone H3-K36 methylation; IMP:MGI.
GO; GO:0033135; P:regulation of peptidyl-serine phosphorylation; IMP:MGI.
GO; GO:1903025; P:regulation of RNA polymerase II regulatory region sequence-specific DNA binding; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.40.10; -; 5.
InterPro; IPR006560; AWS_dom.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR000313; PWWP_dom.
InterPro; IPR001214; SET_dom.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00855; PWWP; 2.
Pfam; PF00856; SET; 1.
SMART; SM00570; AWS; 1.
SMART; SM00249; PHD; 5.
SMART; SM00508; PostSET; 1.
SMART; SM00293; PWWP; 2.
SMART; SM00317; SET; 1.
SUPFAM; SSF57903; SSF57903; 3.
PROSITE; PS51215; AWS; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50812; PWWP; 2.
PROSITE; PS50280; SET; 1.
PROSITE; PS01359; ZF_PHD_1; 2.
PROSITE; PS50016; ZF_PHD_2; 2.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Chromatin regulator;
Chromosomal rearrangement; Chromosome; Complete proteome;
Disease mutation; Isopeptide bond; Metal-binding; Methyltransferase;
Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene;
Reference proteome; Repeat; Repressor; S-adenosyl-L-methionine;
Transcription; Transcription regulation; Transferase; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1 2696 Histone-lysine N-methyltransferase, H3
lysine-36 and H4 lysine-20 specific.
/FTId=PRO_0000186070.
DOMAIN 323 388 PWWP 1. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
DOMAIN 1756 1818 PWWP 2. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
DOMAIN 1890 1940 AWS. {ECO:0000255|PROSITE-
ProRule:PRU00562}.
DOMAIN 1942 2059 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 2066 2082 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
ZN_FING 1543 1589 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1590 1646 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 1707 1751 PHD-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 2118 2165 PHD-type 4; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00146}.
REGION 1952 1954 S-adenosyl-L-methionine binding.
REGION 1994 1997 S-adenosyl-L-methionine binding.
REGION 2020 2021 S-adenosyl-L-methionine binding.
REGION 2060 2066 Inhibits enzyme activity in the absence
of bound histone.
COMPBIAS 2207 2421 Pro-rich.
BINDING 2065 2065 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190,
ECO:0000269|PubMed:21196496}.
BINDING 2071 2071 S-adenosyl-L-methionine.
{ECO:0000255|PROSITE-ProRule:PRU00190,
ECO:0000269|PubMed:21196496}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000250|UniProtKB:O88491}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 766 766 Phosphoserine.
{ECO:0000244|PubMed:17487921}.
MOD_RES 1510 1510 Phosphoserine.
{ECO:0000250|UniProtKB:O88491}.
MOD_RES 2369 2369 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 2462 2462 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 2471 2471 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
CROSSLNK 906 906 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 1339 1339 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 2616 2616 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
VAR_SEQ 1 269 Missing (in isoform 2).
{ECO:0000303|PubMed:11509567}.
/FTId=VSP_007682.
VAR_SEQ 270 279 QLNSINLSFQ -> MPLKTRTALS (in isoform 2).
{ECO:0000303|PubMed:11509567}.
/FTId=VSP_007683.
VAR_SEQ 310 412 Missing (in isoform 3).
{ECO:0000303|PubMed:11493482}.
/FTId=VSP_007684.
VARIANT 614 614 V -> L (in dbSNP:rs3733875).
{ECO:0000269|PubMed:12464997}.
/FTId=VAR_015775.
VARIANT 691 691 A -> T (in dbSNP:rs28932177).
{ECO:0000269|PubMed:12464997}.
/FTId=VAR_015776.
VARIANT 726 726 S -> P (in dbSNP:rs28932178).
{ECO:0000269|PubMed:12464997,
ECO:0000269|PubMed:18987736}.
/FTId=VAR_015777.
VARIANT 1036 1036 A -> P (in dbSNP:rs28932179).
{ECO:0000269|PubMed:12464997}.
/FTId=VAR_015778.
VARIANT 1091 1091 L -> I (in dbSNP:rs35597015).
{ECO:0000269|PubMed:12464997}.
/FTId=VAR_015779.
VARIANT 1616 1616 H -> L (in SOTOS1).
{ECO:0000269|PubMed:12464997}.
/FTId=VAR_015780.
VARIANT 1637 1637 L -> P (in SOTOS1).
{ECO:0000269|PubMed:12464997}.
/FTId=VAR_015781.
VARIANT 1674 1674 C -> W (in SOTOS1).
{ECO:0000269|PubMed:12464997}.
/FTId=VAR_015782.
VARIANT 1687 1687 I -> N (in SOTOS1).
{ECO:0000269|PubMed:12807965}.
/FTId=VAR_015783.
VARIANT 1792 1792 G -> V (in SOTOS1).
{ECO:0000269|PubMed:12464997}.
/FTId=VAR_015784.
VARIANT 1925 1925 C -> R (in SOTOS1).
{ECO:0000269|PubMed:12464997}.
/FTId=VAR_015785.
VARIANT 1955 1955 G -> D (in SOTOS1).
{ECO:0000269|PubMed:12807965}.
/FTId=VAR_015786.
VARIANT 1984 1984 R -> Q (in SOTOS1; loss of enzyme
activity; dbSNP:rs587784169).
{ECO:0000269|PubMed:12807965,
ECO:0000269|PubMed:21196496}.
/FTId=VAR_015787.
VARIANT 1997 1997 Y -> C (in SOTOS1; dbSNP:rs797045825).
{ECO:0000269|PubMed:12807965}.
/FTId=VAR_015788.
VARIANT 2005 2005 R -> Q (in SOTOS1; strongly reduced
enzyme activity; dbSNP:rs587784174).
{ECO:0000269|PubMed:12464997,
ECO:0000269|PubMed:21196496}.
/FTId=VAR_015789.
VARIANT 2017 2017 R -> Q (in SOTOS1; loss of enzyme
activity; dbSNP:rs587784177).
{ECO:0000269|PubMed:12464997,
ECO:0000269|PubMed:21196496}.
/FTId=VAR_015790.
VARIANT 2017 2017 R -> W (in SOTOS1; dbSNP:rs587784176).
{ECO:0000269|PubMed:12807965}.
/FTId=VAR_015791.
VARIANT 2143 2143 H -> Q (in SOTOS1; dbSNP:rs121908068).
{ECO:0000269|PubMed:12464997}.
/FTId=VAR_015792.
VARIANT 2183 2183 C -> S (in SOTOS1; dbSNP:rs121908069).
{ECO:0000269|PubMed:12464997}.
/FTId=VAR_015793.
VARIANT 2250 2250 M -> I (in dbSNP:rs35848863).
{ECO:0000269|PubMed:12464997}.
/FTId=VAR_015794.
VARIANT 2261 2261 M -> T (in dbSNP:rs34165241).
{ECO:0000269|PubMed:12464997}.
/FTId=VAR_015795.
MUTAGEN 1914 1914 R->C: Reduced enzyme activity.
{ECO:0000269|PubMed:21196496}.
MUTAGEN 1952 1952 R->W: Nearly abolished enzyme activity.
{ECO:0000269|PubMed:21196496}.
CONFLICT 1306 1306 H -> D (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 1397 1397 P -> Q (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 1478 1478 A -> V (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 1959 1960 KT -> QE (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 1963 1963 K -> R (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 1982 1982 R -> M (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 1986 1991 RYAQEH -> KHAHEN (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 1995 1995 N -> H (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2001 2001 L -> I (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2016 2016 A -> S (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2022 2022 C -> S (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2030 2030 Q -> L (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2033 2033 S -> T (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2045 2046 LS -> VC (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2049 2049 K -> P (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2061 2061 E -> D (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2066 2066 G -> E (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2071 2071 K -> R (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2075 2075 P -> S (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2304 2305 TK -> AQ (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2352 2352 R -> S (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2539 2539 L -> S (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2543 2543 P -> S (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2567 2591 PGPLSQSPGLVKQAKQMVGGQQLPA -> QGFFTKSPALVE
NKGKTKWVGRPTNYLH (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2597 2597 G -> W (in Ref. 3; AAK92049).
{ECO:0000305}.
CONFLICT 2608 2612 ASLPT -> PSSPN (in Ref. 3; AAK92049).
{ECO:0000305}.
HELIX 1852 1863 {ECO:0000244|PDB:3OOI}.
HELIX 1889 1891 {ECO:0000244|PDB:3OOI}.
STRAND 1901 1903 {ECO:0000244|PDB:3OOI}.
HELIX 1912 1915 {ECO:0000244|PDB:3OOI}.
TURN 1922 1924 {ECO:0000244|PDB:3OOI}.
HELIX 1928 1930 {ECO:0000244|PDB:3OOI}.
HELIX 1935 1938 {ECO:0000244|PDB:3OOI}.
STRAND 1944 1948 {ECO:0000244|PDB:3OOI}.
STRAND 1950 1960 {ECO:0000244|PDB:3OOI}.
STRAND 1967 1970 {ECO:0000244|PDB:3OOI}.
STRAND 1973 1976 {ECO:0000244|PDB:3OOI}.
HELIX 1978 1990 {ECO:0000244|PDB:3OOI}.
STRAND 1998 2002 {ECO:0000244|PDB:3OOI}.
STRAND 2005 2013 {ECO:0000244|PDB:3OOI}.
HELIX 2015 2018 {ECO:0000244|PDB:3OOI}.
STRAND 2026 2034 {ECO:0000244|PDB:3OOI}.
STRAND 2037 2046 {ECO:0000244|PDB:3OOI}.
SEQUENCE 2696 AA; 296652 MW; 4E80E6DCD9A24C81 CRC64;
MDQTCELPRR NCLLPFSNPV NLDAPEDKDS PFGNGQSNFS EPLNGCTMQL STVSGTSQNA
YGQDSPSCYI PLRRLQDLAS MINVEYLNGS ADGSESFQDP EKSDSRAQTP IVCTSLSPGG
PTALAMKQEP SCNNSPELQV KVTKTIKNGF LHFENFTCVD DADVDSEMDP EQPVTEDESI
EEIFEETQTN ATCNYETKSE NGVKVAMGSE QDSTPESRHG AVKSPFLPLA PQTETQKNKQ
RNEVDGSNEK AALLPAPFSL GDTNITIEEQ LNSINLSFQD DPDSSTSTLG NMLELPGTSS
SSTSQELPFC QPKKKSTPLK YEVGDLIWAK FKRRPWWPCR ICSDPLINTH SKMKVSNRRP
YRQYYVEAFG DPSERAWVAG KAIVMFEGRH QFEELPVLRR RGKQKEKGYR HKVPQKILSK
WEASVGLAEQ YDVPKGSKNR KCIPGSIKLD SEEDMPFEDC TNDPESEHDL LLNGCLKSLA
FDSEHSADEK EKPCAKSRAR KSSDNPKRTS VKKGHIQFEA HKDERRGKIP ENLGLNFISG
DISDTQASNE LSRIANSLTG SNTAPGSFLF SSCGKNTAKK EFETSNGDSL LGLPEGALIS
KCSREKNKPQ RSLVCGSKVK LCYIGAGDEE KRSDSISICT TSDDGSSDLD PIEHSSESDN
SVLEIPDAFD RTENMLSMQK NEKIKYSRFA ATNTRVKAKQ KPLISNSHTD HLMGCTKSAE
PGTETSQVNL SDLKASTLVH KPQSDFTNDA LSPKFNLSSS ISSENSLIKG GAANQALLHS
KSKQPKFRSI KCKHKENPVM AEPPVINEEC SLKCCSSDTK GSPLASISKS GKVDGLKLLN
NMHEKTRDSS DIETAVVKHV LSELKELSYR SLGEDVSDSG TSKPSKPLLF SSASSQNHIP
IEPDYKFSTL LMMLKDMHDS KTKEQRLMTA QNLVSYRSPG RGDCSTNSPV GVSKVLVSGG
STHNSEKKGD GTQNSANPSP SGGDSALSGE LSASLPGLLS DKRDLPASGK SRSDCVTRRN
CGRSKPSSKL RDAFSAQMVK NTVNRKALKT ERKRKLNQLP SVTLDAVLQG DRERGGSLRG
GAEDPSKEDP LQIMGHLTSE DGDHFSDVHF DSKVKQSDPG KISEKGLSFE NGKGPELDSV
MNSENDELNG VNQVVPKKRW QRLNQRRTKP RKRMNRFKEK ENSECAFRVL LPSDPVQEGR
DEFPEHRTPS ASILEEPLTE QNHADCLDSA GPRLNVCDKS SASIGDMEKE PGIPSLTPQA
ELPEPAVRSE KKRLRKPSKW LLEYTEEYDQ IFAPKKKQKK VQEQVHKVSS RCEEESLLAR
GRSSAQNKQV DENSLISTKE EPPVLEREAP FLEGPLAQSE LGGGHAELPQ LTLSVPVAPE
VSPRPALESE ELLVKTPGNY ESKRQRKPTK KLLESNDLDP GFMPKKGDLG LSKKCYEAGH
LENGITESCA TSYSKDFGGG TTKIFDKPRK RKRQRHAAAK MQCKKVKNDD SSKEIPGSEG
ELMPHRTATS PKETVEEGVE HDPGMPASKK MQGERGGGAA LKENVCQNCE KLGELLLCEA
QCCGAFHLEC LGLTEMPRGK FICNECRTGI HTCFVCKQSG EDVKRCLLPL CGKFYHEECV
QKYPPTVMQN KGFRCSLHIC ITCHAANPAN VSASKGRLMR CVRCPVAYHA NDFCLAAGSK
ILASNSIICP NHFTPRRGCR NHEHVNVSWC FVCSEGGSLL CCDSCPAAFH RECLNIDIPE
GNWYCNDCKA GKKPHYREIV WVKVGRYRWW PAEICHPRAV PSNIDKMRHD VGEFPVLFFG
SNDYLWTHQA RVFPYMEGDV SSKDKMGKGV DGTYKKALQE AAARFEELKA QKELRQLQED
RKNDKKPPPY KHIKVNRPIG RVQIFTADLS EIPRCNCKAT DENPCGIDSE CINRMLLYEC
HPTVCPAGGR CQNQCFSKRQ YPEVEIFRTL QRGWGLRTKT DIKKGEFVNE YVGELIDEEE
CRARIRYAQE HDITNFYMLT LDKDRIIDAG PKGNYARFMN HCCQPNCETQ KWSVNGDTRV
GLFALSDIKA GTELTFNYNL ECLGNGKTVC KCGAPNCSGF LGVRPKNQPI ATEEKSKKFK
KKQQGKRRTQ GEITKEREDE CFSCGDAGQL VSCKKPGCPK VYHADCLNLT KRPAGKWECP
WHQCDICGKE AASFCEMCPS SFCKQHREGM LFISKLDGRL SCTEHDPCGP NPLEPGEIRE
YVPPPVPLPP GPSTHLAEQS TGMAAQAPKM SDKPPADTNQ MLSLSKKALA GTCQRPLLPE
RPLERTDSRP QPLDKVRDLA GSGTKSQSLV SSQRPLDRPP AVAGPRPQLS DKPSPVTSPS
SSPSVRSQPL ERPLGTADPR LDKSIGAASP RPQSLEKTSV PTGLRLPPPD RLLITSSPKP
QTSDRPTDKP HASLSQRLPP PEKVLSAVVQ TLVAKEKALR PVDQNTQSKN RAALVMDLID
LTPRQKERAA SPHQVTPQAD EKMPVLESSS WPASKGLGHM PRAVEKGCVS DPLQTSGKAA
APSEDPWQAV KSLTQARLLS QPPAKAFLYE PTTQASGRAS AGAEQTPGPL SQSPGLVKQA
KQMVGGQQLP ALAAKSGQSF RSLGKAPASL PTEEKKLVTT EQSPWALGKA SSRAGLWPIV
AGQTLAQSCW SAGSTQTLAQ TCWSLGRGQD PKPEQNTLPA LNQAPSSHKC AESEQK


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