DNMT1_RAT
ID DNMT1_RAT Reviewed; 1622 AA.
AC Q9Z330; P70487; Q9R252; Q9WTX3; Q9WU57;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2002, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=DNA (cytosine-5)-methyltransferase 1;
DE Short=Dnmt1;
DE EC=2.1.1.37;
DE AltName: Full=DNA MTase RnoIP;
DE Short=M.RnoIP;
DE AltName: Full=DNA methyltransferase I;
DE AltName: Full=MCMT;
GN Name=Dnmt1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Placenta;
RX PubMed=9878564; DOI=10.1006/bbrc.1998.9802;
RA Kimura H., Takeda T., Tanaka S., Ogawa T., Shiota K.;
RT "Expression of rat DNA (cytosine-5) methyltransferase (DNA MTase) in rodent
RT trophoblast giant cells: molecular cloning and characterization of rat DNA
RT MTase.";
RL Biochem. Biophys. Res. Commun. 253:495-501(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 1-144 (ISOFORMS 1 AND 9).
RC TISSUE=Brain;
RA Deng J., Szyf M.;
RT "Multiple N-terminal isoforms of DNA (cytosine-5-)-methyltransferase in
RT vivo.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-356, AND IN VITRO BINDING TO ANNEXIN V.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=8667030; DOI=10.1046/j.1471-4159.1996.67010089.x;
RA Ohsawa K., Imai Y., Ito D., Kohsaka S.;
RT "Molecular cloning and characterization of annexin V-binding proteins with
RT highly hydrophilic peptide structure.";
RL J. Neurochem. 67:89-97(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1169-1517 (ISOFORMS 1; 2; 3; 4; 5; 6;
RP 7 AND 8).
RX PubMed=9722504; DOI=10.1074/jbc.273.36.22869;
RA Deng J., Szyf M.;
RT "Multiple isoforms of DNA methyltransferase are encoded by the vertebrate
RT cytosine DNA methyltransferase gene.";
RL J. Biol. Chem. 273:22869-22872(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; THR-304; SER-718 AND
RP SER-1436, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Methylates CpG residues. Preferentially methylates
CC hemimethylated DNA. Associates with DNA replication sites in S phase
CC maintaining the methylation pattern in the newly synthesized strand,
CC that is essential for epigenetic inheritance. Associates with chromatin
CC during G2 and M phases to maintain DNA methylation independently of
CC replication. It is responsible for maintaining methylation patterns
CC established in development. DNA methylation is coordinated with
CC methylation of histones. Mediates transcriptional repression by direct
CC binding to HDAC2. In association with DNMT3B and via the recruitment of
CC CTCFL/BORIS, involved in activation of BAG1 gene expression by
CC modulating dimethylation of promoter histone H3 at H3K4 and H3K9.
CC Probably forms a corepressor complex required for activated KRAS-
CC mediated promoter hypermethylation and transcriptional silencing of
CC tumor suppressor genes (TSGs) or other tumor-related genes in
CC colorectal cancer (CRC) cells. Also required to maintain a
CC transcriptionally repressive state of genes in undifferentiated
CC embryonic stem cells (ESCs). Associates at promoter regions of tumor
CC suppressor genes (TSGs) leading to their gene silencing. Promotes tumor
CC growth. {ECO:0000250|UniProtKB:P26358}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10018};
CC -!- SUBUNIT: Homodimer. Forms a stable complex with E2F1, BB1 and HDAC1.
CC Forms a complex with DMAP1 and HDAC2, with direct interaction.
CC Interacts with the PRC2/EED-EZH2 complex. Probably part of a
CC corepressor complex containing ZNF304, TRIM28, SETDB1 and DNMT1.
CC Interacts with UHRF1; promoting its recruitment to hemimethylated DNA.
CC Interacts with USP7, promoting its deubiquitination. Interacts with
CC BAZ2A/TIP5. Interacts with PCNA. Interacts with MBD2 and MBD3.
CC Interacts with DNMT3A and DNMT3B. Interacts with UBC9. Interacts with
CC HDAC1. Interacts with CSNK1D. Interacts with SIRT7. Interacts with
CC ZNF263; recruited to the SIX3 promoter along with other proteins
CC involved in chromatin modification and transcriptional corepression
CC where it contributes to transcriptional repression (By similarity).
CC {ECO:0000250|UniProtKB:P13864, ECO:0000250|UniProtKB:P26358}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9Z330-1; Sequence=Displayed;
CC Name=2; Synonyms=SF1;
CC IsoId=Q9Z330-2; Sequence=VSP_005627;
CC Name=3; Synonyms=SF2;
CC IsoId=Q9Z330-3; Sequence=VSP_005625;
CC Name=4; Synonyms=SF3;
CC IsoId=Q9Z330-4; Sequence=VSP_005624;
CC Name=5; Synonyms=SF4;
CC IsoId=Q9Z330-5; Sequence=VSP_005621;
CC Name=6; Synonyms=SF5;
CC IsoId=Q9Z330-6; Sequence=VSP_005622;
CC Name=7; Synonyms=SF6;
CC IsoId=Q9Z330-7; Sequence=VSP_005626;
CC Name=8; Synonyms=SF7;
CC IsoId=Q9Z330-8; Sequence=VSP_005623;
CC Name=9; Synonyms=short;
CC IsoId=Q9Z330-9; Sequence=VSP_005620;
CC -!- TISSUE SPECIFICITY: Isoforms 0 and 8 are highly expressed in placenta,
CC brain, lung, spleen, kidney, heart, and at much lower levels in liver.
CC Isoform 1 is expressed in cerebellum, isoform 2 in muscle and testis,
CC isoform 3 in lung, isoform 4 in spleen and brain, and isoform 5 in
CC brain.
CC -!- DOMAIN: The N-terminal part is required for homodimerization and acts
CC as a regulatory domain.
CC -!- DOMAIN: The CXXC-type zinc finger specifically binds to unmethylated
CC CpG dinucleotides, positioning the autoinhibitory linker between the
CC DNA and the active site, thus providing a mechanism to ensure that only
CC hemimethylated CpG dinucleotides undergo methylation.
CC {ECO:0000250|UniProtKB:P26358}.
CC -!- PTM: Sumoylated; sumoylation increases activity.
CC {ECO:0000250|UniProtKB:P26358}.
CC -!- PTM: Acetylation on multiple lysines, mainly by KAT2B/PCAF, regulates
CC cell cycle G(2)/M transition. Deacetylation of Lys-1116 and Lys-1354 by
CC SIRT1 increases methyltransferase activity.
CC {ECO:0000250|UniProtKB:P26358}.
CC -!- PTM: Phosphorylation of Ser-151 by CDKs is important for enzymatic
CC activity and protein stability. Phosphorylation of Ser-140 by AKT1
CC prevents methylation by SETD7 therebye increasing DNMT1 stability.
CC {ECO:0000250|UniProtKB:P26358}.
CC -!- PTM: Methylation at Lys-139 by SETD7 promotes DNMT1 proteasomal
CC degradation. {ECO:0000250|UniProtKB:P26358}.
CC -!- PTM: Ubiquitinated by UHRF1; interaction with USP7 counteracts
CC ubiquitination by UHRF1 by promoting deubiquitination and preventing
CC degradation by the proteasome. {ECO:0000250|UniProtKB:P13864}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01016}.
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DR EMBL; AB012214; BAA37118.1; -; mRNA.
DR EMBL; AF116344; AAD32541.1; -; mRNA.
DR EMBL; AF116345; AAD32542.1; -; Genomic_DNA.
DR EMBL; D64060; BAA20854.1; -; mRNA.
DR EMBL; AH007612; AAD28102.1; -; Genomic_DNA.
DR PIR; JE0378; JE0378.
DR AlphaFoldDB; Q9Z330; -.
DR SMR; Q9Z330; -.
DR IntAct; Q9Z330; 2.
DR STRING; 10116.ENSRNOP00000063831; -.
DR REBASE; 11410; M.RraDnmtI.
DR REBASE; 3019; M.RnoDnmt1.
DR CarbonylDB; Q9Z330; -.
DR iPTMnet; Q9Z330; -.
DR PhosphoSitePlus; Q9Z330; -.
DR jPOST; Q9Z330; -.
DR PaxDb; Q9Z330; -.
DR PRIDE; Q9Z330; -.
DR UCSC; RGD:620979; rat. [Q9Z330-1]
DR RGD; 620979; Dnmt1.
DR eggNOG; ENOG502QPKK; Eukaryota.
DR InParanoid; Q9Z330; -.
DR PhylomeDB; Q9Z330; -.
DR BioCyc; MetaCyc:MON-8581; -.
DR BRENDA; 2.1.1.37; 5301.
DR Reactome; R-RNO-212300; PRC2 methylates histones and DNA.
DR Reactome; R-RNO-4655427; SUMOylation of DNA methylation proteins.
DR PRO; PR:Q9Z330; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0000792; C:heterochromatin; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005721; C:pericentric heterochromatin; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005657; C:replication fork; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0009008; F:DNA-methyltransferase activity; ISO:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; IPI:RGD.
DR GO; GO:0008327; F:methyl-CpG binding; ISO:RGD.
DR GO; GO:0008168; F:methyltransferase activity; ISO:RGD.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IPI:RGD.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0003723; F:RNA binding; ISO:RGD.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; TAS:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
DR GO; GO:1903926; P:cellular response to bisphenol A; ISO:RGD.
DR GO; GO:0071284; P:cellular response to lead ion; IEP:RGD.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IEP:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:RGD.
DR GO; GO:0044026; P:DNA hypermethylation; IMP:RGD.
DR GO; GO:0006306; P:DNA methylation; ISO:RGD.
DR GO; GO:0043045; P:DNA methylation involved in embryo development; ISO:RGD.
DR GO; GO:0032776; P:DNA methylation on cytosine; IDA:RGD.
DR GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IDA:RGD.
DR GO; GO:0006346; P:DNA methylation-dependent heterochromatin assembly; ISO:RGD.
DR GO; GO:0010216; P:maintenance of DNA methylation; IDA:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:1905460; P:negative regulation of vascular associated smooth muscle cell apoptotic process; ISO:RGD.
DR GO; GO:1905931; P:negative regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0007265; P:Ras protein signal transduction; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0031000; P:response to caffeine; IEP:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0010212; P:response to ionizing radiation; IEP:RGD.
DR GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0033574; P:response to testosterone; IEP:RGD.
DR GO; GO:0009636; P:response to toxic substance; IEP:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; IDA:RGD.
DR Gene3D; 2.30.30.490; -; 2.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR018117; C5_DNA_meth_AS.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR031303; C5_meth_CS.
DR InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
DR InterPro; IPR010506; DMAP1-bd.
DR InterPro; IPR017198; DNMT1-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002857; Znf_CXXC.
DR Pfam; PF01426; BAH; 2.
DR Pfam; PF06464; DMAP_binding; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF12047; DNMT1-RFD; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR PIRSF; PIRSF037404; DNMT1; 1.
DR PRINTS; PR00105; C5METTRFRASE.
DR SMART; SM00439; BAH; 2.
DR SMART; SM01137; DMAP_binding; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51038; BAH; 2.
DR PROSITE; PS00094; C5_MTASE_1; 1.
DR PROSITE; PS00095; C5_MTASE_2; 1.
DR PROSITE; PS51912; DMAP1_BIND; 1.
DR PROSITE; PS51679; SAM_MT_C5; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Chromatin regulator;
KW DNA-binding; Isopeptide bond; Metal-binding; Methylation;
KW Methyltransferase; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1622
FT /note="DNA (cytosine-5)-methyltransferase 1"
FT /id="PRO_0000088036"
FT DOMAIN 16..109
FT /note="DMAP1-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01260"
FT DOMAIN 759..884
FT /note="BAH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 977..1105
FT /note="BAH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT REPEAT 1114..1115
FT /note="1"
FT REPEAT 1116..1117
FT /note="2"
FT REPEAT 1118..1119
FT /note="3"
FT REPEAT 1120..1121
FT /note="4"
FT REPEAT 1122..1123
FT /note="5"
FT REPEAT 1124..1125
FT /note="6"
FT REPEAT 1126..1127
FT /note="7; approximate"
FT DOMAIN 1144..1603
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ZN_FING 650..696
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT REGION 1..342
FT /note="Interaction with the PRC2/EED-EZH2 complex"
FT /evidence="ECO:0000250"
FT REGION 1..145
FT /note="Interaction with DNMT3A"
FT /evidence="ECO:0000250"
FT REGION 100..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..213
FT /note="Interaction with DNMT3B"
FT /evidence="ECO:0000250"
FT REGION 304..610
FT /note="Interaction with the PRC2/EED-EZH2 complex"
FT /evidence="ECO:0000250"
FT REGION 327..556
FT /note="DNA replication foci-targeting sequence"
FT REGION 697..758
FT /note="Autoinhibitory linker"
FT REGION 702..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1127
FT /note="7 X 2 AA tandem repeats of K-G"
FT REGION 1126..1622
FT /note="Interaction with the PRC2/EED-EZH2 complex"
FT /evidence="ECO:0000250"
FT REGION 1144..1622
FT /note="Catalytic"
FT MOTIF 173..200
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 144..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 362
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 424
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 657
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 660
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 663
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 668
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 671
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 674
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 690
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 695
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 1151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT BINDING 1155..1156
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT BINDING 1173..1174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT BINDING 1195..1196
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT BINDING 1196
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT BINDING 1582
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT BINDING 1584
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT SITE 515
FT /note="Important for activity"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 70
FT /note="N6,N6-dimethyllysine; by EHMT2"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT MOD_RES 139
FT /note="N6-methyllysine; by SETD7"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 140
FT /note="Phosphoserine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 163
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 169
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 372
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 736
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 753
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 882
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 895
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 961
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 980
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 1116
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 1118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 1120
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 1122
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 1124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT MOD_RES 1126
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P13864"
FT MOD_RES 1354
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT MOD_RES 1436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 1613
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P26358"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_005620"
FT VAR_SEQ 1202..1410
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_005622"
FT VAR_SEQ 1216..1504
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000305"
FT /id="VSP_005623"
FT VAR_SEQ 1218..1430
FT /note="QKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKNSLVVSFLSYCDYYRPRFFL
FT LENVRNFVSFRRSMVLKLTLRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEK
FT LPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTITMRDTMSDLPEIQNGAS
FT APEISYKWRATVLVPEAAARVALPAHPQGPYPQVHERAGGCRM -> VC (in
FT isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_005621"
FT VAR_SEQ 1226..1477
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005624"
FT VAR_SEQ 1252..1482
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_005625"
FT VAR_SEQ 1259..1481
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000305"
FT /id="VSP_005626"
FT VAR_SEQ 1323..1403
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005627"
FT CONFLICT 17..25
FT /note="AGSLPDHVR -> RQARPRPCP (in Ref. 3; BAA20854)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="A -> V (in Ref. 3; BAA20854)"
FT /evidence="ECO:0000305"
FT CONFLICT 1276
FT /note="F -> S (in Ref. 1; BAA37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 1300
FT /note="T -> I (in Ref. 4; AAD28102)"
FT /evidence="ECO:0000305"
FT CONFLICT 1372
FT /note="M -> V (in Ref. 1; BAA37118)"
FT /evidence="ECO:0000305"
FT CONFLICT 1394..1428
FT /note="KWRATVLVPEAAARVALPAHPQGPYPQVHERAGGC -> NGEPQSWFQRQLR
FT GSHYQPILRDHICKDMSALVAA (in Ref. 1; BAA37118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1622 AA; 182774 MW; FCFA4AAA69E234BA CRC64;
MPARTAPARV PALASPAGSL PDHVRRRLKD LERDGLTEKE CVKEKLNLLH EFLQTEIKSQ
LCDLETKLHK EELSEEGYLA KVKTLLNKDL CLENGTLSLT QKANGCPANG SRPTWKAEMA
DSNRSPRSRP KPRGPRRSKS DSETMIEASS SSVATRRTTR QTTITSHFKG PAKRKPKEDS
EKGNANESAA EERDQDKKRR VAGTESRASR AGESVEKPER VRPGTQLCQE EQGEQEDDRR
PRRQTRELAS RRKSREDPDR EARPGTHLDV DDDDEKDKRS SRPRSQPRDL ATKRRPKEEV
EQITPEPPEG KDEDEREEKR RKTTRKKPEP LSIPVQSRVE RKASQGKASA IPKLNPPQCP
ECGQYLDDPD LKYQQHPVDA VDEPQMLTNE ALSVFDSNSS WFETYDSSPM HKFTFFSVYC
SRGHLCPVDT GLIEKNVELY FSGVAKAIHE ENPSVEGGVN GKNLGPINQW WISGFDGGEK
ALIGFSTAFA EYFLMEPSPE YAPIFGLMQE KIYISKIVVE FLQSNPDAVY EDLINKIETT
VPPSAINVNR FTEDSLLRHA QFVVSQVESY DDAKDDDETP IFLSPCMRSL IHLAGVSLGQ
RRATRRTVIN SAKVKRKGPT KATTTKLVYQ IFDTFFSEQI EKDDKEDKEN TMKRRRCGVC
EVCQQPECGK CKACKDMVKF GGTGRSKQAC LKRRCPNLAV KEADEDEEAD DDIPELPSPK
KLHQGKKKKQ NKDRISWLGE PVKIEENRTY YWKVSIDEET LEVGDCVSVI PDDPSKPLYL
ARVTALWEDK NGQMFHAHWF CAGTDTVLGA TSDPLELFLV GECENMQLSY IHSKVKVIYR
GPSPNWAMEG GMDPEAMLPG AEDGKTYFYQ FWYSQDYARF ESPPKTQPAE DNKHKFCLSC
IRLAELRQKE MPKVLEQLEE VDGRVYCSSI TKNGVVYRLG DSVYLPPEAF TFNIKMASPM
KRSKRDPVNE NPVPRDTYRK YSDYIKGSNL DAPEPYRIGR IKEIYCGKKK GGKVNEADIK
IRLYKFYRPE NTHKSIQATY HADINLLYWS DEEAVVDFSD VQGRCTVEYG EDLLESIQDY
SQGGPDRFYF LEAYNSKTKS FEDPPNHARS PGNKGKGKGK GKGKGKPQVS EPKEPEAAIK
LPKLRTLDVF SGCGGLTEGF HQAGISETLW AIEMWEPAAQ AFRLNNPGTT VFTEDCNVLL
KLVMAGEVTN SLGQRLPQKG DVEMLCGGPP CQGFSGMNRF NSRTYSKFKN SLVVSFLSYC
DYYRPRFFLL ENVRNFVSFR RSMVLKLTLR CLVRMGYQCT FGVLQAGQYG VAQTRRRAII
LAAAPGEKLP LFPEPLHVFA PRACQLSVVV DDKKFVSNIT RLSSGPFRTI TMRDTMSDLP
EIQNGASAPE ISYKWRATVL VPEAAARVAL PAHPQGPYPQ VHERAGGCRM RHIPLSPGSD
WRDLPNIQVR LRDGVITNKL RYTFHDTKNG CSSTGALRGV CSCAEGKTCD PASRQFNTLI
PWCLPHTGNR HNHWAGLYGR LEWDGFFSTT VTNPEPMGKQ GRVLHPEQHR VVSVRECARS
QGFPDTYRLF GNILDRHRQV GNAVPPPLAK AIGLEIKLCL LASAQESASA AVKGKEETTT
ED
