SETD4_HUMAN
ID SETD4_HUMAN Reviewed; 440 AA.
AC Q9NVD3; B4DT14; D3DSG2; D3DSG4; Q8NE19; Q9BU46;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=SET domain-containing protein 4 {ECO:0000305};
DE EC=2.1.1.- {ECO:0000269|PubMed:31308046};
DE EC=2.1.1.364 {ECO:0000250|UniProtKB:P58467};
GN Name=SETD4 {ECO:0000303|PubMed:24738023, ECO:0000312|HGNC:HGNC:1258};
GN Synonyms=C21orf18 {ECO:0000312|HGNC:HGNC:1258},
GN C21orf27 {ECO:0000312|HGNC:HGNC:1258};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RX PubMed=11707072; DOI=10.1006/geno.2001.6640;
RA Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F., Deutsch S.,
RA Ucla C., Rossier C., Lyle R., Guipponi M., Antonarakis S.E.;
RT "From PREDs and open reading frames to cDNA isolation: revisiting the human
RT chromosome 21 transcription map.";
RL Genomics 78:46-54(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; 3 AND 4).
RC TISSUE=Lung, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=24738023;
RA Faria J.A., Correa N.C., de Andrade C., de Angelis Campos A.C.,
RA Dos Santos Samuel de Almeida R., Rodrigues T.S., de Goes A.M., Gomes D.A.,
RA Silva F.P.;
RT "SET domain-containing protein 4 (SETD4) is a newly identified Cytosolic
RT and nuclear lysine methyltransferase involved in breast cancer cell
RT proliferation.";
RL J. Cancer Sci. Ther. 5:58-65(2013).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLY-61 AND ASP-233.
RX PubMed=31308046; DOI=10.1158/0008-5472.can-19-1084;
RA Ye S., Ding Y.F., Jia W.H., Liu X.L., Feng J.Y., Zhu Q., Cai S.L.,
RA Yang Y.S., Lu Q.Y., Huang X.T., Yang J.S., Jia S.N., Ding G.P., Wang Y.H.,
RA Zhou J.J., Chen Y.D., Yang W.J.;
RT "SET domain-containing protein 4 epigenetically controls breast cancer stem
RT cell quiescence.";
RL Cancer Res. 79:4729-4743(2019).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-420.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Histone-lysine N-methyltransferase that acts as a regulator
CC of cell proliferation, cell differentiation and inflammatory response
CC (PubMed:31308046). Regulates the inflammatory response by mediating
CC mono- and dimethylation of 'Lys-4' of histone H3 (H3K4me1 and H3K4me2,
CC respectively), leading to activate the transcription of pro-
CC inflammatory cytokines IL6 and TNF-alpha (By similarity). Also involved
CC in the regulation of stem cell quiescence by catalyzing the
CC trimethylation of 'Lys-20' of histone H4 (H4K20me3), thereby promoting
CC heterochromatin formation (PubMed:31308046). Involved in proliferation,
CC migration, paracrine and myogenic differentiation of bone marrow
CC mesenchymal stem cells (BMSCs) (By similarity).
CC {ECO:0000250|UniProtKB:P58467, ECO:0000269|PubMed:31308046}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC Evidence={ECO:0000250|UniProtKB:P58467};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60268, Rhea:RHEA-COMP:15540, Rhea:RHEA-
CC COMP:15543, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000250|UniProtKB:P58467};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC Evidence={ECO:0000269|PubMed:31308046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555, Rhea:RHEA-
CC COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976;
CC Evidence={ECO:0000269|PubMed:31308046};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4]
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:61992, Rhea:RHEA-
CC COMP:15556, Rhea:RHEA-COMP:15998, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:31308046};
CC -!- INTERACTION:
CC Q9NVD3-4; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-23709068, EBI-752069;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24738023}.
CC Nucleus {ECO:0000269|PubMed:24738023}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=A;
CC IsoId=Q9NVD3-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9NVD3-2; Sequence=VSP_004146;
CC Name=3;
CC IsoId=Q9NVD3-3; Sequence=VSP_026578;
CC Name=4;
CC IsoId=Q9NVD3-4; Sequence=VSP_054087, VSP_054088;
CC -!- MISCELLANEOUS: [Isoform B]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. SETD4 family. {ECO:0000255|PROSITE-ProRule:PRU00190,
CC ECO:0000305}.
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DR EMBL; AF391112; AAL34503.1; -; mRNA.
DR EMBL; AK001660; BAA91819.1; -; mRNA.
DR EMBL; AK300009; BAG61826.1; -; mRNA.
DR EMBL; AP000688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09757.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09758.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09759.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09760.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09762.1; -; Genomic_DNA.
DR EMBL; BC002898; AAH02898.1; -; mRNA.
DR EMBL; BC036556; AAH36556.1; -; mRNA.
DR CCDS; CCDS13640.1; -. [Q9NVD3-1]
DR CCDS; CCDS42923.1; -. [Q9NVD3-4]
DR CCDS; CCDS74792.1; -. [Q9NVD3-3]
DR RefSeq; NP_001007260.1; NM_001007259.2. [Q9NVD3-4]
DR RefSeq; NP_001007262.1; NM_001007261.2.
DR RefSeq; NP_001273681.1; NM_001286752.1. [Q9NVD3-3]
DR RefSeq; NP_059134.1; NM_017438.4. [Q9NVD3-1]
DR RefSeq; XP_011527938.1; XM_011529636.1. [Q9NVD3-1]
DR RefSeq; XP_011527939.1; XM_011529637.1. [Q9NVD3-1]
DR RefSeq; XP_011527940.1; XM_011529638.2. [Q9NVD3-1]
DR RefSeq; XP_011527941.1; XM_011529639.1. [Q9NVD3-1]
DR RefSeq; XP_011527942.1; XM_011529640.2. [Q9NVD3-1]
DR RefSeq; XP_011527944.1; XM_011529642.1. [Q9NVD3-3]
DR RefSeq; XP_011527945.1; XM_011529643.1. [Q9NVD3-3]
DR RefSeq; XP_011527946.1; XM_011529644.1. [Q9NVD3-3]
DR RefSeq; XP_016883892.1; XM_017028403.1.
DR RefSeq; XP_016883893.1; XM_017028404.1. [Q9NVD3-3]
DR RefSeq; XP_016883894.1; XM_017028405.1. [Q9NVD3-4]
DR AlphaFoldDB; Q9NVD3; -.
DR SMR; Q9NVD3; -.
DR BioGRID; 119892; 21.
DR IntAct; Q9NVD3; 16.
DR MINT; Q9NVD3; -.
DR STRING; 9606.ENSP00000382163; -.
DR iPTMnet; Q9NVD3; -.
DR PhosphoSitePlus; Q9NVD3; -.
DR BioMuta; SETD4; -.
DR DMDM; 12229715; -.
DR MassIVE; Q9NVD3; -.
DR PaxDb; Q9NVD3; -.
DR PeptideAtlas; Q9NVD3; -.
DR PRIDE; Q9NVD3; -.
DR ProteomicsDB; 82779; -. [Q9NVD3-1]
DR ProteomicsDB; 82781; -. [Q9NVD3-3]
DR Antibodypedia; 8172; 120 antibodies from 20 providers.
DR DNASU; 54093; -.
DR Ensembl; ENST00000332131.9; ENSP00000329189.4; ENSG00000185917.14. [Q9NVD3-1]
DR Ensembl; ENST00000399207.5; ENSP00000382158.1; ENSG00000185917.14. [Q9NVD3-4]
DR Ensembl; ENST00000399208.6; ENSP00000382159.2; ENSG00000185917.14. [Q9NVD3-4]
DR Ensembl; ENST00000399212.5; ENSP00000382161.1; ENSG00000185917.14. [Q9NVD3-3]
DR Ensembl; ENST00000399215.5; ENSP00000382163.1; ENSG00000185917.14. [Q9NVD3-1]
DR GeneID; 54093; -.
DR KEGG; hsa:54093; -.
DR MANE-Select; ENST00000332131.9; ENSP00000329189.4; NM_017438.5; NP_059134.1.
DR UCSC; uc002yuw.3; human. [Q9NVD3-1]
DR CTD; 54093; -.
DR DisGeNET; 54093; -.
DR GeneCards; SETD4; -.
DR HGNC; HGNC:1258; SETD4.
DR HPA; ENSG00000185917; Low tissue specificity.
DR neXtProt; NX_Q9NVD3; -.
DR OpenTargets; ENSG00000185917; -.
DR PharmGKB; PA25814; -.
DR VEuPathDB; HostDB:ENSG00000185917; -.
DR eggNOG; KOG1337; Eukaryota.
DR GeneTree; ENSGT00940000153577; -.
DR HOGENOM; CLU_029120_3_0_1; -.
DR InParanoid; Q9NVD3; -.
DR OMA; ADEFTCW; -.
DR OrthoDB; 1209399at2759; -.
DR PhylomeDB; Q9NVD3; -.
DR TreeFam; TF106421; -.
DR PathwayCommons; Q9NVD3; -.
DR SignaLink; Q9NVD3; -.
DR BioGRID-ORCS; 54093; 12 hits in 1088 CRISPR screens.
DR ChiTaRS; SETD4; human.
DR GenomeRNAi; 54093; -.
DR Pharos; Q9NVD3; Tbio.
DR PRO; PR:Q9NVD3; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q9NVD3; protein.
DR Bgee; ENSG00000185917; Expressed in oocyte and 163 other tissues.
DR ExpressionAtlas; Q9NVD3; baseline and differential.
DR Genevisible; Q9NVD3; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISS:UniProtKB.
DR GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IDA:UniProtKB.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0044648; P:histone H3-K4 dimethylation; ISS:UniProtKB.
DR GO; GO:0097692; P:histone H3-K4 monomethylation; ISS:UniProtKB.
DR GO; GO:0034773; P:histone H4-K20 trimethylation; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; IBA:GO_Central.
DR GO; GO:0018023; P:peptidyl-lysine trimethylation; IBA:GO_Central.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0071863; P:regulation of cell proliferation in bone marrow; ISS:UniProtKB.
DR CDD; cd19177; SET_SETD4; 1.
DR Gene3D; 3.90.1420.10; -; 1.
DR InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR016852; SET_MeTrfase.
DR InterPro; IPR044429; SETD4_SET.
DR Pfam; PF09273; Rubis-subs-bind; 1.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF027158; Lys_MTase_YDR198C_prd; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Inflammatory response; Methyltransferase;
KW Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..440
FT /note="SET domain-containing protein 4"
FT /id="PRO_0000079509"
FT DOMAIN 48..273
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 272
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT VAR_SEQ 1..25
FT /note="MQKGKGRTSRIRRRKLCGSSESRGV -> M (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026578"
FT VAR_SEQ 70..440
FT /note="EGQMIISLPESCLLTTDTVIRSYLGAYITKWKPPPSPLLALCTFLVSEKHAG
FT HRSLWKPYLEILPKAYTCPVCLEPEVVNLLPKSLKAKAEEQRAHVQEFFASSRDFFSSL
FT QPLFAEAVDSIFSYSALLWAWCTVNTRAVYLRPRQRECLSAEPDTCALAPYLDLLNHSP
FT HVQVKAAFNEETHSYEIRTTSRWRKHEEVFICYGPHDNQRLFLEYGFVSVHNPHACVYV
FT SREILVKYLPSTDKQMDKKISILKDHGYIENLTFGWDGPSWRLLTALKLLCLEAEKFTC
FT WKKVLLGEVISDTNEKTSLDIAQKICYYFIEETNAVLQKVSHMKDEKEALINQLTLVES
FT LWTEELKILRASAETLHSLQTAFT -> VEASSISSAGAVHLFSFRKACWAPISLEALP
FT GDFTQGVYLPCLFGAGSGEPSSQIFKSKG (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11707072,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_004146"
FT VAR_SEQ 301..307
FT /note="EILVKYL -> GWNQLCS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054087"
FT VAR_SEQ 308..440
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054088"
FT VARIANT 387
FT /note="I -> V (in dbSNP:rs2835239)"
FT /id="VAR_021948"
FT VARIANT 420
FT /note="E -> G (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035988"
FT MUTAGEN 61
FT /note="G->V: Abolished histone-lysine N-methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:31308046"
FT MUTAGEN 233
FT /note="D->A: Abolished histone-lysine N-methyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:31308046"
FT CONFLICT 301..440
FT /note="EILVKYLPSTDKQMDKKISILKDHGYIENLTFGWDGPSWRLLTALKLLCLEA
FT EKFTCWKKVLLGEVISDTNEKTSLDIAQKICYYFIEETNAVLQKVSHMKDEKEALINQL
FT TLVESLWTEELKILRASAETLHSLQTAFT -> GWNQLCS (in Ref. 5;
FT AAH02898)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 50416 MW; 9EBCAA05397BE287 CRC64;
MQKGKGRTSR IRRRKLCGSS ESRGVNESHK SEFIELRKWL KARKFQDSNL APACFPGTGR
GLMSQTSLQE GQMIISLPES CLLTTDTVIR SYLGAYITKW KPPPSPLLAL CTFLVSEKHA
GHRSLWKPYL EILPKAYTCP VCLEPEVVNL LPKSLKAKAE EQRAHVQEFF ASSRDFFSSL
QPLFAEAVDS IFSYSALLWA WCTVNTRAVY LRPRQRECLS AEPDTCALAP YLDLLNHSPH
VQVKAAFNEE THSYEIRTTS RWRKHEEVFI CYGPHDNQRL FLEYGFVSVH NPHACVYVSR
EILVKYLPST DKQMDKKISI LKDHGYIENL TFGWDGPSWR LLTALKLLCL EAEKFTCWKK
VLLGEVISDT NEKTSLDIAQ KICYYFIEET NAVLQKVSHM KDEKEALINQ LTLVESLWTE
ELKILRASAE TLHSLQTAFT
