KMT2E_MOUSE
ID KMT2E_MOUSE Reviewed; 1868 AA.
AC Q3UG20; Q3SYI5; Q3TUY2; Q3V410; Q5FWI1; Q6P3B3; Q8BS65; Q8CFX7; Q9CVK6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Inactive histone-lysine N-methyltransferase 2E {ECO:0000305};
DE Short=Inactive lysine N-methyltransferase 2E {ECO:0000305};
DE AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia protein 5 homolog;
GN Name=Kmt2e; Synonyms=Mll5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAE28389.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1153 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE28389.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAC28936.2},
RC Embryonic eye {ECO:0000312|EMBL:BAE43262.1},
RC Melanoma {ECO:0000312|EMBL:BAE28389.1},
RC Pancreas {ECO:0000312|EMBL:BAB25186.1}, and
RC Tongue {ECO:0000312|EMBL:BAE35839.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH89356.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-802 (ISOFORM 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-494 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH64079.1, ECO:0000312|EMBL:AAH89356.1},
RC and FVB/N {ECO:0000312|EMBL:AAH36286.1};
RC TISSUE=Eye {ECO:0000312|EMBL:AAH89356.1},
RC Mammary gland {ECO:0000312|EMBL:AAH64079.1}, and
RC Mammary tumor {ECO:0000312|EMBL:AAH36286.1};
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 [4] {ECO:0000305}
RP INDUCTION.
RX PubMed=18376068; DOI=10.1007/s12038-008-0019-6;
RA Sambasivan R., Pavlath G.K., Dhawan J.;
RT "A gene-trap strategy identifies quiescence-induced genes in synchronized
RT myoblasts.";
RL J. Biosci. 33:27-44(2008).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18854576; DOI=10.1182/blood-2008-06-162263;
RA Heuser M., Yap D.B., Leung M., de Algara T.R., Tafech A., McKinney S.,
RA Dixon J., Thresher R., Colledge B., Carlton M., Humphries R.K.,
RA Aparicio S.A.;
RT "Loss of MLL5 results in pleiotropic hematopoietic defects, reduced
RT neutrophil immune function, and extreme sensitivity to DNA demethylation.";
RL Blood 113:1432-1443(2009).
RN [6]
RP FUNCTION, LACK OF CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18952892; DOI=10.1182/blood-2008-02-142638;
RA Madan V., Madan B., Brykczynska U., Zilbermann F., Hogeveen K., Doehner K.,
RA Doehner H., Weber O., Blum C., Rodewald H.-R., Sassone-Corsi P.,
RA Peters A.H.F.M., Fehling H.J.;
RT "Impaired function of primitive hematopoietic cells in mice lacking the
RT Mixed-Lineage-Leukemia homolog MLL5.";
RL Blood 113:1444-1454(2009).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18818388; DOI=10.1182/blood-2008-05-159905;
RA Zhang Y., Wong J., Klinger M., Tran M.T., Shannon K.M., Killeen N.;
RT "MLL5 contributes to hematopoietic stem cell fitness and homeostasis.";
RL Blood 113:1455-1463(2009).
RN [8]
RP FUNCTION.
RX PubMed=19264965; DOI=10.1073/pnas.0807136106;
RA Sebastian S., Sreenivas P., Sambasivan R., Cheedipudi S., Kandalla P.,
RA Pavlath G.K., Dhawan J.;
RT "MLL5, a trithorax homolog, indirectly regulates H3K4 methylation,
RT represses cyclin A2 expression, and promotes myogenic differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:4719-4724(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-845, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Associates with chromatin regions downstream of
CC transcriptional start sites of active genes and thus regulates gene
CC transcription (By similarity). Chromatin interaction is mediated via
CC the binding to tri-methylated histone H3 at 'Lys-4' (H3K4me3) (By
CC similarity). Key regulator of hematopoiesis involved in terminal
CC myeloid differentiation and in the regulation of hematopoietic stem
CC cell (HSCs) self-renewal by a mechanism that involves DNA methylation
CC (PubMed:18854576, PubMed:18952892, PubMed:18818388). Also acts as an
CC important cell cycle regulator, participating in cell cycle regulatory
CC network machinery at multiple cell cycle stages including G1/S
CC transition, S phase progression and mitotic entry (PubMed:19264965).
CC Recruited to E2F1 responsive promoters by HCFC1 where it stimulates
CC tri-methylation of histone H3 at 'Lys-4' and transcriptional activation
CC and thereby facilitates G1 to S phase transition (By similarity).
CC During myoblast differentiation, required to suppress inappropriate
CC expression of S-phase-promoting genes and maintain expression of
CC determination genes in quiescent cells (PubMed:19264965).
CC {ECO:0000250|UniProtKB:Q8IZD2, ECO:0000269|PubMed:18818388,
CC ECO:0000269|PubMed:18854576, ECO:0000269|PubMed:18952892,
CC ECO:0000269|PubMed:19264965}.
CC -!- SUBUNIT: Component of a complex composed of KMT2E, OGT and USP7; the
CC complex stabilizes KMT2E, preventing KMT2E ubiquitination and
CC proteosomal-mediated degradation. Interacts (via N-terminus) with OGT
CC (via TRP repeats). Interacts with deubiquitinating enzyme USP7 (via
CC MATH domain). Interacts (via HBM motif) with HCFC1 (via Kelch domain).
CC Interacts with E2F1; the interaction is probably indirect and is
CC mediated via HCFC1. {ECO:0000250|UniProtKB:Q8IZD2}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:Q8IZD2}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q8IZD2}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q8IZD2}. Note=Absent from the nucleolus.
CC Localizes to chromosome during interphase and to centrosomes during
CC mitosis. Dissociation from mitotic chromosome is likely due to histone
CC H3 phosphorylation on 'Thr-3' and 'Thr-6'.
CC {ECO:0000250|UniProtKB:Q8IZD2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC IsoId=Q3UG20-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:16141072};
CC IsoId=Q3UG20-2; Sequence=VSP_052813;
CC -!- INDUCTION: Up-regulated in reversibly arrested C2C12 myoblasts.
CC {ECO:0000269|PubMed:18376068}.
CC -!- DOMAIN: The PHD-type domain binds specifically histone H3 tri-
CC methylated at 'Lys-4' (H3K4me3), thus promoting binding to chromatin.
CC {ECO:0000250|UniProtKB:Q8IZD2}.
CC -!- DOMAIN: The SET domain does not bind the methyl group donor S-adenosyl-
CC L-methionine and histone 3 H3K4 peptide as a large loop prevents the
CC docking of the 'Lys-4' side chain. {ECO:0000250|UniProtKB:Q8IZD2}.
CC -!- DOMAIN: The C-terminus domain is responsible for the localization to
CC the centrosome during mitosis. {ECO:0000250|UniProtKB:Q8IZD2}.
CC -!- PTM: Ubiquitinated. Deubiquitinated by USP7.
CC {ECO:0000250|UniProtKB:Q8IZD2}.
CC -!- PTM: O-glycosylated at Ser-435 and Thr-440 in the SET domain by OGT
CC which probably prevents KMT2E proteosomal-mediated degradation.
CC {ECO:0000250|UniProtKB:Q8IZD2}.
CC -!- DISRUPTION PHENOTYPE: Defects in immunity and hematopoiesis. Adult
CC homozygous mice are obtained at reduced frequency because of postnatal
CC lethality. Surviving animals display a variety of abnormalities,
CC including male infertility, retarded growth and defects in multiple
CC hematopoietic lineages. They also show increased susceptibility to
CC spontaneous eye infections associated with a cell-autonomous impairment
CC of neutrophil function. They exhibit a mild impairment of
CC erythropoiesis and hematopoietic stem cells (HSCs) have impaired
CC competitive repopulating capacity both under normal conditions and when
CC subjected to self-renewal stimulation by NUP98-HOXA10. Homozygous HSCs
CC show a dramatic sensitivity to DNA demethylation-induced
CC differentiation (5-azadeoxycytidine). {ECO:0000269|PubMed:18818388,
CC ECO:0000269|PubMed:18854576, ECO:0000269|PubMed:18952892}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. TRX/MLL
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- CAUTION: Does not exhibit histone methyltransferase towards histone H3
CC in vitro (PubMed:18952892). The isolated catalytic SET domain lacks
CC binding activity towards cofactor S-adenosyl-L-methionine; instead of
CC the highly conserved XGXG, Y and NH motifs, KMT2E displays NKKI (Asn-
CC 339-Ile-342), F (Phe-381) and RR (Arg-408-Arg-409) motifs. Also lacks
CC binding activity towards histone H3 due to a poor conservation of the
CC key residues involved in the binding and the presence of large loop
CC which prevents the docking of the H3 'Lys-4' side chain.
CC {ECO:0000250|UniProtKB:Q8IZD2, ECO:0000269|PubMed:18952892}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH36286.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 486.; Evidence={ECO:0000305};
CC Sequence=AAH64079.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 803.; Evidence={ECO:0000305};
CC Sequence=AAH89356.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 495.; Evidence={ECO:0000305};
CC Sequence=AAI03802.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 492.; Evidence={ECO:0000305};
CC Sequence=BAB25186.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC28936.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE28389.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC122022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK007682; BAB25186.1; ALT_INIT; mRNA.
DR EMBL; AK021284; BAE43262.1; -; mRNA.
DR EMBL; AK035078; BAC28936.2; ALT_INIT; mRNA.
DR EMBL; AK148169; BAE28389.1; ALT_FRAME; mRNA.
DR EMBL; AK160519; BAE35839.1; -; mRNA.
DR EMBL; BC036286; AAH36286.1; ALT_SEQ; mRNA.
DR EMBL; BC064079; AAH64079.1; ALT_SEQ; mRNA.
DR EMBL; BC089356; AAH89356.1; ALT_SEQ; mRNA.
DR EMBL; BC103801; AAI03802.1; ALT_SEQ; mRNA.
DR CCDS; CCDS51430.1; -. [Q3UG20-1]
DR RefSeq; NP_081260.1; NM_026984.1. [Q3UG20-1]
DR RefSeq; XP_006535868.1; XM_006535805.3. [Q3UG20-1]
DR AlphaFoldDB; Q3UG20; -.
DR BMRB; Q3UG20; -.
DR SMR; Q3UG20; -.
DR BioGRID; 213280; 3.
DR IntAct; Q3UG20; 1.
DR STRING; 10090.ENSMUSP00000092569; -.
DR GlyGen; Q3UG20; 2 sites.
DR iPTMnet; Q3UG20; -.
DR PhosphoSitePlus; Q3UG20; -.
DR EPD; Q3UG20; -.
DR jPOST; Q3UG20; -.
DR MaxQB; Q3UG20; -.
DR PaxDb; Q3UG20; -.
DR PeptideAtlas; Q3UG20; -.
DR PRIDE; Q3UG20; -.
DR ProteomicsDB; 264857; -. [Q3UG20-1]
DR ProteomicsDB; 264858; -. [Q3UG20-2]
DR Antibodypedia; 31243; 203 antibodies from 32 providers.
DR Ensembl; ENSMUST00000094962; ENSMUSP00000092569; ENSMUSG00000029004. [Q3UG20-1]
DR Ensembl; ENSMUST00000115128; ENSMUSP00000110781; ENSMUSG00000029004. [Q3UG20-1]
DR GeneID; 69188; -.
DR KEGG; mmu:69188; -.
DR UCSC; uc008wqa.2; mouse. [Q3UG20-1]
DR CTD; 55904; -.
DR MGI; MGI:1924825; Kmt2e.
DR VEuPathDB; HostDB:ENSMUSG00000029004; -.
DR eggNOG; KOG1844; Eukaryota.
DR GeneTree; ENSGT00940000157862; -.
DR HOGENOM; CLU_002373_2_1_1; -.
DR InParanoid; Q3UG20; -.
DR OMA; SGWIKSP; -.
DR OrthoDB; 86638at2759; -.
DR PhylomeDB; Q3UG20; -.
DR TreeFam; TF106417; -.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR BioGRID-ORCS; 69188; 7 hits in 77 CRISPR screens.
DR ChiTaRS; Kmt2e; mouse.
DR PRO; PR:Q3UG20; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3UG20; protein.
DR Bgee; ENSMUSG00000029004; Expressed in rostral migratory stream and 265 other tissues.
DR ExpressionAtlas; Q3UG20; baseline and differential.
DR Genevisible; Q3UG20; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000791; C:euchromatin; ISO:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; IBA:GO_Central.
DR GO; GO:0034967; C:Set3 complex; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006306; P:DNA methylation; IMP:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0042119; P:neutrophil activation; IMP:UniProtKB.
DR GO; GO:0002446; P:neutrophil mediated immunity; IMP:UniProtKB.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:1905437; P:positive regulation of histone H3-K4 trimethylation; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0035065; P:regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; ISS:UniProtKB.
DR CDD; cd19182; SET_KMT2E; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR037955; KMT2E.
DR InterPro; IPR044434; KMT2E_SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46462:SF2; PTHR46462:SF2; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Chromatin regulator; Chromosome;
KW Coiled coil; Cytoplasm; Cytoskeleton; Glycoprotein; Growth arrest;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1868
FT /note="Inactive histone-lysine N-methyltransferase 2E"
FT /id="PRO_0000341420"
FT DOMAIN 330..447
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 118..166
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 178..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1038..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1236..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1585..1842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 559..613
FT /evidence="ECO:0000255"
FT MOTIF 63..66
FT /note="HCFC1-binding motif (HBM)"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT COMPBIAS 226..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..667
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..906
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1256..1272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1295..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1338..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1385..1437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1457
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1482..1545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1546..1561
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1585..1606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1628..1645
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1700
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1702..1716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1717..1734
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1752..1766
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1771..1785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT BINDING 143
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT BINDING 160
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT MOD_RES 837
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT MOD_RES 1282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT MOD_RES 1364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT CARBOHYD 435
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT CARBOHYD 440
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZD2"
FT VAR_SEQ 1..580
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052813"
FT CONFLICT 62
FT /note="A -> S (in Ref. 2; BAE43262)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="R -> I (in Ref. 2; BAE28389)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="E -> G (in Ref. 2; BAE28389)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="R -> S (in Ref. 2; BAB25186)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="D -> Y (in Ref. 2; BAC28936)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="E -> G (in Ref. 2; BAE35839)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="E -> G (in Ref. 2; BAE28389)"
FT /evidence="ECO:0000305"
FT CONFLICT 1005
FT /note="S -> R (in Ref. 2; BAC28936)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1868 AA; 204543 MW; B676F509E965415C CRC64;
MSIAIPLGVD TTETSYLEMA AGSEPESVEA SPVVVEKSNS FPHQLYTSSS HHSHSYIGLP
YADHNYGARP PPTPPASPPP SGLISKNEVG IFTTPNFDET SSATTISTSE DGSYGTDVTR
CICGFTHDDG YMICCDKCSV WQHIDCMGID RQHIPDTYLC ERCQPRSLDK ERAVLLQRRK
RENMSDGDTS ATESGDEVPV ELYTAFQHTP TSITLTASRV PKVTDKRRKK SGEKEQNFSK
CKKAFREGSR KSSRVKGSAP EIDPSSDSSN FVWETKIKAW MDRYEEANNN QYSEGVQREA
QRLAQRLGSG NDSKDMNKSE LSTNNSLFRP PVESHIQKNK KILKSAKDLP PDALIIEYRG
KFMLREQFEA NGYFFKRPYP FVLFYSKFHG LEMCVDARTF GNEARFIRRS CTPNAEVRHE
IEEGTIHLYI YSIQSIPKGT EITIAFDFDY GNCKYKVDCA CLKENPECPV LKRSSESTEN
INSGYETRRK KGKKEKDTSK EKDIQNQNMT LDCEGTNNKI RSPETKQRKL SPLRLSVSNN
QEPDFIDDME EKTPISNEVE MESEEQIAER KRKMTREERK MEAILQAFAR LEKREKRREQ
ALERISTAKT EVKPECKESQ VIADAEVVQE QVKEETAIKP AAAKVNRTKQ RKSFSRSRTH
IGQQRRRHRT VSMCSDIPPS SPDIEVLSQQ NEIENTVLAI EPETETAVAE IIPEAEVPAL
NKCPTKYPKT KKHLVNEWLS EKNEKTGKPS DSLSERPLRI TTDPEVLATQ LNSLPGLTYS
PHVYSTPKHY IRFTSPFLSE KKRRKETTEN ISGSCKKRWL KQALEEENST ILHRYHSPCQ
ERSRSPTVNG ENKSPLLLSD SCSLPDLTTP LKKRRLYQLL DTAYSESSTP TPSPYATPTH
TDITPTDPAF ATPPRIKSDD ETYRNGYKPI YSPVTPVTPG TPGNTMHFEN ISSPESSPEI
KRCTYNQEGY DRPSNMLTLG PFRNSNLTEL GLQEIKTIGY TSPRSRTEVN RPCPGEKESV
SDLQLGLDAV EPAALQKSME TPAHDRTEPS NQLDSTHSGR GTMYSSWVKS PDRTGVNFSV
NSNLRDLTPS HQLETGGGFR VSESKCLIQQ DDTRGMFLGA AVFCTSEDGL ASGFGRTVND
NLIDGSCTPQ NPPQKKKVSL LEYRKRQREA RKSGSKPENF ALISVSPHPS GSLSSSGDGC
VHSSENGEQA ENQASLPLPP PAAAAAATAA AAYSASSEEG SSNCPVKDAN SSEKKDPEVQ
WTASTSVEQV RERSYQRALL LSDHRKDKDS GGESPCVSCS PSHVQSPPSS HSNHIPQVHA
QSLAPSLSEL MADPDAEGTE ATSTSECPSP DTSQSPSKTS KPGSPGPINP AQSHGKILTK
PDSHWEATAT VSEADNSVHQ NPEPQHRQLS SNTPALSQNH APQAHALSAN DQLPQKLPSA
PTKLHCPPSP HTENPPKSST PHTPVQHGYL SPKPPSQHLG SPFRPHHSQS PQVGTPQRET
QRNFYAAAQN LQANPQQATS GALFTQTPSG QSSATYSQFN QQSLNSTAPP PPPPPPPSSY
YQNQQPSANF QNYNQLKGSL SQQTVFTSGP NQALPGSTSQ QSVPGHHVTP GHFLPSQNPT
IHHQPAAAAV VPPPPPPPPA PGPHLIQQPS SHQQHSVAHG VGPVHAVTPG SHIHSQTAGH
HLPPPPPPPG PAPHHHPPPH PTTGLQSLQA QHQHVVNSAP PPPPPPPPPP PASVLVSGHH
SASGQALHHP PHQGPPLFPA SAHPAVPPYP SQATHHTTLG PGPQHQPSGT GPHCPLPVAG
PHLQPQGPNS IPTPTASGFC PHPHPGSVAL PHGVQGPQQA SPVPAQIPIH RAQVPPTFQN
NYHGSGWH
