GenomeNet

Database: UniProt
Entry: Q3UG20
LinkDB: Q3UG20
Original site: Q3UG20 
ID   KMT2E_MOUSE             Reviewed;        1868 AA.
AC   Q3UG20; Q3SYI5; Q3TUY2; Q3V410; Q5FWI1; Q6P3B3; Q8BS65; Q8CFX7;
AC   Q9CVK6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   16-JAN-2019, entry version 112.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-494 (ISOFORM 1).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH64079.1,
RC   ECO:0000312|EMBL:AAH89356.1}, 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
RT   project: 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
RT   synchronized 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
RT   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.,
RA   Doehner K., Doehner H., Weber O., Blum C., Rodewald H.-R.,
RA   Sassone-Corsi P., Peters A.H.F.M., Fehling H.J.;
RT   "Impaired function of primitive hematopoietic cells in mice lacking
RT   the 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
RT   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
RT   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
RP   BY 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
RT   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
CC       gene transcription (By similarity). Chromatin interaction is
CC       mediated via the binding to tri-methylated histone H3 at 'Lys-4'
CC       (H3K4me3) (By similarity). Key regulator of hematopoiesis involved
CC       in terminal myeloid differentiation and in the regulation of
CC       hematopoietic stem cell (HSCs) self-renewal by a mechanism that
CC       involves DNA methylation (PubMed:18854576, PubMed:18952892,
CC       PubMed:18818388). Also acts as an important cell cycle regulator,
CC       participating in cell cycle regulatory network machinery at
CC       multiple cell cycle stages including G1/S transition, S phase
CC       progression and mitotic entry (PubMed:19264965). Recruited to E2F1
CC       responsive promoters by HCFC1 where it stimulates tri-methylation
CC       of histone H3 at 'Lys-4' and transcriptional activation and
CC       thereby facilitates G1 to S phase transition (By similarity).
CC       During myoblast differentiation, required to suppress
CC       inappropriate expression of S-phase-promoting genes and maintain
CC       expression of determination genes in quiescent cells
CC       (PubMed:19264965). {ECO:0000250|UniProtKB:Q8IZD2,
CC       ECO:0000269|PubMed:18818388, ECO:0000269|PubMed:18854576,
CC       ECO:0000269|PubMed:18952892, ECO:0000269|PubMed:19264965}.
CC   -!- SUBUNIT: Component of a complex composed of KMT2E, OGT and USP7;
CC       the complex stabilizes KMT2E, preventing KMT2E ubiquitination and
CC       proteosomal-mediated degradation. Interacts (via N-terminus) with
CC       OGT (via TRP repeats). Interacts with deubiquitinating enzyme USP7
CC       (via MATH domain). Interacts (via HBM motif) with HCFC1 (via Kelch
CC       domain). Interacts with E2F1; the interaction is probably indirect
CC       and is 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
CC       during mitosis. Dissociation from mitotic chromosome is likely due
CC       to histone 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         Note=No experimental confirmation available. {ECO:0000305};
CC       Name=2 {ECO:0000269|PubMed:16141072};
CC         IsoId=Q3UG20-2; Sequence=VSP_052813;
CC         Note=No experimental confirmation available. {ECO:0000305};
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
CC       chromatin. {ECO:0000250|UniProtKB:Q8IZD2}.
CC   -!- DOMAIN: The SET domain does not bind the methyl group donor S-
CC       adenosyl-L-methionine and histone 3 H3K4 peptide as a large loop
CC       prevents the docking of the 'Lys-4' side chain.
CC       {ECO:0000250|UniProtKB:Q8IZD2}.
CC   -!- DOMAIN: The C-terminus domain is responsible for the localization
CC       to 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
CC       OGT which probably prevents KMT2E proteosomal-mediated
CC       degradation. {ECO:0000250|UniProtKB:Q8IZD2}.
CC   -!- DISRUPTION PHENOTYPE: Defects in immunity and hematopoiesis. Adult
CC       homozygous mice are obtained at reduced frequency because of
CC       postnatal lethality. Surviving animals display a variety of
CC       abnormalities, including male infertility, retarded growth and
CC       defects in multiple hematopoietic lineages. They also show
CC       increased susceptibility to spontaneous eye infections associated
CC       with a cell-autonomous impairment of neutrophil function. They
CC       exhibit a mild impairment of erythropoiesis and hematopoietic stem
CC       cells (HSCs) have impaired competitive repopulating capacity both
CC       under normal conditions and when subjected to self-renewal
CC       stimulation by NUP98-HOXA10. Homozygous HSCs show a dramatic
CC       sensitivity to DNA demethylation-induced differentiation (5-
CC       azadeoxycytidine). {ECO:0000269|PubMed:18818388,
CC       ECO:0000269|PubMed:18854576, ECO:0000269|PubMed:18952892}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. TRX/MLL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- CAUTION: Does not exhibit histone methyltransferase towards
CC       histone H3 in vitro (PubMed:18952892). The isolated catalytic SET
CC       domain lacks binding activity towards cofactor S-adenosyl-L-
CC       methionine; instead of the highly conserved XGXG, Y and NH motifs,
CC       KMT2E displays NKKI (Asn-339-Ile-342), F (Phe-381) and RR (Arg-
CC       408-Arg-409) motifs. Also lacks binding activity towards histone
CC       H3 due to a poor conservation of the key residues involved in the
CC       binding and the presence of large loop which prevents the docking
CC       of the H3 'Lys-4' side chain. {ECO:0000250|UniProtKB:Q8IZD2,
CC       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; Positions=12; Evidence={ECO:0000305};
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   UniGene; Mm.205190; -.
DR   ProteinModelPortal; Q3UG20; -.
DR   SMR; Q3UG20; -.
DR   BioGrid; 213280; 1.
DR   IntAct; Q3UG20; 1.
DR   STRING; 10090.ENSMUSP00000092569; -.
DR   iPTMnet; Q3UG20; -.
DR   PhosphoSitePlus; Q3UG20; -.
DR   MaxQB; Q3UG20; -.
DR   PaxDb; Q3UG20; -.
DR   PeptideAtlas; Q3UG20; -.
DR   PRIDE; Q3UG20; -.
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   eggNOG; KOG1844; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000157862; -.
DR   HOVERGEN; HBG105683; -.
DR   InParanoid; Q3UG20; -.
DR   KO; K09189; -.
DR   OMA; TIYSSWV; -.
DR   OrthoDB; 86638at2759; -.
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   ChiTaRS; Kmt2e; mouse.
DR   PRO; PR:Q3UG20; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000029004; Expressed in 305 organ(s), highest expression level in rostral migratory stream.
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:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0035327; C:transcriptionally active chromatin; ISO:MGI.
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:0007050; P:cell cycle arrest; 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:0048384; P:retinoic acid receptor signaling pathway; ISS:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR037955; KMT2E.
DR   InterPro; IPR001214; SET_dom.
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; PTHR44512:SF1; PTHR44512:SF1; 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   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; Complete proteome; Cytoplasm; Cytoskeleton; Glycoprotein;
KW   Growth arrest; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   1868       Inactive histone-lysine N-
FT                                methyltransferase 2E.
FT                                /FTId=PRO_0000341420.
FT   DOMAIN      330    447       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     118    166       PHD-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   COILED      559    613       {ECO:0000255}.
FT   MOTIF        63     66       HCFC1-binding motif (HBM).
FT                                {ECO:0000250|UniProtKB:Q8IZD2}.
FT   COMPBIAS   1549   1856       Pro-rich. {ECO:0000255}.
FT   METAL       121    121       Zinc 1. {ECO:0000250|UniProtKB:Q8IZD2}.
FT   METAL       123    123       Zinc 1. {ECO:0000250|UniProtKB:Q8IZD2}.
FT   METAL       135    135       Zinc 2. {ECO:0000250|UniProtKB:Q8IZD2}.
FT   METAL       138    138       Zinc 2. {ECO:0000250|UniProtKB:Q8IZD2}.
FT   METAL       143    143       Zinc 1; via pros nitrogen.
FT                                {ECO:0000250|UniProtKB:Q8IZD2}.
FT   METAL       146    146       Zinc 1. {ECO:0000250|UniProtKB:Q8IZD2}.
FT   METAL       160    160       Zinc 2. {ECO:0000250|UniProtKB:Q8IZD2}.
FT   METAL       163    163       Zinc 2. {ECO:0000250|UniProtKB:Q8IZD2}.
FT   MOD_RES     837    837       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8IZD2}.
FT   MOD_RES     845    845       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1070   1070       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8IZD2}.
FT   MOD_RES    1282   1282       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8IZD2}.
FT   MOD_RES    1364   1364       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8IZD2}.
FT   CARBOHYD    435    435       O-linked (GlcNAc) serine.
FT                                {ECO:0000250|UniProtKB:Q8IZD2}.
FT   CARBOHYD    440    440       O-linked (GlcNAc) threonine.
FT                                {ECO:0000250|UniProtKB:Q8IZD2}.
FT   VAR_SEQ       1    580       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_052813.
FT   CONFLICT     62     62       A -> S (in Ref. 2; BAE43262).
FT                                {ECO:0000305}.
FT   CONFLICT    181    181       R -> I (in Ref. 2; BAE28389).
FT                                {ECO:0000305}.
FT   CONFLICT    320    320       E -> G (in Ref. 2; BAE28389).
FT                                {ECO:0000305}.
FT   CONFLICT    489    489       R -> S (in Ref. 2; BAB25186).
FT                                {ECO:0000305}.
FT   CONFLICT    512    512       D -> Y (in Ref. 2; BAC28936).
FT                                {ECO:0000305}.
FT   CONFLICT    550    550       E -> G (in Ref. 2; BAE35839).
FT                                {ECO:0000305}.
FT   CONFLICT    562    562       E -> G (in Ref. 2; BAE28389).
FT                                {ECO:0000305}.
FT   CONFLICT   1005   1005       S -> R (in Ref. 2; BAC28936).
FT                                {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
//
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