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Entry version 113 (08 May 2019)
Sequence version 2 (10 Jun 2008)
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Protein

Inactive histone-lysine N-methyltransferase 2E

Gene

Kmt2e

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription (By similarity). Chromatin interaction is mediated via the binding to tri-methylated histone H3 at 'Lys-4' (H3K4me3) (By similarity). Key regulator of hematopoiesis involved in terminal myeloid differentiation and in the regulation of hematopoietic stem cell (HSCs) self-renewal by a mechanism that involves DNA methylation (PubMed:18854576, PubMed:18952892, PubMed:18818388). Also acts as an important cell cycle regulator, participating in cell cycle regulatory network machinery at multiple cell cycle stages including G1/S transition, S phase progression and mitotic entry (PubMed:19264965). Recruited to E2F1 responsive promoters by HCFC1 where it stimulates tri-methylation of histone H3 at 'Lys-4' and transcriptional activation and thereby facilitates G1 to S phase transition (By similarity). During myoblast differentiation, required to suppress inappropriate expression of S-phase-promoting genes and maintain expression of determination genes in quiescent cells (PubMed:19264965).By similarity4 Publications

Caution

Does not exhibit histone methyltransferase towards histone H3 in vitro (PubMed:18952892). The isolated catalytic SET domain lacks binding activity towards cofactor S-adenosyl-L-methionine; instead of the highly conserved XGXG, Y and NH motifs, KMT2E displays NKKI (Asn-339-Ile-342), F (Phe-381) and RR (Arg-408-Arg-409) motifs. Also lacks binding activity towards histone H3 due to a poor conservation of the key residues involved in the binding and the presence of large loop which prevents the docking of the H3 'Lys-4' side chain.By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi121Zinc 1By similarity1
Metal bindingi123Zinc 1By similarity1
Metal bindingi135Zinc 2By similarity1
Metal bindingi138Zinc 2By similarity1
Metal bindingi143Zinc 1; via pros nitrogenBy similarity1
Metal bindingi146Zinc 1By similarity1
Metal bindingi160Zinc 2By similarity1
Metal bindingi163Zinc 2By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri118 – 166PHD-typePROSITE-ProRule annotationAdd BLAST49

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionChromatin regulator
Biological processCell cycle, Growth arrest, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-3214841 PKMTs methylate histone lysines
R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Inactive histone-lysine N-methyltransferase 2ECurated
Short name:
Inactive lysine N-methyltransferase 2ECurated
Alternative name(s):
Myeloid/lymphoid or mixed-lineage leukemia protein 5 homolog
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Kmt2e
Synonyms:Mll5
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 5

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1924825 Kmt2e

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Defects in immunity and hematopoiesis. Adult homozygous mice are obtained at reduced frequency because of postnatal lethality. Surviving animals display a variety of abnormalities, including male infertility, retarded growth and defects in multiple hematopoietic lineages. They also show increased susceptibility to spontaneous eye infections associated with a cell-autonomous impairment of neutrophil function. They exhibit a mild impairment of erythropoiesis and hematopoietic stem cells (HSCs) have impaired competitive repopulating capacity both under normal conditions and when subjected to self-renewal stimulation by NUP98-HOXA10. Homozygous HSCs show a dramatic sensitivity to DNA demethylation-induced differentiation (5-azadeoxycytidine).3 Publications

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003414201 – 1868Inactive histone-lysine N-methyltransferase 2EAdd BLAST1868

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi435O-linked (GlcNAc) serineBy similarity1
Glycosylationi440O-linked (GlcNAc) threonineBy similarity1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei837PhosphoserineBy similarity1
Modified residuei845PhosphoserineCombined sources1
Modified residuei1070PhosphoserineBy similarity1
Modified residuei1282PhosphoserineBy similarity1
Modified residuei1364PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Ubiquitinated. Deubiquitinated by USP7.By similarity
O-glycosylated at Ser-435 and Thr-440 in the SET domain by OGT which probably prevents KMT2E proteosomal-mediated degradation.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q3UG20

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q3UG20

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q3UG20

PeptideAtlas

More...
PeptideAtlasi
Q3UG20

PRoteomics IDEntifications database

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PRIDEi
Q3UG20

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q3UG20

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q3UG20

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in reversibly arrested C2C12 myoblasts.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000029004 Expressed in 305 organ(s), highest expression level in rostral migratory stream

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q3UG20 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q3UG20 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of a complex composed of KMT2E, OGT and USP7; the complex stabilizes KMT2E, preventing KMT2E ubiquitination and proteosomal-mediated degradation.

Interacts (via N-terminus) with OGT (via TRP repeats).

Interacts with deubiquitinating enzyme USP7 (via MATH domain).

Interacts (via HBM motif) with HCFC1 (via Kelch domain).

Interacts with E2F1; the interaction is probably indirect and is mediated via HCFC1.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
213280, 1 interactor

Protein interaction database and analysis system

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IntActi
Q3UG20, 1 interactor

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000092569

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q3UG20

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini330 – 447SETPROSITE-ProRule annotationAdd BLAST118

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili559 – 613Sequence analysisAdd BLAST55

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi63 – 66HCFC1-binding motif (HBM)By similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1549 – 1856Pro-richSequence analysisAdd BLAST308

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The PHD-type domain binds specifically histone H3 tri-methylated at 'Lys-4' (H3K4me3), thus promoting binding to chromatin.By similarity
The SET domain does not bind the methyl group donor S-adenosyl-L-methionine and histone 3 H3K4 peptide as a large loop prevents the docking of the 'Lys-4' side chain.By similarity
The C-terminus domain is responsible for the localization to the centrosome during mitosis.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri118 – 166PHD-typePROSITE-ProRule annotationAdd BLAST49

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1844 Eukaryota
COG2940 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000157862

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q3UG20

KEGG Orthology (KO)

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KOi
K09189

Identification of Orthologs from Complete Genome Data

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OMAi
TIYSSWV

Database of Orthologous Groups

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OrthoDBi
86638at2759

TreeFam database of animal gene trees

More...
TreeFami
TF106417

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.40.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR037955 KMT2E
IPR001214 SET_dom
IPR019786 Zinc_finger_PHD-type_CS
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR013083 Znf_RING/FYVE/PHD

The PANTHER Classification System

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PANTHERi
PTHR46462:SF2 PTHR46462:SF2, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00628 PHD, 1 hit
PF00856 SET, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00249 PHD, 1 hit
SM00317 SET, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF57903 SSF57903, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50280 SET, 1 hit
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 12 Publications (identifier: Q3UG20-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSIAIPLGVD TTETSYLEMA AGSEPESVEA SPVVVEKSNS FPHQLYTSSS
60 70 80 90 100
HHSHSYIGLP YADHNYGARP PPTPPASPPP SGLISKNEVG IFTTPNFDET
110 120 130 140 150
SSATTISTSE DGSYGTDVTR CICGFTHDDG YMICCDKCSV WQHIDCMGID
160 170 180 190 200
RQHIPDTYLC ERCQPRSLDK ERAVLLQRRK RENMSDGDTS ATESGDEVPV
210 220 230 240 250
ELYTAFQHTP TSITLTASRV PKVTDKRRKK SGEKEQNFSK CKKAFREGSR
260 270 280 290 300
KSSRVKGSAP EIDPSSDSSN FVWETKIKAW MDRYEEANNN QYSEGVQREA
310 320 330 340 350
QRLAQRLGSG NDSKDMNKSE LSTNNSLFRP PVESHIQKNK KILKSAKDLP
360 370 380 390 400
PDALIIEYRG KFMLREQFEA NGYFFKRPYP FVLFYSKFHG LEMCVDARTF
410 420 430 440 450
GNEARFIRRS CTPNAEVRHE IEEGTIHLYI YSIQSIPKGT EITIAFDFDY
460 470 480 490 500
GNCKYKVDCA CLKENPECPV LKRSSESTEN INSGYETRRK KGKKEKDTSK
510 520 530 540 550
EKDIQNQNMT LDCEGTNNKI RSPETKQRKL SPLRLSVSNN QEPDFIDDME
560 570 580 590 600
EKTPISNEVE MESEEQIAER KRKMTREERK MEAILQAFAR LEKREKRREQ
610 620 630 640 650
ALERISTAKT EVKPECKESQ VIADAEVVQE QVKEETAIKP AAAKVNRTKQ
660 670 680 690 700
RKSFSRSRTH IGQQRRRHRT VSMCSDIPPS SPDIEVLSQQ NEIENTVLAI
710 720 730 740 750
EPETETAVAE IIPEAEVPAL NKCPTKYPKT KKHLVNEWLS EKNEKTGKPS
760 770 780 790 800
DSLSERPLRI TTDPEVLATQ LNSLPGLTYS PHVYSTPKHY IRFTSPFLSE
810 820 830 840 850
KKRRKETTEN ISGSCKKRWL KQALEEENST ILHRYHSPCQ ERSRSPTVNG
860 870 880 890 900
ENKSPLLLSD SCSLPDLTTP LKKRRLYQLL DTAYSESSTP TPSPYATPTH
910 920 930 940 950
TDITPTDPAF ATPPRIKSDD ETYRNGYKPI YSPVTPVTPG TPGNTMHFEN
960 970 980 990 1000
ISSPESSPEI KRCTYNQEGY DRPSNMLTLG PFRNSNLTEL GLQEIKTIGY
1010 1020 1030 1040 1050
TSPRSRTEVN RPCPGEKESV SDLQLGLDAV EPAALQKSME TPAHDRTEPS
1060 1070 1080 1090 1100
NQLDSTHSGR GTMYSSWVKS PDRTGVNFSV NSNLRDLTPS HQLETGGGFR
1110 1120 1130 1140 1150
VSESKCLIQQ DDTRGMFLGA AVFCTSEDGL ASGFGRTVND NLIDGSCTPQ
1160 1170 1180 1190 1200
NPPQKKKVSL LEYRKRQREA RKSGSKPENF ALISVSPHPS GSLSSSGDGC
1210 1220 1230 1240 1250
VHSSENGEQA ENQASLPLPP PAAAAAATAA AAYSASSEEG SSNCPVKDAN
1260 1270 1280 1290 1300
SSEKKDPEVQ WTASTSVEQV RERSYQRALL LSDHRKDKDS GGESPCVSCS
1310 1320 1330 1340 1350
PSHVQSPPSS HSNHIPQVHA QSLAPSLSEL MADPDAEGTE ATSTSECPSP
1360 1370 1380 1390 1400
DTSQSPSKTS KPGSPGPINP AQSHGKILTK PDSHWEATAT VSEADNSVHQ
1410 1420 1430 1440 1450
NPEPQHRQLS SNTPALSQNH APQAHALSAN DQLPQKLPSA PTKLHCPPSP
1460 1470 1480 1490 1500
HTENPPKSST PHTPVQHGYL SPKPPSQHLG SPFRPHHSQS PQVGTPQRET
1510 1520 1530 1540 1550
QRNFYAAAQN LQANPQQATS GALFTQTPSG QSSATYSQFN QQSLNSTAPP
1560 1570 1580 1590 1600
PPPPPPPSSY YQNQQPSANF QNYNQLKGSL SQQTVFTSGP NQALPGSTSQ
1610 1620 1630 1640 1650
QSVPGHHVTP GHFLPSQNPT IHHQPAAAAV VPPPPPPPPA PGPHLIQQPS
1660 1670 1680 1690 1700
SHQQHSVAHG VGPVHAVTPG SHIHSQTAGH HLPPPPPPPG PAPHHHPPPH
1710 1720 1730 1740 1750
PTTGLQSLQA QHQHVVNSAP PPPPPPPPPP PASVLVSGHH SASGQALHHP
1760 1770 1780 1790 1800
PHQGPPLFPA SAHPAVPPYP SQATHHTTLG PGPQHQPSGT GPHCPLPVAG
1810 1820 1830 1840 1850
PHLQPQGPNS IPTPTASGFC PHPHPGSVAL PHGVQGPQQA SPVPAQIPIH
1860
RAQVPPTFQN NYHGSGWH
Note: No experimental confirmation available.Curated
Length:1,868
Mass (Da):204,543
Last modified:June 10, 2008 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB676F509E965415C
GO
Isoform 21 Publication (identifier: Q3UG20-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-580: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:1,288
Mass (Da):138,681
Checksum:i2166B0C437DBCC75
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2JDZ2A0A0G2JDZ2_MOUSE
Inactive histone-lysine N-methyltra...
Kmt2e mCG_114469
377Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WSN9A0A087WSN9_MOUSE
Inactive histone-lysine N-methyltra...
Kmt2e
245Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0G2JH19A0A0G2JH19_MOUSE
Inactive histone-lysine N-methyltra...
Kmt2e
244Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0G2JDX7A0A0G2JDX7_MOUSE
Inactive histone-lysine N-methyltra...
Kmt2e
183Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0A6YW47A0A0A6YW47_MOUSE
Inactive histone-lysine N-methyltra...
Kmt2e
21Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH36286 differs from that shown. Contaminating sequence. Potential poly-A sequence starting in position 486.Curated
The sequence AAH64079 differs from that shown. Contaminating sequence. Potential poly-A sequence starting in position 803.Curated
The sequence AAH89356 differs from that shown. Contaminating sequence. Potential poly-A sequence starting in position 495.Curated
The sequence AAI03802 differs from that shown. Contaminating sequence. Potential poly-A sequence starting in position 492.Curated
The sequence BAB25186 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAC28936 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAE28389 differs from that shown. Reason: Frameshift at position 12.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti62A → S in BAE43262 (PubMed:16141072).Curated1
Sequence conflicti181R → I in BAE28389 (PubMed:16141072).Curated1
Sequence conflicti320E → G in BAE28389 (PubMed:16141072).Curated1
Sequence conflicti489R → S in BAB25186 (PubMed:16141072).Curated1
Sequence conflicti512D → Y in BAC28936 (PubMed:16141072).Curated1
Sequence conflicti550E → G in BAE35839 (PubMed:16141072).Curated1
Sequence conflicti562E → G in BAE28389 (PubMed:16141072).Curated1
Sequence conflicti1005S → R in BAC28936 (PubMed:16141072).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0528131 – 580Missing in isoform 2. 2 PublicationsAdd BLAST580

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AC122022 Genomic DNA No translation available.
AK007682 mRNA Translation: BAB25186.1 Different initiation.
AK021284 mRNA Translation: BAE43262.1
AK035078 mRNA Translation: BAC28936.2 Different initiation.
AK148169 mRNA Translation: BAE28389.1 Frameshift.
AK160519 mRNA Translation: BAE35839.1
BC036286 mRNA Translation: AAH36286.1 Sequence problems.
BC064079 mRNA Translation: AAH64079.1 Sequence problems.
BC089356 mRNA Translation: AAH89356.1 Sequence problems.
BC103801 mRNA Translation: AAI03802.1 Sequence problems.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS51430.1 [Q3UG20-1]

NCBI Reference Sequences

More...
RefSeqi
NP_081260.1, NM_026984.1 [Q3UG20-1]
XP_006535868.1, XM_006535805.3 [Q3UG20-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000094962; ENSMUSP00000092569; ENSMUSG00000029004 [Q3UG20-1]
ENSMUST00000115128; ENSMUSP00000110781; ENSMUSG00000029004 [Q3UG20-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
69188

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:69188

UCSC genome browser

More...
UCSCi
uc008wqa.2 mouse [Q3UG20-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC122022 Genomic DNA No translation available.
AK007682 mRNA Translation: BAB25186.1 Different initiation.
AK021284 mRNA Translation: BAE43262.1
AK035078 mRNA Translation: BAC28936.2 Different initiation.
AK148169 mRNA Translation: BAE28389.1 Frameshift.
AK160519 mRNA Translation: BAE35839.1
BC036286 mRNA Translation: AAH36286.1 Sequence problems.
BC064079 mRNA Translation: AAH64079.1 Sequence problems.
BC089356 mRNA Translation: AAH89356.1 Sequence problems.
BC103801 mRNA Translation: AAI03802.1 Sequence problems.
CCDSiCCDS51430.1 [Q3UG20-1]
RefSeqiNP_081260.1, NM_026984.1 [Q3UG20-1]
XP_006535868.1, XM_006535805.3 [Q3UG20-1]

3D structure databases

SMRiQ3UG20
ModBaseiSearch...

Protein-protein interaction databases

BioGridi213280, 1 interactor
IntActiQ3UG20, 1 interactor
STRINGi10090.ENSMUSP00000092569

PTM databases

iPTMnetiQ3UG20
PhosphoSitePlusiQ3UG20

Proteomic databases

EPDiQ3UG20
MaxQBiQ3UG20
PaxDbiQ3UG20
PeptideAtlasiQ3UG20
PRIDEiQ3UG20

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000094962; ENSMUSP00000092569; ENSMUSG00000029004 [Q3UG20-1]
ENSMUST00000115128; ENSMUSP00000110781; ENSMUSG00000029004 [Q3UG20-1]
GeneIDi69188
KEGGimmu:69188
UCSCiuc008wqa.2 mouse [Q3UG20-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
55904
MGIiMGI:1924825 Kmt2e

Phylogenomic databases

eggNOGiKOG1844 Eukaryota
COG2940 LUCA
GeneTreeiENSGT00940000157862
InParanoidiQ3UG20
KOiK09189
OMAiTIYSSWV
OrthoDBi86638at2759
TreeFamiTF106417

Enzyme and pathway databases

ReactomeiR-MMU-3214841 PKMTs methylate histone lysines
R-MMU-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Kmt2e mouse

Protein Ontology

More...
PROi
PR:Q3UG20

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000029004 Expressed in 305 organ(s), highest expression level in rostral migratory stream
ExpressionAtlasiQ3UG20 baseline and differential
GenevisibleiQ3UG20 MM

Family and domain databases

Gene3Di3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR037955 KMT2E
IPR001214 SET_dom
IPR019786 Zinc_finger_PHD-type_CS
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR019787 Znf_PHD-finger
IPR013083 Znf_RING/FYVE/PHD
PANTHERiPTHR46462:SF2 PTHR46462:SF2, 1 hit
PfamiView protein in Pfam
PF00628 PHD, 1 hit
PF00856 SET, 1 hit
SMARTiView protein in SMART
SM00249 PHD, 1 hit
SM00317 SET, 1 hit
SUPFAMiSSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS50280 SET, 1 hit
PS01359 ZF_PHD_1, 1 hit
PS50016 ZF_PHD_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKMT2E_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q3UG20
Secondary accession number(s): Q3SYI5
, Q3TUY2, Q3V410, Q5FWI1, Q6P3B3, Q8BS65, Q8CFX7, Q9CVK6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: June 10, 2008
Last modified: May 8, 2019
This is version 113 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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