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Q8IZD2

- KMT2E_HUMAN

UniProt

Q8IZD2 - KMT2E_HUMAN

Protein

Histone-lysine N-methyltransferase 2E

Gene

KMT2E

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Mar 2003)
      Previous versions | rss
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    Functioni

    Histone methyltransferase that specifically mono- and dimethylates 'Lys-4' of histone H3 (H3K4me1 and H3K4me2). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. 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. Plays an essential role in retinoic-acid-induced granulopoiesis by acting as a coactivator of RAR-alpha (RARA) in target gene promoters. Also acts as an important cell cycle regulator, participating in cell cycle regulatory network machinery at multiple cell cycle stages. Required to suppress inappropriate expression of S-phase-promoting genes and maintain expression of determination genes in quiescent cells. Overexpression inhibits cell cycle progression, while knockdown induces cell cycle arrest at both the G1 and G2/M phases.
    Isoform NKp44L: Cellular ligand for NCR2/NKp44, may play a role as a danger signal in cytotoxicity and NK-cell-mediated innate immunity.

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri118 – 16649PHD-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. histone methyltransferase activity (H3-K4 specific) Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. transcription coactivator activity Source: UniProtKB
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell cycle arrest Source: UniProtKB-KW
    2. cellular response to retinoic acid Source: BHF-UCL
    3. DNA methylation Source: UniProtKB
    4. erythrocyte differentiation Source: UniProtKB
    5. histone H3-K4 methylation Source: BHF-UCL
    6. neutrophil activation Source: UniProtKB
    7. neutrophil mediated immunity Source: UniProtKB
    8. positive regulation of granulocyte differentiation Source: BHF-UCL
    9. positive regulation of transcription, DNA-templated Source: UniProtKB
    10. retinoic acid receptor signaling pathway Source: UniProtKB
    11. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Transferase

    Keywords - Biological processi

    Cell cycle, Growth arrest, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, S-adenosyl-L-methionine, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase 2E (EC:2.1.1.43)
    Short name:
    Lysine N-methyltransferase 2E
    Alternative name(s):
    Myeloid/lymphoid or mixed-lineage leukemia protein 5
    Gene namesi
    Name:KMT2E
    Synonyms:MLL5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:18541. KMT2E.

    Subcellular locationi

    Nucleus speckle 1 Publication
    Note: Absent from the nucleolus.1 Publication
    Isoform NKp44L : Cytoplasm 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. MLL5-L complex Source: UniProtKB
    3. nuclear speck Source: UniProtKB-SubCell
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi334 – 3341S → A: Does not affect O-glycosylation by OGT. 1 Publication
    Mutagenesisi345 – 3451S → A: Does not affect O-glycosylation by OGT. 1 Publication
    Mutagenesisi358 – 3581Y → A: Loss of methyltransferase activity. 1 Publication
    Mutagenesisi386 – 3861S → A: Does not affect O-glycosylation by OGT. 1 Publication
    Mutagenesisi399 – 3991T → A: Does not affect O-glycosylation by OGT. 1 Publication
    Mutagenesisi410 – 4101S → A: Does not affect O-glycosylation by OGT. 1 Publication
    Mutagenesisi412 – 4121T → A: Does not affect O-glycosylation by OGT. 1 Publication
    Mutagenesisi425 – 4251T → A: Does not affect O-glycosylation by OGT. 1 Publication
    Mutagenesisi432 – 4321S → A: Does not affect O-glycosylation by OGT. 1 Publication
    Mutagenesisi435 – 4351S → A: Does not affect O-glycosylation by OGT. 1 Publication
    Mutagenesisi440 – 4401T → A: Abolishes O-glycosylation by OGT and prevents coactivator activity toward RARA in granulopoiesis. 1 Publication
    Mutagenesisi441 – 4411E → A: Loss of methyltransferase activity. 1 Publication
    Mutagenesisi443 – 4431T → A: Does not affect O-glycosylation by OGT. 1 Publication

    Organism-specific databases

    PharmGKBiPA38568.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18581858Histone-lysine N-methyltransferase 2EPRO_0000341419Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi440 – 4401O-linked (GlcNAc)1 Publication

    Post-translational modificationi

    O-glycosylation at Thr-440 in the SET domain by OGT is essential for the histone methyltransferase and the coactivator activity toward RARA in granulopoiesis. The absence of Thr-440 glycosylation in assays done in vitro may explain why some authors did not detected any histone methyltransferase activity for this protein.1 Publication

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ8IZD2.
    PaxDbiQ8IZD2.
    PRIDEiQ8IZD2.

    PTM databases

    PhosphoSiteiQ8IZD2.

    Expressioni

    Tissue specificityi

    Widely expressed in both adult and fetal tissues. Highest levels of expression observed in fetal thymus and kidney and in adult hematopoietic tissues, jejunum and cerebellum. Isoform NKp44L is not detected on circulating cells from healthy individuals, but it is expressed on a large panel of the tumor and transformed cells.2 Publications

    Gene expression databases

    ArrayExpressiQ8IZD2.
    BgeeiQ8IZD2.
    GenevestigatoriQ8IZD2.

    Organism-specific databases

    HPAiHPA056125.

    Interactioni

    Subunit structurei

    Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with RARA.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TP53P046374EBI-2689959,EBI-366083

    Protein-protein interaction databases

    BioGridi120990. 12 interactions.
    IntActiQ8IZD2. 9 interactions.

    Structurei

    Secondary structure

    1
    1858
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi132 – 1343
    Turni136 – 1383
    Beta strandi141 – 1433
    Helixi144 – 1474
    Beta strandi156 – 1583
    Turni161 – 1655
    Helixi170 – 1789

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LV9NMR-A109-188[»]
    4L58X-ray1.48A117-181[»]
    ProteinModelPortaliQ8IZD2.
    SMRiQ8IZD2. Positions 109-188, 353-461.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini330 – 447118SETPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili559 – 61557Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1433 – 1846414Pro-richSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri118 – 16649PHD-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2940.
    HOVERGENiHBG105683.
    InParanoidiQ8IZD2.
    KOiK09189.
    OMAiETECANH.
    OrthoDBiEOG76472V.
    PhylomeDBiQ8IZD2.
    TreeFamiTF106417.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR001214. SET_dom.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00628. PHD. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view]
    SMARTiSM00249. PHD. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 1 hit.
    PROSITEiPS50280. SET. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view]

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform 12 Publications (identifier: Q8IZD2-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' 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

    MSIVIPLGVD TAETSYLEMA AGSEPESVEA SPVVVEKSNS YPHQLYTSSS     50
    HHSHSYIGLP YADHNYGARP PPTPPASPPP SVLISKNEVG IFTTPNFDET 100
    SSATTISTSE DGSYGTDVTR CICGFTHDDG YMICCDKCSV WQHIDCMGID 150
    RQHIPDTYLC ERCQPRNLDK ERAVLLQRRK RENMSDGDTS ATESGDEVPV 200
    ELYTAFQHTP TSITLTASRV SKVNDKRRKK SGEKEQHISK CKKAFREGSR 250
    KSSRVKGSAP EIDPSSDGSN FGWETKIKAW MDRYEEANNN QYSEGVQREA 300
    QRIALRLGNG NDKKEMNKSD LNTNNLLFKP PVESHIQKNK KILKSAKDLP 350
    PDALIIEYRG KFMLREQFEA NGYFFKRPYP FVLFYSKFHG LEMCVDARTF 400
    GNEARFIRRS CTPNAEVRHE IQDGTIHLYI YSIHSIPKGT EITIAFDFDY 450
    GNCKYKVDCA CLKENPECPV LKRSSESMEN INSGYETRRK KGKKDKDISK 500
    EKDTQNQNIT LDCEGTTNKM KSPETKQRKL SPLRLSVSNN QEPDFIDDIE 550
    EKTPISNEVE MESEEQIAER KRKMTREERK MEAILQAFAR LEKREKRREQ 600
    ALERISTAKT EVKTECKDTQ IVSDAEVIQE QAKEENASKP TPAKVNRTKQ 650
    RKSFSRSRTH IGQQRRRHRT VSMCSDIQPS SPDIEVTSQQ NDIENTVLTI 700
    EPETETALAE IITETEVPAL NKCPTKYPKT KKHLVNEWLS EKNEKTGKPS 750
    DGLSERPLRI TTDPEVLATQ LNSLPGLTYS PHVYSTPKHY IRFTSPFLSE 800
    KRRRKEPTEN ISGSCKKRWL KQALEEENSA ILHRFNSPCQ ERSRSPAVNG 850
    ENKSPLLLND SCSLPDLTTP LKKRRFYQLL DSVYSETSTP TPSPYATPTH 900
    TDITPMDPSF ATPPRIKSDD ETCRNGYKPI YSPVTPVTPG TPGNTMHFEN 950
    ISSPESSPEI KRRTYSQEGY DRSSTMLTLG PFRNSNLTEL GLQEIKTIGY 1000
    TSPRSRTEVN RQCPGEKEPV SDLQLGLDAV EPTALHKTLE TPAHDRAEPN 1050
    SQLDSTHSGR GTMYSSWVKS PDRTGVNFSV NSNLRDLTPS HQLEVGGGFR 1100
    ISESKCLMQD DTRGMFMETT VFCTSEDGLV SGFGRTVNDN LIDGNCTPQN 1150
    PPQKKKVSLL EYRKRQREAR KSGSKTENFP LISVSPHASG SLSNNGDGCA 1200
    SSNDNGEQVD HTASLPLPTP ATVYNATSEE TSNNCPVKDA TASEKNEPEV 1250
    QWTASTSVEQ VRERSYQRAL LLSDHRKDKD SGGESPCVSC SPSHVQSSPS 1300
    SHSNHIPQLQ AKGPVPSFSE LMEDPDPENP EPTTTNECPS PDTSQNTCKS 1350
    PPKMSKPGSP GSVIPAQAHG KIFTKPDPQW DSTVSASEAE NGVHLKTELQ 1400
    QKQLSNNNQA LSKNHPPQTH VRNSSEQLSQ KLPSVPTKLH CPPSPHLENP 1450
    PKSSTPHTPV QHGYLSPKPP SQQLGSPYRP HHSQSPQVGT PQREPQRNFY 1500
    PAAQNLPANT QQATSGTLFT QTPSGQSSAT YSQFNQQSLN STAPPPPPPP 1550
    PPSSSYYQNQ QPSANFQNYN QLKGSLSQQT VFTSGPNQAL PGTTSQQTVP 1600
    GHHVTPGHFL PSQNPTIHHQ TAAAVVPPPP PPPPAPGPHL VQQPNSHQQH 1650
    SVAHVVGPVH AVTPGSHIHS QTAGHHLPPP PPPPGPAPHH HPPPHPSTGL 1700
    QGLQAQHQHV VNSAPPPPPP PPPSSVLASG HHTTSAQALH HPPHQGPPLF 1750
    PSSAHPTVPP YPSQATHHTT LGPGPQHQPS GTGPHCPLPV TGPHLQPQGP 1800
    NSIPTPTASG FCPHPGSVAL PHGVQGPQQA SPVPGQIPIH RAQVPPTFQN 1850
    NYHGSGWH 1858
    Length:1,858
    Mass (Da):204,965
    Last modified:March 1, 2003 - v1
    Checksum:i8ACCB3CDB5BFCEFA
    GO
    Isoform 21 Publication (identifier: Q8IZD2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         494-573: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:1,778
    Mass (Da):195,675
    Checksum:iAEA0E38D5D008BE7
    GO
    Isoform 31 Publication (identifier: Q8IZD2-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         575-609: TREERKMEAILQAFARLEKREKRREQALERISTAK → VSWEASSLGLVTAALHMVIVAAFTWAFTLFFEVSE
         610-1858: Missing.

    Show »
    Length:609
    Mass (Da):68,926
    Checksum:iCAC22E252873885E
    GO
    Isoform 41 Publication (identifier: Q8IZD2-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         850-865: GENKSPLLLNDSCSLP → EYFFPRKFSRNKETHL
         866-1858: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:865
    Mass (Da):98,795
    Checksum:i7E1470684F22660D
    GO
    Isoform 51 Publication (identifier: Q8IZD2-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1508-1653: ANTQQATSGT...PNSHQQHSVA → VFWLLGIIPH...DSKNIFLNVL
         1654-1858: Missing.

    Show »
    Length:1,653
    Mass (Da):185,802
    Checksum:i6AF69A147E64F516
    GO
    Isoform 61 Publication (identifier: Q8IZD2-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1443-1621: PSPHLENPPK...SQNPTIHHQT → SSPSTTPSIH...ALKWTPKTFF
         1622-1858: Missing.

    Show »
    Length:1,621
    Mass (Da):180,779
    Checksum:i97E5EB49B9961FEA
    GO
    Isoform 71 Publication (identifier: Q8IZD2-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1282-1323: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:1,816
    Mass (Da):200,635
    Checksum:i16311FD3AC2DC1EF
    GO
    Isoform NKp44L (identifier: Q8IZD2-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1157-1168: VSLLEYRKRQRE → SPVGNFVGSNVV
         1169-1858: Missing.

    Show »
    Length:1,168
    Mass (Da):131,737
    Checksum:iB5D59D07B6ED13FA
    GO

    Sequence cautioni

    The sequence AAH01296.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 492.
    The sequence AAH40004.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 227.
    The sequence AAH53906.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 227.
    The sequence AAI42988.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 492.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti496 – 4961K → E in AAM74947. (PubMed:12101424)Curated
    Sequence conflicti496 – 4961K → E in AGE34449. (PubMed:23958951)Curated
    Sequence conflicti496 – 4961K → E in AK000940. (PubMed:14702039)Curated
    Sequence conflicti516 – 5161T → A in AAM74947. (PubMed:12101424)Curated
    Sequence conflicti516 – 5161T → A in AGE34449. (PubMed:23958951)Curated
    Sequence conflicti516 – 5161T → A in AK000940. (PubMed:14702039)Curated
    Sequence conflicti594 – 5941R → K in AK000940. (PubMed:14702039)Curated
    Sequence conflicti1020 – 10201V → A in AAM74947. (PubMed:12101424)Curated
    Sequence conflicti1073 – 10731R → S in AAM74947. (PubMed:12101424)Curated
    Sequence conflicti1090 – 10901S → P in AAM74947. (PubMed:12101424)Curated
    Sequence conflicti1099 – 10991F → S in AAM74947. (PubMed:12101424)Curated
    Sequence conflicti1168 – 11681E → K in AAM74947. (PubMed:12101424)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1424 – 14241S → P.
    Corresponds to variant rs35605511 [ dbSNP | Ensembl ].
    VAR_052656

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei494 – 57380Missing in isoform 2. 1 PublicationVSP_052803Add
    BLAST
    Alternative sequencei575 – 60935TREER…ISTAK → VSWEASSLGLVTAALHMVIV AAFTWAFTLFFEVSE in isoform 3. 1 PublicationVSP_052804Add
    BLAST
    Alternative sequencei610 – 18581249Missing in isoform 3. 1 PublicationVSP_052805Add
    BLAST
    Alternative sequencei850 – 86516GENKS…SCSLP → EYFFPRKFSRNKETHL in isoform 4. 1 PublicationVSP_052806Add
    BLAST
    Alternative sequencei866 – 1858993Missing in isoform 4. 1 PublicationVSP_052807Add
    BLAST
    Alternative sequencei1157 – 116812VSLLE…KRQRE → SPVGNFVGSNVV in isoform NKp44L. 1 PublicationVSP_053834Add
    BLAST
    Alternative sequencei1169 – 1858690Missing in isoform NKp44L. 1 PublicationVSP_053835Add
    BLAST
    Alternative sequencei1282 – 132342Missing in isoform 7. 1 PublicationVSP_052808Add
    BLAST
    Alternative sequencei1443 – 1621179PSPHL…IHHQT → SSPSTTPSIHRTPRSTSTTP ACCKFSTPTTPSAATFQCFG FWASYHISSSLTPPTSSRTS TFSFECSSNCTTVSLTSYTS YHFGTGTPAPAFWNRATLSI TCHRSSSPAPRTKQYSNTYC FRVLSSSWLCGPATWGSRTS AGISSAWTDSNSQSTGATNI SKQLPWVRVALKWTPKTFF in isoform 6. 1 PublicationVSP_052809Add
    BLAST
    Alternative sequencei1508 – 1653146ANTQQ…QHSVA → VFWLLGIIPHQLKPYTTHLI KDLHFFLRVLIQLYHRIPHK LHIIPLWDRDPSTSLLEQGH IVHYLSQVLISSPKDQTVFQ HLLLQGSVLILALWPCHMGF KDLSRHLQCLDRFQFTEHRC HQHFKTITMGQGGIKMDSKN IFLNVL in isoform 5. 1 PublicationVSP_052810Add
    BLAST
    Alternative sequencei1622 – 1858237Missing in isoform 6. 1 PublicationVSP_052811Add
    BLAST
    Alternative sequencei1654 – 1858205Missing in isoform 5. 1 PublicationVSP_052812Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF519459 mRNA. Translation: AAM74947.1.
    JQ809698 mRNA. Translation: AGE34449.1.
    AY147037 mRNA. Translation: AAN17675.1.
    AY157990 mRNA. Translation: AAN76325.1.
    AY195568 mRNA. Translation: AAO47009.1.
    AY195569 mRNA. Translation: AAO47010.1.
    AY222296 mRNA. Translation: AAO64395.1.
    AY234382 mRNA. Translation: AAO89072.1.
    AY438698 mRNA. Translation: AAR13893.1.
    AC005065 Genomic DNA. No translation available.
    AC005070 Genomic DNA. No translation available.
    AC007384 Genomic DNA. No translation available.
    CH471070 Genomic DNA. Translation: EAW83356.1.
    BC001296 mRNA. Translation: AAH01296.1. Sequence problems.
    BC040004 mRNA. Translation: AAH40004.1. Sequence problems.
    BC053906 mRNA. Translation: AAH53906.1. Sequence problems.
    BC062583 mRNA. Translation: AAH62583.1.
    BC142987 mRNA. Translation: AAI42988.1. Sequence problems.
    AK000940 mRNA. No translation available.
    CCDSiCCDS34723.1. [Q8IZD2-1]
    RefSeqiNP_061152.3. NM_018682.3. [Q8IZD2-1]
    NP_891847.1. NM_182931.2. [Q8IZD2-1]
    XP_005250550.1. XM_005250493.1. [Q8IZD2-1]
    XP_006716112.1. XM_006716049.1. [Q8IZD2-7]
    UniGeneiHs.592262.

    Genome annotation databases

    EnsembliENST00000257745; ENSP00000257745; ENSG00000005483. [Q8IZD2-1]
    ENST00000311117; ENSP00000312379; ENSG00000005483. [Q8IZD2-1]
    ENST00000334877; ENSP00000335599; ENSG00000005483. [Q8IZD2-7]
    ENST00000334884; ENSP00000335398; ENSG00000005483. [Q8IZD2-4]
    ENST00000476671; ENSP00000417888; ENSG00000005483. [Q8IZD2-3]
    GeneIDi55904.
    KEGGihsa:55904.
    UCSCiuc003vcl.3. human. [Q8IZD2-3]
    uc003vcm.3. human. [Q8IZD2-1]

    Polymorphism databases

    DMDMi74723669.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF519459 mRNA. Translation: AAM74947.1 .
    JQ809698 mRNA. Translation: AGE34449.1 .
    AY147037 mRNA. Translation: AAN17675.1 .
    AY157990 mRNA. Translation: AAN76325.1 .
    AY195568 mRNA. Translation: AAO47009.1 .
    AY195569 mRNA. Translation: AAO47010.1 .
    AY222296 mRNA. Translation: AAO64395.1 .
    AY234382 mRNA. Translation: AAO89072.1 .
    AY438698 mRNA. Translation: AAR13893.1 .
    AC005065 Genomic DNA. No translation available.
    AC005070 Genomic DNA. No translation available.
    AC007384 Genomic DNA. No translation available.
    CH471070 Genomic DNA. Translation: EAW83356.1 .
    BC001296 mRNA. Translation: AAH01296.1 . Sequence problems.
    BC040004 mRNA. Translation: AAH40004.1 . Sequence problems.
    BC053906 mRNA. Translation: AAH53906.1 . Sequence problems.
    BC062583 mRNA. Translation: AAH62583.1 .
    BC142987 mRNA. Translation: AAI42988.1 . Sequence problems.
    AK000940 mRNA. No translation available.
    CCDSi CCDS34723.1. [Q8IZD2-1 ]
    RefSeqi NP_061152.3. NM_018682.3. [Q8IZD2-1 ]
    NP_891847.1. NM_182931.2. [Q8IZD2-1 ]
    XP_005250550.1. XM_005250493.1. [Q8IZD2-1 ]
    XP_006716112.1. XM_006716049.1. [Q8IZD2-7 ]
    UniGenei Hs.592262.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LV9 NMR - A 109-188 [» ]
    4L58 X-ray 1.48 A 117-181 [» ]
    ProteinModelPortali Q8IZD2.
    SMRi Q8IZD2. Positions 109-188, 353-461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120990. 12 interactions.
    IntActi Q8IZD2. 9 interactions.

    PTM databases

    PhosphoSitei Q8IZD2.

    Polymorphism databases

    DMDMi 74723669.

    Proteomic databases

    MaxQBi Q8IZD2.
    PaxDbi Q8IZD2.
    PRIDEi Q8IZD2.

    Protocols and materials databases

    DNASUi 55904.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257745 ; ENSP00000257745 ; ENSG00000005483 . [Q8IZD2-1 ]
    ENST00000311117 ; ENSP00000312379 ; ENSG00000005483 . [Q8IZD2-1 ]
    ENST00000334877 ; ENSP00000335599 ; ENSG00000005483 . [Q8IZD2-7 ]
    ENST00000334884 ; ENSP00000335398 ; ENSG00000005483 . [Q8IZD2-4 ]
    ENST00000476671 ; ENSP00000417888 ; ENSG00000005483 . [Q8IZD2-3 ]
    GeneIDi 55904.
    KEGGi hsa:55904.
    UCSCi uc003vcl.3. human. [Q8IZD2-3 ]
    uc003vcm.3. human. [Q8IZD2-1 ]

    Organism-specific databases

    CTDi 55904.
    GeneCardsi GC07P104655.
    HGNCi HGNC:18541. KMT2E.
    HPAi HPA056125.
    MIMi 608444. gene.
    neXtProti NX_Q8IZD2.
    PharmGKBi PA38568.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOVERGENi HBG105683.
    InParanoidi Q8IZD2.
    KOi K09189.
    OMAi ETECANH.
    OrthoDBi EOG76472V.
    PhylomeDBi Q8IZD2.
    TreeFami TF106417.

    Miscellaneous databases

    ChiTaRSi MLL5. human.
    GenomeRNAii 55904.
    NextBioi 61277.
    PROi Q8IZD2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IZD2.
    Bgeei Q8IZD2.
    Genevestigatori Q8IZD2.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi 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.
    [Graphical view ]
    Pfami PF00628. PHD. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view ]
    SMARTi SM00249. PHD. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 1 hit.
    PROSITEi PS50280. SET. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "MLL5, a homolog of Drosophila trithorax located within a segment of chromosome band 7q22 implicated in myeloid leukemia."
      Emerling B.M., Bonifas J., Kratz C.P., Donovan S., Taylor B.R., Green E.D., Le Beau M.M., Shannon K.M.
      Oncogene 21:4849-4854(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    2. "Identification of a cellular ligand for the natural cytotoxicity receptor NKp44."
      Baychelier F., Sennepin A., Ermonval M., Dorgham K., Debre P., Vieillard V.
      Blood 122:2935-2942(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NKP44L), FUNCTION (ISOFORM NKP44L), SUBCELLULAR LOCATION (ISOFORM NKP44L), TISSUE SPECIFICITY.
    3. "Identification and characterization of a novel gene located in the commonly deleted region 7q22-q31.1 in myeloid leukemias."
      Dohner K., Obermiller R.T., Lipka D.B., Hofmann K., Habdank M., Fazekas G., Frohling S., Lichter P., Scherer S.W., Dohner H.
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [MRNA] OF 624-1858 (ISOFORM 4), NUCLEOTIDE SEQUENCE [MRNA] OF 1149-1251 (ISOFORMS 1/2/4/6/7), NUCLEOTIDE SEQUENCE [MRNA] OF 1190-1355 (ISOFORM 7), NUCLEOTIDE SEQUENCE [MRNA] OF 1415-1858 (ISOFORMS 5 AND 6).
      Tissue: BrainImported and Peripheral blood leukocyteImported.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-491.
      Tissue: ChoriocarcinomaImported, LiverImported and UterusImported.
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-594.
      Tissue: Embryo.
    8. "MLL 5 protein forms intranuclear foci, and overexpression inhibits cell cycle progression."
      Deng L.-W., Chiu I., Strominger J.L.
      Proc. Natl. Acad. Sci. U.S.A. 101:757-762(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "RNA interference against mixed lineage leukemia 5 resulted in cell cycle arrest."
      Cheng F., Liu J., Zhou S.H., Wang X.N., Chew J.F., Deng L.-W.
      Int. J. Biochem. Cell Biol. 40:2472-2481(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
      Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
      Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE MLL5-L COMPLEX, GLYCOSYLATION AT THR-440, INTERACTION WITH RARA, MUTAGENESIS OF SER-334; SER-345; TYR-358; SER-386; THR-399; SER-410; THR-412; THR-425; SER-432; SER-435; THR-440; GLU-441 AND THR-443.

    Entry informationi

    Entry nameiKMT2E_HUMAN
    AccessioniPrimary (citable) accession number: Q8IZD2
    Secondary accession number(s): B6ZDE4
    , B6ZDM3, M4K8J3, Q6P5Y2, Q6PKG4, Q6T316, Q86TI3, Q86W12, Q86WG0, Q86WL2, Q8IV78, Q8IWR5, Q8NFF8, Q9NWE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 10, 2008
    Last sequence update: March 1, 2003
    Last modified: October 1, 2014
    This is version 99 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3