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Protein

Histone-lysine N-methyltransferase 2E

Gene

KMT2E

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • enzyme binding Source: UniProtKB
  • histone methyltransferase activity (H3-K4 specific) Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell cycle arrest Source: UniProtKB-KW
  • cellular response to retinoic acid Source: BHF-UCL
  • chromatin organization Source: Reactome
  • DNA methylation Source: UniProtKB
  • erythrocyte differentiation Source: UniProtKB
  • histone H3-K4 methylation Source: BHF-UCL
  • neutrophil activation Source: UniProtKB
  • neutrophil mediated immunity Source: UniProtKB
  • positive regulation of granulocyte differentiation Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • retinoic acid receptor signaling pathway Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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

Enzyme and pathway databases

ReactomeiREACT_268728. PKMTs methylate histone lysines.

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 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:18541. KMT2E.

Subcellular locationi

Isoform NKp44L :

GO - Cellular componenti

Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiKMT2E.
DMDMi74723669.

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

BgeeiQ8IZD2.
ExpressionAtlasiQ8IZD2. baseline and differential.
GenevisibleiQ8IZD2. HS.

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.
STRINGi9606.ENSP00000257745.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LV9NMR-A109-188[»]
4L58X-ray1.48A117-181[»]
ProteinModelPortaliQ8IZD2.
SMRiQ8IZD2. Positions 109-188.
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.
GeneTreeiENSGT00520000055602.
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. AlignAdd to basket

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

        10         20         30         40         50
MSIVIPLGVD TAETSYLEMA AGSEPESVEA SPVVVEKSNS YPHQLYTSSS
60 70 80 90 100
HHSHSYIGLP YADHNYGARP PPTPPASPPP SVLISKNEVG IFTTPNFDET
110 120 130 140 150
SSATTISTSE DGSYGTDVTR CICGFTHDDG YMICCDKCSV WQHIDCMGID
160 170 180 190 200
RQHIPDTYLC ERCQPRNLDK ERAVLLQRRK RENMSDGDTS ATESGDEVPV
210 220 230 240 250
ELYTAFQHTP TSITLTASRV SKVNDKRRKK SGEKEQHISK CKKAFREGSR
260 270 280 290 300
KSSRVKGSAP EIDPSSDGSN FGWETKIKAW MDRYEEANNN QYSEGVQREA
310 320 330 340 350
QRIALRLGNG NDKKEMNKSD LNTNNLLFKP PVESHIQKNK KILKSAKDLP
360 370 380 390 400
PDALIIEYRG KFMLREQFEA NGYFFKRPYP FVLFYSKFHG LEMCVDARTF
410 420 430 440 450
GNEARFIRRS CTPNAEVRHE IQDGTIHLYI YSIHSIPKGT EITIAFDFDY
460 470 480 490 500
GNCKYKVDCA CLKENPECPV LKRSSESMEN INSGYETRRK KGKKDKDISK
510 520 530 540 550
EKDTQNQNIT LDCEGTTNKM KSPETKQRKL SPLRLSVSNN QEPDFIDDIE
560 570 580 590 600
EKTPISNEVE MESEEQIAER KRKMTREERK MEAILQAFAR LEKREKRREQ
610 620 630 640 650
ALERISTAKT EVKTECKDTQ IVSDAEVIQE QAKEENASKP TPAKVNRTKQ
660 670 680 690 700
RKSFSRSRTH IGQQRRRHRT VSMCSDIQPS SPDIEVTSQQ NDIENTVLTI
710 720 730 740 750
EPETETALAE IITETEVPAL NKCPTKYPKT KKHLVNEWLS EKNEKTGKPS
760 770 780 790 800
DGLSERPLRI TTDPEVLATQ LNSLPGLTYS PHVYSTPKHY IRFTSPFLSE
810 820 830 840 850
KRRRKEPTEN ISGSCKKRWL KQALEEENSA ILHRFNSPCQ ERSRSPAVNG
860 870 880 890 900
ENKSPLLLND SCSLPDLTTP LKKRRFYQLL DSVYSETSTP TPSPYATPTH
910 920 930 940 950
TDITPMDPSF ATPPRIKSDD ETCRNGYKPI YSPVTPVTPG TPGNTMHFEN
960 970 980 990 1000
ISSPESSPEI KRRTYSQEGY DRSSTMLTLG PFRNSNLTEL GLQEIKTIGY
1010 1020 1030 1040 1050
TSPRSRTEVN RQCPGEKEPV SDLQLGLDAV EPTALHKTLE TPAHDRAEPN
1060 1070 1080 1090 1100
SQLDSTHSGR GTMYSSWVKS PDRTGVNFSV NSNLRDLTPS HQLEVGGGFR
1110 1120 1130 1140 1150
ISESKCLMQD DTRGMFMETT VFCTSEDGLV SGFGRTVNDN LIDGNCTPQN
1160 1170 1180 1190 1200
PPQKKKVSLL EYRKRQREAR KSGSKTENFP LISVSPHASG SLSNNGDGCA
1210 1220 1230 1240 1250
SSNDNGEQVD HTASLPLPTP ATVYNATSEE TSNNCPVKDA TASEKNEPEV
1260 1270 1280 1290 1300
QWTASTSVEQ VRERSYQRAL LLSDHRKDKD SGGESPCVSC SPSHVQSSPS
1310 1320 1330 1340 1350
SHSNHIPQLQ AKGPVPSFSE LMEDPDPENP EPTTTNECPS PDTSQNTCKS
1360 1370 1380 1390 1400
PPKMSKPGSP GSVIPAQAHG KIFTKPDPQW DSTVSASEAE NGVHLKTELQ
1410 1420 1430 1440 1450
QKQLSNNNQA LSKNHPPQTH VRNSSEQLSQ KLPSVPTKLH CPPSPHLENP
1460 1470 1480 1490 1500
PKSSTPHTPV QHGYLSPKPP SQQLGSPYRP HHSQSPQVGT PQREPQRNFY
1510 1520 1530 1540 1550
PAAQNLPANT QQATSGTLFT QTPSGQSSAT YSQFNQQSLN STAPPPPPPP
1560 1570 1580 1590 1600
PPSSSYYQNQ QPSANFQNYN QLKGSLSQQT VFTSGPNQAL PGTTSQQTVP
1610 1620 1630 1640 1650
GHHVTPGHFL PSQNPTIHHQ TAAAVVPPPP PPPPAPGPHL VQQPNSHQQH
1660 1670 1680 1690 1700
SVAHVVGPVH AVTPGSHIHS QTAGHHLPPP PPPPGPAPHH HPPPHPSTGL
1710 1720 1730 1740 1750
QGLQAQHQHV VNSAPPPPPP PPPSSVLASG HHTTSAQALH HPPHQGPPLF
1760 1770 1780 1790 1800
PSSAHPTVPP YPSQATHHTT LGPGPQHQPS GTGPHCPLPV TGPHLQPQGP
1810 1820 1830 1840 1850
NSIPTPTASG FCPHPGSVAL PHGVQGPQQA SPVPGQIPIH RAQVPPTFQN

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

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:
EMBLi
GenBanki
DDBJi
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]
ENST00000334884; ENSP00000335398; ENSG00000005483. [Q8IZD2-4]
ENST00000476671; ENSP00000417888; ENSG00000005483. [Q8IZD2-3]
GeneIDi55904.
KEGGihsa:55904.
UCSCiuc003vcl.3. human. [Q8IZD2-3]
uc003vcm.3. human. [Q8IZD2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LV9NMR-A109-188[»]
4L58X-ray1.48A117-181[»]
ProteinModelPortaliQ8IZD2.
SMRiQ8IZD2. Positions 109-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120990. 12 interactions.
IntActiQ8IZD2. 9 interactions.
STRINGi9606.ENSP00000257745.

PTM databases

PhosphoSiteiQ8IZD2.

Polymorphism and mutation databases

BioMutaiKMT2E.
DMDMi74723669.

Proteomic databases

MaxQBiQ8IZD2.
PaxDbiQ8IZD2.
PRIDEiQ8IZD2.

Protocols and materials databases

DNASUi55904.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi55904.
GeneCardsiGC07P104655.
HGNCiHGNC:18541. KMT2E.
HPAiHPA056125.
MIMi608444. gene.
neXtProtiNX_Q8IZD2.
PharmGKBiPA38568.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00520000055602.
HOVERGENiHBG105683.
InParanoidiQ8IZD2.
KOiK09189.
OMAiETECANH.
OrthoDBiEOG76472V.
PhylomeDBiQ8IZD2.
TreeFamiTF106417.

Enzyme and pathway databases

ReactomeiREACT_268728. PKMTs methylate histone lysines.

Miscellaneous databases

GenomeRNAii55904.
NextBioi61277.
PROiQ8IZD2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IZD2.
ExpressionAtlasiQ8IZD2. baseline and differential.
GenevisibleiQ8IZD2. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: June 24, 2015
This is version 108 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.