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Protein

Inactive histone-lysine N-methyltransferase 2E

Gene

KMT2E

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

Functioni

Associates with chromatin regions downstream of transcriptional start sites of active genes and thus regulates gene transcription (PubMed:23629655, PubMed:24130829, PubMed:23798402). Chromatin interaction is mediated via the binding to tri-methylated histone H3 at 'Lys-4' (H3K4me3) (PubMed:24130829, PubMed:23798402). 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 (By similarity). 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:14718661, PubMed:18573682, PubMed:19264965, PubMed:23629655). 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 (PubMed:23629655). During myoblast differentiation, required to suppress inappropriate expression of S-phase-promoting genes and maintain expression of determination genes in quiescent cells (By similarity).By similarity5 Publications
Isoform NKp44L: Cellular ligand for NCR2/NKp44, may play a role as a danger signal in cytotoxicity and NK-cell-mediated innate immunity.1 Publication

Caution

Isoform 3 was originally thought to display histone methyltransferase activity only following O-glycosylation at Thr-440 (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203). Does not exhibit histone methyltransferase towards histone H3 in vitro (PubMed:19264965, PubMed:27812132). 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 (PubMed:27812132). 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 (PubMed:27812132).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi121Zinc 1Combined sources2 Publications1
Metal bindingi123Zinc 1Combined sources2 Publications1
Metal bindingi135Zinc 2Combined sources2 Publications1
Metal bindingi138Zinc 2Combined sources2 Publications1
Metal bindingi143Zinc 1; via pros nitrogenCombined sources2 Publications1
Metal bindingi146Zinc 1Combined sources2 Publications1
Metal bindingi160Zinc 2Combined sources2 Publications1
Metal bindingi163Zinc 2Combined sources2 Publications1

Regions

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

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • histone-lysine N-methyltransferase activity Source: Reactome
  • metal ion binding Source: UniProtKB-KW
  • methylated histone binding Source: UniProtKB

GO - Biological processi

  • cell cycle arrest Source: UniProtKB-KW
  • DNA methylation Source: UniProtKB
  • erythrocyte differentiation Source: UniProtKB
  • neutrophil activation Source: UniProtKB
  • neutrophil mediated immunity Source: UniProtKB
  • positive regulation of G1/S transition of mitotic cell cycle Source: UniProtKB
  • positive regulation of histone H3-K4 trimethylation Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of megakaryocyte differentiation Source: Reactome
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

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

Enzyme and pathway databases

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

Names & Taxonomyi

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
Gene namesi
Name:KMT2E
Synonyms:MLL5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000005483.19
HGNCiHGNC:18541 KMT2E
MIMi608444 gene
neXtProtiNX_Q8IZD2

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Chromosome, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi63 – 66DHNY → AAAA: Abolishes interaction with HCFC1. 1 Publication4
Mutagenesisi125F → A: No effect on binding to tri-methylated 'Lys-4' of histone H3 (H3K4me3). 1 Publication1
Mutagenesisi128D → K: Severe reduction in the binding to tri-methylated 'Lys-4' of histone H3 (H3K4me3). 1 Publication1
Mutagenesisi131Y → A or K: Severe reduction in the binding to tri-methylated 'Lys-4' of histone H3 (H3K4me3). 1 Publication1
Mutagenesisi141W → A: Loss of binding to tri-methylated 'Lys-4' of histone H3 (H3K4me3). 1 Publication1
Mutagenesisi411C → A: Fails to activate the cell cycle regulated element (CCRE) in the cyclin A promoter. 1 Publication1

Organism-specific databases

DisGeNETi55904
OpenTargetsiENSG00000005483
PharmGKBiPA38568

Polymorphism and mutation databases

BioMutaiKMT2E
DMDMi74723669

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003414191 – 1858Inactive histone-lysine N-methyltransferase 2EAdd BLAST1858

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi435O-linked (GlcNAc) serine1 Publication1
Glycosylationi440O-linked (GlcNAc) threonine1 Publication1
Modified residuei623PhosphoserineCombined sources1
Modified residuei837PhosphoserineCombined sources1
Modified residuei845PhosphoserineBy similarity1
Modified residuei1070PhosphoserineCombined sources1
Modified residuei1273PhosphoserineCombined sources1
Modified residuei1359PhosphoserineCombined sources1

Post-translational modificationi

Ubiquitinated. Deubiquitinated by USP7.1 Publication
O-glycosylated at Ser-435 and Thr-440 in the SET domain by OGT which probably prevents KMT2E proteasomal-mediated degradation.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ8IZD2
MaxQBiQ8IZD2
PaxDbiQ8IZD2
PeptideAtlasiQ8IZD2
PRIDEiQ8IZD2

PTM databases

iPTMnetiQ8IZD2
PhosphoSitePlusiQ8IZD2

Expressioni

Tissue specificityi

Widely expressed in both adult and fetal tissues (PubMed:12101424, PubMed:23958951). Highest levels of expression observed in fetal thymus and kidney and in adult hematopoietic tissues, jejunum and cerebellum (PubMed:12101424, PubMed:23958951). Isoform NKp44L: Not detected on circulating cells from healthy individuals, but is expressed on a large panel of tumor and transformed cells (PubMed:23958951).2 Publications

Gene expression databases

BgeeiENSG00000005483
ExpressionAtlasiQ8IZD2 baseline and differential
GenevisibleiQ8IZD2 HS

Organism-specific databases

HPAiHPA022812
HPA056125

Interactioni

Subunit structurei

Component of a complex composed of KMT2E (isoform 3), OGT and USP7; the complex stabilizes KMT2E, preventing KMT2E ubiquitination and proteosomal-mediated degradation (PubMed:26678539). Isoform 3 interacts (via N-terminus) with OGT (via TRP repeats) (PubMed:26678539, PubMed:23629655). Isoform 3 interacts with deubiquitinating enzyme USP7 (via MATH domain) (PubMed:26678539). Isoform 3 interacts (via HBM motif) with HCFC1 (via Kelch domain) (PubMed:23629655). Isoform 3 interacts with E2F1; the interaction is probably indirect and is mediated via HCFC1 (PubMed:23629655).2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120990, 37 interactors
IntActiQ8IZD2, 11 interactors
STRINGi9606.ENSP00000257745

Structurei

Secondary structure

11858
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi132 – 134Combined sources3
Turni136 – 138Combined sources3
Beta strandi141 – 143Combined sources3
Helixi144 – 147Combined sources4
Beta strandi156 – 158Combined sources3
Turni161 – 165Combined sources5
Helixi170 – 178Combined sources9
Beta strandi344 – 347Combined sources4
Beta strandi354 – 357Combined sources4
Beta strandi360 – 364Combined sources5
Helixi365 – 370Combined sources6
Beta strandi382 – 385Combined sources4
Turni387 – 390Combined sources4
Beta strandi393 – 396Combined sources4
Helixi403 – 406Combined sources4
Beta strandi414 – 422Combined sources9
Beta strandi425 – 434Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LV9NMR-A109-188[»]
4L58X-ray1.48A117-181[»]
5HT6X-ray2.09A/B323-458[»]
ProteinModelPortaliQ8IZD2
SMRiQ8IZD2
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini330 – 447SETPROSITE-ProRule annotationAdd BLAST118

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili559 – 615Sequence analysisAdd BLAST57

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi63 – 66HCFC1-binding motif (HBM)1 Publication4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1433 – 1846Pro-richSequence analysisAdd BLAST414

Domaini

The PHD-type domain binds specifically histone H3 tri-methylated at 'Lys-4' (H3K4me3), thus promoting binding to chromatin.2 Publications
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.1 Publication
The C-terminus domain is responsible for the localization to the centrosome during mitosis.1 Publication

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.PROSITE-ProRule annotation

Zinc finger

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

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG1844 Eukaryota
COG2940 LUCA
GeneTreeiENSGT00520000055602
HOVERGENiHBG105683
InParanoidiQ8IZD2
KOiK09189
OMAiKHYIRFT
OrthoDBiEOG091G00UT
PhylomeDBiQ8IZD2
TreeFamiTF106417

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
PANTHERiPTHR44512:SF1 PTHR44512:SF1, 2 hits
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

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 NKp44L1 Publication (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 differs from that shown. Contaminating sequence. Potential poly-A sequence starting in position 492.Curated
The sequence AAH40004 differs from that shown. Contaminating sequence. Potential poly-A sequence starting in position 227.Curated
The sequence AAH53906 differs from that shown. Contaminating sequence. Potential poly-A sequence starting in position 227.Curated
The sequence AAI42988 differs from that shown. Contaminating sequence. Potential poly-A sequence starting in position 492.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti496K → E in AAM74947 (PubMed:12101424).Curated1
Sequence conflicti496K → E in AGE34449 (PubMed:23958951).Curated1
Sequence conflicti496K → E in AK000940 (PubMed:14702039).Curated1
Sequence conflicti516T → A in AAM74947 (PubMed:12101424).Curated1
Sequence conflicti516T → A in AGE34449 (PubMed:23958951).Curated1
Sequence conflicti516T → A in AK000940 (PubMed:14702039).Curated1
Sequence conflicti594R → K in AK000940 (PubMed:14702039).Curated1
Sequence conflicti1020V → A in AAM74947 (PubMed:12101424).Curated1
Sequence conflicti1073R → S in AAM74947 (PubMed:12101424).Curated1
Sequence conflicti1090S → P in AAM74947 (PubMed:12101424).Curated1
Sequence conflicti1099F → S in AAM74947 (PubMed:12101424).Curated1
Sequence conflicti1168E → K in AAM74947 (PubMed:12101424).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0526561424S → P. Corresponds to variant dbSNP:rs35605511Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_052803494 – 573Missing in isoform 2. 1 PublicationAdd BLAST80
Alternative sequenceiVSP_052804575 – 609TREER…ISTAK → VSWEASSLGLVTAALHMVIV AAFTWAFTLFFEVSE in isoform 3. 1 PublicationAdd BLAST35
Alternative sequenceiVSP_052805610 – 1858Missing in isoform 3. 1 PublicationAdd BLAST1249
Alternative sequenceiVSP_052806850 – 865GENKS…SCSLP → EYFFPRKFSRNKETHL in isoform 4. 1 PublicationAdd BLAST16
Alternative sequenceiVSP_052807866 – 1858Missing in isoform 4. 1 PublicationAdd BLAST993
Alternative sequenceiVSP_0538341157 – 1168VSLLE…KRQRE → SPVGNFVGSNVV in isoform NKp44L. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_0538351169 – 1858Missing in isoform NKp44L. 1 PublicationAdd BLAST690
Alternative sequenceiVSP_0528081282 – 1323Missing in isoform 7. 1 PublicationAdd BLAST42
Alternative sequenceiVSP_0528091443 – 1621PSPHL…IHHQT → SSPSTTPSIHRTPRSTSTTP ACCKFSTPTTPSAATFQCFG FWASYHISSSLTPPTSSRTS TFSFECSSNCTTVSLTSYTS YHFGTGTPAPAFWNRATLSI TCHRSSSPAPRTKQYSNTYC FRVLSSSWLCGPATWGSRTS AGISSAWTDSNSQSTGATNI SKQLPWVRVALKWTPKTFF in isoform 6. 1 PublicationAdd BLAST179
Alternative sequenceiVSP_0528101508 – 1653ANTQQ…QHSVA → VFWLLGIIPHQLKPYTTHLI KDLHFFLRVLIQLYHRIPHK LHIIPLWDRDPSTSLLEQGH IVHYLSQVLISSPKDQTVFQ HLLLQGSVLILALWPCHMGF KDLSRHLQCLDRFQFTEHRC HQHFKTITMGQGGIKMDSKN IFLNVL in isoform 5. 1 PublicationAdd BLAST146
Alternative sequenceiVSP_0528111622 – 1858Missing in isoform 6. 1 PublicationAdd BLAST237
Alternative sequenceiVSP_0528121654 – 1858Missing in isoform 5. 1 PublicationAdd BLAST205

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_011514702.1, XM_011516400.1 [Q8IZD2-1]
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.5 human [Q8IZD2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

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 historyiIntegrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: March 1, 2003
Last modified: April 25, 2018
This is version 130 of the entry and version 1 of the sequence. See 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

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