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Q8IZD2 (KMT2E_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase 2E

Short name=Lysine N-methyltransferase 2E
EC=2.1.1.43
Alternative name(s):
Myeloid/lymphoid or mixed-lineage leukemia protein 5
Gene names
Name:KMT2E
Synonyms:MLL5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1858 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.8 Ref.9 Ref.10

Isoform NKp44L:Cellular ligand for NCR2/NKp44, may play a role as a danger signal in cytotoxicity and NK-cell-mediated innate immunity. Ref.2 Ref.8 Ref.9 Ref.10

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.10

Subunit structure

Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with RARA. Ref.10

Subcellular location

Nucleus speckle. Note: Absent from the nucleolus. Ref.2 Ref.8

Isoform NKp44L: Cytoplasm. Cell membrane; Peripheral membrane protein Ref.2 Ref.8.

Tissue specificity

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. Ref.1 Ref.2

Post-translational modification

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.

Sequence similarities

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

Contains 1 PHD-type zinc finger.

Contains 1 SET domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processCell cycle
Growth arrest
Transcription
Transcription regulation
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   PTMGlycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Inferred from sequence or structural similarity. Source: UniProtKB

cell cycle arrest

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to retinoic acid

Inferred from direct assay Ref.10. Source: BHF-UCL

erythrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3-K4 methylation

Inferred from direct assay Ref.10. Source: BHF-UCL

neutrophil activation

Inferred from sequence or structural similarity. Source: UniProtKB

neutrophil mediated immunity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of granulocyte differentiation

Inferred from mutant phenotype Ref.10. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.10. Source: UniProtKB

retinoic acid receptor signaling pathway

Inferred from mutant phenotype Ref.10. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMLL5-L complex

Inferred from direct assay Ref.10. Source: UniProtKB

nuclear speck

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionenzyme binding

Inferred from physical interaction Ref.10. Source: UniProtKB

histone methyltransferase activity (H3-K4 specific)

Inferred from direct assay Ref.10. Source: UniProtKB

transcription coactivator activity

Inferred from mutant phenotype Ref.10. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TP53P046374EBI-2689959,EBI-366083

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.2 (identifier: Q8IZD2-1)

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.
Isoform 2 Ref.2 (identifier: Q8IZD2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     494-573: Missing.
Note: No experimental confirmation available.
Isoform 3 Ref.3 Ref.6 (identifier: Q8IZD2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     575-609: TREERKMEAILQAFARLEKREKRREQALERISTAK → VSWEASSLGLVTAALHMVIVAAFTWAFTLFFEVSE
     610-1858: Missing.
Isoform 4 Ref.2 (identifier: Q8IZD2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     850-865: GENKSPLLLNDSCSLP → EYFFPRKFSRNKETHL
     866-1858: Missing.
Note: No experimental confirmation available.
Isoform 5 Ref.2 (identifier: Q8IZD2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1508-1653: ANTQQATSGT...PNSHQQHSVA → VFWLLGIIPH...DSKNIFLNVL
     1654-1858: Missing.
Isoform 6 Ref.2 (identifier: Q8IZD2-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1443-1621: PSPHLENPPK...SQNPTIHHQT → SSPSTTPSIH...ALKWTPKTFF
     1622-1858: Missing.
Isoform 7 Ref.2 (identifier: Q8IZD2-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1282-1323: Missing.
Note: No experimental confirmation available.
Isoform NKp44L (identifier: Q8IZD2-8)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18581858Histone-lysine N-methyltransferase 2E
PRO_0000341419

Regions

Domain330 – 447118SET
Zinc finger118 – 16649PHD-type
Coiled coil559 – 61557 Potential
Compositional bias1433 – 1846414Pro-rich

Amino acid modifications

Glycosylation4401O-linked (GlcNAc) Ref.10

Natural variations

Alternative sequence494 – 57380Missing in isoform 2. Ref.2
VSP_052803
Alternative sequence575 – 60935TREER…ISTAK → VSWEASSLGLVTAALHMVIV AAFTWAFTLFFEVSE in isoform 3. Ref.3 Ref.6
VSP_052804
Alternative sequence610 – 18581249Missing in isoform 3. Ref.3 Ref.6
VSP_052805
Alternative sequence850 – 86516GENKS…SCSLP → EYFFPRKFSRNKETHL in isoform 4. Ref.2
VSP_052806
Alternative sequence866 – 1858993Missing in isoform 4. Ref.2
VSP_052807
Alternative sequence1157 – 116812VSLLE…KRQRE → SPVGNFVGSNVV in isoform NKp44L.
VSP_053834
Alternative sequence1169 – 1858690Missing in isoform NKp44L.
VSP_053835
Alternative sequence1282 – 132342Missing in isoform 7. Ref.2
VSP_052808
Alternative sequence1443 – 1621179PSPHL…IHHQT → SSPSTTPSIHRTPRSTSTTP ACCKFSTPTTPSAATFQCFG FWASYHISSSLTPPTSSRTS TFSFECSSNCTTVSLTSYTS YHFGTGTPAPAFWNRATLSI TCHRSSSPAPRTKQYSNTYC FRVLSSSWLCGPATWGSRTS AGISSAWTDSNSQSTGATNI SKQLPWVRVALKWTPKTFF in isoform 6. Ref.2
VSP_052809
Alternative sequence1508 – 1653146ANTQQ…QHSVA → VFWLLGIIPHQLKPYTTHLI KDLHFFLRVLIQLYHRIPHK LHIIPLWDRDPSTSLLEQGH IVHYLSQVLISSPKDQTVFQ HLLLQGSVLILALWPCHMGF KDLSRHLQCLDRFQFTEHRC HQHFKTITMGQGGIKMDSKN IFLNVL in isoform 5. Ref.2
VSP_052810
Alternative sequence1622 – 1858237Missing in isoform 6. Ref.2
VSP_052811
Alternative sequence1654 – 1858205Missing in isoform 5. Ref.2
VSP_052812
Natural variant14241S → P.
Corresponds to variant rs35605511 [ dbSNP | Ensembl ].
VAR_052656

Experimental info

Mutagenesis3341S → A: Does not affect O-glycosylation by OGT. Ref.10
Mutagenesis3451S → A: Does not affect O-glycosylation by OGT. Ref.10
Mutagenesis3581Y → A: Loss of methyltransferase activity. Ref.10
Mutagenesis3861S → A: Does not affect O-glycosylation by OGT. Ref.10
Mutagenesis3991T → A: Does not affect O-glycosylation by OGT. Ref.10
Mutagenesis4101S → A: Does not affect O-glycosylation by OGT. Ref.10
Mutagenesis4121T → A: Does not affect O-glycosylation by OGT. Ref.10
Mutagenesis4251T → A: Does not affect O-glycosylation by OGT. Ref.10
Mutagenesis4321S → A: Does not affect O-glycosylation by OGT. Ref.10
Mutagenesis4351S → A: Does not affect O-glycosylation by OGT. Ref.10
Mutagenesis4401T → A: Abolishes O-glycosylation by OGT and prevents coactivator activity toward RARA in granulopoiesis. Ref.10
Mutagenesis4411E → A: Loss of methyltransferase activity. Ref.10
Mutagenesis4431T → A: Does not affect O-glycosylation by OGT. Ref.10
Sequence conflict4961K → E in AAM74947. Ref.1
Sequence conflict4961K → E in AGE34449. Ref.2
Sequence conflict4961K → E in AK000940. Ref.7
Sequence conflict5161T → A in AAM74947. Ref.1
Sequence conflict5161T → A in AGE34449. Ref.2
Sequence conflict5161T → A in AK000940. Ref.7
Sequence conflict5941R → K in AK000940. Ref.7
Sequence conflict10201V → A in AAM74947. Ref.1
Sequence conflict10731R → S in AAM74947. Ref.1
Sequence conflict10901S → P in AAM74947. Ref.1
Sequence conflict10991F → S in AAM74947. Ref.1
Sequence conflict11681E → K in AAM74947. Ref.1

Secondary structure

.............. 1858
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 8ACCB3CDB5BFCEFA

FASTA1,858204,965
        10         20         30         40         50         60 
MSIVIPLGVD TAETSYLEMA AGSEPESVEA SPVVVEKSNS YPHQLYTSSS HHSHSYIGLP 

        70         80         90        100        110        120 
YADHNYGARP PPTPPASPPP SVLISKNEVG IFTTPNFDET SSATTISTSE DGSYGTDVTR 

       130        140        150        160        170        180 
CICGFTHDDG YMICCDKCSV WQHIDCMGID RQHIPDTYLC ERCQPRNLDK ERAVLLQRRK 

       190        200        210        220        230        240 
RENMSDGDTS ATESGDEVPV ELYTAFQHTP TSITLTASRV SKVNDKRRKK SGEKEQHISK 

       250        260        270        280        290        300 
CKKAFREGSR KSSRVKGSAP EIDPSSDGSN FGWETKIKAW MDRYEEANNN QYSEGVQREA 

       310        320        330        340        350        360 
QRIALRLGNG NDKKEMNKSD LNTNNLLFKP PVESHIQKNK KILKSAKDLP PDALIIEYRG 

       370        380        390        400        410        420 
KFMLREQFEA NGYFFKRPYP FVLFYSKFHG LEMCVDARTF GNEARFIRRS CTPNAEVRHE 

       430        440        450        460        470        480 
IQDGTIHLYI YSIHSIPKGT EITIAFDFDY GNCKYKVDCA CLKENPECPV LKRSSESMEN 

       490        500        510        520        530        540 
INSGYETRRK KGKKDKDISK EKDTQNQNIT LDCEGTTNKM KSPETKQRKL SPLRLSVSNN 

       550        560        570        580        590        600 
QEPDFIDDIE EKTPISNEVE MESEEQIAER KRKMTREERK MEAILQAFAR LEKREKRREQ 

       610        620        630        640        650        660 
ALERISTAKT EVKTECKDTQ IVSDAEVIQE QAKEENASKP TPAKVNRTKQ RKSFSRSRTH 

       670        680        690        700        710        720 
IGQQRRRHRT VSMCSDIQPS SPDIEVTSQQ NDIENTVLTI EPETETALAE IITETEVPAL 

       730        740        750        760        770        780 
NKCPTKYPKT KKHLVNEWLS EKNEKTGKPS DGLSERPLRI TTDPEVLATQ LNSLPGLTYS 

       790        800        810        820        830        840 
PHVYSTPKHY IRFTSPFLSE KRRRKEPTEN ISGSCKKRWL KQALEEENSA ILHRFNSPCQ 

       850        860        870        880        890        900 
ERSRSPAVNG ENKSPLLLND SCSLPDLTTP LKKRRFYQLL DSVYSETSTP TPSPYATPTH 

       910        920        930        940        950        960 
TDITPMDPSF ATPPRIKSDD ETCRNGYKPI YSPVTPVTPG TPGNTMHFEN ISSPESSPEI 

       970        980        990       1000       1010       1020 
KRRTYSQEGY DRSSTMLTLG PFRNSNLTEL GLQEIKTIGY TSPRSRTEVN RQCPGEKEPV 

      1030       1040       1050       1060       1070       1080 
SDLQLGLDAV EPTALHKTLE TPAHDRAEPN SQLDSTHSGR GTMYSSWVKS PDRTGVNFSV 

      1090       1100       1110       1120       1130       1140 
NSNLRDLTPS HQLEVGGGFR ISESKCLMQD DTRGMFMETT VFCTSEDGLV SGFGRTVNDN 

      1150       1160       1170       1180       1190       1200 
LIDGNCTPQN PPQKKKVSLL EYRKRQREAR KSGSKTENFP LISVSPHASG SLSNNGDGCA 

      1210       1220       1230       1240       1250       1260 
SSNDNGEQVD HTASLPLPTP ATVYNATSEE TSNNCPVKDA TASEKNEPEV QWTASTSVEQ 

      1270       1280       1290       1300       1310       1320 
VRERSYQRAL LLSDHRKDKD SGGESPCVSC SPSHVQSSPS SHSNHIPQLQ AKGPVPSFSE 

      1330       1340       1350       1360       1370       1380 
LMEDPDPENP EPTTTNECPS PDTSQNTCKS PPKMSKPGSP GSVIPAQAHG KIFTKPDPQW 

      1390       1400       1410       1420       1430       1440 
DSTVSASEAE NGVHLKTELQ QKQLSNNNQA LSKNHPPQTH VRNSSEQLSQ KLPSVPTKLH 

      1450       1460       1470       1480       1490       1500 
CPPSPHLENP PKSSTPHTPV QHGYLSPKPP SQQLGSPYRP HHSQSPQVGT PQREPQRNFY 

      1510       1520       1530       1540       1550       1560 
PAAQNLPANT QQATSGTLFT QTPSGQSSAT YSQFNQQSLN STAPPPPPPP PPSSSYYQNQ 

      1570       1580       1590       1600       1610       1620 
QPSANFQNYN QLKGSLSQQT VFTSGPNQAL PGTTSQQTVP GHHVTPGHFL PSQNPTIHHQ 

      1630       1640       1650       1660       1670       1680 
TAAAVVPPPP PPPPAPGPHL VQQPNSHQQH SVAHVVGPVH AVTPGSHIHS QTAGHHLPPP 

      1690       1700       1710       1720       1730       1740 
PPPPGPAPHH HPPPHPSTGL QGLQAQHQHV VNSAPPPPPP PPPSSVLASG HHTTSAQALH 

      1750       1760       1770       1780       1790       1800 
HPPHQGPPLF PSSAHPTVPP YPSQATHHTT LGPGPQHQPS GTGPHCPLPV TGPHLQPQGP 

      1810       1820       1830       1840       1850 
NSIPTPTASG FCPHPGSVAL PHGVQGPQQA SPVPGQIPIH RAQVPPTFQN NYHGSGWH 

« Hide

Isoform 2 [UniParc].

Checksum: AEA0E38D5D008BE7
Show »

FASTA1,778195,675
Isoform 3 [UniParc].

Checksum: CAC22E252873885E
Show »

FASTA60968,926
Isoform 4 [UniParc].

Checksum: 7E1470684F22660D
Show »

FASTA86598,795
Isoform 5 [UniParc].

Checksum: 6AF69A147E64F516
Show »

FASTA1,653185,802
Isoform 6 [UniParc].

Checksum: 97E5EB49B9961FEA
Show »

FASTA1,621180,779
Isoform 7 [UniParc].

Checksum: 16311FD3AC2DC1EF
Show »

FASTA1,816200,635
Isoform NKp44L [UniParc].

Checksum: B5D59D07B6ED13FA
Show »

FASTA1,168131,737

References

« Hide 'large scale' references
[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: Brain and Peripheral blood leukocyte.
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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: Choriocarcinoma, Liver and Uterus.
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_061152.3. NM_018682.3.
NP_891847.1. NM_182931.2.
XP_005250550.1. XM_005250493.1.
UniGeneHs.592262.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LV9NMR-A109-188[»]
4L58X-ray1.48A117-181[»]
ProteinModelPortalQ8IZD2.
SMRQ8IZD2. Positions 109-188, 353-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120990. 12 interactions.
IntActQ8IZD2. 9 interactions.

PTM databases

PhosphoSiteQ8IZD2.

Polymorphism databases

DMDM74723669.

Proteomic databases

PaxDbQ8IZD2.
PRIDEQ8IZD2.

Protocols and materials databases

DNASU55904.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257745; ENSP00000257745; ENSG00000005483. [Q8IZD2-1]
ENST00000311117; ENSP00000312379; ENSG00000005483. [Q8IZD2-1]
ENST00000334877; ENSP00000335599; ENSG00000005483. [Q8IZD2-7]
ENST00000334884; ENSP00000335398; ENSG00000005483. [Q8IZD2-4]
ENST00000476671; ENSP00000417888; ENSG00000005483. [Q8IZD2-3]
GeneID55904.
KEGGhsa:55904.
UCSCuc003vcl.3. human. [Q8IZD2-3]
uc003vcm.3. human. [Q8IZD2-1]

Organism-specific databases

CTD55904.
GeneCardsGC07P104655.
HGNCHGNC:18541. KMT2E.
HPAHPA056125.
MIM608444. gene.
neXtProtNX_Q8IZD2.
PharmGKBPA38568.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2940.
HOVERGENHBG105683.
InParanoidQ8IZD2.
KOK09189.
OMAPSANFQN.
OrthoDBEOG76472V.
PhylomeDBQ8IZD2.
TreeFamTF106417.

Gene expression databases

ArrayExpressQ8IZD2.
BgeeQ8IZD2.
GenevestigatorQ8IZD2.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR001214. 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]
PfamPF00628. PHD. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTSM00249. PHD. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 1 hit.
PROSITEPS50280. SET. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMLL5. human.
GenomeRNAi55904.
NextBio61277.
PROQ8IZD2.
SOURCESearch...

Entry information

Entry nameKMT2E_HUMAN
AccessionPrimary (citable) accession number: Q8IZD2
Secondary accession number(s): B6ZDE4 expand/collapse secondary AC list , B6ZDM3, M4K8J3, Q6P5Y2, Q6PKG4, Q6T316, Q86TI3, Q86W12, Q86WG0, Q86WL2, Q8IV78, Q8IWR5, Q8NFF8, Q9NWE7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM