HUMAN:KMT2A

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	KMT2A (synonyms: ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1)
Protein Name(s)	Histone-lysine N-methyltransferase 2A Lysine N-methyltransferase 2A ALL-1 CXXC-type zinc finger protein 7 Myeloid/lymphoid or mixed-lineage leukemia Myeloid/lymphoid or mixed-lineage leukemia protein 1 Trithorax-like protein Zinc finger protein HRX MLL cleavage product N320 N-terminal cleavage product of 320 kDa p320 MLL cleavage product C180 C-terminal cleavage product of 180 kDa p180
External Links
UniProt	Q03164
EMBL	L04284 Z69744 Z69745 Z69746 Z69747 Z69748 Z69749 Z69750 Z69751 Z69752 Z69753 Z69754 Z69755 Z69756 Z69757 Z69758 Z69759 Z69760 Z69761 Z69762 Z69763 Z69764 Z69765 Z69766 Z69767 Z69768 Z69769 Z69770 Z69772 Z69773 Z69774 Z69775 Z69776 Z69777 Z69778 Z69779 Z69780 AY373585 AP000941 AP001267 D14540 AB209508 L04731 L01986 X83604 S78570 U04737 S66432 AF232001 AF231998
CCDS	CCDS31686.1 CCDS55791.1
PIR	A44265 I52578 I53035
RefSeq	NP_001184033.1 NP_005924.2
UniGene	Hs.258855
PDB	2AGH 2J2S 2JYI 2KKF 2KU7 2KYU 2LXS 2LXT 2MSR 2W5Y 2W5Z 3EG6 3EMH 3LQH 3LQI 3LQJ 3P4F 3U85 3U88 4ESG 4GQ6 4NW3
PDBsum	2AGH 2J2S 2JYI 2KKF 2KU7 2KYU 2LXS 2LXT 2MSR 2W5Y 2W5Z 3EG6 3EMH 3LQH 3LQI 3LQJ 3P4F 3U85 3U88 4ESG 4GQ6 4NW3
ProteinModelPortal	Q03164
SMR	Q03164
BioGrid	110443
DIP	DIP-29221N
IntAct	Q03164
MINT	MINT-4532017
STRING	9606.ENSP00000352262
ChEMBL	CHEMBL1293299
PhosphoSite	Q03164
DMDM	146345435
MaxQB	Q03164
PaxDb	Q03164
PRIDE	Q03164
Ensembl	ENST00000389506 ENST00000534358
GeneID	4297
KEGG	hsa:4297
UCSC	uc001pta.3
CTD	4297
GeneCards	GC11P118313
HGNC	HGNC:7132
HPA	CAB017794 CAB024270 HPA044910
MIM	159555 605130
neXtProt	NX_Q03164
Orphanet	98837 98831 98835 98836 99860 319182
PharmGKB	PA241
eggNOG	COG2940
GeneTree	ENSGT00760000119228
HOVERGEN	HBG051927
InParanoid	Q03164
KO	K09186
OMA	RIMSPMR
OrthoDB	EOG7XH6NX
PhylomeDB	Q03164
TreeFam	TF319820
ChiTaRS	KMT2A
EvolutionaryTrace	Q03164
GeneWiki	MLL_(gene)
GenomeRNAi	4297
NextBio	16915
PRO	PR:Q03164
Proteomes	UP000005640
Bgee	Q03164
CleanEx	HS_MLL
ExpressionAtlas	Q03164
Genevestigator	Q03164
GO	GO:0005737 GO:0035097 GO:0071339 GO:0005634 GO:0003680 GO:0003682 GO:0042800 GO:0042802 GO:0070577 GO:0042803 GO:0003700 GO:0044212 GO:0045322 GO:0008270 GO:0009952 GO:0006915 GO:0006306 GO:0035162 GO:0051568 GO:0080182 GO:0043984 GO:0008285 GO:2001040 GO:0045944 GO:0045893 GO:0032411 GO:0006461 GO:0051569 GO:0006366
Gene3D	1.20.920.10 3.30.40.10
InterPro	IPR017956 IPR001487 IPR003889 IPR003888 IPR016569 IPR003616 IPR001214 IPR002857 IPR011011 IPR001965 IPR019787 IPR013083
Pfam	PF05965 PF05964 PF00628 PF00856 PF02008
PIRSF	PIRSF010354
SMART	SM00384 SM00297 SM00542 SM00541 SM00249 SM00508 SM00317
SUPFAM	SSF47370 SSF57903
PROSITE	PS50014 PS51543 PS51542 PS50868 PS50280 PS51058 PS01359 PS50016

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0005634	nucleus	PMID:22046413^[1]	ECO:0000314			C	Fig. 2B	complete CACAO 2701
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	GO_REF:0000113	ECO:0005556	multiple sequence alignment evidence used in manual assertion	UniProtKB:A1A5S2 UniProtKB:P13864 UniProtKB:P55200	F	Seeded From UniProt	complete
enables	GO:0000981	DNA-binding transcription factor activity, RNA polymerase II-specific	PMID:19274049^[2]	ECO:0000255	match to sequence model evidence used in manual assertion	InterPro:IPR000637	F	Seeded From UniProt	complete
enables	GO:0045322	unmethylated CpG binding	PMID:20010842^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:22046413^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0000980	RNA polymerase II distal enhancer sequence-specific DNA binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P55200	F	Seeded From UniProt	complete
involved_in	GO:2000615	regulation of histone H3-K9 acetylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P55200	P	Seeded From UniProt	complete
involved_in	GO:0071440	regulation of histone H3-K14 acetylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P55200	P	Seeded From UniProt	complete
involved_in	GO:0051571	positive regulation of histone H3-K4 methylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P55200	P	Seeded From UniProt	complete
involved_in	GO:0032922	circadian regulation of gene expression	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P55200	P	Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:20010842^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1905642	negative regulation of DNA methylation	PMID:20010842^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003700	DNA-binding transcription factor activity	PMID:10821850^[4]	ECO:0000303	author statement without traceable support used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:2001040	positive regulation of cellular response to drug	PMID:20861184^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0080182	histone H3-K4 trimethylation	PMID:20861184^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045944	positive regulation of transcription by RNA polymerase II	PMID:20861184^[5]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032411	positive regulation of transporter activity	PMID:20861184^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0071339	MLL1 complex	PMID:15960975^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0070577	lysine-acetylated histone binding	PMID:19187761^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0051568	histone H3-K4 methylation	PMID:15960975^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0051568	histone H3-K4 methylation	PMID:19556245^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045893	positive regulation of transcription, DNA-templated	PMID:15960975^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0045322	unmethylated CpG binding	PMID:16990798^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0044212	transcription regulatory region DNA binding	PMID:20484083^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0043984	histone H4-K16 acetylation	PMID:15960975^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:11313484^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042800	histone methyltransferase activity (H3-K4 specific)	PMID:15960975^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042800	histone methyltransferase activity (H3-K4 specific)	PMID:19556245^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042800	histone methyltransferase activity (H3-K4 specific)	PMID:19187761^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0035097	histone methyltransferase complex	PMID:19556245^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:19187761^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:16990798^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0065003	protein-containing complex assembly	PMID:15199122^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:11313484^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
	GO:0097692	histone H3-K4 monomethylation	PMID:26324722^[13]	ECO:0000314			P	Figure 1A	complete CACAO 11228
part_of	GO:0005634	nucleus	PMID:1423624^[14]	ECO:0000303	author statement without traceable support used in manual assertion		C	Seeded From UniProt	complete
	GO:0044648	histone H3-K4 dimethylation	PMID:25561738^[15]	ECO:0000314			P	Figure 2C	complete CACAO 11756
enables	GO:0003680	AT DNA binding	PMID:1423624^[14]	ECO:0000303	author statement without traceable support used in manual assertion		F	Seeded From UniProt	complete
	GO:0097692	histone H3-K4 monomethylation	PMID:25561738^[15]	ECO:0000314			P	Figure 2C	complete CACAO 11757
enables	GO:0042800	histone methyltransferase activity (H3-K4 specific)	PMID:22012064^[16]	ECO:0000269	experimental evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:15640349^[17]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:11313484^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q03164	F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:10656681^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q03164	F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002857	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR003888 InterPro:IPR003889	C	Seeded From UniProt	complete
involved_in	GO:0006355	regulation of transcription, DNA-templated	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016569	P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002857 InterPro:IPR016569	F	Seeded From UniProt	complete
part_of	GO:0035097	histone methyltransferase complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016569	C	Seeded From UniProt	complete
enables	GO:0042800	histone methyltransferase activity (H3-K4 specific)	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016569 InterPro:IPR037927	F	Seeded From UniProt	complete
involved_in	GO:0051568	histone H3-K4 methylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016569	P	Seeded From UniProt	complete
part_of	GO:0071339	MLL1 complex	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR037927	C	Seeded From UniProt	complete
enables	GO:0018024	histone-lysine N-methyltransferase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.1.1.43	F	Seeded From UniProt	complete
involved_in	GO:0006366	transcription by RNA polymerase II	PMID:10821850^[4]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0035162	embryonic hemopoiesis	PMID:15618964^[19]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:1902036	regulation of hematopoietic stem cell differentiation	Reactome:R-HSA-8939236	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045652	regulation of megakaryocyte differentiation	Reactome:R-HSA-8936459	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-NUL-8865525 Reactome:R-NUL-8865513 Reactome:R-HSA-8937050 Reactome:R-HSA-8937037 Reactome:R-HSA-8937016 Reactome:R-HSA-8936979 Reactome:R-HSA-8936621 Reactome:R-HSA-8936616 Reactome:R-HSA-8936481 Reactome:R-HSA-8935740 Reactome:R-HSA-8865482 Reactome:R-HSA-5637686 Reactome:R-HSA-5244692 Reactome:R-HSA-5159245	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
involved_in	GO:0006325	chromatin organization	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0156	P	Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0053	P	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
enables	GO:0008168	methyltransferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0489	F	Seeded From UniProt	complete
involved_in	GO:0032259	methylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0489	P	Seeded From UniProt	complete
involved_in	GO:0048511	rhythmic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0090	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Dey, P et al. (2011) Human RNA polymerase II-association factor 1 (hPaf1/PD2) regulates histone methylation and chromatin remodeling in pancreatic cancer. PLoS ONE 6 e26926 PubMed GONUTS page
↑ Vaquerizas, JM et al. (2009) A census of human transcription factors: function, expression and evolution. Nat. Rev. Genet. 10 252-63 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Cierpicki, T et al. (2010) Structure of the MLL CXXC domain-DNA complex and its functional role in MLL-AF9 leukemia. Nat. Struct. Mol. Biol. 17 62-8 PubMed GONUTS page
↑ ^4.0 ^4.1 Choi, Y et al. (2000) Divergent hTAFII31-binding motifs hidden in activation domains. J. Biol. Chem. 275 15912-6 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 Huo, H et al. (2010) Histone methyltransferase MLL1 regulates MDR1 transcription and chemoresistance. Cancer Res. 70 8726-35 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 Dou, Y et al. (2005) Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell 121 873-85 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Southall, SM et al. (2009) Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks. Mol. Cell 33 181-91 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Patel, A et al. (2009) On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. J. Biol. Chem. 284 24242-56 PubMed GONUTS page
↑ ^9.0 ^9.1 Allen, MD et al. (2006) Solution structure of the nonmethyl-CpG-binding CXXC domain of the leukaemia-associated MLL histone methyltransferase. EMBO J. 25 4503-12 PubMed GONUTS page
↑ Nakata, Y et al. (2010) c-Myb, Menin, GATA-3, and MLL form a dynamic transcription complex that plays a pivotal role in human T helper type 2 cell development. Blood 116 1280-90 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Fair, K et al. (2001) Protein interactions of the MLL PHD fingers modulate MLL target gene regulation in human cells. Mol. Cell. Biol. 21 3589-97 PubMed GONUTS page
↑ Yokoyama, A et al. (2004) Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression. Mol. Cell. Biol. 24 5639-49 PubMed GONUTS page
↑ Shinsky, SA & Cosgrove, MS (2015) Unique Role of the WD-40 Repeat Protein 5 (WDR5) Subunit within the Mixed Lineage Leukemia 3 (MLL3) Histone Methyltransferase Complex. J. Biol. Chem. 290 25819-33 PubMed GONUTS page
↑ ^14.0 ^14.1 Tkachuk, DC et al. (1992) Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias. Cell 71 691-700 PubMed GONUTS page
↑ ^15.0 ^15.1 Shinsky, SA et al. (2015) Biochemical reconstitution and phylogenetic comparison of human SET1 family core complexes involved in histone methylation. J. Biol. Chem. 290 6361-75 PubMed GONUTS page
↑ Huang, G et al. (2011) The ability of MLL to bind RUNX1 and methylate H3K4 at PU.1 regulatory regions is impaired by MDS/AML-associated RUNX1/AML1 mutations. Blood 118 6544-52 PubMed GONUTS page
↑ Milne, TA et al. (2005) Menin and MLL cooperatively regulate expression of cyclin-dependent kinase inhibitors. Proc. Natl. Acad. Sci. U.S.A. 102 749-54 PubMed GONUTS page
↑ Rozovskaia, T et al. (2000) Self-association of the SET domains of human ALL-1 and of Drosophila TRITHORAX and ASH1 proteins. Oncogene 19 351-7 PubMed GONUTS page
↑ Li, ZY et al. (2005) New insight into the molecular mechanisms of MLL-associated leukemia. Leukemia 19 183-90 PubMed GONUTS page

[PMID:22046413-1] 1.0 ^1.1 Dey, P et al. (2011) Human RNA polymerase II-association factor 1 (hPaf1/PD2) regulates histone methylation and chromatin remodeling in pancreatic cancer. PLoS ONE 6 e26926 PubMed GONUTS page

[PMID:19274049-2] Vaquerizas, JM et al. (2009) A census of human transcription factors: function, expression and evolution. Nat. Rev. Genet. 10 252-63 PubMed GONUTS page

[PMID:20010842-3] 3.0 ^3.1 ^3.2 Cierpicki, T et al. (2010) Structure of the MLL CXXC domain-DNA complex and its functional role in MLL-AF9 leukemia. Nat. Struct. Mol. Biol. 17 62-8 PubMed GONUTS page

[PMID:10821850-4] 4.0 ^4.1 Choi, Y et al. (2000) Divergent hTAFII31-binding motifs hidden in activation domains. J. Biol. Chem. 275 15912-6 PubMed GONUTS page

[PMID:20861184-5] 5.0 ^5.1 ^5.2 ^5.3 Huo, H et al. (2010) Histone methyltransferase MLL1 regulates MDR1 transcription and chemoresistance. Cancer Res. 70 8726-35 PubMed GONUTS page

[PMID:15960975-6] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 Dou, Y et al. (2005) Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF. Cell 121 873-85 PubMed GONUTS page

[PMID:19187761-7] 7.0 ^7.1 ^7.2 Southall, SM et al. (2009) Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks. Mol. Cell 33 181-91 PubMed GONUTS page

[PMID:19556245-8] 8.0 ^8.1 ^8.2 Patel, A et al. (2009) On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex. J. Biol. Chem. 284 24242-56 PubMed GONUTS page

[PMID:16990798-9] 9.0 ^9.1 Allen, MD et al. (2006) Solution structure of the nonmethyl-CpG-binding CXXC domain of the leukaemia-associated MLL histone methyltransferase. EMBO J. 25 4503-12 PubMed GONUTS page

[PMID:20484083-10] Nakata, Y et al. (2010) c-Myb, Menin, GATA-3, and MLL form a dynamic transcription complex that plays a pivotal role in human T helper type 2 cell development. Blood 116 1280-90 PubMed GONUTS page

[PMID:11313484-11] 11.0 ^11.1 ^11.2 Fair, K et al. (2001) Protein interactions of the MLL PHD fingers modulate MLL target gene regulation in human cells. Mol. Cell. Biol. 21 3589-97 PubMed GONUTS page

[PMID:15199122-12] Yokoyama, A et al. (2004) Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression. Mol. Cell. Biol. 24 5639-49 PubMed GONUTS page

[PMID:26324722-13] Shinsky, SA & Cosgrove, MS (2015) Unique Role of the WD-40 Repeat Protein 5 (WDR5) Subunit within the Mixed Lineage Leukemia 3 (MLL3) Histone Methyltransferase Complex. J. Biol. Chem. 290 25819-33 PubMed GONUTS page

[PMID:1423624-14] 14.0 ^14.1 Tkachuk, DC et al. (1992) Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias. Cell 71 691-700 PubMed GONUTS page

[PMID:25561738-15] 15.0 ^15.1 Shinsky, SA et al. (2015) Biochemical reconstitution and phylogenetic comparison of human SET1 family core complexes involved in histone methylation. J. Biol. Chem. 290 6361-75 PubMed GONUTS page

[PMID:22012064-16] Huang, G et al. (2011) The ability of MLL to bind RUNX1 and methylate H3K4 at PU.1 regulatory regions is impaired by MDS/AML-associated RUNX1/AML1 mutations. Blood 118 6544-52 PubMed GONUTS page

[PMID:15640349-17] Milne, TA et al. (2005) Menin and MLL cooperatively regulate expression of cyclin-dependent kinase inhibitors. Proc. Natl. Acad. Sci. U.S.A. 102 749-54 PubMed GONUTS page

[PMID:10656681-18] Rozovskaia, T et al. (2000) Self-association of the SET domains of human ALL-1 and of Drosophila TRITHORAX and ASH1 proteins. Oncogene 19 351-7 PubMed GONUTS page

[PMID:15618964-19] Li, ZY et al. (2005) New insight into the molecular mechanisms of MLL-associated leukemia. Leukemia 19 183-90 PubMed GONUTS page

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HUMAN:KMT2A

Contents

Annotations

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References

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