HUMAN:MLL1

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Species (Taxon ID)	Homo sapiens (Human). ([1])
Gene Name(s)	MLL (synonyms: ALL1, CXXC7, HRX, HTRX, KMT2A, MLL1, TRX1)
Protein Name(s)	Histone-lysine N-methyltransferase MLL ALL-1 CXXC-type zinc finger protein 7 Lysine N-methyltransferase 2A KMT2A 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
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 D14540 AB209508 L04731 L01986 X83604 S78570 U04737 S66432 AF231998
IPI	IPI00009286 IPI00218500
PIR	A44265 I52578 I53035
RefSeq	NP_001184033.1 NP_005924.2
UniGene	Hs.258855
PDB	2AGH 2J2S 2JYI 2KKF 2KU7 2KYU 2W5Y 2W5Z 3EG6 3EMH 3LQH 3LQI 3LQJ 3P4F
PDBsum	2AGH 2J2S 2JYI 2KKF 2KU7 2KYU 2W5Y 2W5Z 3EG6 3EMH 3LQH 3LQI 3LQJ 3P4F
ProteinModelPortal	Q03164
SMR	Q03164
DIP	DIP-29221N
IntAct	Q03164
STRING	Q03164
PhosphoSite	Q03164
PRIDE	Q03164
Ensembl	ENST00000359313
GeneID	4297
KEGG	hsa:4297
UCSC	uc001pta.1
CTD	4297
GeneCards	GC11P114244
HGNC	HGNC:7132
HPA	CAB017794 CAB024270
MIM	159555
neXtProt	NX_Q03164
Orphanet	86851 99860
PharmGKB	PA241
eggNOG	prNOG07665
HOVERGEN	HBG051927
InParanoid	Q03164
OMA	NGVTQKI
NextBio	16915
ArrayExpress	Q03164
Bgee	Q03164
CleanEx	HS_MLL
Genevestigator	Q03164
GermOnline	ENSG00000118058
GO	GO:0071339 GO:0003680 GO:0070577 GO:0042800 GO:0042803 GO:0003700 GO:0044212 GO:0045322 GO:0008270 GO:0006915 GO:0035162 GO:0043984 GO:0045893 GO:0006461 GO:0006366
InterPro	IPR017956 IPR001487 IPR003889 IPR018516 IPR003888 IPR018518 IPR016569 IPR003616 IPR001214 IPR002857 IPR011011 IPR001965 IPR019787 IPR013083
Gene3D	G3DSA:1.20.920.10 G3DSA:3.30.40.10
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	Evidence Code	with/from	Aspect	Notes	Status
	GO:0003677	DNA binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002857	F	Seeded From UniProt
	GO:0003677	DNA binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR017956	F	Seeded From UniProt
	GO:0003677	DNA binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR018516	F	Seeded From UniProt
	GO:0003677	DNA binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR018518	F	Seeded From UniProt
	GO:0003677	DNA binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0238	F	Seeded From UniProt
	GO:0003680	AT DNA binding	PMID:1423624^[1]	NAS: Non-traceable Author Statement		F	Seeded From UniProt
	GO:0003700	sequence-specific DNA binding transcription factor activity	PMID:10821850^[2]	NAS: Non-traceable Author Statement		F	Seeded From UniProt
	GO:0005515	protein binding	PMID:11313484^[3]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UNP9	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15199122^[4]	IPI: Inferred from Physical Interaction	UniProtKB:O00255	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15960975^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P61964	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15960975^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q15291	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15960975^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9H7Z6	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:15960975^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9H7Z6	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19187761^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q15291	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19187761^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UBL3	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:19556245^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P61964	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20541251^[8]	IPI: Inferred from Physical Interaction	UniProtKB:P68431	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20541251^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UNP9	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20541477^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q6P1J9	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20541477^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q6PD62	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20541477^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q8N7H5	F	Seeded From UniProt
	GO:0005515	protein binding	PMID:20581860^[10]	IPI: Inferred from Physical Interaction	UniProtKB:Q92794	F	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR003888	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR003889	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR018516	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR018518	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C	Seeded From UniProt
	GO:0005634	nucleus	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0191	C	Seeded From UniProt
	GO:0005634	nucleus	PMID:11313484^[3]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005634	nucleus	PMID:1423624^[1]	NAS: Non-traceable Author Statement		C	Seeded From UniProt
	GO:0005634	nucleus	PMID:15640349^[11]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0006351	transcription, DNA-dependent	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0804	P	Seeded From UniProt
	GO:0006355	regulation of transcription, DNA-dependent	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016569	P	Seeded From UniProt
	GO:0006355	regulation of transcription, DNA-dependent	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0805	P	Seeded From UniProt
	GO:0006355	regulation of transcription, DNA-dependent	PMID:10821850^[2]	NAS: Non-traceable Author Statement		P	Seeded From UniProt
	GO:0006366	transcription from RNA polymerase II promoter	PMID:10821850^[2]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0006461	protein complex assembly	PMID:15199122^[4]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0006915	apoptosis	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0053	P	Seeded From UniProt
	GO:0008168	methyltransferase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0489	F	Seeded From UniProt
	GO:0008270	zinc ion binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR001965	F	Seeded From UniProt
	GO:0008270	zinc ion binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002857	F	Seeded From UniProt
	GO:0008270	zinc ion binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016569	F	Seeded From UniProt
	GO:0008270	zinc ion binding	PMID:16990798^[12]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0008270	zinc ion binding	PMID:19187761^[6]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0016568	chromatin modification	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0156	P	Seeded From UniProt
	GO:0016740	transferase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0808	F	Seeded From UniProt
	GO:0018024	histone-lysine N-methyltransferase activity	GO_REF:0000003	IEA: Inferred from Electronic Annotation	EC:2.1.1.43	F	Seeded From UniProt
	GO:0032259	methylation	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0489	P	Seeded From UniProt
	GO:0035097	histone methyltransferase complex	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016569	C	Seeded From UniProt
	GO:0035097	histone methyltransferase complex	PMID:19556245^[7]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0035162	embryonic hemopoiesis	PMID:15618964^[13]	TAS: Traceable Author Statement		P	Seeded From UniProt
	GO:0042800	histone methyltransferase activity (H3-K4 specific)	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016569	F	Seeded From UniProt
	GO:0042800	histone methyltransferase activity (H3-K4 specific)	PMID:15960975^[5]	IMP: Inferred from Mutant Phenotype		F	Seeded From UniProt
	GO:0042800	histone methyltransferase activity (H3-K4 specific)	PMID:19187761^[6]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0042800	histone methyltransferase activity (H3-K4 specific)	PMID:19556245^[7]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0042802	identical protein binding	PMID:10656681^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q03164	F	Seeded From UniProt
	GO:0042803	protein homodimerization activity	PMID:11313484^[3]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0043984	histone H4-K16 acetylation	PMID:15960975^[5]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0044212	transcription regulatory region DNA binding	PMID:20484083^[15]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0045322	unmethylated CpG binding	PMID:16990798^[12]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0045893	positive regulation of transcription, DNA-dependent	PMID:15960975^[5]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0046872	metal ion binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0479	F	Seeded From UniProt
	GO:0051568	histone H3-K4 methylation	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR016569	P	Seeded From UniProt
	GO:0051568	histone H3-K4 methylation	PMID:15960975^[5]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt
	GO:0051568	histone H3-K4 methylation	PMID:19556245^[7]	IDA: Inferred from Direct Assay		P	Seeded From UniProt
	GO:0070577	histone acetyl-lysine binding	PMID:19187761^[6]	IDA: Inferred from Direct Assay		F	Seeded From UniProt
	GO:0071339	MLL1 complex	PMID:15960975^[5]	IDA: Inferred from Direct Assay		C	Seeded From UniProt
	GO:0005634	nucleus	PMID:22046413^[16]	IDA: Inferred from Direct Assay		C	Fig. 2B	complete
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Notes

References

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

↑ ^1.0 ^1.1 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
↑ ^2.0 ^2.1 ^2.2 Choi Y et al. (2000) Divergent hTAFII31-binding motifs hidden in activation domains. J Biol Chem 275: 15912-6 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 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
↑ ^4.0 ^4.1 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
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 ^5.8 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
↑ ^6.0 ^6.1 ^6.2 ^6.3 ^6.4 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
↑ ^7.0 ^7.1 ^7.2 ^7.3 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
↑ ^8.0 ^8.1 Wang Z et al. (2010) Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Cell 141: 1183-94 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Muntean AG et al. (2010) The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. Cancer Cell 17: 609-21 PubMed GONUTS page
↑ Paggetti J et al. (2010) Crosstalk between leukemia-associated proteins MOZ and MLL regulates HOX gene expression in human cord blood CD34+ cells. Oncogene 29: 5019-31 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
↑ ^12.0 ^12.1 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
↑ Li ZY et al. (2005) New insight into the molecular mechanisms of MLL-associated leukemia. Leukemia 19: 183-90 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
↑ 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
↑ 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:1423624-0] 1.0 ^1.1 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:10821850-1] 2.0 ^2.1 ^2.2 Choi Y et al. (2000) Divergent hTAFII31-binding motifs hidden in activation domains. J Biol Chem 275: 15912-6 PubMed GONUTS page

[PMID:11313484-2] 3.0 ^3.1 ^3.2 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:15199122-3] 4.0 ^4.1 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:15960975-4] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 ^5.8 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:19187761-5] 6.0 ^6.1 ^6.2 ^6.3 ^6.4 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:19556245-6] 7.0 ^7.1 ^7.2 ^7.3 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:20541251-7] 8.0 ^8.1 Wang Z et al. (2010) Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression. Cell 141: 1183-94 PubMed GONUTS page

[PMID:20541477-8] 9.0 ^9.1 ^9.2 Muntean AG et al. (2010) The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis. Cancer Cell 17: 609-21 PubMed GONUTS page

[PMID:20581860-9] Paggetti J et al. (2010) Crosstalk between leukemia-associated proteins MOZ and MLL regulates HOX gene expression in human cord blood CD34+ cells. Oncogene 29: 5019-31 PubMed GONUTS page

[PMID:15640349-10] 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:16990798-11] 12.0 ^12.1 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:15618964-12] Li ZY et al. (2005) New insight into the molecular mechanisms of MLL-associated leukemia. Leukemia 19: 183-90 PubMed GONUTS page

[PMID:10656681-13] 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:20484083-14] 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:22046413-15] 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

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[16]

HUMAN:MLL1

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