Q03164 (MLL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone-lysine N-methyltransferase MLL
EC=2.1.1.43

Alternative name(s):
ALL-1
CXXC-type zinc finger protein 7
Lysine N-methyltransferase 2A
Short name=KMT2A
Trithorax-like protein
Zinc finger protein HRX

Cleaved into the following 2 chains:

1. MLL cleavage product N320
   Alternative name(s):
   N-terminal cleavage product of 320 kDa
   Short name=p320
2. MLL cleavage product C180
   Alternative name(s):
   C-terminal cleavage product of 180 kDa
   Short name=p180

Gene names

Name:	MLL
Synonyms:	ALL1, CXXC7, HRX, HTRX, KMT2A, MLL1, TRX1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	3969 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Histone methyltransferase that plays an essential role in early development and hematopoiesis. Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of 'Lys-4' of histone H3 (H3K4me) complex and acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation. Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. Has no activity toward histone H3 phosphorylated on 'Thr-3', less activity toward H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher activity toward H3 acetylated on 'Lys-9'. Required for transcriptional activation of HOXA9. Promotes PPP1R15A-induced apoptosis. Ref.17 Ref.24 Ref.32 Ref.37
Catalytic activity	S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.24 Ref.47
Subunit structure	MLL cleavage product N320 heterodimerizes with MLL cleavage product C180 (via SET and FYRC domains). Component of some MLL1/MLL complex, at least composed of the core components MLL, ASH2L, HCFC1/HCF1, HCFC2, WDR5, DPY30 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with WDR5; the interaction is direct. Interacts with KAT8/MOF; the interaction is direct. Interacts with SBF1 and PPP1R15A. Ref.13 Ref.16 Ref.17 Ref.25 Ref.30 Ref.32 Ref.34 Ref.37 Ref.47
Subcellular location	Nucleus. MLL cleavage product N320: Nucleus. MLL cleavage product C180: Nucleus. Note: Localizes to a diffuse nuclear pattern when not associated with MLL cleavage product N320. Ref.13
Tissue specificity	Heart, lung, brain and T- and B-lymphocytes.
Domain	the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors. Ref.33 Ref.44 Ref.47 The SET domain structure is atypical and is not in an optimal position to have methyltransferase activity. It requires other components of the MLL1/MLL complex, such as ASH2L or RBBP5, to order the active site and obtain optimal histone methyltransferase activity. Ref.33 Ref.44 Ref.47 The CXXC-type zinc finger binds bind to nonmethyl-CpG dinucleotides. Ref.33 Ref.44 Ref.47
Post-translational modification	Proteolytic cleavage by TASP1 generates MLL cleavage product N320 and MLL cleavage product C180, which reassemble through a non-covalent association. 2 cleavage sites exist, cleavage site 1 (CS1) and cleavage site 2 (CS2), to generate MLL cleavage products N320 and C180. CS2 is the major site.
Involvement in disease	Wiedemann-Steiner syndrome (WDSTS) [MIM:605130]: A syndrome characterized by hairy elbows (hypertrichosis cubiti), intellectual disability, a distinctive facial appearance, and short stature. Facial characteristics include long eyelashes, thick or arched eyebrows with a lateral flare, and downslanting and vertically narrow palpebral fissures. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17 Ref.43 Chromosomal aberrations involving MLL are a cause of acute leukemias. Translocation t(1;11)(q21;q23) with MLLT11/AF1Q; translocation t(3;11)(p21;q23) with NCKIPSD/AF3p21; translocation t(3,11)(q25,q23) with GMPS; translocation t(4;11)(q21;q23) with AFF1/MLLT2/AF4; insertion ins(5;11)(q31;q13q23) with AFF4/AF5Q31; translocation t(5;11)(q12;q23) with AF5-alpha/CENPK; translocation t(6;11)(q27;q23) with MLLT4/AF6; translocation t(9;11)(p22;q23) with MLLT3/AF9; translocation t(10;11)(p11.2;q23) with ABI1; translocation t(10;11)(p12;q23) with MLLT10/AF10; t(11;15)(q23;q14) with CASC5 and ZFYVE19; translocation t(11;17)(q23;q21) with MLLT6/AF17; translocation t(11;19)(q23;p13.3) with ELL; translocation t(11;19)(q23;p13.3) with MLLT1/ENL; translocation t(11;19)(q23;p23) with GAS7; translocation t(X;11)(q13;q23) with FOXO4/AFX1. Translocation t(3;11)(q28;q23) with LPP. Translocation t(10;11)(q22;q23) with TET1. Translocation t(9;11)(q34;q23) with DAB2IP. Translocation t(4;11)(p12;q23) with FRYL. Fusion proteins MLL-MLLT1, MLL-MLLT3 and MLL-ELL interact with PPP1R15A and, on the contrary to unfused MLL, inhibit PPP1R15A-induced apoptosis. Ref.17 A chromosomal aberration involving MLL may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with SEPT11. Ref.17
Sequence similarities	Belongs to the histone-lysine methyltransferase family. TRX/MLL subfamily. Contains 3 A.T hook DNA-binding domains. Contains 1 bromo domain. Contains 1 CXXC-type zinc finger. Contains 1 FYR C-terminal domain. Contains 1 FYR N-terminal domain. Contains 3 PHD-type zinc fingers. Contains 1 post-SET domain. Contains 1 SET domain.
Sequence caution	The sequence AAA58669.1 differs from that shown. Reason: Frameshift at positions 317 and 380. The sequence AAG26332.2 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence BAD92745.1 differs from that shown. Reason: Frameshift at position 1098.

Ontologies

Keywords
Biological process	Apoptosis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Bromodomain Repeat Zinc-finger
Ligand	DNA-binding Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Chromatin regulator Methyltransferase Transferase
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW embryonic hemopoiesis Traceable author statement PubMed 15618964. Source: UniProtKB histone H3-K4 trimethylation Inferred from direct assay PubMed 20861184. Source: BHF-UCL histone H4-K16 acetylation Inferred from mutant phenotype Ref.32. Source: UniProtKB positive regulation of cellular response to drug Inferred from mutant phenotype PubMed 20861184. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 20861184. Source: BHF-UCL positive regulation of transporter activity Inferred from mutant phenotype PubMed 20861184. Source: BHF-UCL protein complex assembly Inferred from direct assay Ref.30. Source: UniProtKB transcription from RNA polymerase II promoter Traceable author statement PubMed 10821850. Source: ProtInc
Cellular_component	MLL1 complex Inferred from direct assay Ref.32. Source: UniProtKB
Molecular_function	AT DNA binding Non-traceable author statement Ref.1. Source: UniProtKB histone acetyl-lysine binding Inferred from direct assay Ref.47. Source: UniProtKB histone methyltransferase activity (H3-K4 specific) Inferred from direct assay Ref.47Ref.37. Source: UniProtKB protein homodimerization activity Inferred from direct assay PubMed 11313484. Source: UniProtKB sequence-specific DNA binding transcription factor activity Non-traceable author statement PubMed 10821850. Source: ProtInc transcription regulatory region DNA binding Inferred from direct assay PubMed 20484083. Source: UniProtKB unmethylated CpG binding Inferred from direct assay Ref.44. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.44Ref.47. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		5	EBI-591370,EBI-591370
CDC73	Q6P1J9	4	EBI-591370,EBI-930143
CTR9	Q6PD62	5	EBI-591370,EBI-1019583
HIST1H3D	P68431	10	EBI-591370,EBI-79722
KAT6A	Q92794	10	EBI-2638616,EBI-948013
KAT8	Q9H7Z6	3	EBI-591370,EBI-896414
PAF1	Q8N7H5	4	EBI-591370,EBI-2607770
PPIE	Q9UNP9	5	EBI-591370,EBI-591818
RBBP5	Q15291	4	EBI-591370,EBI-592823
WDR5	P61964	9	EBI-591370,EBI-540834

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q03164-1)

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 14P-18B (identifier: Q03164-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1407-1444: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 3969

3969

Histone-lysine N-methyltransferase MLL

PRO_0000124876

Chain

1 – 2718

2718

MLL cleavage product N320

PRO_0000390949

Chain

2719 – 3969

1251

MLL cleavage product C180

PRO_0000390950

Regions

Domain

1703 – 1748

46

Bromo; divergent

Domain

2018 – 2074

57

FYR N-terminal

Domain

3666 – 3747

82

FYR C-terminal

Domain

3828 – 3949

122

SET

Domain

3953 – 3969

17

Post-SET

DNA binding

169 – 180

12

A.T hook 1 Ref.44

DNA binding

217 – 227

11

A.T hook 2 Ref.44

DNA binding

301 – 309

9

A.T hook 3 Ref.44

Zinc finger

1147 – 1195

49

CXXC-type

Zinc finger

1431 – 1482

52

PHD-type 1

Zinc finger

1479 – 1533

55

PHD-type 2

Zinc finger

1566 – 1627

62

PHD-type 3

Region

3906 – 3907

2

S-adenosyl-L-methionine binding

Motif

2847 – 2855

9

9aaTAD

Compositional bias

17 – 102

86

Ala/Gly/Ser-rich

Compositional bias

137 – 143

7

Poly-Gly

Compositional bias

561 – 564

4

Poly-Pro

Compositional bias

568 – 571

4

Poly-Pro

Sites

Metal binding

3909

1

Zinc

Metal binding

3957

1

Zinc

Metal binding

3959

1

Zinc

Metal binding

3964

1

Zinc

Binding site

3839

1

S-adenosyl-L-methionine

Binding site

3841

1

S-adenosyl-L-methionine

Binding site

3883

1

S-adenosyl-L-methionine

Binding site

3958

1

S-adenosyl-L-methionine

Site

1334 – 1335

2

Breakpoint for translocation to form MLL-ZFYVE19 oncogene

Site

1362 – 1363

2

Breakpoint for translocation to form MLL-AF3P21 and MLL-CASC5 oncogenes

Site

1362 – 1363

2

Breakpoint for translocation to form MLL-CENPK oncogene

Site

1362

1

Breakpoint for translocation to form MLL-FRYL fusion protein

Site

1406 – 1407

2

Breakpoint for translocation to form MLL-AFF4 fusion protein

Site

1444 – 1445

2

Breakpoint for translocation to form MLL-GAS7 oncogene

Site

1444 – 1445

2

Breakpoint for translocation to form MLL-LPP

Site

2666 – 2667

2

Cleavage; by TASP1, site 1

Site

2718 – 2719

2

Cleavage; by TASP1, site 2

Site

3765

1

Important for WDR5-recognition and binding

Amino acid modifications

Modified residue

153

1

Phosphoserine Ref.36 Ref.39 Ref.41

Modified residue

197

1

Phosphoserine Ref.36 Ref.41

Modified residue

518

1

Phosphoserine Ref.36

Modified residue

636

1

N6-acetyllysine Ref.40

Modified residue

680

1

Phosphoserine Ref.36

Modified residue

840

1

Phosphothreonine Ref.36

Modified residue

926

1

Phosphoserine Ref.41

Modified residue

1056

1

Phosphoserine Ref.36

Modified residue

1130

1

N6-acetyllysine Ref.40

Modified residue

1235

1

N6-acetyllysine Ref.40

Modified residue

1845

1

Phosphothreonine Ref.36

Modified residue

1858

1

Phosphoserine Ref.38

Modified residue

2098

1

Phosphoserine Ref.36 Ref.39

Modified residue

2147

1

Phosphothreonine Ref.36

Modified residue

2151

1

Phosphoserine Ref.36

Modified residue

2201

1

Phosphoserine Ref.42

Modified residue

2525

1

Phosphothreonine Ref.36

Modified residue

2955

1

Phosphoserine Ref.36 Ref.41

Modified residue

3036

1

Phosphoserine Ref.36

Modified residue

3372

1

Phosphothreonine Ref.36 Ref.41

Modified residue

3511

1

Phosphoserine Ref.36

Modified residue

3515

1

Phosphoserine Ref.39

Cross-link

216

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.35

Cross-link

220

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.35

Cross-link

221

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.35

Natural variations

Alternative sequence

1407 – 1444

38

Missing in isoform 14P-18B.

VSP_006666

Natural variant

30

1

A → G. Ref.2
Corresponds to variant rs9332745 [ dbSNP | Ensembl ].

VAR_021317

Natural variant

53

1

A → V. Ref.3
Corresponds to variant rs9332747 [ dbSNP | Ensembl ].

VAR_021318

Natural variant

502

1

E → K. Ref.3
Corresponds to variant rs9332772 [ dbSNP | Ensembl ].

VAR_021319

Natural variant

1975

1

Q → P.
Corresponds to variant rs693598 [ dbSNP | Ensembl ].

VAR_052652

Natural variant

2319

1

S → T. Ref.3
Corresponds to variant rs9332837 [ dbSNP | Ensembl ].

VAR_021320

Natural variant

2354

1

P → R. Ref.3
Corresponds to variant rs9332838 [ dbSNP | Ensembl ].

VAR_021321

Natural variant

2387

1

Q → R. Ref.3
Corresponds to variant rs9332839 [ dbSNP | Ensembl ].

VAR_021322

Natural variant

3714

1

V → I. Ref.3
Corresponds to variant rs9332859 [ dbSNP | Ensembl ].

VAR_021323

Natural variant

3773

1

S → A. Ref.3
Corresponds to variant rs9332861 [ dbSNP | Ensembl ].

VAR_021324

Experimental info

Mutagenesis

1151

1

R → A: Impairs DNA-binding. Ref.44

Mutagenesis

1153

1

R → A: No effect on stability or DNA-binding. Ref.44

Mutagenesis

1154

1

R → A: Impairs DNA-binding. Ref.44

Mutagenesis

1155

1

C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.44

Mutagenesis

1158

1

C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.44

Mutagenesis

1161

1

C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.44

Mutagenesis

1162

1

Q → A: No effect on stability or DNA-binding. Ref.44

Mutagenesis

1166

1

D → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.44

Mutagenesis

1167

1

C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.44

Mutagenesis

1170

1

C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.44

Mutagenesis

1172

1

N → A: No effect on stability or DNA-binding. Ref.44

Mutagenesis

1173

1

C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.44

Mutagenesis

1175

1

D → A: Impairs DNA-binding. Ref.44

Mutagenesis

1176

1

K → A: Impairs DNA-binding. Ref.44

Mutagenesis

1178 – 1181

4

KFGG → AAAA: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.44

Mutagenesis

1178

1

K → A: Impairs DNA-binding. Ref.44

Mutagenesis

1179

1

F → A: Impairs DNA-binding. Ref.44

Mutagenesis

1183

1

N → A: Impairs DNA-binding. Ref.44

Mutagenesis

1185

1

K → A: Impairs DNA-binding. Ref.44

Mutagenesis

1186

1

K → A: Impairs DNA-binding. Ref.44

Mutagenesis

1187

1

Q → A: Impairs DNA-binding. Ref.44

Mutagenesis

1188

1

C → A: No effect on stability or DNA-binding. Ref.44

Mutagenesis

1189

1

C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.44

Mutagenesis

1192

1

R → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.44

Mutagenesis

1193

1

K → A: Impairs DNA-binding. Ref.44

Mutagenesis

1194

1

C → A: Impair zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.44

Mutagenesis

1195

1

Q → A: No effect on stability or DNA-binding. Ref.44

Mutagenesis

1196

1

N → A: No effect on stability or DNA-binding. Ref.44

Mutagenesis

2666 – 2667

2

DG → AA: Reduces cleavage without abolishing it. Abolishes cleavage by TASP1; when associated with 2718-A--A-2720.

Mutagenesis

2718 – 2720

3

DGV → AAA: Abolishes cleavage by TASP1; when associated with 2666-A-A-2667. Ref.13 Ref.25

Mutagenesis

3858

1

Y → A: Impairs methyltransferase activity toward unmodified or monomethylated H3K4me. Ref.47

Mutagenesis

3858

1

Y → F: Slightly affects methyltransferase activity toward unmodified or monomethylated H3K4me. Ref.47

Mutagenesis

3867

1

Q → A: Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3871. Ref.47

Mutagenesis

3869

1

D → A: Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3872. Ref.47

Mutagenesis

3871

1

R → A: Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3867. Ref.47

Mutagenesis

3872

1

E → A: Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3869. Ref.47

Mutagenesis

3874

1

Y → A: Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3878. Ref.47

Mutagenesis

3878

1

K → A: Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3874. Ref.47

Mutagenesis

3906

1

N → A: Loss of the histone H3 methyltransferase activity. Ref.37

Mutagenesis

3942

1

Y → A or F: Impairs methyltransferase activity toward unmodified or monomethylated H3K4me. Ref.37 Ref.47

Mutagenesis

3942

1

Y → F: Shifts from a specific monomethyltransferase to a di- and trimethyltransferase activity. Ref.37 Ref.47

Sequence conflict

144

1

E → ELTTQIPCSWRTKGHIHDKK TEPFRLLAWSWCLN in CAA93625. Ref.2

Sequence conflict

556

1

Q → E in CAA93625. Ref.2

Sequence conflict

556

1

Q → E in L04731. Ref.5

Sequence conflict

1487

1

R → G in AAA18644. Ref.11

Sequence conflict

1603

1

S → SGTE in CAA93625. Ref.2

Sequence conflict

1603

1

S → SGTE in L04731. Ref.5

Sequence conflict

1603

1

S → SGTE in CAA58584. Ref.9

Sequence conflict

1616

1

S → C in AAB34770. Ref.10

Sequence conflict

1937

1

Q → H in AAA92511. Ref.7

Sequence conflict

2181

1

P → S in AAA92511. Ref.7

Sequence conflict

3556

1

K → N in L04731. Ref.5

Sequence conflict

3718

1

R → G in CAA93625. Ref.2

Sequence conflict

3759

1

N → D in CAA93625. Ref.2

Sequence conflict

3813

1

D → G in CAA93625. Ref.2

Sequence conflict

3901

1

A → R in AAA58669. Ref.1

Secondary structure

1

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3969

Helix Strand Turn

Details...

Helix

24 – 28

5

Beta strand

33 – 35

3

Helix

114 – 133

20

Beta strand

1151 – 1154

4

Beta strand

1156 – 1158

3

Turn

1159 – 1162

4

Beta strand

1168 – 1170

3

Helix

1171 – 1174

4

Helix

1177 – 1179

3

Beta strand

1183 – 1185

3

Turn

1190 – 1192

3

Beta strand

1197 – 1200

4

Turn

1204 – 1206

3

Beta strand

1566 – 1568

3

Turn

1570 – 1572

3

Beta strand

1575 – 1577

3

Turn

1578 – 1582

5

Beta strand

1585 – 1587

3

Turn

1589 – 1591

3

Beta strand

1594 – 1596

3

Helix

1597 – 1599

3

Helix

1604 – 1612

9

Helix

1614 – 1617

4

Turn

1622 – 1624

3

Beta strand

1627 – 1629

3

Helix

1631 – 1652

22

Helix

1655 – 1661

7

Helix

1708 – 1716

9

Helix

1723 – 1740

18

Helix

1745 – 1765

21

Helix

1771 – 1773

3

Helix

2847 – 2856

10

Helix

3764 – 3766

3

Helix

3796 – 3799

4

Helix

3809 – 3811

3

Helix

3816 – 3820

5

Helix

3823 – 3830

8

Beta strand

3831 – 3835

5

Beta strand

3837 – 3847

11

Beta strand

3854 – 3857

4

Beta strand

3860 – 3864

5

Helix

3865 – 3867

3

Helix

3868 – 3878

11

Beta strand

3884 – 3886

3

Beta strand

3888 – 3894

7

Turn

3896 – 3898

3

Helix

3901 – 3904

4

Beta strand

3912 – 3920

9

Beta strand

3923 – 3932

10

Beta strand

3939 – 3942

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2007. Version 5. Checksum: 1150F37EAB1430D3	FASTA	3,969	431,764
	10 20 30 40 50 60 MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPPVGGGG PGAPPSPPAV 70 80 90 100 110 120 AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS SGPALLRVGP GFDAALQVSA 130 140 150 160 170 180 AIGTNLRRFR AVFGESGGGG GSGEDEQFLG FGSDEEVRVR SPTRSPSVKT SPRKPRGRPR 190 200 210 220 230 240 SGSDRNSAIL SDPSVFSPLN KSETKSGDKI KKKDSKSIEK KRGRPPTFPG VKIKITHGKD 250 260 270 280 290 300 ISELPKGNKE DSLKKIKRTP SATFQQATKI KKLRAGKLSP LKSKFKTGKL QIGRKGVQIV 310 320 330 340 350 360 RRRGRPPSTE RIKTPSGLLI NSELEKPQKV RKDKEGTPPL TKEDKTVVRQ SPRRIKPVRI 370 380 390 400 410 420 IPSSKRTDAT IAKQLLQRAK KGAQKKIEKE AAQLQGRKVK TQVKNIRQFI MPVVSAISSR 430 440 450 460 470 480 IIKTPRRFIE DEDYDPPIKI ARLESTPNSR FSAPSCGSSE KSSAASQHSS QMSSDSSRSS 490 500 510 520 530 540 SPSVDTSTDS QASEEIQVLP EERSDTPEVH PPLPISQSPE NESNDRRSRR YSVSERSFGS 550 560 570 580 590 600 RTTKKLSTLQ SAPQQQTSSS PPPPLLTPPP PLQPASSISD HTPWLMPPTI PLASPFLPAS 610 620 630 640 650 660 TAPMQGKRKS ILREPTFRWT SLKHSRSEPQ YFSSAKYAKE GLIRKPIFDN FRPPPLTPED 670 680 690 700 710 720 VGFASGFSAS GTAASARLFS PLHSGTRFDM HKRSPLLRAP RFTPSEAHSR IFESVTLPSN 730 740 750 760 770 780 RTSAGTSSSG VSNRKRKRKV FSPIRSEPRS PSHSMRTRSG RLSSSELSPL TPPSSVSSSL 790 800 810 820 830 840 SISVSPLATS ALNPTFTFPS HSLTQSGESA EKNQRPRKQT SAPAEPFSSS SPTPLFPWFT 850 860 870 880 890 900 PGSQTERGRN KDKAPEELSK DRDADKSVEK DKSRERDRER EKENKRESRK EKRKKGSEIQ 910 920 930 940 950 960 SSSALYPVGR VSKEKVVGED VATSSSAKKA TGRKKSSSHD SGTDITSVTL GDTTAVKTKI 970 980 990 1000 1010 1020 LIKKGRGNLE KTNLDLGPTA PSLEKEKTLC LSTPSSSTVK HSTSSIGSML AQADKLPMTD 1030 1040 1050 1060 1070 1080 KRVASLLKKA KAQLCKIEKS KSLKQTDQPK AQGQESDSSE TSVRGPRIKH VCRRAAVALG 1090 1100 1110 1120 1130 1140 RKRAVFPDDM PTLSALPWEE REKILSSMGN DDKSSIAGSE DAEPLAPPIK PIKPVTRNKA 1150 1160 1170 1180 1190 1200 PQEPPVKKGR RSRRCGQCPG CQVPEDCGVC TNCLDKPKFG GRNIKKQCCK MRKCQNLQWM 1210 1220 1230 1240 1250 1260 PSKAYLQKQA KAVKKKEKKS KTSEKKDSKE SSVVKNVVDS SQKPTPSARE DPAPKKSSSE 1270 1280 1290 1300 1310 1320 PPPRKPVEEK SEEGNVSAPG PESKQATTPA SRKSSKQVSQ PALVIPPQPP TTGPPRKEVP 1330 1340 1350 1360 1370 1380 KTTPSEPKKK QPPPPESGPE QSKQKKVAPR PSIPVKQKPK EKEKPPPVNK QENAGTLNIL 1390 1400 1410 1420 1430 1440 STLSNGNSSK QKIPADGVHR IRVDFKEDCE AENVWEMGGL GILTSVPITP RVVCFLCASS 1450 1460 1470 1480 1490 1500 GHVEFVYCQV CCEPFHKFCL EENERPLEDQ LENWCCRRCK FCHVCGRQHQ ATKQLLECNK 1510 1520 1530 1540 1550 1560 CRNSYHPECL GPNYPTKPTK KKKVWICTKC VRCKSCGSTT PGKGWDAQWS HDFSLCHDCA 1570 1580 1590 1600 1610 1620 KLFAKGNFCP LCDKCYDDDD YESKMMQCGK CDRWVHSKCE NLSDEMYEIL SNLPESVAYT 1630 1640 1650 1660 1670 1680 CVNCTERHPA EWRLALEKEL QISLKQVLTA LLNSRTTSHL LRYRQAAKPP DLNPETEESI 1690 1700 1710 1720 1730 1740 PSRSSPEGPD PPVLTEVSKQ DDQQPLDLEG VKRKMDQGNY TSVLEFSDDI VKIIQAAINS 1750 1760 1770 1780 1790 1800 DGGQPEIKKA NSMVKSFFIR QMERVFPWFS VKKSRFWEPN KVSSNSGMLP NAVLPPSLDH 1810 1820 1830 1840 1850 1860 NYAQWQEREE NSHTEQPPLM KKIIPAPKPK GPGEPDSPTP LHPPTPPILS TDRSREDSPE 1870 1880 1890 1900 1910 1920 LNPPPGIEDN RQCALCLTYG DDSANDAGRL LYIGQNEWTH VNCALWSAEV FEDDDGSLKN 1930 1940 1950 1960 1970 1980 VHMAVIRGKQ LRCEFCQKPG ATVGCCLTSC TSNYHFMCSR AKNCVFLDDK KVYCQRHRDL 1990 2000 2010 2020 2030 2040 IKGEVVPENG FEVFRRVFVD FEGISLRRKF LNGLEPENIH MMIGSMTIDC LGILNDLSDC 2050 2060 2070 2080 2090 2100 EDKLFPIGYQ CSRVYWSTTD ARKRCVYTCK IVECRPPVVE PDINSTVEHD ENRTIAHSPT 2110 2120 2130 2140 2150 2160 SFTESSSKES QNTAEIISPP SPDRPPHSQT SGSCYYHVIS KVPRIRTPSY SPTQRSPGCR 2170 2180 2190 2200 2210 2220 PLPSAGSPTP TTHEIVTVGD PLLSSGLRSI GSRRHSTSSL SPQRSKLRIM SPMRTGNTYS 2230 2240 2250 2260 2270 2280 RNNVSSVSTT GTATDLESSA KVVDHVLGPL NSSTSLGQNT STSSNLQRTV VTVGNKNSHL 2290 2300 2310 2320 2330 2340 DGSSSSEMKQ SSASDLVSKS SSLKGEKTKV LSSKSSEGSA HNVAYPGIPK LAPQVHNTTS 2350 2360 2370 2380 2390 2400 RELNVSKIGS FAEPSSVSFS SKEALSFPHL HLRGQRNDRD QHTDSTQSAN SSPDEDTEVK 2410 2420 2430 2440 2450 2460 TLKLSGMSNR SSIINEHMGS SSRDRRQKGK KSCKETFKEK HSSKSFLEPG QVTTGEEGNL 2470 2480 2490 2500 2510 2520 KPEFMDEVLT PEYMGQRPCN NVSSDKIGDK GLSMPGVPKA PPMQVEGSAK ELQAPRKRTV 2530 2540 2550 2560 2570 2580 KVTLTPLKME NESQSKNALK ESSPASPLQI ESTSPTEPIS ASENPGDGPV AQPSPNNTSC 2590 2600 2610 2620 2630 2640 QDSQSNNYQN LPVQDRNLML PDGPKPQEDG SFKRRYPRRS ARARSNMFFG LTPLYGVRSY 2650 2660 2670 2680 2690 2700 GEEDIPFYSS STGKKRGKRS AEGQVDGADD LSTSDEDDLY YYNFTRTVIS SGGEERLASH 2710 2720 2730 2740 2750 2760 NLFREEEQCD LPKISQLDGV DDGTESDTSV TATTRKSSQI PKRNGKENGT ENLKIDRPED 2770 2780 2790 2800 2810 2820 AGEKEHVTKS SVGHKNEPKM DNCHSVSRVK TQGQDSLEAQ LSSLESSRRV HTSTPSDKNL 2830 2840 2850 2860 2870 2880 LDTYNTELLK SDSDNNNSDD CGNILPSDIM DFVLKNTPSM QALGESPESS SSELLNLGEG 2890 2900 2910 2920 2930 2940 LGLDSNREKD MGLFEVFSQQ LPTTEPVDSS VSSSISAEEQ FELPLELPSD LSVLTTRSPT 2950 2960 2970 2980 2990 3000 VPSQNPSRLA VISDSGEKRV TITEKSVASS ESDPALLSPG VDPTPEGHMT PDHFIQGHMD 3010 3020 3030 3040 3050 3060 ADHISSPPCG SVEQGHGNNQ DLTRNSSTPG LQVPVSPTVP IQNQKYVPNS TDSPGPSQIS 3070 3080 3090 3100 3110 3120 NAAVQTTPPH LKPATEKLIV VNQNMQPLYV LQTLPNGVTQ KIQLTSSVSS TPSVMETNTS 3130 3140 3150 3160 3170 3180 VLGPMGGGLT LTTGLNPSLP TSQSLFPSAS KGLLPMSHHQ HLHSFPAATQ SSFPPNISNP 3190 3200 3210 3220 3230 3240 PSGLLIGVQP PPDPQLLVSE SSQRTDLSTT VATPSSGLKK RPISRLQTRK NKKLAPSSTP 3250 3260 3270 3280 3290 3300 SNIAPSDVVS NMTLINFTPS QLPNHPSLLD LGSLNTSSHR TVPNIIKRSK SSIMYFEPAP 3310 3320 3330 3340 3350 3360 LLPQSVGGTA ATAAGTSTIS QDTSHLTSGS VSGLASSSSV LNVVSMQTTT TPTSSASVPG 3370 3380 3390 3400 3410 3420 HVTLTNPRLL GTPDIGSISN LLIKASQQSL GIQDQPVALP PSSGMFPQLG TSQTPSTAAI 3430 3440 3450 3460 3470 3480 TAASSICVLP STQTTGITAA SPSGEADEHY QLQHVNQLLA SKTGIHSSQR DLDSASGPQV 3490 3500 3510 3520 3530 3540 SNFTQTVDAP NSMGLEQNKA LSSAVQASPT SPGGSPSSPS SGQRSASPSV PGPTKPKPKT 3550 3560 3570 3580 3590 3600 KRFQLPLDKG NGKKHKVSHL RTSSSEAHIP DQETTSLTSG TGTPGAEAEQ QDTASVEQSS 3610 3620 3630 3640 3650 3660 QKECGQPAGQ VAVLPEVQVT QNPANEQESA EPKTVEEEES NFSSPLMLWL QQEQKRKESI 3670 3680 3690 3700 3710 3720 TEKKPKKGLV FEISSDDGFQ ICAESIEDAW KSLTDKVQEA RSNARLKQLS FAGVNGLRML 3730 3740 3750 3760 3770 3780 GILHDAVVFL IEQLSGAKHC RNYKFRFHKP EEANEPPLNP HGSARAEVHL RKSAFDMFNF 3790 3800 3810 3820 3830 3840 LASKHRQPPE YNPNDEEEEE VQLKSARRAT SMDLPMPMRF RHLKKTSKEA VGVYRSPIHG 3850 3860 3870 3880 3890 3900 RGLFCKRNID AGEMVIEYAG NVIRSIQTDK REKYYDSKGI GCYMFRIDDS EVVDATMHGN 3910 3920 3930 3940 3950 3960 AARFINHSCE PNCYSRVINI DGQKHIVIFA MRKIYRGEEL TYDYKFPIED ASNKLPCNCG AKKCRKFLN
	Isoform 14P-18B [UniParc]. Checksum: B8E736C88E83D50B	FASTA	3,931	427,733
	10 20 30 40 50 60 MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPPVGGGG PGAPPSPPAV 70 80 90 100 110 120 AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS SGPALLRVGP GFDAALQVSA 130 140 150 160 170 180 AIGTNLRRFR AVFGESGGGG GSGEDEQFLG FGSDEEVRVR SPTRSPSVKT SPRKPRGRPR 190 200 210 220 230 240 SGSDRNSAIL SDPSVFSPLN KSETKSGDKI KKKDSKSIEK KRGRPPTFPG VKIKITHGKD 250 260 270 280 290 300 ISELPKGNKE DSLKKIKRTP SATFQQATKI KKLRAGKLSP LKSKFKTGKL QIGRKGVQIV 310 320 330 340 350 360 RRRGRPPSTE RIKTPSGLLI NSELEKPQKV RKDKEGTPPL TKEDKTVVRQ SPRRIKPVRI 370 380 390 400 410 420 IPSSKRTDAT IAKQLLQRAK KGAQKKIEKE AAQLQGRKVK TQVKNIRQFI MPVVSAISSR 430 440 450 460 470 480 IIKTPRRFIE DEDYDPPIKI ARLESTPNSR FSAPSCGSSE KSSAASQHSS QMSSDSSRSS 490 500 510 520 530 540 SPSVDTSTDS QASEEIQVLP EERSDTPEVH PPLPISQSPE NESNDRRSRR YSVSERSFGS 550 560 570 580 590 600 RTTKKLSTLQ SAPQQQTSSS PPPPLLTPPP PLQPASSISD HTPWLMPPTI PLASPFLPAS 610 620 630 640 650 660 TAPMQGKRKS ILREPTFRWT SLKHSRSEPQ YFSSAKYAKE GLIRKPIFDN FRPPPLTPED 670 680 690 700 710 720 VGFASGFSAS GTAASARLFS PLHSGTRFDM HKRSPLLRAP RFTPSEAHSR IFESVTLPSN 730 740 750 760 770 780 RTSAGTSSSG VSNRKRKRKV FSPIRSEPRS PSHSMRTRSG RLSSSELSPL TPPSSVSSSL 790 800 810 820 830 840 SISVSPLATS ALNPTFTFPS HSLTQSGESA EKNQRPRKQT SAPAEPFSSS SPTPLFPWFT 850 860 870 880 890 900 PGSQTERGRN KDKAPEELSK DRDADKSVEK DKSRERDRER EKENKRESRK EKRKKGSEIQ 910 920 930 940 950 960 SSSALYPVGR VSKEKVVGED VATSSSAKKA TGRKKSSSHD SGTDITSVTL GDTTAVKTKI 970 980 990 1000 1010 1020 LIKKGRGNLE KTNLDLGPTA PSLEKEKTLC LSTPSSSTVK HSTSSIGSML AQADKLPMTD 1030 1040 1050 1060 1070 1080 KRVASLLKKA KAQLCKIEKS KSLKQTDQPK AQGQESDSSE TSVRGPRIKH VCRRAAVALG 1090 1100 1110 1120 1130 1140 RKRAVFPDDM PTLSALPWEE REKILSSMGN DDKSSIAGSE DAEPLAPPIK PIKPVTRNKA 1150 1160 1170 1180 1190 1200 PQEPPVKKGR RSRRCGQCPG CQVPEDCGVC TNCLDKPKFG GRNIKKQCCK MRKCQNLQWM 1210 1220 1230 1240 1250 1260 PSKAYLQKQA KAVKKKEKKS KTSEKKDSKE SSVVKNVVDS SQKPTPSARE DPAPKKSSSE 1270 1280 1290 1300 1310 1320 PPPRKPVEEK SEEGNVSAPG PESKQATTPA SRKSSKQVSQ PALVIPPQPP TTGPPRKEVP 1330 1340 1350 1360 1370 1380 KTTPSEPKKK QPPPPESGPE QSKQKKVAPR PSIPVKQKPK EKEKPPPVNK QENAGTLNIL 1390 1400 1410 1420 1430 1440 STLSNGNSSK QKIPADGVHR IRVDFKFVYC QVCCEPFHKF CLEENERPLE DQLENWCCRR 1450 1460 1470 1480 1490 1500 CKFCHVCGRQ HQATKQLLEC NKCRNSYHPE CLGPNYPTKP TKKKKVWICT KCVRCKSCGS 1510 1520 1530 1540 1550 1560 TTPGKGWDAQ WSHDFSLCHD CAKLFAKGNF CPLCDKCYDD DDYESKMMQC GKCDRWVHSK 1570 1580 1590 1600 1610 1620 CENLSDEMYE ILSNLPESVA YTCVNCTERH PAEWRLALEK ELQISLKQVL TALLNSRTTS 1630 1640 1650 1660 1670 1680 HLLRYRQAAK PPDLNPETEE SIPSRSSPEG PDPPVLTEVS KQDDQQPLDL EGVKRKMDQG 1690 1700 1710 1720 1730 1740 NYTSVLEFSD DIVKIIQAAI NSDGGQPEIK KANSMVKSFF IRQMERVFPW FSVKKSRFWE 1750 1760 1770 1780 1790 1800 PNKVSSNSGM LPNAVLPPSL DHNYAQWQER EENSHTEQPP LMKKIIPAPK PKGPGEPDSP 1810 1820 1830 1840 1850 1860 TPLHPPTPPI LSTDRSREDS PELNPPPGIE DNRQCALCLT YGDDSANDAG RLLYIGQNEW 1870 1880 1890 1900 1910 1920 THVNCALWSA EVFEDDDGSL KNVHMAVIRG KQLRCEFCQK PGATVGCCLT SCTSNYHFMC 1930 1940 1950 1960 1970 1980 SRAKNCVFLD DKKVYCQRHR DLIKGEVVPE NGFEVFRRVF VDFEGISLRR KFLNGLEPEN 1990 2000 2010 2020 2030 2040 IHMMIGSMTI DCLGILNDLS DCEDKLFPIG YQCSRVYWST TDARKRCVYT CKIVECRPPV 2050 2060 2070 2080 2090 2100 VEPDINSTVE HDENRTIAHS PTSFTESSSK ESQNTAEIIS PPSPDRPPHS QTSGSCYYHV 2110 2120 2130 2140 2150 2160 ISKVPRIRTP SYSPTQRSPG CRPLPSAGSP TPTTHEIVTV GDPLLSSGLR SIGSRRHSTS 2170 2180 2190 2200 2210 2220 SLSPQRSKLR IMSPMRTGNT YSRNNVSSVS TTGTATDLES SAKVVDHVLG PLNSSTSLGQ 2230 2240 2250 2260 2270 2280 NTSTSSNLQR TVVTVGNKNS HLDGSSSSEM KQSSASDLVS KSSSLKGEKT KVLSSKSSEG 2290 2300 2310 2320 2330 2340 SAHNVAYPGI PKLAPQVHNT TSRELNVSKI GSFAEPSSVS FSSKEALSFP HLHLRGQRND 2350 2360 2370 2380 2390 2400 RDQHTDSTQS ANSSPDEDTE VKTLKLSGMS NRSSIINEHM GSSSRDRRQK GKKSCKETFK 2410 2420 2430 2440 2450 2460 EKHSSKSFLE PGQVTTGEEG NLKPEFMDEV LTPEYMGQRP CNNVSSDKIG DKGLSMPGVP 2470 2480 2490 2500 2510 2520 KAPPMQVEGS AKELQAPRKR TVKVTLTPLK MENESQSKNA LKESSPASPL QIESTSPTEP 2530 2540 2550 2560 2570 2580 ISASENPGDG PVAQPSPNNT SCQDSQSNNY QNLPVQDRNL MLPDGPKPQE DGSFKRRYPR 2590 2600 2610 2620 2630 2640 RSARARSNMF FGLTPLYGVR SYGEEDIPFY SSSTGKKRGK RSAEGQVDGA DDLSTSDEDD 2650 2660 2670 2680 2690 2700 LYYYNFTRTV ISSGGEERLA SHNLFREEEQ CDLPKISQLD GVDDGTESDT SVTATTRKSS 2710 2720 2730 2740 2750 2760 QIPKRNGKEN GTENLKIDRP EDAGEKEHVT KSSVGHKNEP KMDNCHSVSR VKTQGQDSLE 2770 2780 2790 2800 2810 2820 AQLSSLESSR RVHTSTPSDK NLLDTYNTEL LKSDSDNNNS DDCGNILPSD IMDFVLKNTP 2830 2840 2850 2860 2870 2880 SMQALGESPE SSSSELLNLG EGLGLDSNRE KDMGLFEVFS QQLPTTEPVD SSVSSSISAE 2890 2900 2910 2920 2930 2940 EQFELPLELP SDLSVLTTRS PTVPSQNPSR LAVISDSGEK RVTITEKSVA SSESDPALLS 2950 2960 2970 2980 2990 3000 PGVDPTPEGH MTPDHFIQGH MDADHISSPP CGSVEQGHGN NQDLTRNSST PGLQVPVSPT 3010 3020 3030 3040 3050 3060 VPIQNQKYVP NSTDSPGPSQ ISNAAVQTTP PHLKPATEKL IVVNQNMQPL YVLQTLPNGV 3070 3080 3090 3100 3110 3120 TQKIQLTSSV SSTPSVMETN TSVLGPMGGG LTLTTGLNPS LPTSQSLFPS ASKGLLPMSH 3130 3140 3150 3160 3170 3180 HQHLHSFPAA TQSSFPPNIS NPPSGLLIGV QPPPDPQLLV SESSQRTDLS TTVATPSSGL 3190 3200 3210 3220 3230 3240 KKRPISRLQT RKNKKLAPSS TPSNIAPSDV VSNMTLINFT PSQLPNHPSL LDLGSLNTSS 3250 3260 3270 3280 3290 3300 HRTVPNIIKR SKSSIMYFEP APLLPQSVGG TAATAAGTST ISQDTSHLTS GSVSGLASSS 3310 3320 3330 3340 3350 3360 SVLNVVSMQT TTTPTSSASV PGHVTLTNPR LLGTPDIGSI SNLLIKASQQ SLGIQDQPVA 3370 3380 3390 3400 3410 3420 LPPSSGMFPQ LGTSQTPSTA AITAASSICV LPSTQTTGIT AASPSGEADE HYQLQHVNQL 3430 3440 3450 3460 3470 3480 LASKTGIHSS QRDLDSASGP QVSNFTQTVD APNSMGLEQN KALSSAVQAS PTSPGGSPSS 3490 3500 3510 3520 3530 3540 PSSGQRSASP SVPGPTKPKP KTKRFQLPLD KGNGKKHKVS HLRTSSSEAH IPDQETTSLT 3550 3560 3570 3580 3590 3600 SGTGTPGAEA EQQDTASVEQ SSQKECGQPA GQVAVLPEVQ VTQNPANEQE SAEPKTVEEE 3610 3620 3630 3640 3650 3660 ESNFSSPLML WLQQEQKRKE SITEKKPKKG LVFEISSDDG FQICAESIED AWKSLTDKVQ 3670 3680 3690 3700 3710 3720 EARSNARLKQ LSFAGVNGLR MLGILHDAVV FLIEQLSGAK HCRNYKFRFH KPEEANEPPL 3730 3740 3750 3760 3770 3780 NPHGSARAEV HLRKSAFDMF NFLASKHRQP PEYNPNDEEE EEVQLKSARR ATSMDLPMPM 3790 3800 3810 3820 3830 3840 RFRHLKKTSK EAVGVYRSPI HGRGLFCKRN IDAGEMVIEY AGNVIRSIQT DKREKYYDSK 3850 3860 3870 3880 3890 3900 GIGCYMFRID DSEVVDATMH GNAARFINHS CEPNCYSRVI NIDGQKHIVI FAMRKIYRGE 3910 3920 3930 ELTYDYKFPI EDASNKLPCN CGAKKCRKFL N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias." Tkachuk D.C., Kohler S., Cleary M.L. Cell 71:691-700(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Exon/intron structure of the human ALL-1 (MLL) gene involved in translocations to chromosomal region 11q23 and acute leukaemias." Nilson I., Loechner K., Siegler G., Greil J., Beck J.D., Fey G.H., Marschalek R. Br. J. Haematol. 93:966-972(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-30.
[3]	NIEHS SNPs program Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-53; LYS-502; THR-2319; ARG-2354; ARG-2387; ILE-3714 AND ALA-3773.
[4]	"Two distinct portions of LTG19/ENL at 19p13 are involved in t(11;19) leukemia." Yamamoto K., Seto M., Komatsu H., Iida S., Akao Y., Kojima S., Kodera Y., Nakazawa S., Ariyoshi Y., Takahashi T., Ueda R. Oncogene 8:2617-2625(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1909.
[5]	"The t(4;11) chromosome translocation of human acute leukemias fuses the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene." Gu Y., Nakamura T., Alder H., Prasad R., Canaani O., Cimino G., Croce C.M., Canaani E. Cell 71:701-708(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 63-3969, CHROMOSOMAL TRANSLOCATION WITH AFF1/MLLT2.
[6]	"Homo sapiens protein coding cDNA." Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 812-3969. Tissue: Brain.
[7]	"A trithorax-like gene is interrupted by chromosome 11q23 translocations in acute leukaemias." Djabali M., Selleri L., Parry P., Bower M., Young B.D., Evans G.A. Nat. Genet. 2:113-118(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1112-1140 AND 1552-162, NUCLEOTIDE SEQUENCE [MRNA] OF 1317-2328. Tissue: Brain.
[8]	Erratum Djabali M., Selleri L., Parry P., Bower M., Young B., Evans G.A. Nat. Genet. 4:431-431(1993) [PubMed] [Europe PMC] [Abstract]
[9]	"Molecular analysis of the chromosomal breakpoint and fusion transcripts in the acute lymphoblastic SEM cell line with chromosomal translocation t(4;11)." Marschalek R., Greil J., Lochner K., Nilson I., Siegler G., Zweckbronner I., Beck J.D., Fey G.H. Br. J. Haematol. 90:308-320(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1212-1603.
[10]	"The human MLL gene: nucleotide sequence, homology to the Drosophila trx zinc-finger domain, and alternative splicing." Mbangkollo D., Burnett R., McCabe N., Thirman M., Gill H., Yu H., Rowley J.D., Diaz M.O. DNA Cell Biol. 14:475-483(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1251-1654 (ISOFORM 14P-18B).
[11]	"Sequence analysis of the breakpoint cluster region in the ALL-1 gene involved in acute leukemia." Gu Y., Alder H., Nakamura T., Schichman S.A., Prasad R., Canaani O., Saito H., Croce C.M., Canaani E. Cancer Res. 54:2327-2330(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1251-1538.
[12]	"A method for identifying genes within yeast artificial chromosomes: application to isolation of MLL fusion cDNAs from acute leukaemia translocations." Forster A., Rabbitts T.H. Oncogene 8:3157-3160(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1421-1540.
[13]	"Proteolytic cleavage of MLL generates a complex of N- and C-terminal fragments that confers protein stability and subnuclear localization." Hsieh J.J.-D., Ernst P., Erdjument-Bromage H., Tempst P., Korsmeyer S.J. Mol. Cell. Biol. 23:186-194(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2719-2730, CLEAVAGE, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF 2718-ASP--VAL-2720.
[14]	"Fusion of the MLL gene with two different genes, AF-6 and AF-5alpha, by a complex translocation involving chromosomes 5, 6, 8 and 11 in infant leukemia." Taki T., Hayashi Y., Taniwaki M., Seto M., Ueda R., Hanada R., Suzukawa K., Yokota J., Morishita K. Oncogene 13:2121-2130(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH CENPK.
[15]	"ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL gene in acute myeloid leukemia with t(10;11)(p11.2;q23)." Taki T., Shibuya N., Taniwaki M., Hanada R., Morishita K., Bessho F., Yanagisawa M., Hayashi Y. Blood 92:1125-1130(1998) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH ABI1.
[16]	"Association of SET domain and myotubularin-related proteins modulates growth control." Cui X., De Vivo I., Slany R., Miyamoto A., Firestein R., Cleary M.L. Nat. Genet. 18:331-337(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SBF1.
[17]	"Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and associate with the GADD34 and hSNF5/INI1 proteins." Adler H.T., Chinery R., Wu D.Y., Kussick S.J., Payne J.M., Fornace A.J. Jr., Tkachuk D.C. Mol. Cell. Biol. 19:7050-7060(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPP1R15A, DISEASE, FUNCTION.
[18]	"AF5q31, a newly identified AF4-related gene, is fused to MLL in infant acute lymphoblastic leukemia with ins(5;11)(q31;q13q23)." Taki T., Kano H., Taniwaki M., Sako M., Yanagisawa M., Hayashi Y. Proc. Natl. Acad. Sci. U.S.A. 96:14535-14540(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH AFF4. Tissue: Placenta.
[19]	"Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed lineage leukemia protein in a therapy-related leukemia with t(3;11)(p21;q23)." Sano K., Hayakawa A., Piao J.-H., Kosaka Y., Nakamura H. Blood 95:1066-1068(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH NCKIPSD/AF3P21.
[20]	"t(3;11) translocation in treatment-related acute myeloid leukemia fuses MLL with the GMPS (guanosine 5-prime monophosphate synthetase) gene." Pegram L.D., Megonigal M.D., Lange B.J., Nowell P.C., Rowley J.D., Rappaport E.F., Felix C.A. Blood 96:4360-4362(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH GMPS.
[21]	"Detection of leukemia-associated MLL-GAS7 translocation early during chemotherapy with DNA topoisomerase II inhibitors." Megonigal M.D., Cheung N.-K.V., Rappaport E.F., Nowell P.C., Wilson R.B., Jones D.H., Addya K., Leonard D.G.B., Kushner B.H., Williams T.M., Lange B.J., Felix C.A. Proc. Natl. Acad. Sci. U.S.A. 97:2814-2819(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH GAS7.
[22]	"Human LPP gene is fused to MLL in a secondary acute leukemia with a t(3;11) (q28;q23)." Daheron L., Veinstein A., Brizard F., Drabkin H., Lacotte L., Guilhot F., Larsen C.J., Brizard A., Roche J. Genes Chromosomes Cancer 31:382-389(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH LPP.
[23]	"LCX, leukemia-associated protein with a CXXC domain, is fused to MLL in acute myeloid leukemia with trilineage dysplasia having t(10;11)(q22;q23)." Ono R., Taki T., Taketani T., Taniwaki M., Kobayashi H., Hayashi Y. Cancer Res. 62:4075-4080(2002) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH TET1.
[24]	"ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation." Nakamura T., Mori T., Tada S., Krajewski W., Rozovskaia T., Wassell R., Dubois G., Mazo A., Croce C.M., Canaani E. Mol. Cell 10:1119-1128(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[25]	"Taspase1: a threonine aspartase required for cleavage of MLL and proper HOX gene expression." Hsieh J.J.-D., Cheng E.H.-Y., Korsmeyer S.J. Cell 115:293-303(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE, INTERACTION WITH TASP1, MUTAGENESIS OF 2666-ASP-GLY-2667 AND 2718-ASP--VAL-2720.
[26]	"A t(11;15) fuses MLL to two different genes, AF15q14 and a novel gene MPFYVE on chromosome 15." Chinwalla V., Chien A., Odero M., Neilly M.B., Zeleznik-Le N.J., Rowley J.D. Oncogene 22:1400-1410(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH ZFYVE19 AND CASC5.
[27]	"Characterization of the MLL partner gene AF15q14 involved in t(11;15)(q23;q14)." Kuefer M.U., Chinwalla V., Zeleznik-Le N.J., Behm F.G., Naeve C.W., Rakestraw K.M., Mukatira S.T., Raimondi S.C., Morris S.W. Oncogene 22:1418-1424(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH CASC5.
[28]	"Identification of a novel RAS GTPase-activating protein (RASGAP) gene at 9q34 as an MLL fusion partner in a patient with de novo acute myeloid leukemia." von Bergh A.R.M., Wijers P.M., Groot A.J., van Zelderen-Bhola S., Falkenburg J.H.F., Kluin P.M., Schuuring E. Genes Chromosomes Cancer 39:324-334(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH DAB2IP.
[29]	"FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell line CNLBC1 derived from chronic neutrophilic leukemia in transformation with t(4;11)(q21;q23)." Kojima K., Sakai I., Hasegawa A., Niiya H., Azuma T., Matsuo Y., Fujii N., Tanimoto M., Fujita S. Leukemia 18:998-1005(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH SEPT11.
[30]	"Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression." Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J., Kitabayashi I., Herr W., Cleary M.L. Mol. Cell. Biol. 24:5639-5649(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[31]	"AF4p12, a human homologue to the furry gene of Drosophila, as a novel MLL fusion partner." Hayette S., Cornillet-Lefebvre P., Tigaud I., Struski S., Forissier S., Berchet A., Doll D., Gillot L., Brahim W., Delabesse E., Magaud J.-P., Rimokh R. Cancer Res. 65:6521-6525(2005) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH FRYL.
[32]	"Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF." Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G. Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE MLL1/MLL COMPLEX, INTERACTION WITH KAT8.
[33]	"Nine-amino-acid transactivation domain: establishment and prediction utilities." Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M. Genomics 89:756-768(2007) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN.
[34]	"PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex." Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T., Dressler G.R., Copeland T.D., Kalkum M., Ge K. J. Biol. Chem. 282:20395-20406(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
[35]	"The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells." Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D. J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-216; LYS-220 AND LYS-221, MASS SPECTROMETRY. Tissue: Lung adenocarcinoma.
[36]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-197; SER-518; SER-680; THR-840; SER-1056; THR-1845; SER-2098; THR-2147; SER-2151; THR-2525; SER-2955; SER-3036; THR-3372 AND SER-3511, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[37]	"On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex." Patel A., Dharmarajan V., Vought V.E., Cosgrove M.S. J. Biol. Chem. 284:24242-24256(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CHARACTERIZATION OF THE MLL1/MLL COMPLEX, INTERACTION WITH WDR5, MUTAGENESIS OF ASN-3906 AND TYR-3942.
[38]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1858, MASS SPECTROMETRY.
[39]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-2098 AND SER-3515, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[40]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-636; LYS-1130 AND LYS-1235, MASS SPECTROMETRY.
[41]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-197; SER-926; SER-2955 AND THR-3372, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[42]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2201, MASS SPECTROMETRY.
[43]	"De novo mutations in MLL cause Wiedemann-Steiner syndrome." Jones W.D., Dafou D., McEntagart M., Woollard W.J., Elmslie F.V., Holder-Espinasse M., Irving M., Saggar A.K., Smithson S., Trembath R.C., Deshpande C., Simpson M.A. Am. J. Hum. Genet. 91:358-364(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN WDSTS.
[44]	"Solution structure of the nonmethyl-CpG-binding CXXC domain of the leukaemia-associated MLL histone methyltransferase." Allen M.D., Grummitt C.G., Hilcenko C., Min S.Y., Tonkin L.M., Johnson C.M., Freund S.M., Bycroft M., Warren A.J. EMBO J. 25:4503-4512(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1146-1214 IN COMPLEX WITH ZINC, DOMAIN CXXC-TYPE ZINC FINGER, DNA-BINDING, MUTAGENESIS OF ARG-1151; ARG-1153; ARG-1154; CYS-1155; CYS-1158; CYS-1161; GLN-1162; ASP-1166; CYS-1167; CYS-1170; ASN-1172; CYS-1173; ASP-1175; LYS-1176; 1178-LYS--GLY-1181; LYS-1178; PHE-1179; ASN-1183; LYS-1185; LYS-1186; GLN-1187; CYS-1188; CYS-1189; ARG-1192; LYS-1193; CYS-1194; GLN-1195 AND ASN-1196.
[45]	"Structural basis for cooperative transcription factor binding to the CBP coactivator." De Guzman R.N., Goto N.K., Dyson H.J., Wright P.E. J. Mol. Biol. 355:1005-1013(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2842-2869 IN COMPLEX WITH CREBBP.
[46]	"Structure of WDR5 bound to mixed lineage leukemia protein-1 peptide." Patel A., Dharmarajan V., Cosgrove M.S. J. Biol. Chem. 283:32158-32161(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.37 ANGSTROMS) OF 3764-3776 IN COMPLEX WITH WDR5.
[47]	"Structural basis for the requirement of additional factors for MLL1 SET domain activity and recognition of epigenetic marks." Southall S.M., Wong P.S., Odho Z., Roe S.M., Wilson J.R. Mol. Cell 33:181-191(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3785-3969 IN COMPLEX WITH ZINC; S-ADENOSYL-L-HOMOCYSTEINE AND HISTONE H3 PEPTIDE, CATALYTIC ACTIVITY, DOMAIN SET, INTERACTION WITH ASH2L AND RBBP5, MUTAGENESIS OF TYR-3858; GLN-3867; ASP-3869; ARG-3871; GLU-3872; TYR-3874; LYS-3878 AND TYR-3942.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L04284 mRNA. Translation: AAA58669.1. Frameshift.
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 Genomic DNA. Translation: CAA93625.1.
AY373585 Genomic DNA. Translation: AAQ63624.1.
D14540 mRNA. Translation: BAA03407.1.
AB209508 mRNA. Translation: BAD92745.1. Frameshift.
L04731 mRNA. No translation available.
L01986 mRNA. Translation: AAA92511.1.
X83604 Genomic DNA. Translation: CAA58584.1.
S78570 mRNA. Translation: AAB34770.1.
U04737 Genomic DNA. Translation: AAA18644.1.
S66432 mRNA. Translation: AAB28545.1.
AF231998 mRNA. Translation: AAG26332.2. Sequence problems.

IPI

IPI00009286.
IPI00218500.

PIR

A44265.
I52578.
I53035.

RefSeq

NP_001184033.1. NM_001197104.1.
NP_005924.2. NM_005933.3.

UniGene

Hs.258855.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AGH	NMR	-	C	2842-2869	[»]
2J2S	NMR	-	A	1146-1214	[»]
2JYI	NMR	-	A	1147-1203	[»]
2KKF	NMR	-	A	1147-1203	[»]
2KU7	NMR	-	A	1585-1628	[»]
2KYU	NMR	-	A	1564-1628	[»]
2W5Y	X-ray	2.00	A	3785-3969	[»]
2W5Z	X-ray	2.20	A	3785-3969	[»]
3EG6	X-ray	1.72	C	3762-3773	[»]
3EMH	X-ray	1.37	B	3764-3776	[»]
3LQH	X-ray	1.72	A	1566-1784	[»]
3LQI	X-ray	1.92	A/B/C	1566-1784	[»]
3LQJ	X-ray	1.90	A/B	1566-1784	[»]
3P4F	X-ray	2.35	C	3761-3770	[»]
3U85	X-ray	3.00	B	6-25	[»]
3U88	X-ray	3.00	M/N	6-153	[»]
4ESG	X-ray	1.70	C/D	3755-3771	[»]
4GQ6	X-ray	1.55	B	6-15	[»]

ProteinModelPortal

Q03164.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29221N.

IntAct

Q03164. 31 interactions.

STRING

9606.ENSP00000352262.

PTM databases

PhosphoSite

Q03164.

Polymorphism databases

DMDM

146345435.

Proteomic databases

PaxDb

Q03164.

PRIDE

Q03164.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000354520; ENSP00000346516; ENSG00000118058.
ENST00000389506; ENSP00000374157; ENSG00000118058.
ENST00000594623; ENSP00000471365; ENSG00000267910.
ENST00000601525; ENSP00000469803; ENSG00000267910.

GeneID

4297.

KEGG

hsa:4297.

UCSC

uc001pta.3. human.

Organism-specific databases

CTD

4297.

GeneCards

GC11P118341.

HGNC

HGNC:7132. MLL.

HPA

CAB017794.
CAB024270.

MIM

159555. gene+phenotype.
605130. phenotype.

neXtProt

NX_Q03164.

Orphanet

86851. Acute leukemia of ambiguous lineage.
98831. Acute myeloid leukemia with 11q23 abnormalities.
99860. Precursor B-cell acute lymphoblastic leukemia.

PharmGKB

PA241.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2940.

HOVERGEN

HBG051927.

InParanoid

Q03164.

KO

K09186.

Gene expression databases

ArrayExpress

Q03164.

Bgee

Q03164.

CleanEx

HS_MLL.

Genevestigator

Q03164.

GermOnline

ENSG00000118058. Homo sapiens.

Family and domain databases

Gene3D

1.20.920.10. 1 hit.
3.30.40.10. 2 hits.

InterPro

IPR017956. AT_hook_DNA-bd_motif.
IPR001487. Bromodomain.
IPR003889. FYrich_C.
IPR003888. FYrich_N.
IPR016569. MeTrfase_trithorax.
IPR003616. Post-SET_dom.
IPR001214. SET_dom.
IPR002857. Znf_CXXC.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]

Pfam

PF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 2 hits.
PF00856. SET. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]

PIRSF

PIRSF010354. Methyltransferase_trithorax. 1 hit.

SMART

SM00384. AT_hook. 3 hits.
SM00297. BROMO. 1 hit.
SM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
SM00249. PHD. 4 hits.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]

SUPFAM

SSF47370. Bromodomain. 1 hit.
SSF57903. FYVE_PHD_ZnF. 2 hits.

PROSITE

PS50014. BROMODOMAIN_2. 1 hit.
PS51543. FYRC. 1 hit.
PS51542. FYRN. 1 hit.
PS50868. POST_SET. 1 hit.
PS50280. SET. 1 hit.
PS51058. ZF_CXXC. 1 hit.
PS01359. ZF_PHD_1. 3 hits.
PS50016. ZF_PHD_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1293299.

ChiTaRS

MLL. human.

EvolutionaryTrace

Q03164.

GenomeRNAi

4297.

NextBio

16915.

SOURCE

Search...

Entry information

Entry name

MLL1_HUMAN

Accession

Primary (citable) accession number: Q03164
Secondary accession number(s): Q13743 , Q13744, Q14845, Q16364, Q59FF2, Q6UBD1, Q9UD94, Q9UMA3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	May 1, 2007
Last modified:	May 1, 2013
This is version 168 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.