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Q03164 (KMT2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 182. Feed History...

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

Names and origin

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

Short name=Lysine N-methyltransferase 2A
EC=2.1.1.43
Alternative name(s):
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

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:KMT2A
Synonyms:ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3969 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.19 Ref.25 Ref.33 Ref.39

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.25 Ref.50

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 KMT2A/MLL1, 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. Interacts with ZNF335. Ref.15 Ref.18 Ref.19 Ref.26 Ref.31 Ref.33 Ref.35 Ref.39 Ref.46 Ref.50

Subcellular location

Nucleus Ref.15.

MLL cleavage product N320: Nucleus Ref.15.

MLL cleavage product C180: Nucleus. Note: Localizes to a diffuse nuclear pattern when not associated with MLL cleavage product N320. Ref.15

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.34 Ref.47 Ref.50

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.34 Ref.47 Ref.50

The CXXC-type zinc finger binds bind to nonmethyl-CpG dinucleotides. Ref.34 Ref.47 Ref.50

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.19 Ref.45

Chromosomal aberrations involving KMT2A 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 KMT2A-MLLT1, KMT2A-MLLT3 and KMT2A-ELL interact with PPP1R15A and, on the contrary to unfused KMT2A, inhibit PPP1R15A-induced apoptosis. Ref.19

A chromosomal aberration involving KMT2A may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with SEPT11. Ref.19

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily. 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 processApoptosis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseProto-oncogene
   DomainBromodomain
Repeat
Zinc-finger
   LigandDNA-binding
Metal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA methylation

Inferred from electronic annotation. Source: Ensembl

anterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

embryonic hemopoiesis

Traceable author statement PubMed 15618964. Source: UniProtKB

histone H3-K4 methylation

Inferred from direct assay Ref.39. Source: UniProtKB

histone H3-K4 trimethylation

Inferred from direct assay PubMed 20861184. Source: BHF-UCL

histone H4-K16 acetylation

Inferred from mutant phenotype Ref.33. Source: UniProtKB

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

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 transcription, DNA-templated

Inferred from mutant phenotype Ref.33. Source: UniProtKB

positive regulation of transporter activity

Inferred from mutant phenotype PubMed 20861184. Source: BHF-UCL

protein complex assembly

Inferred from direct assay Ref.31. Source: UniProtKB

regulation of histone H3-K4 methylation

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement PubMed 10821850. Source: ProtInc

   Cellular_componentMLL1 complex

Inferred from direct assay Ref.33. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

histone methyltransferase complex

Inferred from direct assay Ref.39. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 11313484. Source: UniProtKB

   Molecular_functionAT DNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

histone methyltransferase activity (H3-K4 specific)

Inferred from direct assay Ref.50Ref.39. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 10656681PubMed 11313484. Source: IntAct

lysine-acetylated histone binding

Inferred from direct assay Ref.50. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20581860. Source: IntAct

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.47. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.47Ref.50. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 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 2 (identifier: Q03164-2)

Also known as: 14P-18B;

The sequence of this isoform differs from the canonical sequence as follows:
     1407-1444: Missing.
Isoform 3 (identifier: Q03164-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1603-1603: S → SGTE

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 39693969Histone-lysine N-methyltransferase 2A
PRO_0000124876
Chain1 – 27182718MLL cleavage product N320
PRO_0000390949
Chain2719 – 39691251MLL cleavage product C180
PRO_0000390950

Regions

Domain1703 – 174846Bromo; divergent
Domain2018 – 207457FYR N-terminal
Domain3666 – 374782FYR C-terminal
Domain3829 – 3945117SET
Domain3953 – 396917Post-SET
DNA binding169 – 18012A.T hook 1 Ref.47
DNA binding217 – 22711A.T hook 2 Ref.47
DNA binding301 – 3099A.T hook 3 Ref.47
Zinc finger1147 – 119549CXXC-type
Zinc finger1431 – 148252PHD-type 1
Zinc finger1479 – 153355PHD-type 2
Zinc finger1566 – 162762PHD-type 3
Region3906 – 39072S-adenosyl-L-methionine binding
Motif2847 – 285599aaTAD
Compositional bias17 – 10286Ala/Gly/Ser-rich
Compositional bias137 – 1437Poly-Gly
Compositional bias561 – 5644Poly-Pro
Compositional bias568 – 5714Poly-Pro

Sites

Metal binding39091Zinc
Metal binding39571Zinc
Metal binding39591Zinc
Metal binding39641Zinc
Binding site38391S-adenosyl-L-methionine
Binding site38411S-adenosyl-L-methionine
Binding site38831S-adenosyl-L-methionine
Binding site39581S-adenosyl-L-methionine
Site1334 – 13352Breakpoint for translocation to form KMT2A-ZFYVE19 oncogene
Site1362 – 13632Breakpoint for translocation to form KMT2A-AF3P21 and KMT2A-CASC5 oncogenes
Site1362 – 13632Breakpoint for translocation to form KMT2A-CENPK oncogene
Site13621Breakpoint for translocation to form KMT2A-FRYL fusion protein
Site1406 – 14072Breakpoint for translocation to form KMT2A-AFF4 fusion protein
Site1444 – 14452Breakpoint for translocation to form KMT2A-GAS7 oncogene
Site1444 – 14452Breakpoint for translocation to form KMT2A-LPP
Site2666 – 26672Cleavage; by TASP1, site 1
Site2718 – 27192Cleavage; by TASP1, site 2
Site37651Important for WDR5-recognition and binding

Amino acid modifications

Modified residue1531Phosphoserine Ref.37 Ref.41 Ref.43
Modified residue1971Phosphoserine Ref.37 Ref.43
Modified residue2391N6-acetyllysine By similarity
Modified residue3731N6-acetyllysine By similarity
Modified residue5181Phosphoserine Ref.37
Modified residue6361N6-acetyllysine Ref.42
Modified residue6801Phosphoserine Ref.37
Modified residue8401Phosphothreonine Ref.37
Modified residue9261Phosphoserine Ref.43
Modified residue10561Phosphoserine Ref.37
Modified residue11301N6-acetyllysine Ref.42
Modified residue12351N6-acetyllysine Ref.42
Modified residue18451Phosphothreonine Ref.37
Modified residue18581Phosphoserine Ref.40
Modified residue20981Phosphoserine Ref.37 Ref.41
Modified residue21471Phosphothreonine Ref.37
Modified residue21511Phosphoserine Ref.37
Modified residue22011Phosphoserine Ref.44
Modified residue25251Phosphothreonine Ref.37
Modified residue29551Phosphoserine Ref.37 Ref.43
Modified residue29581N6-acetyllysine By similarity
Modified residue30361Phosphoserine Ref.37
Modified residue33721Phosphothreonine Ref.37 Ref.43
Modified residue34621N6-acetyllysine By similarity
Modified residue35111Phosphoserine Ref.37
Modified residue35151Phosphoserine Ref.41
Cross-link216Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.36
Cross-link220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.36
Cross-link221Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.36

Natural variations

Alternative sequence1407 – 144438Missing in isoform 2.
VSP_006666
Alternative sequence16031S → SGTE in isoform 3.
VSP_046879
Natural variant301A → G. Ref.2
Corresponds to variant rs9332745 [ dbSNP | Ensembl ].
VAR_021317
Natural variant531A → V. Ref.3
Corresponds to variant rs9332747 [ dbSNP | Ensembl ].
VAR_021318
Natural variant5021E → K. Ref.3
Corresponds to variant rs9332772 [ dbSNP | Ensembl ].
VAR_021319
Natural variant19751Q → P.
Corresponds to variant rs693598 [ dbSNP | Ensembl ].
VAR_052652
Natural variant23191S → T. Ref.3
Corresponds to variant rs9332837 [ dbSNP | Ensembl ].
VAR_021320
Natural variant23541P → R. Ref.3
Corresponds to variant rs9332838 [ dbSNP | Ensembl ].
VAR_021321
Natural variant23871Q → R. Ref.3
Corresponds to variant rs9332839 [ dbSNP | Ensembl ].
VAR_021322
Natural variant37141V → I. Ref.3
Corresponds to variant rs9332859 [ dbSNP | Ensembl ].
VAR_021323
Natural variant37731S → A. Ref.3
Corresponds to variant rs9332861 [ dbSNP | Ensembl ].
VAR_021324

Experimental info

Mutagenesis11511R → A: Impairs DNA-binding. Ref.47
Mutagenesis11531R → A: No effect on stability or DNA-binding. Ref.47
Mutagenesis11541R → A: Impairs DNA-binding. Ref.47
Mutagenesis11551C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.47
Mutagenesis11581C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.47
Mutagenesis11611C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.47
Mutagenesis11621Q → A: No effect on stability or DNA-binding. Ref.47
Mutagenesis11661D → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.47
Mutagenesis11671C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.47
Mutagenesis11701C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.47
Mutagenesis11721N → A: No effect on stability or DNA-binding. Ref.47
Mutagenesis11731C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.47
Mutagenesis11751D → A: Impairs DNA-binding. Ref.47
Mutagenesis11761K → A: Impairs DNA-binding. Ref.47
Mutagenesis1178 – 11814KFGG → AAAA: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.47
Mutagenesis11781K → A: Impairs DNA-binding. Ref.47
Mutagenesis11791F → A: Impairs DNA-binding. Ref.47
Mutagenesis11831N → A: Impairs DNA-binding. Ref.47
Mutagenesis11851K → A: Impairs DNA-binding. Ref.47
Mutagenesis11861K → A: Impairs DNA-binding. Ref.47
Mutagenesis11871Q → A: Impairs DNA-binding. Ref.47
Mutagenesis11881C → A: No effect on stability or DNA-binding. Ref.47
Mutagenesis11891C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.47
Mutagenesis11921R → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.47
Mutagenesis11931K → A: Impairs DNA-binding. Ref.47
Mutagenesis11941C → A: Impair zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. Ref.47
Mutagenesis11951Q → A: No effect on stability or DNA-binding. Ref.47
Mutagenesis11961N → A: No effect on stability or DNA-binding. Ref.47
Mutagenesis2666 – 26672DG → AA: Reduces cleavage without abolishing it. Abolishes cleavage by TASP1; when associated with 2718-A--A-2720.
Mutagenesis2718 – 27203DGV → AAA: Abolishes cleavage by TASP1; when associated with 2666-A-A-2667. Ref.15 Ref.26
Mutagenesis38581Y → A: Impairs methyltransferase activity toward unmodified or monomethylated H3K4me. Ref.50
Mutagenesis38581Y → F: Slightly affects methyltransferase activity toward unmodified or monomethylated H3K4me. Ref.50
Mutagenesis38671Q → A: Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3871. Ref.50
Mutagenesis38691D → A: Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3872. Ref.50
Mutagenesis38711R → A: Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3867. Ref.50
Mutagenesis38721E → A: Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3869. Ref.50
Mutagenesis38741Y → A: Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3878. Ref.50
Mutagenesis38781K → A: Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3874. Ref.50
Mutagenesis39061N → A: Loss of the histone H3 methyltransferase activity. Ref.39
Mutagenesis39421Y → A or F: Impairs methyltransferase activity toward unmodified or monomethylated H3K4me. Ref.39 Ref.50
Mutagenesis39421Y → F: Shifts from a specific monomethyltransferase to a di- and trimethyltransferase activity. Ref.39 Ref.50
Sequence conflict1441E → ELTTQIPCSWRTKGHIHDKK TEPFRLLAWSWCLN in CAA93625. Ref.2
Sequence conflict5561Q → E in CAA93625. Ref.2
Sequence conflict5561Q → E in L04731. Ref.6
Sequence conflict13471V → A in AAG26335. Ref.13
Sequence conflict14871R → G in AAA18644. Ref.12
Sequence conflict14901Q → R in AAG26335. Ref.13
Sequence conflict15071P → L in AAG26335. Ref.13
Sequence conflict15131N → T in AAG26335. Ref.13
Sequence conflict16001E → G in AAG26335. Ref.13
Sequence conflict16161S → C in AAB34770. Ref.11
Sequence conflict19371Q → H in AAA92511. Ref.8
Sequence conflict21811P → S in AAA92511. Ref.8
Sequence conflict35561K → N in L04731. Ref.6
Sequence conflict37181R → G in CAA93625. Ref.2
Sequence conflict37591N → D in CAA93625. Ref.2
Sequence conflict38131D → G in CAA93625. Ref.2
Sequence conflict39011A → R in AAA58669. Ref.1

Secondary structure

.......................................................................................... 3969
Helix Strand Turn

Details...

Sequences

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

Last modified May 1, 2007. Version 5.
Checksum: 1150F37EAB1430D3

FASTA3,969431,764
        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 

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Isoform 2 (14P-18B) [UniParc].

Checksum: B8E736C88E83D50B
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FASTA3,931427,733
Isoform 3 [UniParc].

Checksum: 18CFDD8B9A763204
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FASTA3,972432,052

References

« Hide '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] (ISOFORM 3), 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]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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.
[6]"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 (ISOFORM 3), CHROMOSOMAL TRANSLOCATION WITH AFF1/MLLT2.
[7]"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.
[8]"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.
[9]Erratum
Djabali M., Selleri L., Parry P., Bower M., Young B., Evans G.A.
Nat. Genet. 4:431-431(1993) [PubMed] [Europe PMC] [Abstract]
[10]"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 (ISOFORM 3).
[11]"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 2).
[12]"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.
[13]"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: NUCLEOTIDE SEQUENCE [MRNA] OF 1311-1687 (ISOFORM 3), CHROMOSOMAL TRANSLOCATION WITH GAS7.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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.
[24]"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.
[25]"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.
[26]"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.
[27]"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.
[28]"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.
[29]"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.
[30]"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.
[31]"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.
[32]"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.
[33]"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.
[34]"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.
[35]"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.
[36]"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.
Tissue: Lung adenocarcinoma.
[37]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[38]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"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.
[40]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[42]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[43]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[44]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[45]"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.
[46]"Microcephaly gene links trithorax and REST/NRSF to control neural stem cell proliferation and differentiation."
Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D., Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J., Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A., Mahajnah M., Shenhav R., Walsh C.A.
Cell 151:1097-1112(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZNF335.
[47]"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.
[48]"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.
[49]"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.
[50]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L04284 mRNA. Translation: AAA58669.1. Frameshift.
Z69744 expand/collapse EMBL AC list , 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.
AP000941 Genomic DNA. No translation available.
AP001267 Genomic DNA. No translation available.
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.
AF232001 mRNA. Translation: AAG26335.2.
AF231998 mRNA. Translation: AAG26332.2. Sequence problems.
CCDSCCDS31686.1. [Q03164-1]
CCDS55791.1. [Q03164-3]
PIRA44265.
I52578.
I53035.
RefSeqNP_001184033.1. NM_001197104.1. [Q03164-3]
NP_005924.2. NM_005933.3. [Q03164-1]
UniGeneHs.258855.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AGHNMR-C2840-2869[»]
2J2SNMR-A1143-1214[»]
2JYINMR-A1147-1203[»]
2KKFNMR-A1147-1203[»]
2KU7NMR-A1585-1628[»]
2KYUNMR-A1564-1628[»]
2LXSNMR-B2840-2858[»]
2LXTNMR-B2840-2858[»]
2W5YX-ray2.00A3785-3969[»]
2W5ZX-ray2.20A3785-3969[»]
3EG6X-ray1.72C3762-3773[»]
3EMHX-ray1.37B3764-3776[»]
3LQHX-ray1.72A1566-1784[»]
3LQIX-ray1.92A/B/C1566-1784[»]
3LQJX-ray1.90A/B1566-1784[»]
3P4FX-ray2.35C3761-3770[»]
3U85X-ray3.00B6-25[»]
3U88X-ray3.00M/N103-153[»]
4ESGX-ray1.70C/D3755-3771[»]
4GQ6X-ray1.55B6-15[»]
4NW3X-ray2.82A1147-1204[»]
ProteinModelPortalQ03164.
SMRQ03164. Positions 6-39, 103-135, 1146-1214, 1434-1539, 1564-1779, 1872-1977, 2840-2869, 3790-3969.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110443. 75 interactions.
DIPDIP-29221N.
IntActQ03164. 32 interactions.
MINTMINT-4532017.
STRING9606.ENSP00000352262.

Chemistry

ChEMBLCHEMBL1293299.

PTM databases

PhosphoSiteQ03164.

Polymorphism databases

DMDM146345435.

Proteomic databases

MaxQBQ03164.
PaxDbQ03164.
PRIDEQ03164.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354520; ENSP00000346516; ENSG00000118058. [Q03164-2]
ENST00000389506; ENSP00000374157; ENSG00000118058. [Q03164-1]
ENST00000534358; ENSP00000436786; ENSG00000118058. [Q03164-3]
ENST00000594623; ENSP00000471365; ENSG00000267910. [Q03164-2]
ENST00000595462; ENSP00000472616; ENSG00000267910. [Q03164-3]
ENST00000601525; ENSP00000469803; ENSG00000267910. [Q03164-1]
GeneID4297.
KEGGhsa:4297.
UCSCuc001pta.3. human. [Q03164-1]

Organism-specific databases

CTD4297.
GeneCardsGC11P118311.
HGNCHGNC:7132. KMT2A.
HPACAB017794.
CAB024270.
HPA044910.
MIM159555. gene+phenotype.
605130. phenotype.
neXtProtNX_Q03164.
Orphanet98837. Acute biphenotypic leukemia.
98831. Acute myeloid leukemia with 11q23 abnormalities.
98835. Acute undifferentiated leukemia.
98836. Bilineal acute leukemia.
99860. Precursor B-cell acute lymphoblastic leukemia.
319182. Wiedemann-Steiner syndrome.
PharmGKBPA241.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2940.
HOVERGENHBG051927.
InParanoidQ03164.
KOK09186.
OMARIMSPMR.
OrthoDBEOG7XH6NX.
PhylomeDBQ03164.
TreeFamTF319820.

Gene expression databases

ArrayExpressQ03164.
BgeeQ03164.
CleanExHS_MLL.
GenevestigatorQ03164.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.30.40.10. 2 hits.
InterProIPR017956. 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]
PfamPF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 2 hits.
PF00856. SET. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]
PIRSFPIRSF010354. Methyltransferase_trithorax. 1 hit.
SMARTSM00384. 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]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF57903. SSF57903. 2 hits.
PROSITEPS50014. 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]
ProtoNetSearch...

Other

ChiTaRSMLL. human.
EvolutionaryTraceQ03164.
GeneWikiMLL_(gene).
GenomeRNAi4297.
NextBio16915.
PROQ03164.
SOURCESearch...

Entry information

Entry nameKMT2A_HUMAN
AccessionPrimary (citable) accession number: Q03164
Secondary accession number(s): E9PQG7 expand/collapse secondary AC list , Q13743, Q13744, Q14845, Q16364, Q59FF2, Q6UBD1, Q9HBJ3, Q9UD94, Q9UMA3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: May 1, 2007
Last modified: July 9, 2014
This is version 182 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM