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Q03164

- KMT2A_HUMAN

UniProt

Q03164 - KMT2A_HUMAN

Protein

Histone-lysine N-methyltransferase 2A

Gene

KMT2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 184 (01 Oct 2014)
      Sequence version 5 (01 May 2007)
      Previous versions | rss
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    Functioni

    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.4 Publications

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1334 – 13352Breakpoint for translocation to form KMT2A-ZFYVE19 oncogene
    Sitei1362 – 13632Breakpoint for translocation to form KMT2A-AF3P21 and KMT2A-CASC5 oncogenes
    Sitei1362 – 13632Breakpoint for translocation to form KMT2A-CENPK oncogene
    Sitei1362 – 13621Breakpoint for translocation to form KMT2A-FRYL fusion protein
    Sitei1406 – 14072Breakpoint for translocation to form KMT2A-AFF4 fusion protein
    Sitei1444 – 14452Breakpoint for translocation to form KMT2A-GAS7 oncogene
    Sitei1444 – 14452Breakpoint for translocation to form KMT2A-LPP
    Sitei2666 – 26672Cleavage; by TASP1, site 1
    Sitei2718 – 27192Cleavage; by TASP1, site 2
    Sitei3765 – 37651Important for WDR5-recognition and binding
    Binding sitei3839 – 38391S-adenosyl-L-methionine
    Binding sitei3841 – 38411S-adenosyl-L-methionine
    Binding sitei3883 – 38831S-adenosyl-L-methionine
    Metal bindingi3909 – 39091Zinc2 Publications
    Metal bindingi3957 – 39571Zinc2 Publications
    Binding sitei3958 – 39581S-adenosyl-L-methionine
    Metal bindingi3959 – 39591Zinc2 Publications
    Metal bindingi3964 – 39641Zinc2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi169 – 18012A.T hook 1Add
    BLAST
    DNA bindingi217 – 22711A.T hook 2Add
    BLAST
    DNA bindingi301 – 3099A.T hook 3
    Zinc fingeri1147 – 119549CXXC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1431 – 148252PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1479 – 153355PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1566 – 162762PHD-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. AT DNA binding Source: UniProtKB
    2. chromatin binding Source: Ensembl
    3. histone methyltransferase activity (H3-K4 specific) Source: UniProtKB
    4. identical protein binding Source: IntAct
    5. lysine-acetylated histone binding Source: UniProtKB
    6. protein binding Source: IntAct
    7. protein homodimerization activity Source: UniProtKB
    8. sequence-specific DNA binding transcription factor activity Source: ProtInc
    9. transcription regulatory region DNA binding Source: UniProtKB
    10. unmethylated CpG binding Source: UniProtKB
    11. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. anterior/posterior pattern specification Source: Ensembl
    2. apoptotic process Source: UniProtKB-KW
    3. DNA methylation Source: Ensembl
    4. embryonic hemopoiesis Source: UniProtKB
    5. histone H3-K4 methylation Source: UniProtKB
    6. histone H3-K4 trimethylation Source: BHF-UCL
    7. histone H4-K16 acetylation Source: UniProtKB
    8. negative regulation of cell proliferation Source: Ensembl
    9. positive regulation of cellular response to drug Source: BHF-UCL
    10. positive regulation of transcription, DNA-templated Source: UniProtKB
    11. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    12. positive regulation of transporter activity Source: BHF-UCL
    13. protein complex assembly Source: UniProtKB
    14. regulation of histone H3-K4 methylation Source: Ensembl
    15. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Chromatin regulator, Methyltransferase, Transferase

    Keywords - Biological processi

    Apoptosis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, S-adenosyl-L-methionine, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase 2A (EC:2.1.1.43)
    Short name:
    Lysine N-methyltransferase 2A
    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:
    Alternative name(s):
    N-terminal cleavage product of 320 kDa
    Short name:
    p320
    Alternative name(s):
    C-terminal cleavage product of 180 kDa
    Short name:
    p180
    Gene namesi
    Name:KMT2A
    Synonyms:ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:7132. KMT2A.

    Subcellular locationi

    Nucleus 1 Publication
    Chain MLL cleavage product C180 : Nucleus
    Note: Localizes to a diffuse nuclear pattern when not associated with MLL cleavage product N320.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. histone methyltransferase complex Source: UniProtKB
    3. MLL1 complex Source: UniProtKB
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.1 Publication
    A chromosomal aberration involving KMT2A may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with SEPT11.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1151 – 11511R → A: Impairs DNA-binding. 1 Publication
    Mutagenesisi1153 – 11531R → A: No effect on stability or DNA-binding. 1 Publication
    Mutagenesisi1154 – 11541R → A: Impairs DNA-binding. 1 Publication
    Mutagenesisi1155 – 11551C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. 1 Publication
    Mutagenesisi1158 – 11581C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. 1 Publication
    Mutagenesisi1161 – 11611C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. 1 Publication
    Mutagenesisi1162 – 11621Q → A: No effect on stability or DNA-binding. 1 Publication
    Mutagenesisi1166 – 11661D → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. 1 Publication
    Mutagenesisi1167 – 11671C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. 1 Publication
    Mutagenesisi1170 – 11701C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. 1 Publication
    Mutagenesisi1172 – 11721N → A: No effect on stability or DNA-binding. 1 Publication
    Mutagenesisi1173 – 11731C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. 1 Publication
    Mutagenesisi1175 – 11751D → A: Impairs DNA-binding. 1 Publication
    Mutagenesisi1176 – 11761K → A: Impairs DNA-binding. 1 Publication
    Mutagenesisi1178 – 11814KFGG → AAAA: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. 1 Publication
    Mutagenesisi1178 – 11781K → A: Impairs DNA-binding. 1 Publication
    Mutagenesisi1179 – 11791F → A: Impairs DNA-binding. 1 Publication
    Mutagenesisi1183 – 11831N → A: Impairs DNA-binding. 1 Publication
    Mutagenesisi1185 – 11851K → A: Impairs DNA-binding. 1 Publication
    Mutagenesisi1186 – 11861K → A: Impairs DNA-binding. 1 Publication
    Mutagenesisi1187 – 11871Q → A: Impairs DNA-binding. 1 Publication
    Mutagenesisi1188 – 11881C → A: No effect on stability or DNA-binding. 1 Publication
    Mutagenesisi1189 – 11891C → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. 1 Publication
    Mutagenesisi1192 – 11921R → A: Abolishes zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. 1 Publication
    Mutagenesisi1193 – 11931K → A: Impairs DNA-binding. 1 Publication
    Mutagenesisi1194 – 11941C → A: Impair zinc-binding, leading to unfold the CXXC-type zinc finger and abolish DNA-binding. 1 Publication
    Mutagenesisi1195 – 11951Q → A: No effect on stability or DNA-binding. 1 Publication
    Mutagenesisi1196 – 11961N → A: No effect on stability or DNA-binding. 1 Publication
    Mutagenesisi2666 – 26672DG → AA: Reduces cleavage without abolishing it. Abolishes cleavage by TASP1; when associated with 2718-A--A-2720.
    Mutagenesisi2718 – 27203DGV → AAA: Abolishes cleavage by TASP1; when associated with 2666-A-A-2667.
    Mutagenesisi3858 – 38581Y → A: Impairs methyltransferase activity toward unmodified or monomethylated H3K4me. 1 Publication
    Mutagenesisi3858 – 38581Y → F: Slightly affects methyltransferase activity toward unmodified or monomethylated H3K4me. 1 Publication
    Mutagenesisi3867 – 38671Q → A: Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3871. 1 Publication
    Mutagenesisi3869 – 38691D → A: Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3872. 1 Publication
    Mutagenesisi3871 – 38711R → A: Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3867. 1 Publication
    Mutagenesisi3872 – 38721E → A: Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3869. 1 Publication
    Mutagenesisi3874 – 38741Y → A: Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3878. 1 Publication
    Mutagenesisi3878 – 38781K → A: Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3874. 1 Publication
    Mutagenesisi3906 – 39061N → A: Loss of the histone H3 methyltransferase activity. 1 Publication
    Mutagenesisi3942 – 39421Y → A or F: Impairs methyltransferase activity toward unmodified or monomethylated H3K4me. 2 Publications
    Mutagenesisi3942 – 39421Y → F: Shifts from a specific monomethyltransferase to a di- and trimethyltransferase activity. 2 Publications

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    MIMi159555. gene+phenotype.
    605130. phenotype.
    Orphaneti98837. 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.
    PharmGKBiPA241.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 39693969Histone-lysine N-methyltransferase 2APRO_0000124876Add
    BLAST
    Chaini1 – 27182718MLL cleavage product N320PRO_0000390949Add
    BLAST
    Chaini2719 – 39691251MLL cleavage product C180PRO_0000390950Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei153 – 1531Phosphoserine3 Publications
    Modified residuei197 – 1971Phosphoserine2 Publications
    Cross-linki216 – 216Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki220 – 220Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki221 – 221Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei239 – 2391N6-acetyllysineBy similarity
    Modified residuei373 – 3731N6-acetyllysineBy similarity
    Modified residuei518 – 5181Phosphoserine1 Publication
    Modified residuei636 – 6361N6-acetyllysine1 Publication
    Modified residuei680 – 6801Phosphoserine1 Publication
    Modified residuei840 – 8401Phosphothreonine1 Publication
    Modified residuei926 – 9261Phosphoserine1 Publication
    Modified residuei1056 – 10561Phosphoserine1 Publication
    Modified residuei1130 – 11301N6-acetyllysine1 Publication
    Modified residuei1235 – 12351N6-acetyllysine1 Publication
    Modified residuei1845 – 18451Phosphothreonine1 Publication
    Modified residuei1858 – 18581Phosphoserine1 Publication
    Modified residuei2098 – 20981Phosphoserine2 Publications
    Modified residuei2147 – 21471Phosphothreonine1 Publication
    Modified residuei2151 – 21511Phosphoserine1 Publication
    Modified residuei2201 – 22011Phosphoserine1 Publication
    Modified residuei2525 – 25251Phosphothreonine1 Publication
    Modified residuei2955 – 29551Phosphoserine2 Publications
    Modified residuei2958 – 29581N6-acetyllysineBy similarity
    Modified residuei3036 – 30361Phosphoserine1 Publication
    Modified residuei3372 – 33721Phosphothreonine2 Publications
    Modified residuei3462 – 34621N6-acetyllysineBy similarity
    Modified residuei3511 – 35111Phosphoserine1 Publication
    Modified residuei3515 – 35151Phosphoserine1 Publication

    Post-translational modificationi

    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.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ03164.
    PaxDbiQ03164.
    PRIDEiQ03164.

    PTM databases

    PhosphoSiteiQ03164.

    Expressioni

    Tissue specificityi

    Heart, lung, brain and T- and B-lymphocytes.

    Gene expression databases

    ArrayExpressiQ03164.
    BgeeiQ03164.
    CleanExiHS_MLL.
    GenevestigatoriQ03164.

    Organism-specific databases

    HPAiCAB017794.
    CAB024270.
    HPA044910.

    Interactioni

    Subunit structurei

    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 ZNF335.13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself5EBI-591370,EBI-591370
    CDC73Q6P1J94EBI-591370,EBI-930143
    CrebbpP454817EBI-591370,EBI-296306From a different organism.
    CTR9Q6PD625EBI-591370,EBI-1019583
    HIST1H3DP6843111EBI-591370,EBI-79722
    KAT6AQ9279410EBI-2638616,EBI-948013
    KAT8Q9H7Z63EBI-591370,EBI-896414
    PAF1Q8N7H54EBI-591370,EBI-2607770
    PAX5Q025482EBI-2610266,EBI-296331
    PPIEQ9UNP94EBI-591370,EBI-591818
    RBBP5Q152916EBI-591370,EBI-592823
    WDR5P6196410EBI-591370,EBI-540834

    Protein-protein interaction databases

    BioGridi110443. 77 interactions.
    DIPiDIP-29221N.
    IntActiQ03164. 33 interactions.
    MINTiMINT-4532017.
    STRINGi9606.ENSP00000352262.

    Structurei

    Secondary structure

    1
    3969
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi114 – 13320
    Beta strandi1151 – 11544
    Beta strandi1156 – 11583
    Helixi1159 – 11624
    Beta strandi1168 – 11703
    Helixi1171 – 11755
    Helixi1177 – 11793
    Beta strandi1183 – 11853
    Turni1190 – 11923
    Beta strandi1197 – 12004
    Turni1204 – 12063
    Beta strandi1566 – 15683
    Turni1570 – 15723
    Beta strandi1575 – 15773
    Turni1578 – 15825
    Beta strandi1585 – 15873
    Turni1589 – 15913
    Beta strandi1594 – 15963
    Helixi1597 – 15993
    Helixi1604 – 16129
    Helixi1614 – 16174
    Turni1622 – 16243
    Beta strandi1627 – 16293
    Helixi1631 – 165222
    Helixi1655 – 16617
    Helixi1708 – 17169
    Helixi1723 – 174018
    Helixi1745 – 176521
    Helixi1771 – 17733
    Helixi2847 – 285610
    Helixi3764 – 37663
    Helixi3796 – 37994
    Helixi3809 – 38113
    Helixi3816 – 38205
    Helixi3823 – 38308
    Beta strandi3831 – 38355
    Beta strandi3837 – 384711
    Beta strandi3854 – 38574
    Beta strandi3860 – 38645
    Helixi3865 – 38673
    Helixi3868 – 387811
    Beta strandi3884 – 38863
    Beta strandi3888 – 38947
    Turni3896 – 38983
    Helixi3901 – 39044
    Beta strandi3912 – 39209
    Beta strandi3923 – 393210
    Beta strandi3939 – 39424

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ03164.
    SMRiQ03164. Positions 6-39, 103-135, 1146-1214, 1434-1539, 1564-1779, 1872-1977, 2840-2869, 3790-3969.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03164.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1703 – 174846Bromo; divergentPROSITE-ProRule annotationAdd
    BLAST
    Domaini2018 – 207457FYR N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini3666 – 374782FYR C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini3829 – 3945117SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini3953 – 396917Post-SETPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni3906 – 39072S-adenosyl-L-methionine binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2847 – 285599aaTAD

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi17 – 10286Ala/Gly/Ser-richAdd
    BLAST
    Compositional biasi137 – 1437Poly-Gly
    Compositional biasi561 – 5644Poly-Pro
    Compositional biasi568 – 5714Poly-Pro

    Domaini

    the 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
    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.
    The CXXC-type zinc finger binds bind to nonmethyl-CpG dinucleotides.

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.PROSITE-ProRule annotation
    Contains 3 A.T hook DNA-binding domains.Curated
    Contains 1 bromo domain.PROSITE-ProRule annotation
    Contains 1 CXXC-type zinc finger.PROSITE-ProRule annotation
    Contains 1 FYR C-terminal domain.PROSITE-ProRule annotation
    Contains 1 FYR N-terminal domain.PROSITE-ProRule annotation
    Contains 3 PHD-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 post-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1147 – 119549CXXC-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1431 – 148252PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1479 – 153355PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1566 – 162762PHD-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2940.
    HOVERGENiHBG051927.
    InParanoidiQ03164.
    KOiK09186.
    OMAiRIMSPMR.
    OrthoDBiEOG7XH6NX.
    PhylomeDBiQ03164.
    TreeFamiTF319820.

    Family and domain databases

    Gene3Di1.20.920.10. 1 hit.
    3.30.40.10. 2 hits.
    InterProiIPR017956. 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]
    PfamiPF05965. FYRC. 1 hit.
    PF05964. FYRN. 1 hit.
    PF00628. PHD. 2 hits.
    PF00856. SET. 1 hit.
    PF02008. zf-CXXC. 1 hit.
    [Graphical view]
    PIRSFiPIRSF010354. Methyltransferase_trithorax. 1 hit.
    SMARTiSM00384. 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]
    SUPFAMiSSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 2 hits.
    PROSITEiPS50014. 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]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q03164-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPPVGGGG     50
    PGAPPSPPAV AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS 100
    SGPALLRVGP GFDAALQVSA AIGTNLRRFR AVFGESGGGG GSGEDEQFLG 150
    FGSDEEVRVR SPTRSPSVKT SPRKPRGRPR SGSDRNSAIL SDPSVFSPLN 200
    KSETKSGDKI KKKDSKSIEK KRGRPPTFPG VKIKITHGKD ISELPKGNKE 250
    DSLKKIKRTP SATFQQATKI KKLRAGKLSP LKSKFKTGKL QIGRKGVQIV 300
    RRRGRPPSTE RIKTPSGLLI NSELEKPQKV RKDKEGTPPL TKEDKTVVRQ 350
    SPRRIKPVRI IPSSKRTDAT IAKQLLQRAK KGAQKKIEKE AAQLQGRKVK 400
    TQVKNIRQFI MPVVSAISSR IIKTPRRFIE DEDYDPPIKI ARLESTPNSR 450
    FSAPSCGSSE KSSAASQHSS QMSSDSSRSS SPSVDTSTDS QASEEIQVLP 500
    EERSDTPEVH PPLPISQSPE NESNDRRSRR YSVSERSFGS RTTKKLSTLQ 550
    SAPQQQTSSS PPPPLLTPPP PLQPASSISD HTPWLMPPTI PLASPFLPAS 600
    TAPMQGKRKS ILREPTFRWT SLKHSRSEPQ YFSSAKYAKE GLIRKPIFDN 650
    FRPPPLTPED VGFASGFSAS GTAASARLFS PLHSGTRFDM HKRSPLLRAP 700
    RFTPSEAHSR IFESVTLPSN RTSAGTSSSG VSNRKRKRKV FSPIRSEPRS 750
    PSHSMRTRSG RLSSSELSPL TPPSSVSSSL SISVSPLATS ALNPTFTFPS 800
    HSLTQSGESA EKNQRPRKQT SAPAEPFSSS SPTPLFPWFT PGSQTERGRN 850
    KDKAPEELSK DRDADKSVEK DKSRERDRER EKENKRESRK EKRKKGSEIQ 900
    SSSALYPVGR VSKEKVVGED VATSSSAKKA TGRKKSSSHD SGTDITSVTL 950
    GDTTAVKTKI LIKKGRGNLE KTNLDLGPTA PSLEKEKTLC LSTPSSSTVK 1000
    HSTSSIGSML AQADKLPMTD KRVASLLKKA KAQLCKIEKS KSLKQTDQPK 1050
    AQGQESDSSE TSVRGPRIKH VCRRAAVALG RKRAVFPDDM PTLSALPWEE 1100
    REKILSSMGN DDKSSIAGSE DAEPLAPPIK PIKPVTRNKA PQEPPVKKGR 1150
    RSRRCGQCPG CQVPEDCGVC TNCLDKPKFG GRNIKKQCCK MRKCQNLQWM 1200
    PSKAYLQKQA KAVKKKEKKS KTSEKKDSKE SSVVKNVVDS SQKPTPSARE 1250
    DPAPKKSSSE PPPRKPVEEK SEEGNVSAPG PESKQATTPA SRKSSKQVSQ 1300
    PALVIPPQPP TTGPPRKEVP KTTPSEPKKK QPPPPESGPE QSKQKKVAPR 1350
    PSIPVKQKPK EKEKPPPVNK QENAGTLNIL STLSNGNSSK QKIPADGVHR 1400
    IRVDFKEDCE AENVWEMGGL GILTSVPITP RVVCFLCASS GHVEFVYCQV 1450
    CCEPFHKFCL EENERPLEDQ LENWCCRRCK FCHVCGRQHQ ATKQLLECNK 1500
    CRNSYHPECL GPNYPTKPTK KKKVWICTKC VRCKSCGSTT PGKGWDAQWS 1550
    HDFSLCHDCA KLFAKGNFCP LCDKCYDDDD YESKMMQCGK CDRWVHSKCE 1600
    NLSDEMYEIL SNLPESVAYT CVNCTERHPA EWRLALEKEL QISLKQVLTA 1650
    LLNSRTTSHL LRYRQAAKPP DLNPETEESI PSRSSPEGPD PPVLTEVSKQ 1700
    DDQQPLDLEG VKRKMDQGNY TSVLEFSDDI VKIIQAAINS DGGQPEIKKA 1750
    NSMVKSFFIR QMERVFPWFS VKKSRFWEPN KVSSNSGMLP NAVLPPSLDH 1800
    NYAQWQEREE NSHTEQPPLM KKIIPAPKPK GPGEPDSPTP LHPPTPPILS 1850
    TDRSREDSPE LNPPPGIEDN RQCALCLTYG DDSANDAGRL LYIGQNEWTH 1900
    VNCALWSAEV FEDDDGSLKN VHMAVIRGKQ LRCEFCQKPG ATVGCCLTSC 1950
    TSNYHFMCSR AKNCVFLDDK KVYCQRHRDL IKGEVVPENG FEVFRRVFVD 2000
    FEGISLRRKF LNGLEPENIH MMIGSMTIDC LGILNDLSDC EDKLFPIGYQ 2050
    CSRVYWSTTD ARKRCVYTCK IVECRPPVVE PDINSTVEHD ENRTIAHSPT 2100
    SFTESSSKES QNTAEIISPP SPDRPPHSQT SGSCYYHVIS KVPRIRTPSY 2150
    SPTQRSPGCR PLPSAGSPTP TTHEIVTVGD PLLSSGLRSI GSRRHSTSSL 2200
    SPQRSKLRIM SPMRTGNTYS RNNVSSVSTT GTATDLESSA KVVDHVLGPL 2250
    NSSTSLGQNT STSSNLQRTV VTVGNKNSHL DGSSSSEMKQ SSASDLVSKS 2300
    SSLKGEKTKV LSSKSSEGSA HNVAYPGIPK LAPQVHNTTS RELNVSKIGS 2350
    FAEPSSVSFS SKEALSFPHL HLRGQRNDRD QHTDSTQSAN SSPDEDTEVK 2400
    TLKLSGMSNR SSIINEHMGS SSRDRRQKGK KSCKETFKEK HSSKSFLEPG 2450
    QVTTGEEGNL KPEFMDEVLT PEYMGQRPCN NVSSDKIGDK GLSMPGVPKA 2500
    PPMQVEGSAK ELQAPRKRTV KVTLTPLKME NESQSKNALK ESSPASPLQI 2550
    ESTSPTEPIS ASENPGDGPV AQPSPNNTSC QDSQSNNYQN LPVQDRNLML 2600
    PDGPKPQEDG SFKRRYPRRS ARARSNMFFG LTPLYGVRSY GEEDIPFYSS 2650
    STGKKRGKRS AEGQVDGADD LSTSDEDDLY YYNFTRTVIS SGGEERLASH 2700
    NLFREEEQCD LPKISQLDGV DDGTESDTSV TATTRKSSQI PKRNGKENGT 2750
    ENLKIDRPED AGEKEHVTKS SVGHKNEPKM DNCHSVSRVK TQGQDSLEAQ 2800
    LSSLESSRRV HTSTPSDKNL LDTYNTELLK SDSDNNNSDD CGNILPSDIM 2850
    DFVLKNTPSM QALGESPESS SSELLNLGEG LGLDSNREKD MGLFEVFSQQ 2900
    LPTTEPVDSS VSSSISAEEQ FELPLELPSD LSVLTTRSPT VPSQNPSRLA 2950
    VISDSGEKRV TITEKSVASS ESDPALLSPG VDPTPEGHMT PDHFIQGHMD 3000
    ADHISSPPCG SVEQGHGNNQ DLTRNSSTPG LQVPVSPTVP IQNQKYVPNS 3050
    TDSPGPSQIS NAAVQTTPPH LKPATEKLIV VNQNMQPLYV LQTLPNGVTQ 3100
    KIQLTSSVSS TPSVMETNTS VLGPMGGGLT LTTGLNPSLP TSQSLFPSAS 3150
    KGLLPMSHHQ HLHSFPAATQ SSFPPNISNP PSGLLIGVQP PPDPQLLVSE 3200
    SSQRTDLSTT VATPSSGLKK RPISRLQTRK NKKLAPSSTP SNIAPSDVVS 3250
    NMTLINFTPS QLPNHPSLLD LGSLNTSSHR TVPNIIKRSK SSIMYFEPAP 3300
    LLPQSVGGTA ATAAGTSTIS QDTSHLTSGS VSGLASSSSV LNVVSMQTTT 3350
    TPTSSASVPG HVTLTNPRLL GTPDIGSISN LLIKASQQSL GIQDQPVALP 3400
    PSSGMFPQLG TSQTPSTAAI TAASSICVLP STQTTGITAA SPSGEADEHY 3450
    QLQHVNQLLA SKTGIHSSQR DLDSASGPQV SNFTQTVDAP NSMGLEQNKA 3500
    LSSAVQASPT SPGGSPSSPS SGQRSASPSV PGPTKPKPKT KRFQLPLDKG 3550
    NGKKHKVSHL RTSSSEAHIP DQETTSLTSG TGTPGAEAEQ QDTASVEQSS 3600
    QKECGQPAGQ VAVLPEVQVT QNPANEQESA EPKTVEEEES NFSSPLMLWL 3650
    QQEQKRKESI TEKKPKKGLV FEISSDDGFQ ICAESIEDAW KSLTDKVQEA 3700
    RSNARLKQLS FAGVNGLRML GILHDAVVFL IEQLSGAKHC RNYKFRFHKP 3750
    EEANEPPLNP HGSARAEVHL RKSAFDMFNF LASKHRQPPE YNPNDEEEEE 3800
    VQLKSARRAT SMDLPMPMRF RHLKKTSKEA VGVYRSPIHG RGLFCKRNID 3850
    AGEMVIEYAG NVIRSIQTDK REKYYDSKGI GCYMFRIDDS EVVDATMHGN 3900
    AARFINHSCE PNCYSRVINI DGQKHIVIFA MRKIYRGEEL TYDYKFPIED 3950
    ASNKLPCNCG AKKCRKFLN 3969
    Length:3,969
    Mass (Da):431,764
    Last modified:May 1, 2007 - v5
    Checksum:i1150F37EAB1430D3
    GO
    Isoform 2 (identifier: Q03164-2) [UniParc]FASTAAdd to Basket

    Also known as: 14P-18B

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

    Show »
    Length:3,931
    Mass (Da):427,733
    Checksum:iB8E736C88E83D50B
    GO
    Isoform 3 (identifier: Q03164-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:3,972
    Mass (Da):432,052
    Checksum:i18CFDD8B9A763204
    GO

    Sequence cautioni

    The sequence AAG26332.2 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAA58669.1 differs from that shown. Reason: Frameshift at positions 317 and 380.
    The sequence BAD92745.1 differs from that shown. Reason: Frameshift at position 1098.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti144 – 1441E → ELTTQIPCSWRTKGHIHDKK TEPFRLLAWSWCLN in CAA93625. (PubMed:8703835)Curated
    Sequence conflicti556 – 5561Q → E in CAA93625. (PubMed:8703835)Curated
    Sequence conflicti556 – 5561Q → E in L04731. (PubMed:1423625)Curated
    Sequence conflicti1347 – 13471V → A in AAG26335. (PubMed:10706619)Curated
    Sequence conflicti1487 – 14871R → G in AAA18644. (PubMed:8162575)Curated
    Sequence conflicti1490 – 14901Q → R in AAG26335. (PubMed:10706619)Curated
    Sequence conflicti1507 – 15071P → L in AAG26335. (PubMed:10706619)Curated
    Sequence conflicti1513 – 15131N → T in AAG26335. (PubMed:10706619)Curated
    Sequence conflicti1600 – 16001E → G in AAG26335. (PubMed:10706619)Curated
    Sequence conflicti1616 – 16161S → C in AAB34770. (PubMed:7598802)Curated
    Sequence conflicti1937 – 19371Q → H in AAA92511. (PubMed:1303259)Curated
    Sequence conflicti2181 – 21811P → S in AAA92511. (PubMed:1303259)Curated
    Sequence conflicti3556 – 35561K → N in L04731. (PubMed:1423625)Curated
    Sequence conflicti3718 – 37181R → G in CAA93625. (PubMed:8703835)Curated
    Sequence conflicti3759 – 37591N → D in CAA93625. (PubMed:8703835)Curated
    Sequence conflicti3813 – 38131D → G in CAA93625. (PubMed:8703835)Curated
    Sequence conflicti3901 – 39011A → R in AAA58669. (PubMed:1423624)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti30 – 301A → G.1 Publication
    Corresponds to variant rs9332745 [ dbSNP | Ensembl ].
    VAR_021317
    Natural varianti53 – 531A → V.1 Publication
    Corresponds to variant rs9332747 [ dbSNP | Ensembl ].
    VAR_021318
    Natural varianti502 – 5021E → K.1 Publication
    Corresponds to variant rs9332772 [ dbSNP | Ensembl ].
    VAR_021319
    Natural varianti1975 – 19751Q → P.
    Corresponds to variant rs693598 [ dbSNP | Ensembl ].
    VAR_052652
    Natural varianti2319 – 23191S → T.1 Publication
    Corresponds to variant rs9332837 [ dbSNP | Ensembl ].
    VAR_021320
    Natural varianti2354 – 23541P → R.1 Publication
    Corresponds to variant rs9332838 [ dbSNP | Ensembl ].
    VAR_021321
    Natural varianti2387 – 23871Q → R.1 Publication
    Corresponds to variant rs9332839 [ dbSNP | Ensembl ].
    VAR_021322
    Natural varianti3714 – 37141V → I.1 Publication
    Corresponds to variant rs9332859 [ dbSNP | Ensembl ].
    VAR_021323
    Natural varianti3773 – 37731S → A.1 Publication
    Corresponds to variant rs9332861 [ dbSNP | Ensembl ].
    VAR_021324

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1407 – 144438Missing in isoform 2. 1 PublicationVSP_006666Add
    BLAST
    Alternative sequencei1603 – 16031S → SGTE in isoform 3. 2 PublicationsVSP_046879

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    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.
    CCDSiCCDS31686.1. [Q03164-1]
    CCDS55791.1. [Q03164-3]
    PIRiA44265.
    I52578.
    I53035.
    RefSeqiNP_001184033.1. NM_001197104.1. [Q03164-3]
    NP_005924.2. NM_005933.3. [Q03164-1]
    UniGeneiHs.258855.

    Genome annotation databases

    EnsembliENST00000389506; ENSP00000374157; ENSG00000118058. [Q03164-1]
    ENST00000534358; ENSP00000436786; ENSG00000118058. [Q03164-3]
    GeneIDi4297.
    KEGGihsa:4297.
    UCSCiuc001pta.3. human. [Q03164-1]

    Polymorphism databases

    DMDMi146345435.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    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.
    CCDSi CCDS31686.1. [Q03164-1 ]
    CCDS55791.1. [Q03164-3 ]
    PIRi A44265.
    I52578.
    I53035.
    RefSeqi NP_001184033.1. NM_001197104.1. [Q03164-3 ]
    NP_005924.2. NM_005933.3. [Q03164-1 ]
    UniGenei Hs.258855.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2AGH NMR - C 2840-2869 [» ]
    2J2S NMR - A 1143-1214 [» ]
    2JYI NMR - A 1147-1203 [» ]
    2KKF NMR - A 1147-1203 [» ]
    2KU7 NMR - A 1585-1628 [» ]
    2KYU NMR - A 1564-1628 [» ]
    2LXS NMR - B 2840-2858 [» ]
    2LXT NMR - B 2840-2858 [» ]
    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 103-153 [» ]
    4ESG X-ray 1.70 C/D 3755-3771 [» ]
    4GQ6 X-ray 1.55 B 6-15 [» ]
    4NW3 X-ray 2.82 A 1147-1204 [» ]
    ProteinModelPortali Q03164.
    SMRi Q03164. Positions 6-39, 103-135, 1146-1214, 1434-1539, 1564-1779, 1872-1977, 2840-2869, 3790-3969.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110443. 77 interactions.
    DIPi DIP-29221N.
    IntActi Q03164. 33 interactions.
    MINTi MINT-4532017.
    STRINGi 9606.ENSP00000352262.

    Chemistry

    ChEMBLi CHEMBL1293299.

    PTM databases

    PhosphoSitei Q03164.

    Polymorphism databases

    DMDMi 146345435.

    Proteomic databases

    MaxQBi Q03164.
    PaxDbi Q03164.
    PRIDEi Q03164.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389506 ; ENSP00000374157 ; ENSG00000118058 . [Q03164-1 ]
    ENST00000534358 ; ENSP00000436786 ; ENSG00000118058 . [Q03164-3 ]
    GeneIDi 4297.
    KEGGi hsa:4297.
    UCSCi uc001pta.3. human. [Q03164-1 ]

    Organism-specific databases

    CTDi 4297.
    GeneCardsi GC11P118311.
    HGNCi HGNC:7132. KMT2A.
    HPAi CAB017794.
    CAB024270.
    HPA044910.
    MIMi 159555. gene+phenotype.
    605130. phenotype.
    neXtProti NX_Q03164.
    Orphaneti 98837. 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.
    PharmGKBi PA241.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOVERGENi HBG051927.
    InParanoidi Q03164.
    KOi K09186.
    OMAi RIMSPMR.
    OrthoDBi EOG7XH6NX.
    PhylomeDBi Q03164.
    TreeFami TF319820.

    Miscellaneous databases

    ChiTaRSi MLL. human.
    EvolutionaryTracei Q03164.
    GeneWikii MLL_(gene).
    GenomeRNAii 4297.
    NextBioi 16915.
    PROi Q03164.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q03164.
    Bgeei Q03164.
    CleanExi HS_MLL.
    Genevestigatori Q03164.

    Family and domain databases

    Gene3Di 1.20.920.10. 1 hit.
    3.30.40.10. 2 hits.
    InterProi 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 ]
    Pfami PF05965. FYRC. 1 hit.
    PF05964. FYRN. 1 hit.
    PF00628. PHD. 2 hits.
    PF00856. SET. 1 hit.
    PF02008. zf-CXXC. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF010354. Methyltransferase_trithorax. 1 hit.
    SMARTi 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 ]
    SUPFAMi SSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 2 hits.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. 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. 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. Cited for: INVOLVEMENT IN WDSTS.
    46. 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.

    Entry informationi

    Entry nameiKMT2A_HUMAN
    AccessioniPrimary (citable) accession number: Q03164
    Secondary accession number(s): E9PQG7
    , Q13743, Q13744, Q14845, Q16364, Q59FF2, Q6UBD1, Q9HBJ3, Q9UD94, Q9UMA3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 184 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3