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Q03164

- KMT2A_HUMAN

UniProt

Q03164 - KMT2A_HUMAN

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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

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 homodimerization activity Source: UniProtKB
  7. sequence-specific DNA binding transcription factor activity Source: ProtInc
  8. transcription regulatory region DNA binding Source: UniProtKB
  9. unmethylated CpG binding Source: UniProtKB
  10. 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
Complete GO annotation...

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi2718 – 27203DGV → AAA: Abolishes cleavage by TASP1; when associated with 2666-A-A-2667. 2 Publications
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

BgeeiQ03164.
CleanExiHS_MLL.
ExpressionAtlasiQ03164. baseline and differential.
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
WDR5P619649EBI-591370,EBI-540834

Protein-protein interaction databases

BioGridi110443. 79 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 – 13320Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi1151 – 11544Combined sources
Beta strandi1156 – 11583Combined sources
Helixi1159 – 11624Combined sources
Beta strandi1168 – 11703Combined sources
Helixi1171 – 11755Combined sources
Helixi1177 – 11793Combined sources
Beta strandi1183 – 11853Combined sources
Turni1190 – 11923Combined sources
Beta strandi1197 – 12004Combined sources
Turni1204 – 12063Combined sources
Beta strandi1566 – 15683Combined sources
Turni1570 – 15723Combined sources
Beta strandi1575 – 15773Combined sources
Turni1578 – 15825Combined sources
Beta strandi1585 – 15873Combined sources
Turni1589 – 15913Combined sources
Beta strandi1594 – 15963Combined sources
Helixi1597 – 15993Combined sources
Helixi1604 – 16129Combined sources
Helixi1614 – 16174Combined sources
Turni1622 – 16243Combined sources
Beta strandi1627 – 16293Combined sources
Helixi1631 – 165222Combined sources
Helixi1655 – 16617Combined sources
Helixi1708 – 17169Combined sources
Helixi1723 – 174018Combined sources
Helixi1745 – 176521Combined sources
Helixi1771 – 17733Combined sources
Helixi2847 – 285610Combined sources
Helixi3764 – 37663Combined sources
Helixi3796 – 37994Combined sources
Helixi3809 – 38113Combined sources
Helixi3816 – 38205Combined sources
Helixi3823 – 38308Combined sources
Beta strandi3831 – 38355Combined sources
Beta strandi3837 – 384711Combined sources
Beta strandi3854 – 38574Combined sources
Beta strandi3860 – 38645Combined sources
Helixi3865 – 38673Combined sources
Helixi3868 – 387811Combined sources
Beta strandi3884 – 38863Combined sources
Beta strandi3888 – 38947Combined sources
Turni3896 – 38983Combined sources
Helixi3901 – 39044Combined sources
Beta strandi3912 – 39209Combined sources
Beta strandi3923 – 393210Combined sources
Beta strandi3939 – 39424Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
2MSRNMR-A140-160[»]
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.
GeneTreeiENSGT00760000119228.
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

        10         20         30         40         50
MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPPVGGGG
60 70 80 90 100
PGAPPSPPAV AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS
110 120 130 140 150
SGPALLRVGP GFDAALQVSA AIGTNLRRFR AVFGESGGGG GSGEDEQFLG
160 170 180 190 200
FGSDEEVRVR SPTRSPSVKT SPRKPRGRPR SGSDRNSAIL SDPSVFSPLN
210 220 230 240 250
KSETKSGDKI KKKDSKSIEK KRGRPPTFPG VKIKITHGKD ISELPKGNKE
260 270 280 290 300
DSLKKIKRTP SATFQQATKI KKLRAGKLSP LKSKFKTGKL QIGRKGVQIV
310 320 330 340 350
RRRGRPPSTE RIKTPSGLLI NSELEKPQKV RKDKEGTPPL TKEDKTVVRQ
360 370 380 390 400
SPRRIKPVRI IPSSKRTDAT IAKQLLQRAK KGAQKKIEKE AAQLQGRKVK
410 420 430 440 450
TQVKNIRQFI MPVVSAISSR IIKTPRRFIE DEDYDPPIKI ARLESTPNSR
460 470 480 490 500
FSAPSCGSSE KSSAASQHSS QMSSDSSRSS SPSVDTSTDS QASEEIQVLP
510 520 530 540 550
EERSDTPEVH PPLPISQSPE NESNDRRSRR YSVSERSFGS RTTKKLSTLQ
560 570 580 590 600
SAPQQQTSSS PPPPLLTPPP PLQPASSISD HTPWLMPPTI PLASPFLPAS
610 620 630 640 650
TAPMQGKRKS ILREPTFRWT SLKHSRSEPQ YFSSAKYAKE GLIRKPIFDN
660 670 680 690 700
FRPPPLTPED VGFASGFSAS GTAASARLFS PLHSGTRFDM HKRSPLLRAP
710 720 730 740 750
RFTPSEAHSR IFESVTLPSN RTSAGTSSSG VSNRKRKRKV FSPIRSEPRS
760 770 780 790 800
PSHSMRTRSG RLSSSELSPL TPPSSVSSSL SISVSPLATS ALNPTFTFPS
810 820 830 840 850
HSLTQSGESA EKNQRPRKQT SAPAEPFSSS SPTPLFPWFT PGSQTERGRN
860 870 880 890 900
KDKAPEELSK DRDADKSVEK DKSRERDRER EKENKRESRK EKRKKGSEIQ
910 920 930 940 950
SSSALYPVGR VSKEKVVGED VATSSSAKKA TGRKKSSSHD SGTDITSVTL
960 970 980 990 1000
GDTTAVKTKI LIKKGRGNLE KTNLDLGPTA PSLEKEKTLC LSTPSSSTVK
1010 1020 1030 1040 1050
HSTSSIGSML AQADKLPMTD KRVASLLKKA KAQLCKIEKS KSLKQTDQPK
1060 1070 1080 1090 1100
AQGQESDSSE TSVRGPRIKH VCRRAAVALG RKRAVFPDDM PTLSALPWEE
1110 1120 1130 1140 1150
REKILSSMGN DDKSSIAGSE DAEPLAPPIK PIKPVTRNKA PQEPPVKKGR
1160 1170 1180 1190 1200
RSRRCGQCPG CQVPEDCGVC TNCLDKPKFG GRNIKKQCCK MRKCQNLQWM
1210 1220 1230 1240 1250
PSKAYLQKQA KAVKKKEKKS KTSEKKDSKE SSVVKNVVDS SQKPTPSARE
1260 1270 1280 1290 1300
DPAPKKSSSE PPPRKPVEEK SEEGNVSAPG PESKQATTPA SRKSSKQVSQ
1310 1320 1330 1340 1350
PALVIPPQPP TTGPPRKEVP KTTPSEPKKK QPPPPESGPE QSKQKKVAPR
1360 1370 1380 1390 1400
PSIPVKQKPK EKEKPPPVNK QENAGTLNIL STLSNGNSSK QKIPADGVHR
1410 1420 1430 1440 1450
IRVDFKEDCE AENVWEMGGL GILTSVPITP RVVCFLCASS GHVEFVYCQV
1460 1470 1480 1490 1500
CCEPFHKFCL EENERPLEDQ LENWCCRRCK FCHVCGRQHQ ATKQLLECNK
1510 1520 1530 1540 1550
CRNSYHPECL GPNYPTKPTK KKKVWICTKC VRCKSCGSTT PGKGWDAQWS
1560 1570 1580 1590 1600
HDFSLCHDCA KLFAKGNFCP LCDKCYDDDD YESKMMQCGK CDRWVHSKCE
1610 1620 1630 1640 1650
NLSDEMYEIL SNLPESVAYT CVNCTERHPA EWRLALEKEL QISLKQVLTA
1660 1670 1680 1690 1700
LLNSRTTSHL LRYRQAAKPP DLNPETEESI PSRSSPEGPD PPVLTEVSKQ
1710 1720 1730 1740 1750
DDQQPLDLEG VKRKMDQGNY TSVLEFSDDI VKIIQAAINS DGGQPEIKKA
1760 1770 1780 1790 1800
NSMVKSFFIR QMERVFPWFS VKKSRFWEPN KVSSNSGMLP NAVLPPSLDH
1810 1820 1830 1840 1850
NYAQWQEREE NSHTEQPPLM KKIIPAPKPK GPGEPDSPTP LHPPTPPILS
1860 1870 1880 1890 1900
TDRSREDSPE LNPPPGIEDN RQCALCLTYG DDSANDAGRL LYIGQNEWTH
1910 1920 1930 1940 1950
VNCALWSAEV FEDDDGSLKN VHMAVIRGKQ LRCEFCQKPG ATVGCCLTSC
1960 1970 1980 1990 2000
TSNYHFMCSR AKNCVFLDDK KVYCQRHRDL IKGEVVPENG FEVFRRVFVD
2010 2020 2030 2040 2050
FEGISLRRKF LNGLEPENIH MMIGSMTIDC LGILNDLSDC EDKLFPIGYQ
2060 2070 2080 2090 2100
CSRVYWSTTD ARKRCVYTCK IVECRPPVVE PDINSTVEHD ENRTIAHSPT
2110 2120 2130 2140 2150
SFTESSSKES QNTAEIISPP SPDRPPHSQT SGSCYYHVIS KVPRIRTPSY
2160 2170 2180 2190 2200
SPTQRSPGCR PLPSAGSPTP TTHEIVTVGD PLLSSGLRSI GSRRHSTSSL
2210 2220 2230 2240 2250
SPQRSKLRIM SPMRTGNTYS RNNVSSVSTT GTATDLESSA KVVDHVLGPL
2260 2270 2280 2290 2300
NSSTSLGQNT STSSNLQRTV VTVGNKNSHL DGSSSSEMKQ SSASDLVSKS
2310 2320 2330 2340 2350
SSLKGEKTKV LSSKSSEGSA HNVAYPGIPK LAPQVHNTTS RELNVSKIGS
2360 2370 2380 2390 2400
FAEPSSVSFS SKEALSFPHL HLRGQRNDRD QHTDSTQSAN SSPDEDTEVK
2410 2420 2430 2440 2450
TLKLSGMSNR SSIINEHMGS SSRDRRQKGK KSCKETFKEK HSSKSFLEPG
2460 2470 2480 2490 2500
QVTTGEEGNL KPEFMDEVLT PEYMGQRPCN NVSSDKIGDK GLSMPGVPKA
2510 2520 2530 2540 2550
PPMQVEGSAK ELQAPRKRTV KVTLTPLKME NESQSKNALK ESSPASPLQI
2560 2570 2580 2590 2600
ESTSPTEPIS ASENPGDGPV AQPSPNNTSC QDSQSNNYQN LPVQDRNLML
2610 2620 2630 2640 2650
PDGPKPQEDG SFKRRYPRRS ARARSNMFFG LTPLYGVRSY GEEDIPFYSS
2660 2670 2680 2690 2700
STGKKRGKRS AEGQVDGADD LSTSDEDDLY YYNFTRTVIS SGGEERLASH
2710 2720 2730 2740 2750
NLFREEEQCD LPKISQLDGV DDGTESDTSV TATTRKSSQI PKRNGKENGT
2760 2770 2780 2790 2800
ENLKIDRPED AGEKEHVTKS SVGHKNEPKM DNCHSVSRVK TQGQDSLEAQ
2810 2820 2830 2840 2850
LSSLESSRRV HTSTPSDKNL LDTYNTELLK SDSDNNNSDD CGNILPSDIM
2860 2870 2880 2890 2900
DFVLKNTPSM QALGESPESS SSELLNLGEG LGLDSNREKD MGLFEVFSQQ
2910 2920 2930 2940 2950
LPTTEPVDSS VSSSISAEEQ FELPLELPSD LSVLTTRSPT VPSQNPSRLA
2960 2970 2980 2990 3000
VISDSGEKRV TITEKSVASS ESDPALLSPG VDPTPEGHMT PDHFIQGHMD
3010 3020 3030 3040 3050
ADHISSPPCG SVEQGHGNNQ DLTRNSSTPG LQVPVSPTVP IQNQKYVPNS
3060 3070 3080 3090 3100
TDSPGPSQIS NAAVQTTPPH LKPATEKLIV VNQNMQPLYV LQTLPNGVTQ
3110 3120 3130 3140 3150
KIQLTSSVSS TPSVMETNTS VLGPMGGGLT LTTGLNPSLP TSQSLFPSAS
3160 3170 3180 3190 3200
KGLLPMSHHQ HLHSFPAATQ SSFPPNISNP PSGLLIGVQP PPDPQLLVSE
3210 3220 3230 3240 3250
SSQRTDLSTT VATPSSGLKK RPISRLQTRK NKKLAPSSTP SNIAPSDVVS
3260 3270 3280 3290 3300
NMTLINFTPS QLPNHPSLLD LGSLNTSSHR TVPNIIKRSK SSIMYFEPAP
3310 3320 3330 3340 3350
LLPQSVGGTA ATAAGTSTIS QDTSHLTSGS VSGLASSSSV LNVVSMQTTT
3360 3370 3380 3390 3400
TPTSSASVPG HVTLTNPRLL GTPDIGSISN LLIKASQQSL GIQDQPVALP
3410 3420 3430 3440 3450
PSSGMFPQLG TSQTPSTAAI TAASSICVLP STQTTGITAA SPSGEADEHY
3460 3470 3480 3490 3500
QLQHVNQLLA SKTGIHSSQR DLDSASGPQV SNFTQTVDAP NSMGLEQNKA
3510 3520 3530 3540 3550
LSSAVQASPT SPGGSPSSPS SGQRSASPSV PGPTKPKPKT KRFQLPLDKG
3560 3570 3580 3590 3600
NGKKHKVSHL RTSSSEAHIP DQETTSLTSG TGTPGAEAEQ QDTASVEQSS
3610 3620 3630 3640 3650
QKECGQPAGQ VAVLPEVQVT QNPANEQESA EPKTVEEEES NFSSPLMLWL
3660 3670 3680 3690 3700
QQEQKRKESI TEKKPKKGLV FEISSDDGFQ ICAESIEDAW KSLTDKVQEA
3710 3720 3730 3740 3750
RSNARLKQLS FAGVNGLRML GILHDAVVFL IEQLSGAKHC RNYKFRFHKP
3760 3770 3780 3790 3800
EEANEPPLNP HGSARAEVHL RKSAFDMFNF LASKHRQPPE YNPNDEEEEE
3810 3820 3830 3840 3850
VQLKSARRAT SMDLPMPMRF RHLKKTSKEA VGVYRSPIHG RGLFCKRNID
3860 3870 3880 3890 3900
AGEMVIEYAG NVIRSIQTDK REKYYDSKGI GCYMFRIDDS EVVDATMHGN
3910 3920 3930 3940 3950
AARFINHSCE PNCYSRVINI DGQKHIVIFA MRKIYRGEEL TYDYKFPIED
3960
ASNKLPCNCG AKKCRKFLN
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 AAA58669.1 differs from that shown. Reason: Frameshift at positions 317 and 380. Curated
The sequence AAG26332.2 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAD92745.1 differs from that shown. Reason: Frameshift at position 1098. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 [» ]
2MSR NMR - A 140-160 [» ]
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. 79 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 GC11P118313.
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.
GeneTreei ENSGT00760000119228.
HOVERGENi HBG051927.
InParanoidi Q03164.
KOi K09186.
OMAi RIMSPMR.
OrthoDBi EOG7XH6NX.
PhylomeDBi Q03164.
TreeFami TF319820.

Miscellaneous databases

ChiTaRSi KMT2A. human.
EvolutionaryTracei Q03164.
GeneWikii MLL_(gene).
GenomeRNAii 4297.
NextBioi 16915.
PROi Q03164.
SOURCEi Search...

Gene expression databases

Bgeei Q03164.
CleanExi HS_MLL.
ExpressionAtlasi Q03164. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 186 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

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