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Protein

Histone-lysine N-methyltransferase 2A

Gene

KMT2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 (PubMed:12453419, PubMed:20677832, PubMed:26886794). Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity (PubMed:19187761, PubMed:26886794). 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'. Binds to unmethylated CpG elements in the promoter of target genes and helps maintain them in the nonmethylated state (PubMed:20010842). Required for transcriptional activation of HOXA9 (PubMed:12453419, PubMed:20677832, PubMed:20010842). Promotes PPP1R15A-induced apoptosis. Plays a critical role in the control of circadian gene expression and is essential for the transcriptional activation mediated by the CLOCK-ARNTL/BMAL1 heterodimer. Establishes a permissive chromatin state for circadian transcription by mediating a rhythmic methylation of 'Lys-4' of histone H3 (H3K4me) and this histone modification directs the circadian acetylation at H3K9 and H3K14 allowing the recruitment of CLOCK-ARNTL/BMAL1 to chromatin (By similarity).By similarity1 Publication7 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N6-methyl-L-lysine-[histone].3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei3765Important for WDR5-recognition and binding1 Publication1
Binding sitei3839S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources2 Publications1
Binding sitei3841S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources2 Publications1
Binding sitei3883S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources2 Publications1
Metal bindingi3909ZincCombined sources2 Publications1
Metal bindingi3957ZincCombined sources2 Publications1
Binding sitei3958S-adenosyl-L-methioninePROSITE-ProRule annotationCombined sources2 Publications1
Metal bindingi3959ZincCombined sources2 Publications1
Metal bindingi3964ZincCombined sources2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi169 – 180A.T hook 1Add BLAST12
DNA bindingi217 – 227A.T hook 2Add BLAST11
DNA bindingi301 – 309A.T hook 39
Zinc fingeri1147 – 1195CXXC-typePROSITE-ProRule annotationAdd BLAST49
Zinc fingeri1431 – 1482PHD-type 1PROSITE-ProRule annotationAdd BLAST52
Zinc fingeri1479 – 1533PHD-type 2PROSITE-ProRule annotationAdd BLAST55
Zinc fingeri1566 – 1627PHD-type 3PROSITE-ProRule annotationAdd BLAST62
Zinc fingeri1870 – 1910C2HC pre-PHD-typePROSITE-ProRule annotationAdd BLAST41
Zinc fingeri1931 – 1978PHD-type 4PROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

  • AT DNA binding Source: UniProtKB
  • chromatin binding Source: Ensembl
  • DNA binding transcription factor activity Source: ProtInc
  • histone-lysine N-methyltransferase activity Source: Reactome
  • histone methyltransferase activity (H3-K4 specific) Source: UniProtKB
  • identical protein binding Source: IntAct
  • lysine-acetylated histone binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • RNA polymerase II distal enhancer sequence-specific DNA binding Source: UniProtKB
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
  • transcription regulatory region DNA binding Source: UniProtKB
  • unmethylated CpG binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionChromatin regulator, DNA-binding, Methyltransferase, Transferase
Biological processApoptosis, Biological rhythms, Transcription, Transcription regulation
LigandMetal-binding, S-adenosyl-L-methionine, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3214841 PKMTs methylate histone lysines
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function
R-HSA-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
SIGNORiQ03164

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase 2A (EC:2.1.1.433 Publications)
Short name:
Lysine N-methyltransferase 2A
Alternative name(s):
ALL-11 Publication
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
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000118058.20
HGNCiHGNC:7132 KMT2A
MIMi159555 gene+phenotype
neXtProtiNX_Q03164

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Wiedemann-Steiner syndrome (WDSTS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:605130
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 AFDN; 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 KNL1 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)DescriptionActionsGraphical viewLength
Mutagenesisi1150R → A: Impairs DNA-binding. 1 Publication1
Mutagenesisi1151R → A: Impairs DNA-binding. 1 Publication1
Mutagenesisi1153R → A: No effect on stability or DNA-binding. 1 Publication1
Mutagenesisi1154R → A: Impairs DNA-binding. 2 Publications1
Mutagenesisi1155C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication1
Mutagenesisi1158C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication1
Mutagenesisi1161C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication1
Mutagenesisi1162Q → A: No effect on stability or DNA-binding. 1 Publication1
Mutagenesisi1166D → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication1
Mutagenesisi1167C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication1
Mutagenesisi1170C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication1
Mutagenesisi1172N → A: No effect on stability or DNA-binding. 1 Publication1
Mutagenesisi1173C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication1
Mutagenesisi1175D → A: Impairs DNA-binding. 1 Publication1
Mutagenesisi1176K → A: Impairs DNA-binding. 1 Publication1
Mutagenesisi1178 – 1181KFGG → AAAA: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication4
Mutagenesisi1178K → A: Impairs DNA-binding. 1 Publication1
Mutagenesisi1179F → A: Impairs DNA-binding. 1 Publication1
Mutagenesisi1183N → A: Impairs DNA-binding. 1 Publication1
Mutagenesisi1185K → A: Impairs DNA-binding. 2 Publications1
Mutagenesisi1186K → A: Impairs DNA-binding. 1 Publication1
Mutagenesisi1187Q → A: Impairs DNA-binding. 2 Publications1
Mutagenesisi1188C → A: No effect on stability or DNA-binding. 2 Publications1
Mutagenesisi1188C → D: Abolishes DNA-binding and increases CpG methylation of the HOXA9 promoter region. Does not lead to the development of leukemia when overexpressed in mice as gene fusion with MLLT3. 1 Publication1
Mutagenesisi1189C → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication1
Mutagenesisi1192R → A: Abolishes zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication1
Mutagenesisi1193K → A: Impairs DNA-binding. 2 Publications1
Mutagenesisi1194C → A: Impairs zinc-binding and stability of the CXXC-type zinc finger and causes loss of DNA-binding. 1 Publication1
Mutagenesisi1195Q → A: No effect on stability or DNA-binding. 1 Publication1
Mutagenesisi1196N → A: No effect on stability or DNA-binding. 1 Publication1
Mutagenesisi1197L → A: Mildly decreases DNA-binding. 1 Publication1
Mutagenesisi1200M → A: No effect on DNA-binding. 1 Publication1
Mutagenesisi1581Y → A: Decreases affinity for histone H3K4me3. 1 Publication1
Mutagenesisi1587Q → A: Decreases affinity for histone H3K4me3. 1 Publication1
Mutagenesisi1594W → A: Abolishes interaction with histone H3K4me3. 1 Publication1
Mutagenesisi1594W → E: Decreases affinity for histone H3K4me3. 1 Publication1
Mutagenesisi1617V → A: Decreases binding affinity for PPIE. 1 Publication1
Mutagenesisi1619Y → A: May perturb protein folding and thereby decrease binding affinity for PPIE. 1 Publication1
Mutagenesisi2666 – 2667DG → AA: Reduces cleavage without abolishing it. Abolishes cleavage by TASP1; when associated with 2718-A--A-2720. 1 Publication2
Mutagenesisi2718 – 2720DGV → AAA: Abolishes cleavage by TASP1; when associated with 2666-A-A-2667. 2 Publications3
Mutagenesisi3858Y → A: Impairs methyltransferase activity toward unmodified or monomethylated H3K4me. 1 Publication1
Mutagenesisi3858Y → F: Slightly affects methyltransferase activity toward unmodified or monomethylated H3K4me. 1 Publication1
Mutagenesisi3861N → I: Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with L-3867. 1 Publication1
Mutagenesisi3861N → T: Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with V-3867. 1 Publication1
Mutagenesisi3864R → A: Disrupts interaction with ASH2L and RBBP5 and nearly abolishes histone methyltransferase activity. 1 Publication1
Mutagenesisi3867Q → A: Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3871. 1 Publication1
Mutagenesisi3867Q → L: Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with I-3861. 1 Publication1
Mutagenesisi3867Q → V: Leads to stable interaction with ASH2L and RBBP5 in the absence of WDR5; when associated with T-3861. 1 Publication1
Mutagenesisi3869D → A: Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3872. 1 Publication1
Mutagenesisi3871R → A: Slightly affects methyltransferase activity of the enzyme alone, while it impairs methyltransferase activity in complex; when associated with A-3867. 1 Publication1
Mutagenesisi3872E → A: Does not affect methyltransferase activity of the enzyme alone or in complex; when associated with A-3869. 1 Publication1
Mutagenesisi3874Y → A: Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3878. 1 Publication1
Mutagenesisi3878K → A: Affects methyltransferase activity of the enzyme alone, while it does not affect methyltransferase activity in complex; when associated with A-3874. 1 Publication1
Mutagenesisi3906N → A: Loss of the histone H3 methyltransferase activity. 1 Publication1
Mutagenesisi3942Y → A or F: Impairs methyltransferase activity toward unmodified or monomethylated H3K4me. 2 Publications1
Mutagenesisi3942Y → F: Shifts from a specific monomethyltransferase to a di- and trimethyltransferase activity. 2 Publications1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1334 – 1335Breakpoint for translocation to form KMT2A-ZFYVE19 oncogene2
Sitei1362 – 1363Breakpoint for translocation to form KMT2A-AF3P21 and KMT2A-KNL1 oncogenes2
Sitei1362 – 1363Breakpoint for translocation to form KMT2A-CENPK oncogene2
Sitei1362Breakpoint for translocation to form KMT2A-FRYL fusion protein1
Sitei1406 – 1407Breakpoint for translocation to form KMT2A-AFF4 fusion protein2
Sitei1444 – 1445Breakpoint for translocation to form KMT2A-GAS7 oncogene2
Sitei1444 – 1445Breakpoint for translocation to form KMT2A-LPP2

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi4297
MalaCardsiKMT2A
MIMi159555 gene+phenotype
605130 phenotype
OpenTargetsiENSG00000118058
Orphaneti402017 'Acute myeloid leukemia with t(9;11)(p22;q23)'
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
PharmGKBiPA241

Chemistry databases

ChEMBLiCHEMBL1293299

Polymorphism and mutation databases

BioMutaiKMT2A
DMDMi146345435

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001248761 – 3969Histone-lysine N-methyltransferase 2AAdd BLAST3969
ChainiPRO_00003909491 – 2718MLL cleavage product N320Add BLAST2718
ChainiPRO_00003909502719 – 3969MLL cleavage product C180Add BLAST1251

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei153PhosphoserineCombined sources1
Modified residuei197PhosphoserineCombined sources1
Modified residuei239N6-acetyllysineBy similarity1
Modified residuei373N6-acetyllysineBy similarity1
Modified residuei518PhosphoserineCombined sources1
Modified residuei636N6-acetyllysineCombined sources1
Modified residuei680PhosphoserineCombined sources1
Modified residuei840PhosphothreonineCombined sources1
Modified residuei926PhosphoserineCombined sources1
Modified residuei1056PhosphoserineCombined sources1
Modified residuei1130N6-acetyllysineCombined sources1
Modified residuei1235N6-acetyllysineCombined sources1
Modified residuei1837PhosphoserineCombined sources1
Modified residuei1845PhosphothreonineCombined sources1
Modified residuei1858PhosphoserineCombined sources1
Modified residuei2098PhosphoserineCombined sources1
Modified residuei2147PhosphothreonineCombined sources1
Modified residuei2151PhosphoserineCombined sources1
Modified residuei2201PhosphoserineCombined sources1
Modified residuei2525PhosphothreonineCombined sources1
Cross-linki2528Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei2611PhosphoserineCombined sources1
Modified residuei2796PhosphoserineCombined sources1
Modified residuei2955PhosphoserineCombined sources1
Modified residuei2958N6-acetyllysineBy similarity1
Modified residuei3036PhosphoserineCombined sources1
Modified residuei3372PhosphothreonineCombined sources1
Modified residuei3462N6-acetyllysineBy similarity1
Modified residuei3511PhosphoserineCombined sources1
Modified residuei3515PhosphoserineCombined sources1
Modified residuei3527PhosphoserineCombined sources1

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei2666 – 2667Cleavage; by TASP1, site 11 Publication2
Sitei2718 – 2719Cleavage; by TASP1, site 21 Publication2

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ03164
MaxQBiQ03164
PaxDbiQ03164
PeptideAtlasiQ03164
PRIDEiQ03164
ProteomicsDBi58195
58196 [Q03164-2]

PTM databases

CarbonylDBiQ03164
iPTMnetiQ03164
PhosphoSitePlusiQ03164

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000118058
CleanExiHS_MLL
ExpressionAtlasiQ03164 baseline and differential
GenevisibleiQ03164 HS

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 (PubMed:15199122, PubMed:15960975, PubMed:17500065, PubMed:19556245, PubMed:19187761, PubMed:26886794). Interacts with WDR5; the interaction is direct (PubMed:19556245, PubMed:18829459). Interaction with WDR5 is required for stable interaction with ASH2L and RBBP5, and thereby also for optimal histone methyltransferase activity (PubMed:26886794). Interacts with KAT8/MOF; the interaction is direct (PubMed:15960975). Interacts with SBF1 and PPP1R15A (PubMed:9537414, PubMed:10490642). Interacts with ZNF335 (PubMed:23178126). Interacts with CLOCK and ARNTL/BMAL1 in a circadian manner (By similarity). Interacts with PPIE; this results in decreased histone H3 methyltransferase activity (PubMed:20677832, PubMed:20541251). Interacts with CREBBP (PubMed:16253272).By similarity16 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • lysine-acetylated histone binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi110443, 101 interactors
CORUMiQ03164
DIPiDIP-29221N
ELMiQ03164
IntActiQ03164, 50 interactors
MINTiQ03164
STRINGi9606.ENSP00000436786

Chemistry databases

BindingDBiQ03164

Structurei

Secondary structure

13969
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi114 – 133Combined sources20
Beta strandi135 – 138Combined sources4
Beta strandi150 – 152Combined sources3
Beta strandi1151 – 1154Combined sources4
Beta strandi1156 – 1158Combined sources3
Helixi1159 – 1162Combined sources4
Beta strandi1168 – 1170Combined sources3
Helixi1171 – 1175Combined sources5
Helixi1177 – 1179Combined sources3
Beta strandi1183 – 1185Combined sources3
Turni1190 – 1192Combined sources3
Beta strandi1197 – 1200Combined sources4
Turni1204 – 1206Combined sources3
Beta strandi1566 – 1568Combined sources3
Turni1570 – 1572Combined sources3
Beta strandi1575 – 1577Combined sources3
Turni1578 – 1582Combined sources5
Beta strandi1585 – 1587Combined sources3
Turni1589 – 1591Combined sources3
Beta strandi1594 – 1596Combined sources3
Helixi1597 – 1599Combined sources3
Helixi1604 – 1612Combined sources9
Helixi1614 – 1617Combined sources4
Turni1622 – 1624Combined sources3
Beta strandi1627 – 1629Combined sources3
Helixi1631 – 1652Combined sources22
Helixi1655 – 1661Combined sources7
Helixi1708 – 1716Combined sources9
Helixi1723 – 1740Combined sources18
Helixi1745 – 1765Combined sources21
Helixi1771 – 1773Combined sources3
Helixi2847 – 2855Combined sources9
Helixi3764 – 3766Combined sources3
Helixi3796 – 3799Combined sources4
Helixi3809 – 3811Combined sources3
Helixi3816 – 3820Combined sources5
Helixi3823 – 3830Combined sources8
Beta strandi3831 – 3835Combined sources5
Beta strandi3837 – 3847Combined sources11
Beta strandi3854 – 3857Combined sources4
Beta strandi3860 – 3864Combined sources5
Helixi3865 – 3867Combined sources3
Helixi3868 – 3877Combined sources10
Beta strandi3884 – 3886Combined sources3
Beta strandi3888 – 3894Combined sources7
Turni3896 – 3898Combined sources3
Helixi3901 – 3904Combined sources4
Beta strandi3912 – 3920Combined sources9
Beta strandi3923 – 3932Combined sources10
Beta strandi3939 – 3942Combined sources4

3D structure databases

ProteinModelPortaliQ03164
SMRiQ03164
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03164

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1703 – 1748Bromo; divergentPROSITE-ProRule annotationAdd BLAST46
Domaini2018 – 2074FYR N-terminalPROSITE-ProRule annotationAdd BLAST57
Domaini3666 – 3747FYR C-terminalPROSITE-ProRule annotationAdd BLAST82
Domaini3829 – 3945SETPROSITE-ProRule annotationAdd BLAST117
Domaini3953 – 3969Post-SETPROSITE-ProRule annotationAdd BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1584 – 1600Interaction with histone H3K4me31 PublicationAdd BLAST17
Regioni3764 – 3771Interaction with WDR51 Publication8
Regioni3906 – 3907S-adenosyl-L-methionine bindingCombined sources2 Publications2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2847 – 28559aaTAD1 Publication9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi17 – 102Ala/Gly/Ser-richAdd BLAST86
Compositional biasi137 – 143Poly-Gly7
Compositional biasi561 – 564Poly-Pro4
Compositional biasi568 – 571Poly-Pro4

Domaini

The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.1 Publication
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.2 Publications
The CXXC-type zinc finger binds to DNA sequence elements containing nonmethylated CpG dinucleotides.2 Publications
The third PHD-type zinc-finger binds both trimethylated histone H3K4me3 and PPIE; histone and PPIE bind to distinct surfaces (PubMed:20677832, PubMed:20541251). Nevertheless, PPIE binding and histone binding are mutually inhibitory (PubMed:20677832). Isomerization of a peptidylproline bond in the linker between the third PHD-type zinc-finger and the bromo domain disrupts the interaction between the bromo domain and the third PHD-type zinc-finger, and thereby facilitates interaction with PPIE (PubMed:20541251).2 Publications

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1147 – 1195CXXC-typePROSITE-ProRule annotationAdd BLAST49
Zinc fingeri1431 – 1482PHD-type 1PROSITE-ProRule annotationAdd BLAST52
Zinc fingeri1479 – 1533PHD-type 2PROSITE-ProRule annotationAdd BLAST55
Zinc fingeri1566 – 1627PHD-type 3PROSITE-ProRule annotationAdd BLAST62
Zinc fingeri1870 – 1910C2HC pre-PHD-typePROSITE-ProRule annotationAdd BLAST41
Zinc fingeri1931 – 1978PHD-type 4PROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Bromodomain, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1084 Eukaryota
COG2940 LUCA
GeneTreeiENSGT00760000119228
HOVERGENiHBG051927
InParanoidiQ03164
KOiK09186
OMAiRIMSPMR
OrthoDBiEOG091G001P
PhylomeDBiQ03164
TreeFamiTF319820

Family and domain databases

Gene3Di3.30.40.10, 3 hits
InterProiView protein in InterPro
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR034732 EPHD
IPR003889 FYrich_C
IPR003888 FYrich_N
IPR037927 KMT2A
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
PANTHERiPTHR22884:SF387 PTHR22884:SF387, 1 hit
PfamiView protein in Pfam
PF05965 FYRC, 1 hit
PF05964 FYRN, 1 hit
PF00628 PHD, 2 hits
PF00856 SET, 1 hit
PF02008 zf-CXXC, 1 hit
PIRSFiPIRSF010354 Methyltransferase_trithorax, 1 hit
SMARTiView protein in SMART
SM00297 BROMO, 1 hit
SM00542 FYRC, 1 hit
SM00541 FYRN, 1 hit
SM00249 PHD, 4 hits
SM00508 PostSET, 1 hit
SM00317 SET, 1 hit
SUPFAMiSSF47370 SSF47370, 1 hit
SSF57903 SSF57903, 2 hits
PROSITEiView protein in PROSITE
PS50014 BROMODOMAIN_2, 1 hit
PS51805 EPHD, 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

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. AlignAdd to basket

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.

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti144E → ELTTQIPCSWRTKGHIHDKK TEPFRLLAWSWCLN in CAA93625 (PubMed:8703835).Curated1
Sequence conflicti556Q → E in CAA93625 (PubMed:8703835).Curated1
Sequence conflicti556Q → E in L04731 (PubMed:1423625).Curated1
Sequence conflicti1347V → A in AAG26335 (PubMed:10706619).Curated1
Sequence conflicti1487R → G in AAA18644 (PubMed:8162575).Curated1
Sequence conflicti1490Q → R in AAG26335 (PubMed:10706619).Curated1
Sequence conflicti1507P → L in AAG26335 (PubMed:10706619).Curated1
Sequence conflicti1513N → T in AAG26335 (PubMed:10706619).Curated1
Sequence conflicti1600E → G in AAG26335 (PubMed:10706619).Curated1
Sequence conflicti1616S → C in AAB34770 (PubMed:7598802).Curated1
Sequence conflicti1937Q → H in AAA92511 (PubMed:1303259).Curated1
Sequence conflicti2181P → S in AAA92511 (PubMed:1303259).Curated1
Sequence conflicti3556K → N in L04731 (PubMed:1423625).Curated1
Sequence conflicti3718R → G in CAA93625 (PubMed:8703835).Curated1
Sequence conflicti3759N → D in CAA93625 (PubMed:8703835).Curated1
Sequence conflicti3813D → G in CAA93625 (PubMed:8703835).Curated1
Sequence conflicti3901A → R in AAA58669 (PubMed:1423624).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02131730A → G1 PublicationCorresponds to variant dbSNP:rs9332745EnsemblClinVar.1
Natural variantiVAR_02131853A → V1 PublicationCorresponds to variant dbSNP:rs9332747EnsemblClinVar.1
Natural variantiVAR_021319502E → K1 PublicationCorresponds to variant dbSNP:rs9332772EnsemblClinVar.1
Natural variantiVAR_0526521975Q → P. Corresponds to variant dbSNP:rs693598Ensembl.1
Natural variantiVAR_0213202319S → T1 PublicationCorresponds to variant dbSNP:rs9332837Ensembl.1
Natural variantiVAR_0213212354P → R1 PublicationCorresponds to variant dbSNP:rs9332838Ensembl.1
Natural variantiVAR_0213222387Q → R1 PublicationCorresponds to variant dbSNP:rs9332839Ensembl.1
Natural variantiVAR_0213233714V → I1 PublicationCorresponds to variant dbSNP:rs9332859Ensembl.1
Natural variantiVAR_0213243773S → A1 PublicationCorresponds to variant dbSNP:rs9332861Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0066661407 – 1444Missing in isoform 2. 1 PublicationAdd BLAST38
Alternative sequenceiVSP_0468791603S → SGTE in isoform 3. 2 Publications1

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.4 human [Q03164-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Similar proteinsi

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 historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: May 1, 2007
Last modified: July 18, 2018
This is version 224 of the entry and version 5 of the sequence. See 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

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