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UniProtKB - Q03164 (KMT2A_HUMAN)

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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
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

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:
MLL cleavage product N320
Alternative name(s):
N-terminal cleavage product of 320 kDa
Short name:
p320
MLL cleavage product C180
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
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
View the complete GO annotation on QuickGO ...

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.

« 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 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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