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UniProtKB - Q03164 (KMT2A_HUMAN)

Entry version 234 (18 Sep 2019)
Sequence version 5 (01 May 2007)
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Protein

Histone-lysine N-methyltransferase 2A

Gene

KMT2A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei3765Important for WDR5-recognition and binding1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi169 – 180A.T hook 1Add BLAST12
DNA bindingi217 – 227A.T hook 2Add BLAST11
DNA bindingi301 – 309A.T hook 39
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>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

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-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
R-HSA-9616222 Transcriptional regulation of granulopoiesis

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q03164

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:KMT2A
Synonyms:ALL1, CXXC7, HRX, HTRX, MLL, MLL1, TRX1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:7132 KMT2A

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		159555 gene+phenotype

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q03164

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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.
Related information in OMIM
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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

More...DisGeNETi		4297

MalaCards human disease database

More...MalaCardsi		KMT2A
MIMi159555 gene+phenotype
605130 phenotype

Open Targets

More...OpenTargetsi		ENSG00000118058

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		98831 Acute myeloid leukemia with 11q23 abnormalities
402017 Acute myeloid leukemia with t(9;11)(p22;q23)
98835 Acute undifferentiated leukemia
199 Cornelia de Lange syndrome
530995 Mixed phenotype acute leukemia
99860 Precursor B-cell acute lymphoblastic leukemia
319182 Wiedemann-Steiner syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA241

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1293299

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		KMT2A

Domain mapping of disease mutations (DMDM)

More...DMDMi		146345435

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>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
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...EPDi		Q03164

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q03164

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q03164

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q03164

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q03164

PeptideAtlas

More...PeptideAtlasi		Q03164

PRoteomics IDEntifications database

More...PRIDEi		Q03164

ProteomicsDB human proteome resource

More...ProteomicsDBi		23014
58195 [Q03164-1]
58196 [Q03164-2]

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		Q03164

GlyConnect protein glycosylation platform

More...GlyConnecti		2046

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q03164

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q03164

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000118058 Expressed in 244 organ(s), highest expression level in forebrain

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q03164 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q03164 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB017794
CAB024270
HPA044910

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		110443, 129 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q03164

Database of interacting proteins

More...DIPi		DIP-29221N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q03164

Protein interaction database and analysis system

More...IntActi		Q03164, 59 interactors

Molecular INTeraction database

More...MINTi		Q03164

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000436786

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q03164

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

13969
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q03164

Database of comparative protein structure models

More...ModBasei		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q03164

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi2847 – 28559aaTAD1 Publication9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi17 – 102Ala/Gly/Ser-richAdd BLAST86
Compositional biasi137 – 143Poly-Gly7
Compositional biasi561 – 564Poly-Pro4
Compositional biasi568 – 571Poly-Pro4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1084 Eukaryota
COG2940 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160099

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q03164

KEGG Orthology (KO)

More...KOi		K09186

Identification of Orthologs from Complete Genome Data

More...OMAi		GVMYFEQ

Database of Orthologous Groups

More...OrthoDBi		738155at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q03164

TreeFam database of animal gene trees

More...TreeFami		TF319820

Family and domain databases

Conserved Domains Database

More...CDDi		cd15693 ePHD_KMT2A, 1 hit
cd15588 PHD1_KMT2A, 1 hit
cd15590 PHD2_KMT2A, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.40.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001487 Bromodomain
IPR036427 Bromodomain-like_sf
IPR034732 EPHD
IPR003889 FYrich_C
IPR003888 FYrich_N
IPR037927 KMT2A
IPR041958 KMT2A_ePHD
IPR042023 KMT2A_PHD1
IPR042025 KMT2A_PHD2
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

The PANTHER Classification System

More...PANTHERi		PTHR45838:SF2 PTHR45838:SF2, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF05965 FYRC, 1 hit
PF05964 FYRN, 1 hit
PF00628 PHD, 2 hits
PF00856 SET, 1 hit
PF02008 zf-CXXC, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF010354 Methyltransferase_trithorax, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View 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

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47370 SSF47370, 1 hit
SSF57903 SSF57903, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PR05E9PR05_HUMAN
Histone-lysine N-methyltransferase ...
KMT2A
1,439Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C5W4H7C5W4_HUMAN
Histone-lysine N-methyltransferase ...
KMT2A
302Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YEU4H0YEU4_HUMAN
Histone-lysine N-methyltransferase ...
KMT2A
87Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A3B3ITT7A0A3B3ITT7_HUMAN
Histone-lysine N-methyltransferase ...
KMT2A
69Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A3B3ITZ6A0A3B3ITZ6_HUMAN
Histone-lysine N-methyltransferase ...
KMT2A
237Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A3B3ISN4A0A3B3ISN4_HUMAN
Histone-lysine N-methyltransferase ...
KMT2A
173Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H7C5V8H7C5V8_HUMAN
Histone-lysine N-methyltransferase ...
KMT2A
160Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A3B3ITT0A0A3B3ITT0_HUMAN
Histone-lysine N-methyltransferase ...
KMT2A
50Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS31686.1 [Q03164-1]
CCDS55791.1 [Q03164-3]

Protein sequence database of the Protein Information Resource

More...PIRi		A44265
I52578
I53035

NCBI Reference Sequences

More...RefSeqi		NP_001184033.1, NM_001197104.1 [Q03164-3]
NP_005924.2, NM_005933.3 [Q03164-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000389506; ENSP00000374157; ENSG00000118058 [Q03164-1]
ENST00000534358; ENSP00000436786; ENSG00000118058 [Q03164-3]
ENST00000649699; ENSP00000496927; ENSG00000118058 [Q03164-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4297

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:4297

UCSC genome browser

More...UCSCi		uc001pta.4 human [Q03164-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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.
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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB 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[»]
2MTNNMR-A110-160[»]
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[»]
5F5EX-ray1.80A3813-3969[»]
5F6LX-ray1.90A3813-3969[»]
5SVHX-ray2.05B2839-2869[»]
6EMQNMR-A111-160[»]
SMRiQ03164
ModBaseiSearch...

Protein-protein interaction databases

BioGridi110443, 129 interactors
CORUMiQ03164
DIPiDIP-29221N
ELMiQ03164
IntActiQ03164, 59 interactors
MINTiQ03164
STRINGi9606.ENSP00000436786

Chemistry databases

BindingDBiQ03164
ChEMBLiCHEMBL1293299

PTM databases

CarbonylDBiQ03164
GlyConnecti2046
iPTMnetiQ03164
PhosphoSitePlusiQ03164

Polymorphism and mutation databases

BioMutaiKMT2A
DMDMi146345435

Proteomic databases

EPDiQ03164
jPOSTiQ03164
MassIVEiQ03164
MaxQBiQ03164
PaxDbiQ03164
PeptideAtlasiQ03164
PRIDEiQ03164
ProteomicsDBi23014
58195 [Q03164-1]
58196 [Q03164-2]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389506; ENSP00000374157; ENSG00000118058 [Q03164-1]
ENST00000534358; ENSP00000436786; ENSG00000118058 [Q03164-3]
ENST00000649699; ENSP00000496927; ENSG00000118058 [Q03164-2]
GeneIDi4297
KEGGihsa:4297
UCSCiuc001pta.4 human [Q03164-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4297
DisGeNETi4297

GeneCards: human genes, protein and diseases

More...GeneCardsi		KMT2A
HGNCiHGNC:7132 KMT2A
HPAiCAB017794
CAB024270
HPA044910
MalaCardsiKMT2A
MIMi159555 gene+phenotype
605130 phenotype
neXtProtiNX_Q03164
OpenTargetsiENSG00000118058
Orphaneti98831 Acute myeloid leukemia with 11q23 abnormalities
402017 Acute myeloid leukemia with t(9;11)(p22;q23)
98835 Acute undifferentiated leukemia
199 Cornelia de Lange syndrome
530995 Mixed phenotype acute leukemia
99860 Precursor B-cell acute lymphoblastic leukemia
319182 Wiedemann-Steiner syndrome
PharmGKBiPA241

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1084 Eukaryota
COG2940 LUCA
GeneTreeiENSGT00940000160099
InParanoidiQ03164
KOiK09186
OMAiGVMYFEQ
OrthoDBi738155at2759
PhylomeDBiQ03164
TreeFamiTF319820

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
R-HSA-9616222 Transcriptional regulation of granulopoiesis
SIGNORiQ03164

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		KMT2A human
EvolutionaryTraceiQ03164

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		MLL_(gene)

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		4297

Pharos

More...Pharosi		Q03164

Protein Ontology

More...PROi		PR:Q03164

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000118058 Expressed in 244 organ(s), highest expression level in forebrain
ExpressionAtlasiQ03164 baseline and differential
GenevisibleiQ03164 HS

Family and domain databases

CDDicd15693 ePHD_KMT2A, 1 hit
cd15588 PHD1_KMT2A, 1 hit
cd15590 PHD2_KMT2A, 1 hit
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
IPR041958 KMT2A_ePHD
IPR042023 KMT2A_PHD1
IPR042025 KMT2A_PHD2
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
PANTHERiPTHR45838:SF2 PTHR45838:SF2, 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

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiKMT2A_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q03164
Secondary accession number(s): E9PQG7
, Q13743, Q13744, Q14845, Q16364, Q59FF2, Q6UBD1, Q9HBJ3, Q9UD94, Q9UMA3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: May 1, 2007
Last modified: September 18, 2019
This is version 234 of the entry and version 5 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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