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UniProtKB - P42568 (AF9_HUMAN)

Entry version 180 (02 Jun 2021)
Sequence version 2 (25 Nov 2008)
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Protein

Protein AF-9

Gene

MLLT3

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

Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA (PubMed:20159561, PubMed:20471948, PubMed:25417107, PubMed:27105114, PubMed:27545619).

Specifically recognizes and binds acylated histone H3, with a preference for histone H3 that is crotonylated (PubMed:25417107, PubMed:27105114, PubMed:27545619, PubMed:30374167, PubMed:30385749).

Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors (PubMed:25417107, PubMed:27105114, PubMed:27545619).

Recognizes and binds histone H3 crotonylated at 'Lys-9' (H3K9cr), and with slightly lower affinity histone H3 crotonylated at 'Lys-18' (H3K18cr) (PubMed:27105114).

Also recognizes and binds histone H3 acetylated and butyrylated at 'Lys-9' (H3K9ac and H3K9bu, respectively), but with lower affinity than crotonylated histone H3 (PubMed:25417107, PubMed:27105114, PubMed:30385749).

In the SEC complex, MLLT3 is required to recruit the complex to crotonylated histones (PubMed:27105114, PubMed:27545619).

Recruitment of the SEC complex to crotonylated histones promotes recruitment of DOT1L on active chromatin to deposit histone H3 'Lys-79' methylation (H3K79me) (PubMed:25417107).

Plays a key role in hematopoietic stem cell (HSC) maintenance by preserving, rather than confering, HSC stemness (PubMed:31776511).

Acts by binding to the transcription start site of active genes in HSCs and sustaining level of H3K79me2, probably by recruiting DOT1L (PubMed:31776511).

8 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Crotonylated lysine binding is strongly inhibited by the peptide XL-07i, carrying a 2-furancarbonyl side chain and capped with a hydrophobic carboxybenzyl group (PubMed:30374167). XL-07i targets the unique pi-pi-pi stacking interaction at the crotonylation recognition site (PubMed:30374167).1 Publication

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>Sitei58Histone H3K9cr bindingCombined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei80Inhibitor XL-07i; via carbonyl oxygenCombined sources1 Publication1
Binding sitei103Inhibitor XL-07iCombined sources1 Publication1
Sitei103Histone H3K9cr bindingCombined sources2 Publications1
Sitei375KMT2A/MLL1 fusion point (in acute myeloid leukemia patient CO)1 Publication1
Sitei481KMT2A/MLL1 fusion point (in acute myeloid leukemia patient F1)1 Publication1

<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 functionActivator, DNA-binding
Biological processTranscription, Transcription regulation

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P42568

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-112382, Formation of RNA Pol II elongation complex
R-HSA-674695, RNA Polymerase II Pre-transcription Events
R-HSA-75955, RNA Polymerase II Transcription Elongation

SIGNOR Signaling Network Open Resource

More...SIGNORi		P42568

<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%5Fand%5Ftaxonomy%5Fsection">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:
Protein AF-9Curated
Alternative name(s):
ALL1-fused gene from chromosome 9 protein1 Publication
Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein1 Publication
YEATS domain-containing protein 3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:MLLT31 PublicationImported
Synonyms:AF91 Publication, YEATS3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 9

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:7136, MLLT3

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		159558, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P42568

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000171843.15

<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

Keywords - Cellular componenti

Chromosome, 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

A chromosomal aberration involving MLLT3 is associated with acute leukemias. Translocation t(9;11)(p22;q23) with KMT2A/MLL1. The result is a rogue activator protein. Fusion protein KMT2A-MLLT3 interacts with MEN1 and PSIP1 (PubMed:22936661, PubMed:25305204).4 Publications
A chromosomal aberration involving MLLT3 was observed in a patient with neuromotor development delay, cerebellar ataxia and epilepsy. Translocation t(4;9)(q35;p22).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi28F → A: Decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3. 2 Publications1
Mutagenesisi56H → A: Decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3. 2 Publications1
Mutagenesisi58S → A: Decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3. 2 Publications1
Mutagenesisi59F → A: Strongly decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3. 3 Publications1
Mutagenesisi61 – 67RPKRVCK → EPERVCE: Decreased DNA-binding. 1 Publication7
Mutagenesisi77G → A: Decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3. 2 Publications1
Mutagenesisi78 – 79YA → WG: Binds equally well acetylated and crotonylated histone H3. 1 Publication2
Mutagenesisi78Y → A: Strongly decreased binding to crotonylated histone H3. Decreased binding to acetylated histone H3. 3 Publications1
Mutagenesisi78Y → W: Does not affect ability to discriminate between acetylated and crotonylated histone H3. 1 Publication1
Mutagenesisi81F → A: Decreased binding to acetylated histone H3. 1 Publication1
Mutagenesisi103D → A: Decreased binding to acetylated histone H3. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

More...DisGeNETi		4300

MalaCards human disease database

More...MalaCardsi		MLLT3

Open Targets

More...OpenTargetsi		ENSG00000171843

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

More...Orphaneti		402017, Acute myeloid leukemia with t(9;11)(p22;q23)

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30852

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P42568, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4295761

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		MLLT3

Domain mapping of disease mutations (DMDM)

More...DMDMi		215273971

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002159211 – 568Protein AF-9Add BLAST568

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 residuei288PhosphoserineCombined sources1
Modified residuei294PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki339Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei412PhosphoserineCombined sources1
Modified residuei419PhosphoserineCombined sources1
Modified residuei483PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P42568

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P42568

MaxQB - The MaxQuant DataBase

More...MaxQBi		P42568

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

More...PaxDbi		P42568

PeptideAtlas

More...PeptideAtlasi		P42568

PRoteomics IDEntifications database

More...PRIDEi		P42568

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		55517 [P42568-1]
6833

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P42568

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

More...PhosphoSitePlusi		P42568

<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

Enriched in undifferentiated hematopoietic stem cells in fetal liver, cord blood and bone marrow.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000171843, Expressed in subventricular zone (outer) (primate) and 209 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P42568, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P42568, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000171843, Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3) (PubMed:20159561, PubMed:20471948, PubMed:22195968, PubMed:23260655, PubMed:25417107).

Interacts with BCOR (PubMed:10898795).

Interacts with CBX8 (PubMed:11313972).

Interacts with ALKBH4 (PubMed:23145062).

8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		110446, 73 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P42568

Database of interacting proteins

More...DIPi		DIP-56409N

Protein interaction database and analysis system

More...IntActi		P42568, 51 interactors

Molecular INTeraction database

More...MINTi		P42568

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000369695

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P42568

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P42568, protein

<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

1568
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...BMRBi		P42568

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

More...SMRi		P42568

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

<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%5Fand%5Fdomains%5Fsection">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>Domaini1 – 138YEATSPROSITE-ProRule annotationAdd BLAST138

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>Regioni56 – 58Inhibitor XL-07i bindingCombined sources1 Publication3
Regioni78 – 80Histone H3K9cr bindingCombined sources2 Publications3
Regioni106 – 109Inhibitor XL-07i bindingCombined sources1 Publication4
Regioni106 – 108Histone H3K9cr bindingCombined sources2 Publications3
Regioni137 – 475DisorderedSequence analysisAdd BLAST339

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>Motifi295 – 300Nuclear localization signalSequence analysis6

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 type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi143 – 195Polar residuesSequence analysisAdd BLAST53
Compositional biasi196 – 262Basic and acidic residuesSequence analysisAdd BLAST67
Compositional biasi282 – 304Basic and acidic residuesSequence analysisAdd BLAST23
Compositional biasi323 – 354Basic and acidic residuesSequence analysisAdd BLAST32
Compositional biasi373 – 403Polar residuesSequence analysisAdd BLAST31
Compositional biasi414 – 428Acidic residuesSequence analysisAdd BLAST15
Compositional biasi441 – 461Polar residuesSequence analysisAdd BLAST21

<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 YEATS domain specifically recognizes and binds acylated histones, with a marked preference for histones that are crotonylated (PubMed:27105114, PubMed:27545619). Also binds histone H3 acetylated at 'Lys-9' (H3K9ac), but with lower affinity (PubMed:25417107, PubMed:27105114). Binds crotonylated lysine through a non-canonical pi-pi-pi stacking mechanism (PubMed:30374167, PubMed:30385749). The YEATS domain also binds DNA (PubMed:30385749).5 Publications

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3149, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155903

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P42568

Identification of Orthologs from Complete Genome Data

More...OMAi		MSKEPKA

Database for complete collections of gene phylogenies

More...PhylomeDBi		P42568

TreeFam database of animal gene trees

More...TreeFami		TF314586

Family and domain databases

Database of protein disorder

More...DisProti		DP01070

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.60.40.1970, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID00552

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR040930, AF-9_AHD
IPR038704, YEAST_sf
IPR005033, YEATS

The PANTHER Classification System

More...PANTHERi		PTHR23195, PTHR23195, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF17793, AHD, 1 hit
PF03366, YEATS, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51037, YEATS, 1 hit

<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%5Flength">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 (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

This entry describes 2 <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 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P42568-1) [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.

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MASSCAVQVK LELGHRAQVR KKPTVEGFTH DWMVFVRGPE HSNIQHFVEK 
        60         70         80         90        100
VVFHLHESFP RPKRVCKDPP YKVEESGYAG FILPIEVYFK NKEEPRKVRF 
       110        120        130        140        150
DYDLFLHLEG HPPVNHLRCE KLTFNNPTED FRRKLLKAGG DPNRSIHTSS 
       160        170        180        190        200
SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS TSFSKPHKLM 
       210        220        230        240        250
KEHKEKPSKD SREHKSAFKE PSRDHNKSSK ESSKKPKENK PLKEEKIVPK 
       260        270        280        290        300
MAFKEPKPMS KEPKPDSNLL TITSGQDKKA PSKRPPISDS EELSAKKRKK 
       310        320        330        340        350
SSSEALFKSF SSAPPLILTC SADKKQIKDK SHVKMGKVKI ESETSEKKKS 
       360        370        380        390        400
TLPPFDDIVD PNDSDVEENI SSKSDSEQPS PASSSSSSSS SFTPSQTRQQ 
       410        420        430        440        450
GPLRSIMKDL HSDDNEEESD EVEDNDNDSE MERPVNRGGS RSRRVSLSDG 
       460        470        480        490        500
SDSESSSASS PLHHEPPPPL LKTNNNQILE VKSPIKQSKS DKQIKNGECD 
       510        520        530        540        550
KAYLDELVEL HRRLMTLRER HILQQIVNLI EETGHFHITN TTFDFDLCSL 
       560 
DKTTVRKLQS YLETSGTS
Length:568
Mass (Da):63,351
Last modified:November 25, 2008 - v2
<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:i0A020B7FB34132F9
GO
Isoform 2 (identifier: P42568-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MASS → M

Show »
Length:565
Mass (Da):63,106
Checksum:iE8D74987AC7356CC
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0D9SF09A0A0D9SF09_HUMAN
Myeloid/lymphoid or mixed-lineage l...
MLLT3 hCG_1811108
138Annotation 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>
A0A6Q8PGU4A0A6Q8PGU4_HUMAN
Protein AF-9
MLLT3
108Annotation 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>
B1APT5B1APT5_HUMAN
Protein AF-9
MLLT3
162Annotation 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>
A0A6Q8PH64A0A6Q8PH64_HUMAN
Protein AF-9
MLLT3
67Annotation 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>

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 conflicti6A → S in AAA58361 (PubMed:8506309).Curated1
Sequence conflicti6A → S in BAG35760 (PubMed:14702039).Curated1
Sequence conflicti173S → G in AAH36089 (PubMed:15489334).Curated1
Sequence conflicti419S → P in BAG35760 (PubMed:14702039).Curated1

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_0549241 – 4MASS → M in isoform 2. 1 Publication4

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
L13744 mRNA Translation: AAA58361.1
AK301474 mRNA Translation: BAH13491.1
AK312914 mRNA Translation: BAG35760.1
AL354879 Genomic DNA No translation available.
AL512635 Genomic DNA No translation available.
AL513498 Genomic DNA No translation available.
AL163193 Genomic DNA No translation available.
AL627410 Genomic DNA No translation available.
CH471071 Genomic DNA Translation: EAW58631.1
CH471071 Genomic DNA Translation: EAW58632.1
BC036089 mRNA Translation: AAH36089.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS6494.1 [P42568-1]
CCDS69579.1 [P42568-2]

Protein sequence database of the Protein Information Resource

More...PIRi		I39411

NCBI Reference Sequences

More...RefSeqi		NP_001273620.1, NM_001286691.1 [P42568-2]
NP_004520.2, NM_004529.3 [P42568-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000380338; ENSP00000369695; ENSG00000171843 [P42568-1]
ENST00000630269; ENSP00000485996; ENSG00000171843 [P42568-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		4300

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:4300

UCSC genome browser

More...UCSCi		uc003zoe.3, human [P42568-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

<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%5Freferences%5Fsection">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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13744 mRNA Translation: AAA58361.1
AK301474 mRNA Translation: BAH13491.1
AK312914 mRNA Translation: BAG35760.1
AL354879 Genomic DNA No translation available.
AL512635 Genomic DNA No translation available.
AL513498 Genomic DNA No translation available.
AL163193 Genomic DNA No translation available.
AL627410 Genomic DNA No translation available.
CH471071 Genomic DNA Translation: EAW58631.1
CH471071 Genomic DNA Translation: EAW58632.1
BC036089 mRNA Translation: AAH36089.1
CCDSiCCDS6494.1 [P42568-1]
CCDS69579.1 [P42568-2]
PIRiI39411
RefSeqiNP_001273620.1, NM_001286691.1 [P42568-2]
NP_004520.2, NM_004529.3 [P42568-1]

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
2LM0NMR-A490-568[»]
2MV7NMR-A500-568[»]
2N4QNMR-B500-568[»]
2NDFNMR-A1-138[»]
2NDGNMR-A1-138[»]
4TMPX-ray2.30A/C1-138[»]
5HJBX-ray2.70A1-138[»]
5HJDX-ray2.81A/C/E/G/K/N/Q/T1-138[»]
5YYFX-ray1.90A/C1-138[»]
6B7GNMR-A500-568[»]
6L5ZX-ray3.05A1-138[»]
6LS6X-ray2.20A/B1-138[»]
6MILX-ray1.93A/C1-138[»]
6MIMX-ray2.52A/C1-138[»]
BMRBiP42568
SMRiP42568
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi110446, 73 interactors
CORUMiP42568
DIPiDIP-56409N
IntActiP42568, 51 interactors
MINTiP42568
STRINGi9606.ENSP00000369695

Chemistry databases

BindingDBiP42568
ChEMBLiCHEMBL4295761

PTM databases

iPTMnetiP42568
PhosphoSitePlusiP42568

Genetic variation databases

BioMutaiMLLT3
DMDMi215273971

Proteomic databases

jPOSTiP42568
MassIVEiP42568
MaxQBiP42568
PaxDbiP42568
PeptideAtlasiP42568
PRIDEiP42568
ProteomicsDBi55517 [P42568-1]
6833

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		1068, 280 antibodies

The DNASU plasmid repository

More...DNASUi		4300

Genome annotation databases

EnsembliENST00000380338; ENSP00000369695; ENSG00000171843 [P42568-1]
ENST00000630269; ENSP00000485996; ENSG00000171843 [P42568-2]
GeneIDi4300
KEGGihsa:4300
UCSCiuc003zoe.3, human [P42568-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		4300
DisGeNETi4300

GeneCards: human genes, protein and diseases

More...GeneCardsi		MLLT3
HGNCiHGNC:7136, MLLT3
HPAiENSG00000171843, Low tissue specificity
MalaCardsiMLLT3
MIMi159558, gene
neXtProtiNX_P42568
OpenTargetsiENSG00000171843
Orphaneti402017, Acute myeloid leukemia with t(9;11)(p22;q23)
PharmGKBiPA30852
VEuPathDBiHostDB:ENSG00000171843.15

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3149, Eukaryota
GeneTreeiENSGT00940000155903
InParanoidiP42568
OMAiMSKEPKA
PhylomeDBiP42568
TreeFamiTF314586

Enzyme and pathway databases

PathwayCommonsiP42568
ReactomeiR-HSA-112382, Formation of RNA Pol II elongation complex
R-HSA-674695, RNA Polymerase II Pre-transcription Events
R-HSA-75955, RNA Polymerase II Transcription Elongation
SIGNORiP42568

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		4300, 18 hits in 995 CRISPR screens

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

More...ChiTaRSi		MLLT3, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		MLLT3

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

More...GenomeRNAii		4300
PharosiP42568, Tbio

Protein Ontology

More...PROi		PR:P42568
RNActiP42568, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000171843, Expressed in subventricular zone (outer) (primate) and 209 other tissues
ExpressionAtlasiP42568, baseline and differential
GenevisibleiP42568, HS

Family and domain databases

DisProtiDP01070
Gene3Di2.60.40.1970, 1 hit
IDEALiIID00552
InterProiView protein in InterPro
IPR040930, AF-9_AHD
IPR038704, YEAST_sf
IPR005033, YEATS
PANTHERiPTHR23195, PTHR23195, 1 hit
PfamiView protein in Pfam
PF17793, AHD, 1 hit
PF03366, YEATS, 1 hit
PROSITEiView protein in PROSITE
PS51037, YEATS, 1 hit

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 nameiAF9_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: P42568
Secondary accession number(s): B1AMQ2
, B2R7B3, B7Z755, D3DRJ8, Q8IVB0
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 25, 2008
Last modified: June 2, 2021
This is version 180 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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