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Protein

Histone-lysine N-methyltransferase 2D

Gene

KMT2D

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. Methylates 'Lys-4' of histone H3 (H3K4me). H3K4me represents a specific tag for epigenetic transcriptional activation. Acts as a coactivator for estrogen receptor by being recruited by ESR1, thereby activating transcription.3 Publications

Miscellaneous

This gene mapped to a chromosomal region involved in duplications and translocations associated with cancer.

Caution

Another protein KMT2B/MLL4, located on chromosome 19, was first named MLL2 (see AC Q9UMN6). Thus, KMT2B/MLL4 is often referred to as MLL2 and vice versa in the literature.Curated

<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 of the ‘Function’ 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 sitei5451S-adenosyl-L-methioninePROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ 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 bindingi5477ZincBy similarity1
Metal bindingi5525ZincBy similarity1
Metal bindingi5527ZincBy similarity1
Metal bindingi5532ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 fingeri104 – 149C2HC pre-PHD-type 1; degeneratePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri170 – 218PHD-type 1PROSITE-ProRule annotationAdd BLAST49
Zinc fingeri226 – 276PHD-type 2PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri229 – 274RING-type 1; atypicalPROSITE-ProRule annotationAdd BLAST46
Zinc fingeri273 – 323PHD-type 3PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri276 – 321RING-type 2; degeneratePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri1377 – 1430PHD-type 4PROSITE-ProRule annotationAdd BLAST54
Zinc fingeri1427 – 1477PHD-type 5PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri1504 – 1559PHD-type 6PROSITE-ProRule annotationAdd BLAST56
Zinc fingeri1507 – 1557RING-type 3; atypicalPROSITE-ProRule annotationAdd BLAST51
Zinc fingeri5029 – 5069C2HC pre-PHD-type 2PROSITE-ProRule annotationAdd BLAST41
Zinc fingeri5090 – 5137PHD-type 7PROSITE-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

GO - Biological processi

<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, Methyltransferase, Transferase
Biological processTranscription, 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-201722 Formation of the beta-catenin:TCF transactivating complex
R-HSA-3214841 PKMTs methylate histone lysines
R-HSA-3769402 Deactivation of the beta-catenin transactivating complex
R-HSA-5617472 Activation of anterior HOX genes in hindbrain development during early embryogenesis
R-HSA-8936459 RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function

SIGNOR Signaling Network Open Resource

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SIGNORi
O14686

<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 2D (EC:2.1.1.43)
Short name:
Lysine N-methyltransferase 2D
Alternative name(s):
ALL1-related protein
Myeloid/lymphoid or mixed-lineage leukemia protein 2
<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:KMT2D
Synonyms:ALR, MLL2, MLL4
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 12

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000167548.14

Human Gene Nomenclature Database

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HGNCi
HGNC:7133 KMT2D

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602113 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O14686

<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; 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

Kabuki syndrome 1 (KABUK1)9 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA congenital mental retardation syndrome with additional features, including postnatal dwarfism, a peculiar facies characterized by long palpebral fissures with eversion of the lateral third of the lower eyelids, a broad and depressed nasal tip, large prominent earlobes, a cleft or high-arched palate, scoliosis, short fifth finger, persistence of fingerpads, radiographic abnormalities of the vertebrae, hands, and hip joints, and recurrent otitis media in infancy.
See also OMIM:147920
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_074216170Q → H in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_074217170Q → L in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_074218337S → L in KABUK1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs200245957EnsemblClinVar.1
Natural variantiVAR_074219543S → L in KABUK1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs776242478Ensembl.1
Natural variantiVAR_074220647P → Q in KABUK1. 2 PublicationsCorresponds to variant dbSNP:rs200088180EnsemblClinVar.1
Natural variantiVAR_0742211192V → M in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742221258R → Q in KABUK1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1341612248Ensembl.1
Natural variantiVAR_0742231376M → R in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742241380C → R in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742251388R → L in KABUK1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs202217665EnsemblClinVar.1
Natural variantiVAR_0742261417M → V in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742271418L → M in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742281423R → C in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742291424C → F in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742301430C → R in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742311445C → G in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742321453H → R in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742331471C → R in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742341471C → Y in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742351522Q → R in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742361526C → F in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742371718A → V in KABUK1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs111266743Ensembl.1
Natural variantiVAR_0742392841P → T in KABUK1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs763347763Ensembl.1
Natural variantiVAR_0742403876L → R in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742413897L → S in KABUK1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1342235871Ensembl.1
Natural variantiVAR_0742434353P → L in KABUK1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs778418522EnsemblClinVar.1
Natural variantiVAR_0742444420R → Q in KABUK1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs375999143EnsemblClinVar.1
Natural variantiVAR_0742455028D → E in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742465030R → C in KABUK1. 2 Publications1
Natural variantiVAR_0742475034F → V in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742485040D → G in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742495047A → V in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742505048R → C in KABUK1. 4 PublicationsCorresponds to variant dbSNP:rs398123724EnsemblClinVar.1
Natural variantiVAR_0742515048R → H in KABUK1. 2 PublicationsCorresponds to variant dbSNP:rs886041404EnsemblClinVar.1
Natural variantiVAR_0742525059H → P in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0638305109C → F in KABUK1. 2 Publications1
Natural variantiVAR_0742535154R → Q in KABUK1. 2 PublicationsCorresponds to variant dbSNP:rs886043497EnsemblClinVar.1
Natural variantiVAR_0638315179R → H in KABUK1. 3 PublicationsCorresponds to variant dbSNP:rs267607237EnsemblClinVar.1
Natural variantiVAR_0742545189G → R in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0643785210Y → C in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742555214R → C in KABUK1. 3 Publications1
Natural variantiVAR_0638325214R → H in KABUK1. 2 PublicationsCorresponds to variant dbSNP:rs398123729EnsemblClinVar.1
Natural variantiVAR_0638335340R → L in KABUK1. 2 Publications1
Natural variantiVAR_0742565340R → Q in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742575351R → Q in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0643795428G → D in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0742585432R → W in KABUK1; unknown pathological significance. 1 Publication1
Natural variantiVAR_0638345464T → M in KABUK1. 2 PublicationsCorresponds to variant dbSNP:rs267607238EnsemblClinVar.1
Natural variantiVAR_0742595471R → T in KABUK1. 2 Publications1
Natural variantiVAR_0742605481C → Y in KABUK1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1388523736Ensembl.1
Natural variantiVAR_0742615498S → F in KABUK1. 2 Publications1

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

DisGeNET

More...
DisGeNETi
8085

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
KMT2D

MalaCards human disease database

More...
MalaCardsi
KMT2D
MIMi147920 phenotype

Open Targets

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OpenTargetsi
ENSG00000167548

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

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Orphaneti
2322 Kabuki syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA30846

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2189114

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
KMT2D

<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_00001248781 – 5537Histone-lysine N-methyltransferase 2DAdd BLAST5537

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 residuei27PhosphoserineCombined sources1
Modified residuei744PhosphoserineBy similarity1
Modified residuei1151PhosphoserineCombined sources1
Modified residuei1195PhosphothreonineCombined sources1
Modified residuei1249PhosphoserineCombined sources1
Modified residuei1267PhosphothreonineBy similarity1
Modified residuei1270PhosphoserineBy similarity1
Modified residuei1606PhosphoserineCombined sources1
Modified residuei1671PhosphoserineCombined sources1
Modified residuei1820PhosphoserineCombined sources1
Modified residuei1834PhosphoserineCombined sources1
Modified residuei1843PhosphothreonineCombined sources1
Modified residuei1865PhosphothreonineBy similarity1
Modified residuei2239PhosphoserineCombined sources1
Modified residuei2240PhosphothreonineCombined sources1
Modified residuei2246N6-acetyllysineCombined sources1
Modified residuei2260PhosphoserineCombined sources1
Modified residuei2274PhosphoserineCombined sources1
Modified residuei2309PhosphoserineCombined sources1
Modified residuei2311PhosphoserineCombined sources1
Modified residuei2342PhosphoserineBy similarity1
Modified residuei2535Asymmetric dimethylarginineBy similarity1
Modified residuei2640PhosphoserineCombined sources1
Modified residuei2836Asymmetric dimethylarginineBy similarity1
Modified residuei3079N6-acetyllysineCombined sources1
Modified residuei3130PhosphoserineCombined sources1
Modified residuei3197PhosphothreonineCombined sources1
Modified residuei3199PhosphoserineCombined sources1
Modified residuei3433N6-acetyllysineCombined sources1
Modified residuei3727Asymmetric dimethylarginineCombined sources1
Modified residuei4198Asymmetric dimethylarginineBy similarity1
Modified residuei4215PhosphoserineCombined sources1
Modified residuei4359PhosphoserineCombined sources1
Modified residuei4465N6-acetyllysineCombined sources1
Modified residuei4738PhosphoserineCombined 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-linki4756Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei4776N6-acetyllysineCombined sources1
Modified residuei4822PhosphoserineCombined sources1
Modified residuei4849PhosphoserineCombined sources1
Cross-linki4880Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O14686

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O14686

MaxQB - The MaxQuant DataBase

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MaxQBi
O14686

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

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PaxDbi
O14686

PeptideAtlas

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PeptideAtlasi
O14686

PRoteomics IDEntifications database

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PRIDEi
O14686

ProteomicsDB human proteome resource

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ProteomicsDBi
48168
48169 [O14686-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O14686

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

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PhosphoSitePlusi
O14686

<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

Expressed in most adult tissues, including a variety of hematoipoietic cells, with the exception of the liver.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000167548 Expressed in 100 organ(s), highest expression level in left lobe of thyroid gland

CleanEx database of gene expression profiles

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CleanExi
HS_MLL2

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O14686 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O14686 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA035977

<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

Component of the MLL2/3 complex (also named ASCOM complex), at least composed of KMT2D/MLL2 or KMT2C/MLL3, ASH2L, RBBP5, WDR5, NCOA6, DPY30, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin. Interacts with ESR1; interaction is direct.6 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
113758, 38 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O14686

Database of interacting proteins

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DIPi
DIP-37875N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
O14686

Protein interaction database and analysis system

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IntActi
O14686, 27 interactors

Molecular INTeraction database

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MINTi
O14686

STRING: functional protein association networks

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STRINGi
9606.ENSP00000301067

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
O14686

<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

15537
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3UVKX-ray1.40B5337-5347[»]
4ERQX-ray1.91D/E/F5333-5346[»]
4Z4PX-ray2.20A5382-5536[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O14686

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

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SMRi
O14686

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati442 – 44615
Repeati460 – 46425
Repeati469 – 47335
Repeati496 – 50045
Repeati504 – 50855
Repeati521 – 52565
Repeati555 – 55975
Repeati564 – 56885
Repeati573 – 57795
Repeati582 – 586105
Repeati609 – 613115
Repeati618 – 622125
Repeati627 – 631135
Repeati645 – 649145
Repeati663 – 667155
<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>Domaini5175 – 5235FYR N-terminalPROSITE-ProRule annotationAdd BLAST61
Domaini5236 – 5321FYR C-terminalPROSITE-ProRule annotationAdd BLAST86
Domaini5397 – 5513SETPROSITE-ProRule annotationAdd BLAST117
Domaini5521 – 5537Post-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>Regioni439 – 66815 X 5 AA repeats of S/P-P-P-E/P-E/AAdd BLAST230
Regioni5474 – 5475S-adenosyl-L-methionine bindingBy similarity2

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili2669 – 2707Sequence analysisAdd BLAST39
Coiled coili3249 – 3282Sequence analysisAdd BLAST34
Coiled coili3562 – 3614Sequence analysisAdd BLAST53
Coiled coili3714 – 3750Sequence analysisAdd BLAST37
Coiled coili3897 – 3975Sequence analysisAdd BLAST79

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>Motifi2686 – 2690LXXLL motif 15
Motifi3038 – 3042LXXLL motif 25
Motifi4222 – 4236LXXLL motif 3Add BLAST15
Motifi4253 – 4257LXXLL motif 45
Motifi4463 – 4467LXXLL motif 55
Motifi4990 – 4994LXXLL motif 65

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 biasi229 – 326Cys-richAdd BLAST98
Compositional biasi374 – 1197Pro-richAdd BLAST824
Compositional biasi1290 – 1328Arg-richAdd BLAST39
Compositional biasi1351 – 1355Poly-Glu5
Compositional biasi1397 – 1510Cys-richAdd BLAST114
Compositional biasi2107 – 2626Pro-richAdd BLAST520
Compositional biasi2385 – 2392Poly-Pro8
Compositional biasi2707 – 2713Poly-Ala7
Compositional biasi2811 – 2822Gln-richAdd BLAST12
Compositional biasi2862 – 2978Pro-richAdd BLAST117
Compositional biasi3261 – 4275Gln-richAdd BLAST1015
Compositional biasi4241 – 4360Pro-richAdd BLAST120
Compositional biasi4909 – 4977Pro-richAdd BLAST69
Compositional biasi5494 – 5497Poly-Ile4

<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

LXXLL motifs 5 and 6 are essential for the association with ESR1 nuclear receptor.

<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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri104 – 149C2HC pre-PHD-type 1; degeneratePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri170 – 218PHD-type 1PROSITE-ProRule annotationAdd BLAST49
Zinc fingeri226 – 276PHD-type 2PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri229 – 274RING-type 1; atypicalPROSITE-ProRule annotationAdd BLAST46
Zinc fingeri273 – 323PHD-type 3PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri276 – 321RING-type 2; degeneratePROSITE-ProRule annotationAdd BLAST46
Zinc fingeri1377 – 1430PHD-type 4PROSITE-ProRule annotationAdd BLAST54
Zinc fingeri1427 – 1477PHD-type 5PROSITE-ProRule annotationAdd BLAST51
Zinc fingeri1504 – 1559PHD-type 6PROSITE-ProRule annotationAdd BLAST56
Zinc fingeri1507 – 1557RING-type 3; atypicalPROSITE-ProRule annotationAdd BLAST51
Zinc fingeri5029 – 5069C2HC pre-PHD-type 2PROSITE-ProRule annotationAdd BLAST41
Zinc fingeri5090 – 5137PHD-type 7PROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4443 Eukaryota
COG2940 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156707

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG006738

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O14686

KEGG Orthology (KO)

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KOi
K09187

Identification of Orthologs from Complete Genome Data

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OMAi
HLRIPPQ

Database of Orthologous Groups

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OrthoDBi
236292at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O14686

TreeFam database of animal gene trees

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TreeFami
TF354317

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.30.10, 1 hit
3.30.40.10, 6 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR034732 EPHD
IPR003889 FYrich_C
IPR003888 FYrich_N
IPR009071 HMG_box_dom
IPR036910 HMG_box_dom_sf
IPR037890 KMT2D
IPR003616 Post-SET_dom
IPR001214 SET_dom