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UniProtKB - O75164 (KDM4A_HUMAN)

Protein

Lysine-specific demethylase 4A

Gene

KDM4A

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 demethylase that specifically demethylates 'Lys-9' and 'Lys-36' residues of histone H3, thereby playing a central role in histone code (PubMed:26741168). Does not demethylate histone H3 'Lys-4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9' and H3 'Lys-36' residue, while it has no activity on mono- and dimethylated residues. Demethylation of Lys residue generates formaldehyde and succinate. Participates in transcriptional repression of ASCL2 and E2F-responsive promoters via the recruitment of histone deacetylases and NCOR1, respectively.3 Publications
Isoform 2: Crucial for muscle differentiation, promotes transcriptional activation of the Myog gene by directing the removal of repressive chromatin marks at its promoter. Lacks the N-terminal demethylase domain.1 Publication

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Fe2+1 PublicationNote: Binds 1 Fe2+ ion per subunit.1 Publication

<p>This subsection of the ‘Function’ 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

Several specific inhibitors are being developed and tested.1 Publication

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 sitei1322-oxoglutarate1 Publication1
<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 bindingi188Iron; catalyticPROSITE-ProRule annotation1 Publication1 Publication1
Metal bindingi190Iron; catalytic1 Publication1 Publication1
Binding sitei1982-oxoglutarate1 Publication1
Binding sitei2062-oxoglutarate1 Publication1
Metal bindingi234ZincCombined sources1
Metal bindingi240Zinc; via tele nitrogenCombined sources1
Binding sitei2412-oxoglutarateBy similarity1
Metal bindingi276Iron; catalyticPROSITE-ProRule annotation1 Publication1 Publication1
Metal bindingi306ZincCombined sources1
Metal bindingi308ZincCombined sources1
Binding sitei945Histone H3K4me31
Binding sitei967Histone H3K4me31
Binding sitei973Histone H3K4me31

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 fingeri709 – 767PHD-type 1Add BLAST59
Zinc fingeri772 – 805C2HC pre-PHD-typePROSITE-ProRule annotationAdd BLAST34
Zinc fingeri828 – 885PHD-type 2PROSITE-ProRule annotationAdd BLAST58

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the 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, Dioxygenase, Oxidoreductase
Biological processHost-virus interaction, Transcription, Transcription regulation
LigandIron, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.14.11.27 2681
1.14.11.B1 2681
1.14.11.B2 2681

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-3214842 HDMs demethylate histones
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks

<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:
Lysine-specific demethylase 4A (EC:1.14.11.-)
Alternative name(s):
JmjC domain-containing histone demethylation protein 3A
Jumonji domain-containing protein 2A
<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:KDM4A
Synonyms:JHDM3A, JMJD2, JMJD2A, KIAA0677
<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 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000066135.12

Human Gene Nomenclature Database

More...HGNCi		HGNC:22978 KDM4A

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		609764 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_O75164

<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

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>Mutagenesisi133G → A: Abolishes histone demethylase activity; when associated with A-138. 1 Publication1
Mutagenesisi138G → A: Abolishes histone demethylase activity; when associated with A-138. 1 Publication1
Mutagenesisi165G → A: Abolishes histone demethylase activity; when associated with A-165. 1 Publication1
Mutagenesisi170G → A: Abolishes histone demethylase activity; when associated with A-165. 1 Publication1
Mutagenesisi188H → A: Abolishes histone demethylase activity without affecting ability to bind H4K20me2. 2 Publications1
Mutagenesisi288 – 289ST → AI: Displays histone demethylase activity for both dimethylated and H3-K9Me3. 2
Mutagenesisi288 – 289ST → TV, NV or GG: Abolishes histone demethylase activity. 2
Mutagenesisi939D → R: Impairs binding to H4K20me2, promoting partial recruitment of TP53BP1. 1 Publication1
Mutagenesisi945D → A: Impairs binding to H3K4me3. 1 Publication1
Mutagenesisi945D → R: Abolishes binding to H3K4me3. 1 Publication1
Mutagenesisi967W → H: Abolishes binding to H3K4me3. 1 Publication1
Mutagenesisi973Y → A: Abolishes binding to H3K4me3. 2 Publications1

Organism-specific databases

DisGeNET

More...DisGeNETi		9682

Open Targets

More...OpenTargetsi		ENSG00000066135

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA164721403

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5896

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2675

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		KDM4A

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00001831722 – 1064Lysine-specific demethylase 4AAdd BLAST1063

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 residuei2N-acetylalanineCombined sources1
Modified residuei523PhosphoserineCombined 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

Ubiquitinated by RNF8 and RNF168 following DNA damage, leading to its degradation. Degradation promotes accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		O75164

MaxQB - The MaxQuant DataBase

More...MaxQBi		O75164

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

More...PaxDbi		O75164

PeptideAtlas

More...PeptideAtlasi		O75164

PRoteomics IDEntifications database

More...PRIDEi		O75164

ProteomicsDB human proteome resource

More...ProteomicsDBi		49829

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O75164

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

More...PhosphoSitePlusi		O75164

<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

Ubiquitous.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000066135 Expressed in 218 organ(s), highest expression level in lung

CleanEx database of gene expression profiles

More...CleanExi		HS_JMJD2A

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O75164 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		HPA007610

<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

Interacts with histone deacetylase proteins HDAC1, HDAC2 and HDAC3. Interacts with RB and NCOR1.4 Publications
(Microbial infection) Interacts with HTLV-1 Tax protein.1 Publication

<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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		115035, 30 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		O75164

Database of interacting proteins

More...DIPi		DIP-29372N

Protein interaction database and analysis system

More...IntActi		O75164, 29 interactors

Molecular INTeraction database

More...MINTi		O75164

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000361473

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		O75164

<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

11064
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		O75164

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

More...SMRi		O75164

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		O75164

<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>Domaini14 – 56JmjNPROSITE-ProRule annotationAdd BLAST43
Domaini142 – 308JmjCPROSITE-ProRule annotationAdd BLAST167
Domaini897 – 954Tudor 1Add BLAST58
Domaini955 – 1011Tudor 2Add BLAST57

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>Regioni597 – 638Interaction with NCOR11 PublicationAdd BLAST42

<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 2 Tudor domains recognize and bind methylated histone H3 'Lys-4' residue (H3K4me). Double Tudor domain has an interdigitated structure and the unusual fold is required for its ability to bind methylated histone tails. Trimethylated H3 'Lys-4' (H3K4me3) is bound in a cage of 3 aromatic residues, 2 of which are from the Tudor domain 2, while the binding specificity is determined by side-chain interactions involving residues from the Tudor domain 1. The Tudor domains are also able to bind trimethylated histone H3 'Lys-9' (H3K9me3), di- and trimethylated H4 'Lys-20' (H4K20me2 and H4K20me3). Has high affinity for H4K20me2, blocking recruitment of proteins such as TP53BP1.4 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 JHDM3 histone demethylase family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri709 – 767PHD-type 1Add BLAST59
Zinc fingeri772 – 805C2HC pre-PHD-typePROSITE-ProRule annotationAdd BLAST34
Zinc fingeri828 – 885PHD-type 2PROSITE-ProRule annotationAdd BLAST58

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG410IT40 Eukaryota
COG5141 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159643

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000231125

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O75164

KEGG Orthology (KO)

More...KOi		K06709

Identification of Orthologs from Complete Genome Data

More...OMAi		TAGCCVQ

Database of Orthologous Groups

More...OrthoDBi		EOG091G01FR

Database for complete collections of gene phylogenies

More...PhylomeDBi		O75164

TreeFam database of animal gene trees

More...TreeFami		TF106449

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.40.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR034732 EPHD
IPR003347 JmjC_dom
IPR003349 JmjN
IPR002999 Tudor
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR013083 Znf_RING/FYVE/PHD

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02373 JmjC, 1 hit
PF02375 JmjN, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00558 JmjC, 1 hit
SM00545 JmjN, 1 hit
SM00249 PHD, 2 hits
SM00333 TUDOR, 2 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF57903 SSF57903, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51805 EPHD, 1 hit
PS51184 JMJC, 1 hit
PS51183 JMJN, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_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 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 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: O75164-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MASESETLNP SARIMTFYPT MEEFRNFSRY IAYIESQGAH RAGLAKVVPP 
        60         70         80         90        100
KEWKPRASYD DIDDLVIPAP IQQLVTGQSG LFTQYNIQKK AMTVREFRKI 
       110        120        130        140        150
ANSDKYCTPR YSEFEELERK YWKNLTFNPP IYGADVNGTL YEKHVDEWNI 
       160        170        180        190        200
GRLRTILDLV EKESGITIEG VNTPYLYFGM WKTSFAWHTE DMDLYSINYL 
       210        220        230        240        250
HFGEPKSWYS VPPEHGKRLE RLAKGFFPGS AQSCEAFLRH KMTLISPLML 
       260        270        280        290        300
KKYGIPFDKV TQEAGEFMIT FPYGYHAGFN HGFNCAESTN FATRRWIEYG 
       310        320        330        340        350
KQAVLCSCRK DMVKISMDVF VRKFQPERYK LWKAGKDNTV IDHTLPTPEA 
       360        370        380        390        400
AEFLKESELP PRAGNEEECP EEDMEGVEDG EEGDLKTSLA KHRIGTKRHR 
       410        420        430        440        450
VCLEIPQEVS QSELFPKEDL SSEQYEMTEC PAALAPVRPT HSSVRQVEDG 
       460        470        480        490        500
LTFPDYSDST EVKFEELKNV KLEEEDEEEE QAAAALDLSV NPASVGGRLV 
       510        520        530        540        550
FSGSKKKSSS SLGSGSSRDS ISSDSETSEP LSCRAQGQTG VLTVHSYAKG 
       560        570        580        590        600
DGRVTVGEPC TRKKGSAARS FSERELAEVA DEYMFSLEEN KKSKGRRQPL 
       610        620        630        640        650
SKLPRHHPLV LQECVSDDET SEQLTPEEEA EETEAWAKPL SQLWQNRPPN 
       660        670        680        690        700
FEAEKEFNET MAQQAPHCAV CMIFQTYHQV EFGGFNQNCG NASDLAPQKQ 
       710        720        730        740        750
RTKPLIPEMC FTSTGCSTDI NLSTPYLEED GTSILVSCKK CSVRVHASCY 
       760        770        780        790        800
GVPPAKASED WMCSRCSANA LEEDCCLCSL RGGALQRAND DRWVHVSCAV 
       810        820        830        840        850
AILEARFVNI AERSPVDVSK IPLPRFKLKC IFCKKRRKRT AGCCVQCSHG 
       860        870        880        890        900
RCPTAFHVSC AQAAGVMMQP DDWPFVVFIT CFRHKIPNLE RAKGALQSIT 
       910        920        930        940        950
AGQKVISKHK NGRFYQCEVV RLTTETFYEV NFDDGSFSDN LYPEDIVSQD 
       960        970        980        990       1000
CLQFGPPAEG EVVQVRWTDG QVYGAKFVAS HPIQMYQVEF EDGSQLVVKR 
      1010       1020       1030       1040       1050
DDVYTLDEEL PKRVKSRLSV ASDMRFNEIF TEKEVKQEKK RQRVINSRYR 
      1060 
EDYIEPALYR AIME
Length:1,064
Mass (Da):120,662
Last modified:October 5, 2010 - 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:i4A811BEECFEDC6B3
GO
Isoform 2 (identifier: O75164-2) [UniParc]FASTAAdd to basket
Also known as: deltaN-JMJD2A

The sequence of this isoform differs from the canonical sequence as follows:
     1-583: Missing.

Show »
Length:481
Mass (Da):54,697
Checksum:i394B208A6E5483FB
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2R8YDF7A0A2R8YDF7_HUMAN
Lysine-specific demethylase 4A
KDM4A
281Annotation 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>
A0A2R8Y7L1A0A2R8Y7L1_HUMAN
Lysine-specific demethylase 4A
KDM4A
8Annotation 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 BAA31652 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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_023775482A → E2 PublicationsCorresponds to variant dbSNP:rs586339Ensembl.1
Natural variantiVAR_031217877V → G. Corresponds to variant dbSNP:rs12759032Ensembl.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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0442391 – 583Missing in isoform 2. CuratedAdd BLAST583

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
AB014577 mRNA Translation: BAA31652.2 Different initiation.
AC092815 Genomic DNA No translation available.
AL451062 Genomic DNA No translation available.
BC002558 mRNA Translation: AAH02558.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS491.1 [O75164-1]

NCBI Reference Sequences

More...RefSeqi		NP_055478.2, NM_014663.2 [O75164-1]
XP_005271411.1, XM_005271354.3 [O75164-1]
XP_005271412.1, XM_005271355.3 [O75164-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.155983

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000372396; ENSP00000361473; ENSG00000066135 [O75164-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		9682

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:9682

UCSC genome browser

More...UCSCi		uc001cjx.4 human [O75164-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB014577 mRNA Translation: BAA31652.2 Different initiation.
AC092815 Genomic DNA No translation available.
AL451062 Genomic DNA No translation available.
BC002558 mRNA Translation: AAH02558.1
CCDSiCCDS491.1 [O75164-1]
RefSeqiNP_055478.2, NM_014663.2 [O75164-1]
XP_005271411.1, XM_005271354.3 [O75164-1]
XP_005271412.1, XM_005271355.3 [O75164-1]
UniGeneiHs.155983

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
2GF7X-ray2.20A/B/C/D895-1011[»]
2GFAX-ray2.10A/B895-1011[»]
2GP3X-ray2.35A/B2-350[»]
2GP5X-ray2.28A/B2-350[»]
2OQ6X-ray2.00A/B1-359[»]
2OQ7X-ray2.15A/B1-359[»]
2OS2X-ray2.30A/B1-359[»]
2OT7X-ray2.13A/B1-359[»]
2OX0X-ray1.95A/B1-359[»]
2P5BX-ray1.99A/B2-350[»]
2PXJX-ray2.00A/B2-348[»]
2Q8CX-ray2.05A/B1-350[»]
2Q8DX-ray2.29A/B1-350[»]
2Q8EX-ray2.05A/B1-350[»]
2QQRX-ray1.80A/B897-1011[»]
2QQSX-ray2.82A/B897-1011[»]
2VD7X-ray2.25A/B1-359[»]
2WWJX-ray2.60A/B7-353[»]
2YBKX-ray2.40A/B1-359[»]
2YBPX-ray2.02A/B1-359[»]
2YBSX-ray2.32A/B1-359[»]
3NJYX-ray2.60A/B1-359[»]
3PDQX-ray1.99A/B1-359[»]
3RVHX-ray2.25A/B1-359[»]
3U4SX-ray2.15A/B1-359[»]
4AI9X-ray2.25A/B1-359[»]
4BISX-ray2.49A/B1-359[»]
4GD4X-ray2.33A/B1-359[»]
4URAX-ray2.23A/B1-359[»]
4V2VX-ray2.00A/B1-359[»]
4V2WX-ray1.81A/B1-359[»]
5A7NX-ray2.39A/B1-359[»]
5A7OX-ray2.15A/B1-359[»]
5A7PX-ray2.28A/B1-359[»]
5A7QX-ray2.00A/B1-359[»]
5A7SX-ray2.20A/B1-359[»]
5A7WX-ray2.27A/B1-359[»]
5A80X-ray2.28A/B1-359[»]
5ANQX-ray2.00A/B1-359[»]
5D6WX-ray1.99A/B/C/D895-1011[»]
5D6XX-ray2.15A/B895-1011[»]
5D6YX-ray2.29A/B/C/D/E/F895-1011[»]
5F2SX-ray2.08A/B/C/D1-359[»]
5F2WX-ray2.60A/B/C/D1-359[»]
5F32X-ray2.05A/B/C/D1-359[»]
5F37X-ray2.22A/B/C/D1-359[»]
5F39X-ray2.65A/B/C/D1-359[»]
5F3CX-ray2.06A/B/C/D1-359[»]
5F3EX-ray2.16A/B/C/D1-359[»]
5F3GX-ray2.50A/B/C/D1-359[»]
5F3IX-ray2.24A/B/C/D1-359[»]
5F5IX-ray2.63A/B1-359[»]
5FPVX-ray2.44A/B/C/D/E/F/G/H1-359[»]
5FWEX-ray2.05A/B1-359[»]
5FY8X-ray2.34A/B1-359[»]
5FYCX-ray2.26A/B1-359[»]
5FYHX-ray2.35A/B1-359[»]
5FYIX-ray2.10A/B1-359[»]
5LY1X-ray2.50A/B/C/D1-359[»]
5LY2X-ray2.43A/B/C/D1-359[»]
5TVRX-ray2.09A/B1-359[»]
5TVSX-ray2.75A/B1-359[»]
5VARX-ray1.83A897-1011[»]
5VGIX-ray2.07A/B/C/D5-354[»]
5VMPX-ray2.48A/B/C/D5-354[»]
6CG1X-ray2.16A/B/C/D5-354[»]
6CG2X-ray2.34A/B/C/D5-354[»]
6H8PX-ray1.98A/B1-359[»]
ProteinModelPortaliO75164
SMRiO75164
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115035, 30 interactors
CORUMiO75164
DIPiDIP-29372N
IntActiO75164, 29 interactors
MINTiO75164
STRINGi9606.ENSP00000361473

Chemistry databases

BindingDBiO75164
ChEMBLiCHEMBL5896
GuidetoPHARMACOLOGYi2675

PTM databases

iPTMnetiO75164
PhosphoSitePlusiO75164

Polymorphism and mutation databases

BioMutaiKDM4A

Proteomic databases

EPDiO75164
MaxQBiO75164
PaxDbiO75164
PeptideAtlasiO75164
PRIDEiO75164
ProteomicsDBi49829

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372396; ENSP00000361473; ENSG00000066135 [O75164-1]
GeneIDi9682
KEGGihsa:9682
UCSCiuc001cjx.4 human [O75164-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		9682
DisGeNETi9682
EuPathDBiHostDB:ENSG00000066135.12

GeneCards: human genes, protein and diseases

More...GeneCardsi		KDM4A

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0020610
HGNCiHGNC:22978 KDM4A
HPAiHPA007610
MIMi609764 gene
neXtProtiNX_O75164
OpenTargetsiENSG00000066135
PharmGKBiPA164721403

Human Unidentified Gene-Encoded large proteins database

More...HUGEi		Search...

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG410IT40 Eukaryota
COG5141 LUCA
GeneTreeiENSGT00940000159643
HOGENOMiHOG000231125
InParanoidiO75164
KOiK06709
OMAiTAGCCVQ
OrthoDBiEOG091G01FR
PhylomeDBiO75164
TreeFamiTF106449

Enzyme and pathway databases

BRENDAi1.14.11.27 2681
1.14.11.B1 2681
1.14.11.B2 2681
ReactomeiR-HSA-3214842 HDMs demethylate histones
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks

Miscellaneous databases

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

More...ChiTaRSi		KDM4A human
EvolutionaryTraceiO75164

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		JMJD2A

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

More...GenomeRNAii		9682

Protein Ontology

More...PROi		PR:O75164

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000066135 Expressed in 218 organ(s), highest expression level in lung
CleanExiHS_JMJD2A
GenevisibleiO75164 HS

Family and domain databases

Gene3Di3.30.40.10, 2 hits
InterProiView protein in InterPro
IPR034732 EPHD
IPR003347 JmjC_dom
IPR003349 JmjN
IPR002999 Tudor
IPR011011 Znf_FYVE_PHD
IPR001965 Znf_PHD
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF02373 JmjC, 1 hit
PF02375 JmjN, 1 hit
SMARTiView protein in SMART
SM00558 JmjC, 1 hit
SM00545 JmjN, 1 hit
SM00249 PHD, 2 hits
SM00333 TUDOR, 2 hits
SUPFAMiSSF57903 SSF57903, 1 hit
PROSITEiView protein in PROSITE
PS51805 EPHD, 1 hit
PS51184 JMJC, 1 hit
PS51183 JMJN, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		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 nameiKDM4A_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: O75164
Secondary accession number(s): Q5VVB1
<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: August 22, 2003
Last sequence update: October 5, 2010
Last modified: December 5, 2018
This is version 174 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, Complete proteome, Reference proteome

Documents

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