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Protein

Lysine-specific histone demethylase 1A

Gene

KDM1A

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 demethylates both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. Also acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in ANDR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A. Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1. Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. Effector of SNAI1-mediated transcription repression of E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7.6 Publications

Caution

Was previously reported to interact with ASXL1. However, this publication has been retracted.2 Publications

<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

FAD2 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=3.0 µM for H3 monomethyl-K41 Publication
  2. KM=4.2 µM for H3 dimethyl-K41 Publication
  3. KM=3.9 µM for H3 monomethyl-K4-monomethyl-K91 Publication
  4. KM=17.5 µM for monomethyl-K4-acetyl-K91 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 sitei289FAD2 Publications1
    Binding sitei308FAD2 Publications1
    Binding sitei310FAD2 Publications1
    Binding sitei316FAD2 Publications1
    Binding sitei801FAD2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi281 – 309FADSequence analysisAdd BLAST29
    Nucleotide bindingi332 – 333FAD2 Publications2
    Nucleotide bindingi810 – 811FAD2 Publications2

    <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, Developmental protein, Oxidoreductase, Repressor
    Biological processTranscription, Transcription regulation
    LigandFAD, Flavoprotein

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

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

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-3214815 HDACs deacetylate histones
    R-HSA-3214842 HDMs demethylate histones
    R-HSA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
    R-HSA-8943724 Regulation of PTEN gene transcription
    R-HSA-9018519 Estrogen-dependent gene expression
    R-HSA-983231 Factors involved in megakaryocyte development and platelet production

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    O60341

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    O60341

    Protein family/group databases

    MoonDB Database of extreme multifunctional and moonlighting proteins

    More...
    MoonDBi
    O60341 Predicted

    <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 histone demethylase 1A (EC:1.-.-.-)
    Alternative name(s):
    BRAF35-HDAC complex protein BHC110
    Flavin-containing amine oxidase domain-containing 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:KDM1A
    Synonyms:AOF2, KDM1, KIAA0601, LSD1
    <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 1

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000004487.15

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:29079 KDM1A

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    609132 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_O60341

    <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

    Cleft palate, psychomotor retardation, and distinctive facial features (CPRF)3 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA syndrome characterized by cleft palate, developmental delay, psychomotor retardation, and facial dysmorphic features including a prominent forehead, slightly arched eyebrows, elongated palpebral fissures, a wide nasal bridge, thin lips, and widely spaced teeth. Cleft palate is a congenital fissure of the soft and/or hard palate, due to faulty fusion.
    See also OMIM:616728
    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_076366379E → K in CPRF. 1 PublicationCorresponds to variant dbSNP:rs864309715Ensembl.1
    Natural variantiVAR_076367556D → G in CPRF. 2 PublicationsCorresponds to variant dbSNP:rs864309716Ensembl.1
    Natural variantiVAR_076368761Y → H in CPRF. 2 PublicationsCorresponds to variant dbSNP:rs864309714Ensembl.1

    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>Mutagenesisi503K → R: Loss of polyubiquitination. 1 Publication1
    Mutagenesisi535N → A: Strongly reduces demethylase activity. 1 Publication1
    Mutagenesisi564H → A: Strongly reduces demethylase activity. 1 Publication1
    Mutagenesisi661K → A: Abolishes histone demethylase activity. 1 Publication1
    Mutagenesisi761Y → A: Strongly reduces demethylase activity. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    23028

    MalaCards human disease database

    More...
    MalaCardsi
    KDM1A
    MIMi616728 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000004487

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

    More...
    Orphaneti
    477993 Palatal anomalies-widely spaced teeth-facial dysmorphism-developmental delay syndrome

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA165751392

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL6136

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    2669

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    KDM1A

    <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_00000998811 – 852Lysine-specific histone demethylase 1AAdd BLAST852

    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 residuei59PhosphothreonineCombined sources1
    Modified residuei104PhosphothreonineCombined sources1
    Modified residuei126PhosphoserineCombined sources1
    Modified residuei131PhosphoserineCombined sources1
    Modified residuei135PhosphotyrosineCombined sources1
    Modified residuei137PhosphoserineCombined sources1
    Modified residuei166PhosphoserineCombined 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-linki442Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Cross-linki469Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
    Cross-linki503Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei611PhosphoserineCombined sources1
    Modified residuei849PhosphoserineCombined 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

    Polyubiquitinated by JADE2; which leads to its proteasomal degradation.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    O60341

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    O60341

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    O60341

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

    More...
    PaxDbi
    O60341

    PeptideAtlas

    More...
    PeptideAtlasi
    O60341

    PRoteomics IDEntifications database

    More...
    PRIDEi
    O60341

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    49364
    49365 [O60341-2]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    O60341

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

    More...
    PhosphoSitePlusi
    O60341

    <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

    Ubiquitously expressed.1 Publication

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Down-regulated during neural differentiation in neuroblastoma cancer.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000004487 Expressed in 233 organ(s), highest expression level in right testis

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_AOF2

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    O60341 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    O60341 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB005884
    HPA053660

    <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 a RCOR/GFI/KDM1A/HDAC complex (PubMed:12032298, PubMed:11102443). Interacts directly with GFI1 and GFI1B. Interacts with INSM1 (By similarity). Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I (PubMed:12493763, PubMed:16140033, PubMed:16885027). In the complex, RCOR1/CoREST strongly enhances the demethylase activity and protects it from the proteasome while PHF21A/BHC80 inhibits the demethylase activity (PubMed:16079794, PubMed:16956976). Interacts with the androgen receptor (AR) (PubMed:16079795). Interacts with SNAI1 (via SNAG domain) (PubMed:20562920). Interacts (via AOD/Tower domain) with JADE2 (via C-terminus) (PubMed:25018020). Interacts with ESRRB; co-occupes the core set of ESRRB targets (By similarity).By similarity10 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

    WithEntry#Exp.IntActNotes
    AKAP9Q999962EBI-710124,EBI-1048311
    C8orf74Q6P0472EBI-710124,EBI-8466055
    CCDC151A5D8V72EBI-710124,EBI-8466445
    CDCA4Q9BXL82EBI-710124,EBI-1773949
    CEP70Q8NHQ12EBI-710124,EBI-739624
    CHD1O146468EBI-15599570,EBI-1560858
    CHD3Q128734EBI-710124,EBI-523590
    DNAJA3Q96EY12EBI-710124,EBI-356767
    EHMT2Q96KQ72EBI-15599570,EBI-744366
    EHMT2Q96KQ7-13EBI-15599570,EBI-15737402
    FAM9AQ8IZU12EBI-710124,EBI-8468186
    FYCO1Q9BQS82EBI-710124,EBI-2869338
    GSTCDQ8NEC72EBI-710124,EBI-8469616
    GTPBP2Q9BX102EBI-710124,EBI-6115579
    HAUS1Q96CS22EBI-710124,EBI-2514791
    HDAC3O153794EBI-710124,EBI-607682
    HESX1Q9UBX02EBI-710124,EBI-8470369
    HIST3H3Q166952EBI-710124,EBI-358900
    IMMTQ168912EBI-710124,EBI-473801
    KLHDC4Q8TBB52EBI-710124,EBI-8472352
    KRT33BQ145253EBI-710124,EBI-1049638
    LOXL4Q96JB62EBI-710124,EBI-749562
    MBD3O959834EBI-710124,EBI-1783068
    NOTCH1P465318EBI-710124,EBI-636374
    NR1H3Q131332EBI-710124,EBI-781356
    NR2E1Q9Y4662EBI-710124,EBI-11792373
    OFCC1Q8IZS52EBI-710124,EBI-8477661
    PELP1Q8IZL86EBI-710124,EBI-716449
    PHF19Q5T6S32EBI-710124,EBI-2339674
    PPARDQ031812EBI-710124,EBI-6426768
    PRKCBP05771-12EBI-15599570,EBI-5774492
    PSMC1P621912EBI-710124,EBI-357598
    RASSF1Q9NS232EBI-710124,EBI-367363
    RASSF2P507492EBI-710124,EBI-960081
    RBPJQ063304EBI-710124,EBI-632552
    RCOR1Q9UKL06EBI-15599570,EBI-926563
    RCOR2Q8IZ403EBI-710124,EBI-723853
    RCOR3Q9P2K3-24EBI-710124,EBI-1504830
    SAMD3Q8N6K72EBI-710124,EBI-748741
    SERGEFQ9UGK82EBI-710124,EBI-465368
    SF3B2Q134352EBI-710124,EBI-749111
    SMAD9O151982EBI-710124,EBI-748763
    SMARCA4P515323EBI-710124,EBI-302489
    SMARCC1Q929223EBI-710124,EBI-355653
    SNAI1O9586332EBI-710124,EBI-1045459
    SNF8Q96H202EBI-710124,EBI-747719
    SPICE1Q8N0Z33EBI-710124,EBI-2361917
    SPSB1Q96BD62EBI-710124,EBI-2659201
    STX19Q8N4C72EBI-710124,EBI-8484990
    TAL1P175425EBI-15599570,EBI-1753878
    Tal1P220912EBI-15599570,EBI-8006437From Mus musculus.
    TEX9Q8N6V93EBI-710124,EBI-746341
    TP53P046376EBI-15599570,EBI-366083
    TRAF4Q9BUZ43EBI-710124,EBI-3650647
    WASHC3Q9Y3C04EBI-710124,EBI-712969
    ZBED1O960063EBI-710124,EBI-740037

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    116667, 357 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    O60341

    Database of interacting proteins

    More...
    DIPi
    DIP-34641N

    Protein interaction database and analysis system

    More...
    IntActi
    O60341, 289 interactors

    Molecular INTeraction database

    More...
    MINTi
    O60341

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000383042

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    O60341

    <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

    1852
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    2COMNMR-A169-279[»]
    2DW4X-ray2.30A172-831[»]
    2EJRX-ray2.70A172-833[»]
    2H94X-ray2.90A172-835[»]
    2HKOX-ray2.80A172-835[»]
    2IW5X-ray2.57A171-836[»]
    2L3DNMR-A174-273[»]
    2UXNX-ray2.72A171-836[»]
    2UXXX-ray2.74A171-836[»]
    2V1DX-ray3.10A123-852[»]
    2X0LX-ray3.00A123-852[»]
    2XAFX-ray3.25A1-852[»]
    2XAGX-ray3.10A1-852[»]
    2XAHX-ray3.10A1-852[»]
    2XAJX-ray3.30A1-852[»]
    2XAQX-ray3.20A1-852[»]
    2XASX-ray3.20A1-852[»]
    2Y48X-ray3.00A123-852[»]
    2Z3YX-ray2.25A172-833[»]
    2Z5UX-ray2.25A172-833[»]
    3ABTX-ray3.20A172-833[»]
    3ABUX-ray3.10A172-833[»]
    3ZMSX-ray2.96A1-852[»]
    3ZMTX-ray3.10A1-852[»]
    3ZMUX-ray3.20A1-852[»]
    3ZMVX-ray3.00A1-852[»]
    3ZMZX-ray3.00A1-852[»]
    3ZN0X-ray2.80A1-852[»]
    3ZN1X-ray3.10A1-852[»]
    4BAYX-ray3.10A172-852[»]
    4CZZX-ray3.00A1-852[»]
    4KUMX-ray3.05A171-836[»]
    4UV8X-ray2.80A1-852[»]
    4UV9X-ray3.00A1-852[»]
    4UVAX-ray2.90A1-852[»]
    4UVBX-ray2.80A1-852[»]
    4UVCX-ray3.10A1-852[»]
    4UXNX-ray2.85A1-852[»]
    4XBFX-ray2.80A171-836[»]
    5AFWX-ray1.60B108-119[»]
    5H6QX-ray2.53A172-833[»]
    5H6RX-ray2.60A172-833[»]
    5IT3X-ray1.40A/B183-267[»]
    5L3BX-ray3.30A1-852[»]
    5L3CX-ray3.31A1-852[»]
    5L3DX-ray2.60A1-852[»]
    5L3EX-ray2.80A123-852[»]
    5L3FX-ray3.50A123-852[»]
    5L3GX-ray3.10A123-852[»]
    5LBQX-ray3.30A123-852[»]
    5LGNX-ray3.20A172-836[»]
    5LGTX-ray3.00A123-852[»]
    5LGUX-ray3.20A123-852[»]
    5LHGX-ray3.34A1-852[»]
    5LHHX-ray3.05A1-852[»]
    5LHIX-ray3.40A1-852[»]
    5X60X-ray2.69A172-833[»]
    5YJBX-ray2.96A172-833[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    O60341

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

    More...
    SMRi
    O60341

    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
    O60341

    <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>Domaini174 – 273SWIRMPROSITE-ProRule annotationAdd BLAST100

    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>Regioni300 – 852Demethylase activityAdd BLAST553

    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 coili110 – 151Sequence analysisAdd BLAST42
    Coiled coili428 – 514Sequence analysisAdd BLAST87

    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 biasi7 – 42Ala-richAdd BLAST36
    Compositional biasi152 – 156Poly-Pro5

    <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 SWIRM domain may act as an anchor site for a histone tail.1 Publication

    <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 flavin monoamine oxidase family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0029 Eukaryota
    KOG0685 Eukaryota
    ENOG410XSNC LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000157193

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    O60341

    KEGG Orthology (KO)

    More...
    KOi
    K11450

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    LWLENPK

    Database of Orthologous Groups

    More...
    OrthoDBi
    679855at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    O60341

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF312972

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.10.10, 1 hit
    3.50.50.60, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002937 Amino_oxidase
    IPR036188 FAD/NAD-bd_sf
    IPR017366 Hist_Lys-spec_deMease
    IPR009057 Homeobox-like_sf
    IPR007526 SWIRM
    IPR036388 WH-like_DNA-bd_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01593 Amino_oxidase, 1 hit
    PF04433 SWIRM, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF038051 Histone_Lys-demethylase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF46689 SSF46689, 1 hit
    SSF51905 SSF51905, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50934 SWIRM, 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.

    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: O60341-1) [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
    MLSGKKAAAA AAAAAAAATG TEAGPGTAGG SENGSEVAAQ PAGLSGPAEV
    60 70 80 90 100
    GPGAVGERTP RKKEPPRASP PGGLAEPPGS AGPQAGPTVV PGSATPMETG
    110 120 130 140 150
    IAETPEGRRT SRRKRAKVEY REMDESLANL SEDEYYSEEE RNAKAEKEKK
    160 170 180 190 200
    LPPPPPQAPP EEENESEPEE PSGVEGAAFQ SRLPHDRMTS QEAACFPDII
    210 220 230 240 250
    SGPQQTQKVF LFIRNRTLQL WLDNPKIQLT FEATLQQLEA PYNSDTVLVH
    260 270 280 290 300
    RVHSYLERHG LINFGIYKRI KPLPTKKTGK VIIIGSGVSG LAAARQLQSF
    310 320 330 340 350
    GMDVTLLEAR DRVGGRVATF RKGNYVADLG AMVVTGLGGN PMAVVSKQVN
    360 370 380 390 400
    MELAKIKQKC PLYEANGQAV PKEKDEMVEQ EFNRLLEATS YLSHQLDFNV
    410 420 430 440 450
    LNNKPVSLGQ ALEVVIQLQE KHVKDEQIEH WKKIVKTQEE LKELLNKMVN
    460 470 480 490 500
    LKEKIKELHQ QYKEASEVKP PRDITAEFLV KSKHRDLTAL CKEYDELAET
    510 520 530 540 550
    QGKLEEKLQE LEANPPSDVY LSSRDRQILD WHFANLEFAN ATPLSTLSLK
    560 570 580 590 600
    HWDQDDDFEF TGSHLTVRNG YSCVPVALAE GLDIKLNTAV RQVRYTASGC
    610 620 630 640 650
    EVIAVNTRST SQTFIYKCDA VLCTLPLGVL KQQPPAVQFV PPLPEWKTSA
    660 670 680 690 700
    VQRMGFGNLN KVVLCFDRVF WDPSVNLFGH VGSTTASRGE LFLFWNLYKA
    710 720 730 740 750
    PILLALVAGE AAGIMENISD DVIVGRCLAI LKGIFGSSAV PQPKETVVSR
    760 770 780 790 800
    WRADPWARGS YSYVAAGSSG NDYDLMAQPI TPGPSIPGAP QPIPRLFFAG
    810 820 830 840 850
    EHTIRNYPAT VHGALLSGLR EAGRIADQFL GAMYTLPRQA TPGVPAQQSP

    SM
    Length:852
    Mass (Da):92,903
    Last modified:August 16, 2004 - 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:iA61CEDE51E4E0C1D
    GO
    Isoform 2 (identifier: O60341-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         173-173: G → GQAGGLQDDSSGGYGDGQASG
         369-369: A → ADTVK

    Note: No experimental confirmation available.
    Show »
    Length:876
    Mass (Da):95,155
    Checksum:i966CA72A70F68111
    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
    R4GMQ1R4GMQ1_HUMAN
    Lysine-specific histone demethylase...
    KDM1A
    858Annotation score:

    Annotation score:2 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
    R4GMP9R4GMP9_HUMAN
    Lysine-specific histone demethylase...
    KDM1A
    301Annotation 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 BAA25527 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti78P → Q in AAH40194 (PubMed:15489334).Curated1
    Sequence conflicti405P → H in AAH48134 (PubMed:15489334).Curated1
    Sequence conflicti669V → A in CAD38675 (PubMed:17974005).Curated1
    Sequence conflicti814A → V in AAH16639 (PubMed:15489334).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_076366379E → K in CPRF. 1 PublicationCorresponds to variant dbSNP:rs864309715Ensembl.1
    Natural variantiVAR_076367556D → G in CPRF. 2 PublicationsCorresponds to variant dbSNP:rs864309716Ensembl.1
    Natural variantiVAR_076368761Y → H in CPRF. 2 PublicationsCorresponds to variant dbSNP:rs864309714Ensembl.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_011198173G → GQAGGLQDDSSGGYGDGQAS G in isoform 2. 1 Publication1
    Alternative sequenceiVSP_011199369A → ADTVK in isoform 2. 1 Publication1

    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
    AB011173 mRNA Translation: BAA25527.1 Different initiation.
    AL031428 Genomic DNA No translation available.
    BC016639 mRNA Translation: AAH16639.1
    BC025362 mRNA Translation: AAH25362.1
    BC040194 mRNA Translation: AAH40194.3
    BC048134 mRNA Translation: AAH48134.2
    AL833812 mRNA Translation: CAD38675.2

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS30627.1 [O60341-1]
    CCDS53278.1 [O60341-2]

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001009999.1, NM_001009999.2 [O60341-2]
    NP_055828.2, NM_015013.3 [O60341-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.591518

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000356634; ENSP00000349049; ENSG00000004487 [O60341-1]
    ENST00000400181; ENSP00000383042; ENSG00000004487 [O60341-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    23028

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:23028

    UCSC genome browser

    More...
    UCSCi
    uc001bgi.3 human [O60341-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    <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
    AB011173 mRNA Translation: BAA25527.1 Different initiation.
    AL031428 Genomic DNA No translation available.
    BC016639 mRNA Translation: AAH16639.1
    BC025362 mRNA Translation: AAH25362.1
    BC040194 mRNA Translation: AAH40194.3
    BC048134 mRNA Translation: AAH48134.2
    AL833812 mRNA Translation: CAD38675.2
    CCDSiCCDS30627.1 [O60341-1]
    CCDS53278.1 [O60341-2]
    RefSeqiNP_001009999.1, NM_001009999.2 [O60341-2]
    NP_055828.2, NM_015013.3 [O60341-1]
    UniGeneiHs.591518

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2COMNMR-A169-279[»]
    2DW4X-ray2.30A172-831[»]
    2EJRX-ray2.70A172-833[»]
    2H94X-ray2.90A172-835[»]
    2HKOX-ray2.80A172-835[»]
    2IW5X-ray2.57A171-836[»]
    2L3DNMR-A174-273[»]
    2UXNX-ray2.72A171-836[»]
    2UXXX-ray2.74A171-836[»]
    2V1DX-ray3.10A123-852[»]
    2X0LX-ray3.00A123-852[»]
    2XAFX-ray3.25A1-852[»]
    2XAGX-ray3.10A1-852[»]
    2XAHX-ray3.10A1-852[»]
    2XAJX-ray3.30A1-852[»]
    2XAQX-ray3.20A1-852[»]
    2XASX-ray3.20A1-852[»]
    2Y48X-ray3.00A123-852[»]
    2Z3YX-ray2.25A172-833[»]
    2Z5UX-ray2.25A172-833[»]
    3ABTX-ray3.20A172-833[»]
    3ABUX-ray3.10A172-833[»]
    3ZMSX-ray2.96A1-852[»]
    3ZMTX-ray3.10A1-852[»]
    3ZMUX-ray3.20A1-852[»]
    3ZMVX-ray3.00A1-852[»]
    3ZMZX-ray3.00A1-852[»]
    3ZN0X-ray2.80A1-852[»]
    3ZN1X-ray3.10A1-852[»]
    4BAYX-ray3.10A172-852[»]
    4CZZX-ray3.00A1-852[»]
    4KUMX-ray3.05A171-836[»]
    4UV8X-ray2.80A1-852[»]
    4UV9X-ray3.00A1-852[»]
    4UVAX-ray2.90A1-852[»]
    4UVBX-ray2.80A1-852[»]
    4UVCX-ray3.10A1-852[»]
    4UXNX-ray2.85A1-852[»]
    4XBFX-ray2.80A171-836[»]
    5AFWX-ray1.60B108-119[»]
    5H6QX-ray2.53A172-833[»]
    5H6RX-ray2.60A172-833[»]
    5IT3X-ray1.40A/B183-267[»]
    5L3BX-ray3.30A1-852[»]
    5L3CX-ray3.31A1-852[»]
    5L3DX-ray2.60A1-852[»]
    5L3EX-ray2.80A123-852[»]
    5L3FX-ray3.50A123-852[»]
    5L3GX-ray3.10A123-852[»]
    5LBQX-ray3.30A123-852[»]
    5LGNX-ray3.20A172-836[»]
    5LGTX-ray3.00A123-852[»]
    5LGUX-ray3.20A123-852[»]
    5LHGX-ray3.34A1-852[»]
    5LHHX-ray3.05A1-852[»]
    5LHIX-ray3.40A1-852[»]
    5X60X-ray2.69A172-833[»]
    5YJBX-ray2.96A172-833[»]
    ProteinModelPortaliO60341
    SMRiO60341
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116667, 357 interactors
    CORUMiO60341
    DIPiDIP-34641N
    IntActiO60341, 289 interactors
    MINTiO60341
    STRINGi9606.ENSP00000383042

    Chemistry databases

    BindingDBiO60341
    ChEMBLiCHEMBL6136
    GuidetoPHARMACOLOGYi2669

    Protein family/group databases

    MoonDBiO60341 Predicted

    PTM databases

    iPTMnetiO60341
    PhosphoSitePlusiO60341

    Polymorphism and mutation databases

    BioMutaiKDM1A

    Proteomic databases

    EPDiO60341
    jPOSTiO60341
    MaxQBiO60341
    PaxDbiO60341
    PeptideAtlasiO60341
    PRIDEiO60341
    ProteomicsDBi49364
    49365 [O60341-2]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000356634; ENSP00000349049; ENSG00000004487 [O60341-1]
    ENST00000400181; ENSP00000383042; ENSG00000004487 [O60341-2]
    GeneIDi23028
    KEGGihsa:23028
    UCSCiuc001bgi.3 human [O60341-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    23028
    DisGeNETi23028
    EuPathDBiHostDB:ENSG00000004487.15

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    KDM1A
    HGNCiHGNC:29079 KDM1A
    HPAiCAB005884
    HPA053660
    MalaCardsiKDM1A
    MIMi609132 gene
    616728 phenotype
    neXtProtiNX_O60341
    OpenTargetsiENSG00000004487
    Orphaneti477993 Palatal anomalies-widely spaced teeth-facial dysmorphism-developmental delay syndrome
    PharmGKBiPA165751392

    Human Unidentified Gene-Encoded large proteins database

    More...
    HUGEi
    Search...

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0029 Eukaryota
    KOG0685 Eukaryota
    ENOG410XSNC LUCA
    GeneTreeiENSGT00940000157193
    InParanoidiO60341
    KOiK11450
    OMAiLWLENPK
    OrthoDBi679855at2759
    PhylomeDBiO60341
    TreeFamiTF312972

    Enzyme and pathway databases

    BRENDAi1.14.11.B1 2681
    1.14.11.B2 2681
    ReactomeiR-HSA-3214815 HDACs deacetylate histones
    R-HSA-3214842 HDMs demethylate histones
    R-HSA-5625886 Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
    R-HSA-8943724 Regulation of PTEN gene transcription
    R-HSA-9018519 Estrogen-dependent gene expression
    R-HSA-983231 Factors involved in megakaryocyte development and platelet production
    SABIO-RKiO60341
    SIGNORiO60341

    Miscellaneous databases

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

    More...
    ChiTaRSi
    KDM1A human
    EvolutionaryTraceiO60341

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

    More...
    GenomeRNAii
    23028

    Protein Ontology

    More...
    PROi
    PR:O60341

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000004487 Expressed in 233 organ(s), highest expression level in right testis
    CleanExiHS_AOF2
    ExpressionAtlasiO60341 baseline and differential
    GenevisibleiO60341 HS

    Family and domain databases

    Gene3Di1.10.10.10, 1 hit
    3.50.50.60, 2 hits
    InterProiView protein in InterPro
    IPR002937 Amino_oxidase
    IPR036188 FAD/NAD-bd_sf
    IPR017366 Hist_Lys-spec_deMease
    IPR009057 Homeobox-like_sf
    IPR007526 SWIRM
    IPR036388 WH-like_DNA-bd_sf
    PfamiView protein in Pfam
    PF01593 Amino_oxidase, 1 hit
    PF04433 SWIRM, 1 hit
    PIRSFiPIRSF038051 Histone_Lys-demethylase, 1 hit
    SUPFAMiSSF46689 SSF46689, 1 hit
    SSF51905 SSF51905, 1 hit
    PROSITEiView protein in PROSITE
    PS50934 SWIRM, 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 nameiKDM1A_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: O60341
    Secondary accession number(s): A8MWP9
    , Q5TH94, Q5TH95, Q86VT7, Q8IXK4, Q8NDP6, Q8TAZ3, Q96AW4
    <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 16, 2004
    Last sequence update: August 16, 2004
    Last modified: January 16, 2019
    This is version 195 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, Direct protein sequencing, Reference proteome

    Documents

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