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Protein

Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6

Gene

JMJD6

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

Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Acts as a regulator of RNA splicing by mediating 5-hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. In addition to peptidyl-lysine 5-dioxygenase activity, may act as an RNA hydroxylase, as suggested by its ability to bind single strand RNA. Also acts as an arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), thereby playing a role in histone code. However, histone arginine demethylation may not constitute the primary activity in vivo. Has no histone lysine demethylase activity. Required for differentiation of multiple organs during embryogenesis. Acts as a key regulator of hematopoietic differentiation: required for angiogenic sprouting by regulating the pre-mRNA splicing activity of U2AF2/U2AF65. Seems to be necessary for the regulation of macrophage cytokine responses.4 Publications

Caution

Was initially thought to constitute the phosphatidylserine receptor, a receptor that mediates recognition of phosphatidylserine, a specific marker only present at the surface of apoptotic cells. Phosphatidylserine receptor probably participates in apoptotic cell phagocytosis. This protein was identified using phage display expressing mAb 217, an antibody that specifically recognizes phosphatidylserine receptor. However, its nuclear localization and the fact that mAb 217 antibody still recognizes the phosphatidylserine receptor in mice lacking JMJD6, strongly suggest that it does not constitute the receptor for phosphatidylserine and is not involved in apoptotic cell removal.Curated

<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 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=39 µM for 2-oxoglutarate1 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 sitei184SubstrateBy similarity1
    <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 bindingi187Iron; catalytic1
    Metal bindingi189Iron; catalytic1
    Binding sitei1972-oxoglutarate1 Publication1
    Binding sitei204SubstrateBy similarity1
    Metal bindingi273Iron; catalytic1
    Binding sitei2852-oxoglutarate1 Publication1

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

    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, Dioxygenase, Oxidoreductase, RNA-binding
    Biological processDifferentiation, mRNA processing, mRNA splicing, Transcription, Transcription regulation
    LigandIron, Metal-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.14.11.4 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-3214842 HDMs demethylate histones

    <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:
    Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC:1.14.11.-)
    Alternative name(s):
    Histone arginine demethylase JMJD6
    JmjC domain-containing protein 6
    Jumonji domain-containing protein 6
    Lysyl-hydroxylase JMJD6
    Peptide-lysine 5-dioxygenase JMJD6
    Phosphatidylserine receptor
    Short name:
    Protein PTDSR
    <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:JMJD6
    Synonyms:KIAA0585, PTDSR
    <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 17

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000070495.14

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:19355 JMJD6

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    604914 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q6NYC1

    <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>Mutagenesisi131Y → F: Abolishes 2-oxoglutarate-binding and enzyme activity. 1 Publication1
    Mutagenesisi187H → A: Loss of catalytic activity; when associated with A-189 and A-273. 2 Publications1
    Mutagenesisi189D → A: Loss of catalytic activity; when associated with A-187 and A-273. 2 Publications1
    Mutagenesisi204K → A: Impairs enzyme activity without affecting 2-oxoglutarate-binding. 1 Publication1
    Mutagenesisi231E → A: Impairs both hydroxylation activity and 2-oxoglutarate turnover assays. 1 Publication1
    Mutagenesisi273H → A: Loss of catalytic activity; when associated with A-187 and A-189. 1 Publication1
    Mutagenesisi285T → A: Impairs enzyme activity and 2-oxoglutarate-binding. 1 Publication1
    Mutagenesisi287N → A: Impairs enzyme activity. 1 Publication1

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    23210

    Open Targets

    More...
    OpenTargetsi
    ENSG00000070495

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA162392513

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    JMJD6

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    67461014

    <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_00001293691 – 403Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6Add BLAST403

    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 residuei38PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q6NYC1

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q6NYC1

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

    More...
    PaxDbi
    Q6NYC1

    PeptideAtlas

    More...
    PeptideAtlasi
    Q6NYC1

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q6NYC1

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    66781
    66782 [Q6NYC1-2]
    66783 [Q6NYC1-3]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q6NYC1

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

    More...
    PhosphoSitePlusi
    Q6NYC1

    <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

    Highly expressed in the heart, skeletal muscle and kidney. Expressed at moderate or low level in brain, placenta, lung, liver, pancreas, spleen, thymus, prostate, testis and ovary. Up-regulated in many patients with chronic pancreatitis. Expressed in nursing thymic epithelial cells.3 Publications

    <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

    Up-regulated upon cytokine treatment, but not upon TNF treatment.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000070495 Expressed in 228 organ(s), highest expression level in blood

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_JMJD6

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q6NYC1 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q6NYC1 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB004548
    HPA059156

    <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 LUC7L2, LUC7L3 and U2AF2/U2AF65. Interacts with BRD4. Interacts with LIAT1 (By similarity).By similarity4 Publications

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

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    116817, 133 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-60686N

    Protein interaction database and analysis system

    More...
    IntActi
    Q6NYC1, 63 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q6NYC1

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000394085

    <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

    1403
    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
    Q6NYC1

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

    More...
    SMRi
    Q6NYC1

    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
    Q6NYC1

    <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>Domaini141 – 305JmjCPROSITE-ProRule annotationAdd BLAST165

    Motif

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi6 – 10Nuclear localization signal 11 Publication5
    Motifi91 – 95Nuclear localization signal 21 Publication5
    Motifi141 – 145Nuclear localization signal 31 Publication5
    Motifi167 – 170Nuclear localization signal 41 Publication4
    Motifi373 – 378Nuclear localization signal 51 Publication6

    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 biasi340 – 365Ser-richAdd BLAST26

    <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 nuclear localization signal motifs are necessary and sufficient to target it into the nucleus.

    <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 JMJD6 family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG2130 Eukaryota
    ENOG410XQCR LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000156867

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000265824

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG054774

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q6NYC1

    KEGG Orthology (KO)

    More...
    KOi
    K11323

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG091G0AJ6

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q6NYC1

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF314988

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR003347 JmjC_dom

    Pfam protein domain database

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

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00558 JmjC, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51184 JMJC, 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 (3+)i

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

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

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

    Isoform 1 (identifier: Q6NYC1-1) [UniParc]FASTAAdd to basket
    Also known as: Alpha

    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
    MNHKSKKRIR EAKRSARPEL KDSLDWTRHN YYESFSLSPA AVADNVERAD
    60 70 80 90 100
    ALQLSVEEFV ERYERPYKPV VLLNAQEGWS AQEKWTLERL KRKYRNQKFK
    110 120 130 140 150
    CGEDNDGYSV KMKMKYYIEY MESTRDDSPL YIFDSSYGEH PKRRKLLEDY
    160 170 180 190 200
    KVPKFFTDDL FQYAGEKRRP PYRWFVMGPP RSGTGIHIDP LGTSAWNALV
    210 220 230 240 250
    QGHKRWCLFP TSTPRELIKV TRDEGGNQQD EAITWFNVIY PRTQLPTWPP
    260 270 280 290 300
    EFKPLEILQK PGETVFVPGG WWHVVLNLDT TIAITQNFAS STNFPVVWHK
    310 320 330 340 350
    TVRGRPKLSR KWYRILKQEH PELAVLADSV DLQESTGIAS DSSSDSSSSS
    360 370 380 390 400
    SSSSSDSDSE CESGSEGDGT VHRRKKRRTC SMVGNGDTTS QDDCVSKERS

    SSR
    Length:403
    Mass (Da):46,462
    Last modified:July 5, 2004 - v1
    <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:i9C9AADA98B24B035
    GO
    Isoform 2 (identifier: Q6NYC1-2) [UniParc]FASTAAdd to basket
    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         361-402: Missing.
         403-403: R → RIRDTCGGRAHP

    Show »
    Length:372
    Mass (Da):43,109
    Checksum:i14154B874F1983DF
    GO
    Isoform 3 (identifier: Q6NYC1-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         403-403: R → RIRDTCGGRAHP

    Show »
    Length:414
    Mass (Da):47,626
    Checksum:iCD586580857C6C46
    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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    B2WTI4B2WTI4_HUMAN
    Bifunctional arginine demethylase a...
    JMJD6
    361Annotation 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>
    K7EJU9K7EJU9_HUMAN
    Bifunctional arginine demethylase a...
    JMJD6
    395Annotation 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>
    B2WTI3B2WTI3_HUMAN
    Bifunctional arginine demethylase a...
    JMJD6 PTDSR, hCG_30900
    335Annotation 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 AAH47003 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAA25511 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 conflicti136S → G in BAG51050 (PubMed:14702039).Curated1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. 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_014022361 – 402Missing in isoform 2. 1 PublicationAdd BLAST42
    Alternative sequenceiVSP_014023403R → RIRDTCGGRAHP in isoform 2 and isoform 3. 3 Publications1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    AB073711 mRNA Translation: BAC16755.1
    AB011157 mRNA Translation: BAA25511.1 Different initiation.
    AK021780 mRNA Translation: BAG51050.1
    AK294816 mRNA Translation: BAG57932.1
    AC005837 Genomic DNA No translation available.
    CH471099 Genomic DNA Translation: EAW89434.1
    BC047003 mRNA Translation: AAH47003.1 Different initiation.
    BC066654 mRNA Translation: AAH66654.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS42383.1 [Q6NYC1-3]
    CCDS42384.1 [Q6NYC1-1]

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001074930.1, NM_001081461.1 [Q6NYC1-3]
    NP_055982.2, NM_015167.2 [Q6NYC1-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.514505

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000397625; ENSP00000380750; ENSG00000070495 [Q6NYC1-1]
    ENST00000445478; ENSP00000394085; ENSG00000070495 [Q6NYC1-3]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    23210

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:23210

    UCSC genome browser

    More...
    UCSCi
    uc002jsn.2 human [Q6NYC1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    <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
    AB073711 mRNA Translation: BAC16755.1
    AB011157 mRNA Translation: BAA25511.1 Different initiation.
    AK021780 mRNA Translation: BAG51050.1
    AK294816 mRNA Translation: BAG57932.1
    AC005837 Genomic DNA No translation available.
    CH471099 Genomic DNA Translation: EAW89434.1
    BC047003 mRNA Translation: AAH47003.1 Different initiation.
    BC066654 mRNA Translation: AAH66654.1
    CCDSiCCDS42383.1 [Q6NYC1-3]
    CCDS42384.1 [Q6NYC1-1]
    RefSeqiNP_001074930.1, NM_001081461.1 [Q6NYC1-3]
    NP_055982.2, NM_015167.2 [Q6NYC1-1]
    UniGeneiHs.514505

    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
    3K2OX-ray1.75A/B2-335[»]
    3LD8X-ray2.70A1-334[»]
    3LDBX-ray2.70A1-334[»]
    6BNHNMR-B84-96[»]
    6FQCX-ray1.67A/B1-403[»]
    ProteinModelPortaliQ6NYC1
    SMRiQ6NYC1
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116817, 133 interactors
    DIPiDIP-60686N
    IntActiQ6NYC1, 63 interactors
    MINTiQ6NYC1
    STRINGi9606.ENSP00000394085

    PTM databases

    iPTMnetiQ6NYC1
    PhosphoSitePlusiQ6NYC1

    Polymorphism and mutation databases

    BioMutaiJMJD6
    DMDMi67461014

    Proteomic databases

    EPDiQ6NYC1
    MaxQBiQ6NYC1
    PaxDbiQ6NYC1
    PeptideAtlasiQ6NYC1
    PRIDEiQ6NYC1
    ProteomicsDBi66781
    66782 [Q6NYC1-2]
    66783 [Q6NYC1-3]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000397625; ENSP00000380750; ENSG00000070495 [Q6NYC1-1]
    ENST00000445478; ENSP00000394085; ENSG00000070495 [Q6NYC1-3]
    GeneIDi23210
    KEGGihsa:23210
    UCSCiuc002jsn.2 human [Q6NYC1-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    23210
    DisGeNETi23210
    EuPathDBiHostDB:ENSG00000070495.14

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    JMJD6
    HGNCiHGNC:19355 JMJD6
    HPAiCAB004548
    HPA059156
    MIMi604914 gene
    neXtProtiNX_Q6NYC1
    OpenTargetsiENSG00000070495
    PharmGKBiPA162392513

    Human Unidentified Gene-Encoded large proteins database

    More...
    HUGEi
    Search...

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG2130 Eukaryota
    ENOG410XQCR LUCA
    GeneTreeiENSGT00940000156867
    HOGENOMiHOG000265824
    HOVERGENiHBG054774
    InParanoidiQ6NYC1
    KOiK11323
    OrthoDBiEOG091G0AJ6
    PhylomeDBiQ6NYC1
    TreeFamiTF314988

    Enzyme and pathway databases

    BRENDAi1.14.11.4 2681
    ReactomeiR-HSA-3214842 HDMs demethylate histones

    Miscellaneous databases

    EvolutionaryTraceiQ6NYC1

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    JMJD6

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

    More...
    GenomeRNAii
    23210

    Protein Ontology

    More...
    PROi
    PR:Q6NYC1

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000070495 Expressed in 228 organ(s), highest expression level in blood
    CleanExiHS_JMJD6
    ExpressionAtlasiQ6NYC1 baseline and differential
    GenevisibleiQ6NYC1 HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR003347 JmjC_dom
    PfamiView protein in Pfam
    PF02373 JmjC, 1 hit
    SMARTiView protein in SMART
    SM00558 JmjC, 1 hit
    PROSITEiView protein in PROSITE
    PS51184 JMJC, 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 nameiJMJD6_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: Q6NYC1
    Secondary accession number(s): B3KMN8
    , B4DGX1, Q86VY0, Q8IUM5, Q9Y4E2
    <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: June 7, 2005
    Last sequence update: July 5, 2004
    Last modified: December 5, 2018
    This is version 141 of the entry and version 1 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    UniProt is an ELIXIR core data resource
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