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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-Experimental evidence at protein leveli

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

Cofactori

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

Kineticsi

  1. KM=39 µM for 2-oxoglutarate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei184 – 1841SubstrateBy similarity
    Metal bindingi187 – 1871Iron; catalytic
    Metal bindingi189 – 1891Iron; catalytic
    Binding sitei197 – 19712-oxoglutarate1 Publication
    Binding sitei204 – 2041SubstrateBy similarity
    Metal bindingi273 – 2731Iron; catalytic
    Binding sitei285 – 28512-oxoglutarate1 Publication

    GO - Molecular functioni

    • histone demethylase activity (H3-R2 specific) Source: UniProtKB
    • histone demethylase activity (H4-R3 specific) Source: UniProtKB
    • identical protein binding Source: IntAct
    • iron ion binding Source: UniProtKB
    • peptidyl-lysine 5-dioxygenase activity Source: UniProtKB
    • receptor activity Source: Ensembl
    • RNA binding Source: UniProtKB
    • single-stranded RNA binding Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Chromatin regulator, Developmental protein, Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Differentiation, mRNA processing, mRNA splicing, Transcription, Transcription regulation

    Keywords - Ligandi

    Iron, Metal-binding, RNA-binding

    Enzyme and pathway databases

    BRENDAi1.14.11.4. 2681.

    Names & Taxonomyi

    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
    Gene namesi
    Name:JMJD6
    Synonyms:KIAA0585, PTDSR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:19355. JMJD6.

    Subcellular locationi

    • Nucleusnucleoplasm
    • Nucleusnucleolus

    • Note: Mainly found throughout the nucleoplasm outside of regions containing heterochromatic DNA, with some localization in nucleolus. During mitosis, excluded from the nucleus and reappears in the telophase of the cell cycle.

    GO - Cellular componenti

    • nucleolus Source: UniProtKB
    • nucleoplasm Source: UniProtKB
    • nucleus Source: UniProtKB
    • plasma membrane Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi131 – 1311Y → F: Abolishes 2-oxoglutarate-binding and enzyme activity. 1 Publication
    Mutagenesisi187 – 1871H → A: Loss of catalytic activity; when associated with A-189 and A-273. 2 Publications
    Mutagenesisi189 – 1891D → A: Loss of catalytic activity; when associated with A-187 and A-273. 2 Publications
    Mutagenesisi204 – 2041K → A: Impairs enzyme activity without affecting 2-oxoglutarate-binding. 1 Publication
    Mutagenesisi231 – 2311E → A: Impairs both hydroxylation activity and 2-oxoglutarate turnover assays. 1 Publication
    Mutagenesisi273 – 2731H → A: Loss of catalytic activity; when associated with A-187 and A-189. 1 Publication
    Mutagenesisi285 – 2851T → A: Impairs enzyme activity and 2-oxoglutarate-binding. 1 Publication
    Mutagenesisi287 – 2871N → A: Impairs enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA162392513.

    Polymorphism and mutation databases

    BioMutaiJMJD6.
    DMDMi67461014.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 403403Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6PRO_0000129369Add
    BLAST

    Proteomic databases

    MaxQBiQ6NYC1.
    PaxDbiQ6NYC1.
    PRIDEiQ6NYC1.

    PTM databases

    PhosphoSiteiQ6NYC1.

    Expressioni

    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

    Inductioni

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

    Gene expression databases

    BgeeiQ6NYC1.
    CleanExiHS_JMJD6.
    ExpressionAtlasiQ6NYC1. baseline and differential.
    GenevisibleiQ6NYC1. HS.

    Organism-specific databases

    HPAiCAB004548.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-8464037,EBI-8464037
    BRD4O6088510EBI-8464037,EBI-723869
    CDK9P507505EBI-8464037,EBI-1383449
    FRMD6Q96NE93EBI-8464037,EBI-741729
    NAA50Q9GZZ13EBI-8464037,EBI-1052523
    PRPF38AQ8NAV12EBI-8464037,EBI-715374
    U2AF1Q010812EBI-8464037,EBI-632461
    ZCCHC17Q9NP642EBI-8464037,EBI-746345

    Protein-protein interaction databases

    BioGridi116817. 131 interactions.
    DIPiDIP-60686N.
    IntActiQ6NYC1. 31 interactions.
    MINTiMINT-3086431.
    STRINGi9606.ENSP00000394085.

    Structurei

    Secondary structure

    1
    403
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1614Combined sources
    Helixi23 – 275Combined sources
    Helixi31 – 344Combined sources
    Helixi39 – 413Combined sources
    Beta strandi48 – 503Combined sources
    Helixi51 – 533Combined sources
    Helixi56 – 627Combined sources
    Turni63 – 675Combined sources
    Beta strandi70 – 745Combined sources
    Turni75 – 784Combined sources
    Helixi81 – 844Combined sources
    Helixi87 – 937Combined sources
    Beta strandi98 – 1036Combined sources
    Beta strandi109 – 1135Combined sources
    Helixi114 – 12310Combined sources
    Beta strandi132 – 1354Combined sources
    Helixi137 – 1393Combined sources
    Helixi143 – 1497Combined sources
    Helixi154 – 1563Combined sources
    Helixi160 – 1645Combined sources
    Turni166 – 1683Combined sources
    Beta strandi173 – 1786Combined sources
    Beta strandi183 – 1875Combined sources
    Helixi190 – 1923Combined sources
    Beta strandi194 – 2029Combined sources
    Beta strandi204 – 2096Combined sources
    Helixi215 – 2184Combined sources
    Helixi222 – 2254Combined sources
    Helixi226 – 2283Combined sources
    Helixi232 – 2387Combined sources
    Helixi240 – 2445Combined sources
    Helixi250 – 2523Combined sources
    Beta strandi255 – 2595Combined sources
    Beta strandi264 – 2674Combined sources
    Beta strandi272 – 2798Combined sources
    Beta strandi281 – 2888Combined sources
    Turni291 – 2933Combined sources
    Helixi294 – 30411Combined sources
    Helixi306 – 31914Combined sources
    Helixi321 – 33313Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3K2OX-ray1.75A/B2-335[»]
    3LD8X-ray2.70A1-334[»]
    3LDBX-ray2.70A1-334[»]
    ProteinModelPortaliQ6NYC1.
    SMRiQ6NYC1. Positions 1-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6NYC1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini141 – 305165JmjCPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi6 – 105Nuclear localization signal 11 Publication
    Motifi91 – 955Nuclear localization signal 21 Publication
    Motifi141 – 1455Nuclear localization signal 31 Publication
    Motifi167 – 1704Nuclear localization signal 41 Publication
    Motifi373 – 3786Nuclear localization signal 51 Publication

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi340 – 36526Ser-richAdd
    BLAST

    Domaini

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

    Sequence similaritiesi

    Belongs to the JMJD6 family.Curated
    Contains 1 JmjC domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG124833.
    GeneTreeiENSGT00530000063579.
    HOGENOMiHOG000265824.
    HOVERGENiHBG054774.
    InParanoidiQ6NYC1.
    KOiK11323.
    PhylomeDBiQ6NYC1.
    TreeFamiTF314988.

    Family and domain databases

    InterProiIPR003347. JmjC_dom.
    [Graphical view]
    PfamiPF02373. JmjC. 1 hit.
    [Graphical view]
    SMARTiSM00558. JmjC. 1 hit.
    [Graphical view]
    PROSITEiPS51184. JMJC. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    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
    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

    Sequence cautioni

    The sequence AAH47003.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence BAA25511.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1361S → G in BAG51050 (PubMed:14702039).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei361 – 40242Missing in isoform 2. 1 PublicationVSP_014022Add
    BLAST
    Alternative sequencei403 – 4031R → RIRDTCGGRAHP in isoform 2 and isoform 3. 3 PublicationsVSP_014023

    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.

    Genome annotation databases

    EnsembliENST00000397625; ENSP00000380750; ENSG00000070495.
    ENST00000445478; ENSP00000394085; ENSG00000070495. [Q6NYC1-3]
    GeneIDi23210.
    KEGGihsa:23210.
    UCSCiuc002jsn.1. human. [Q6NYC1-3]
    uc002jso.3. human. [Q6NYC1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    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:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3K2OX-ray1.75A/B2-335[»]
    3LD8X-ray2.70A1-334[»]
    3LDBX-ray2.70A1-334[»]
    ProteinModelPortaliQ6NYC1.
    SMRiQ6NYC1. Positions 1-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi116817. 131 interactions.
    DIPiDIP-60686N.
    IntActiQ6NYC1. 31 interactions.
    MINTiMINT-3086431.
    STRINGi9606.ENSP00000394085.

    PTM databases

    PhosphoSiteiQ6NYC1.

    Polymorphism and mutation databases

    BioMutaiJMJD6.
    DMDMi67461014.

    Proteomic databases

    MaxQBiQ6NYC1.
    PaxDbiQ6NYC1.
    PRIDEiQ6NYC1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000397625; ENSP00000380750; ENSG00000070495.
    ENST00000445478; ENSP00000394085; ENSG00000070495. [Q6NYC1-3]
    GeneIDi23210.
    KEGGihsa:23210.
    UCSCiuc002jsn.1. human. [Q6NYC1-3]
    uc002jso.3. human. [Q6NYC1-1]

    Organism-specific databases

    CTDi23210.
    GeneCardsiGC17M074708.
    HGNCiHGNC:19355. JMJD6.
    HPAiCAB004548.
    MIMi604914. gene.
    neXtProtiNX_Q6NYC1.
    PharmGKBiPA162392513.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG124833.
    GeneTreeiENSGT00530000063579.
    HOGENOMiHOG000265824.
    HOVERGENiHBG054774.
    InParanoidiQ6NYC1.
    KOiK11323.
    PhylomeDBiQ6NYC1.
    TreeFamiTF314988.

    Enzyme and pathway databases

    BRENDAi1.14.11.4. 2681.

    Miscellaneous databases

    EvolutionaryTraceiQ6NYC1.
    GeneWikiiJMJD6.
    GenomeRNAii23210.
    NextBioi44753.
    PROiQ6NYC1.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ6NYC1.
    CleanExiHS_JMJD6.
    ExpressionAtlasiQ6NYC1. baseline and differential.
    GenevisibleiQ6NYC1. HS.

    Family and domain databases

    InterProiIPR003347. JmjC_dom.
    [Graphical view]
    PfamiPF02373. JmjC. 1 hit.
    [Graphical view]
    SMARTiSM00558. JmjC. 1 hit.
    [Graphical view]
    PROSITEiPS51184. JMJC. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Identification of an alternative form of phosphatidylserine receptor."
      Izawa M., Takahashi M.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Stomach cancer.
    2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Brain and Embryo.
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Skin and Uterus.
    7. "Nuclear localization of the phosphatidylserine receptor protein via multiple nuclear localization signals."
      Cui P., Qin B., Liu N., Pan G., Pei D.
      Exp. Cell Res. 293:154-163(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNALS.
    8. "Phosphatidylserine receptor cooperates with high-density lipoprotein receptor in recognition of apoptotic cells by thymic nurse cells."
      Cao W.M., Murao K., Imachi H., Hiramine C., Abe H., Yu X., Dobashi H., Wong N.C.W., Takahara J., Ishida T.
      J. Mol. Endocrinol. 32:497-505(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    9. "Phosphatidylserine receptor in chronic pancreatitis: evidence for a macrophage independent role."
      Koeninger J., Balaz P., Wagner M., Shi X., Cima I., Zimmermann A., di Sebastiano P., Buechler M.W., Friess H.
      Ann. Surg. 241:144-151(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    10. "JMJD6 is a histone arginine demethylase."
      Chang B., Chen Y., Zhao Y., Bruick R.K.
      Science 318:444-447(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS HISTONE DEMETHYLASE, MUTAGENESIS OF HIS-187; ASP-189 AND HIS-273.
    11. Cited for: FUNCTION AS LYSYL-HYDROXYLASE, COFACTOR, INTERACTION WITH LUC7L2; LUC7L3 AND U2AF2, MUTAGENESIS OF HIS-187 AND ASP-189.
    12. "Analysis of Jmjd6 cellular localization and testing for its involvement in histone demethylation."
      Hahn P., Wegener I., Burrells A., Bose J., Wolf A., Erck C., Butler D., Schofield C.J., Bottger A., Lengeling A.
      PLoS ONE 5:E13769-E13769(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, RNA-BINDING, FUNCTION.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3."
      Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W., Howley P.M.
      Mol. Cell. Biol. 31:2641-2652(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BRD4.
    15. "Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6."
      Mantri M., Krojer T., Bagg E.A., Webby C.J., Butler D.S., Kochan G., Kavanagh K.L., Oppermann U., McDonough M.A., Schofield C.J.
      J. Mol. Biol. 401:211-222(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-335 IN COMPLEX WITH NICKEL IONS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-131; LYS-204; GLU-231; THR-285 AND ASN-287.
    16. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-334 IN COMPLEX WITH IRON IONS AND 2-OXOGLUTARATE, POSSIBLE FUNCTION, RNA-BINDING.

    Entry informationi

    Entry nameiJMJD6_HUMAN
    AccessioniPrimary (citable) accession number: Q6NYC1
    Secondary accession number(s): B3KMN8
    , B4DGX1, Q86VY0, Q8IUM5, Q9Y4E2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: July 5, 2004
    Last modified: July 22, 2015
    This is version 113 of the entry and version 1 of the sequence. [Complete history]
    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.

    Miscellaneousi

    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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.