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Q6NYC1

- JMJD6_HUMAN

UniProt

Q6NYC1 - JMJD6_HUMAN

Protein

Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6

Gene

JMJD6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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

    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

    1. histone demethylase activity (H3-R2 specific) Source: UniProtKB
    2. histone demethylase activity (H4-R3 specific) Source: UniProtKB
    3. identical protein binding Source: IntAct
    4. iron ion binding Source: UniProtKB
    5. peptidyl-lysine 5-dioxygenase activity Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. receptor activity Source: Ensembl
    8. RNA binding Source: UniProtKB
    9. single-stranded RNA binding Source: UniProtKB

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: Ensembl
    2. erythrocyte development Source: Ensembl
    3. heart development Source: Ensembl
    4. histone H3-R2 demethylation Source: BHF-UCL
    5. histone H4-R3 demethylation Source: BHF-UCL
    6. kidney development Source: Ensembl
    7. lung development Source: Ensembl
    8. macrophage activation Source: Ensembl
    9. mRNA processing Source: UniProtKB-KW
    10. peptidyl-lysine hydroxylation to 5-hydroxy-L-lysine Source: UniProtKB
    11. phosphatidylserine exposure on apoptotic cell surface Source: Ensembl
    12. recognition of apoptotic cell Source: Ensembl
    13. regulation of mRNA splicing, via spliceosome Source: UniProtKB
    14. regulation of transcription, DNA-templated Source: UniProtKB-KW
    15. retina development in camera-type eye Source: Ensembl
    16. RNA splicing Source: UniProtKB-KW
    17. sprouting angiogenesis Source: UniProtKB
    18. T cell differentiation in thymus Source: Ensembl
    19. transcription, DNA-templated Source: UniProtKB-KW

    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

    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: 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

    1. nucleolus Source: UniProtKB
    2. nucleoplasm Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. plasma membrane Source: Ensembl

    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.

    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

    ArrayExpressiQ6NYC1.
    BgeeiQ6NYC1.
    CleanExiHS_JMJD6.
    GenevestigatoriQ6NYC1.

    Organism-specific databases

    HPAiCAB004548.

    Interactioni

    Subunit structurei

    Interacts with LUC7L2, LUC7L3 and U2AF2/U2AF65. Interacts with BRD4.4 Publications

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi116817. 51 interactions.
    DIPiDIP-60686N.
    IntActiQ6NYC1. 29 interactions.
    MINTiMINT-3086431.
    STRINGi9606.ENSP00000394085.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000265824.
    HOVERGENiHBG054774.
    InParanoidiQ6NYC1.
    KOiK11323.
    OMAiANLIAIE.
    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. Align

    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

    MNHKSKKRIR EAKRSARPEL KDSLDWTRHN YYESFSLSPA AVADNVERAD    50
    ALQLSVEEFV ERYERPYKPV VLLNAQEGWS AQEKWTLERL KRKYRNQKFK 100
    CGEDNDGYSV KMKMKYYIEY MESTRDDSPL YIFDSSYGEH PKRRKLLEDY 150
    KVPKFFTDDL FQYAGEKRRP PYRWFVMGPP RSGTGIHIDP LGTSAWNALV 200
    QGHKRWCLFP TSTPRELIKV TRDEGGNQQD EAITWFNVIY PRTQLPTWPP 250
    EFKPLEILQK PGETVFVPGG WWHVVLNLDT TIAITQNFAS STNFPVVWHK 300
    TVRGRPKLSR KWYRILKQEH PELAVLADSV DLQESTGIAS DSSSDSSSSS 350
    SSSSSDSDSE CESGSEGDGT VHRRKKRRTC SMVGNGDTTS QDDCVSKERS 400
    SSR 403
    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.
    The sequence BAA25511.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    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:
    EMBL
    GenBank
    DDBJ
    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. [Q6NYC1-1]
    ENST00000445478; ENSP00000394085; ENSG00000070495. [Q6NYC1-3]
    GeneIDi23210.
    KEGGihsa:23210.
    UCSCiuc002jsn.1. human. [Q6NYC1-3]
    uc002jso.3. human. [Q6NYC1-1]

    Polymorphism databases

    DMDMi67461014.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS42383.1. [Q6NYC1-3 ]
    CCDS42384.1. [Q6NYC1-1 ]
    RefSeqi NP_001074930.1. NM_001081461.1. [Q6NYC1-3 ]
    NP_055982.2. NM_015167.2. [Q6NYC1-1 ]
    UniGenei Hs.514505.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3K2O X-ray 1.75 A/B 2-335 [» ]
    3LD8 X-ray 2.70 A 1-334 [» ]
    3LDB X-ray 2.70 A 1-334 [» ]
    ProteinModelPortali Q6NYC1.
    SMRi Q6NYC1. Positions 1-335.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116817. 51 interactions.
    DIPi DIP-60686N.
    IntActi Q6NYC1. 29 interactions.
    MINTi MINT-3086431.
    STRINGi 9606.ENSP00000394085.

    PTM databases

    PhosphoSitei Q6NYC1.

    Polymorphism databases

    DMDMi 67461014.

    Proteomic databases

    MaxQBi Q6NYC1.
    PaxDbi Q6NYC1.
    PRIDEi Q6NYC1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397625 ; ENSP00000380750 ; ENSG00000070495 . [Q6NYC1-1 ]
    ENST00000445478 ; ENSP00000394085 ; ENSG00000070495 . [Q6NYC1-3 ]
    GeneIDi 23210.
    KEGGi hsa:23210.
    UCSCi uc002jsn.1. human. [Q6NYC1-3 ]
    uc002jso.3. human. [Q6NYC1-1 ]

    Organism-specific databases

    CTDi 23210.
    GeneCardsi GC17M074708.
    HGNCi HGNC:19355. JMJD6.
    HPAi CAB004548.
    MIMi 604914. gene.
    neXtProti NX_Q6NYC1.
    PharmGKBi PA162392513.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG124833.
    HOGENOMi HOG000265824.
    HOVERGENi HBG054774.
    InParanoidi Q6NYC1.
    KOi K11323.
    OMAi ANLIAIE.
    PhylomeDBi Q6NYC1.
    TreeFami TF314988.

    Miscellaneous databases

    EvolutionaryTracei Q6NYC1.
    GeneWikii JMJD6.
    GenomeRNAii 23210.
    NextBioi 44753.
    PROi Q6NYC1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6NYC1.
    Bgeei Q6NYC1.
    CleanExi HS_JMJD6.
    Genevestigatori Q6NYC1.

    Family and domain databases

    InterProi IPR003347. JmjC_dom.
    [Graphical view ]
    Pfami PF02373. JmjC. 1 hit.
    [Graphical view ]
    SMARTi SM00558. JmjC. 1 hit.
    [Graphical view ]
    PROSITEi PS51184. JMJC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 104 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