UniProtKB Entry Q6NYC1 – Comparing version 52 to 71
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… - AC Q6NYC1; Q86VY0; Q8IUM5; Q9Y4E2;
+ AC Q6NYC1; B3KMN8; B4DGX1; Q86VY0; Q8IUM5; Q9Y4E2;
… - DT 28-JUL-2009, entry version 52. - DE RecName: Full=Histone arginine demethylase JMJD6;
+ DT 08-MAR-2011, entry version 71. + DE RecName: Full=Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6;
… + DE AltName: Full=Histone arginine demethylase JMJD6;
… - DE AltName: Full=Protein PTDSR;
+ DE AltName: Full=Lysyl-hydroxylase JMJD6; + DE AltName: Full=Peptide-lysine 5-dioxygenase JMJD6;
… + DE Short=Protein PTDSR;
… + RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). + RC TISSUE=Brain, and Embryo; + RX PubMed=14702039; DOI=10.1038/ng1285; + RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., + RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., + RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., + RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., + RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., + RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., + RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., + RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., + RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., + RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., + RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., + RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., + RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., + RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., + RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., + RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., + RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., + RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., + RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., + RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., + RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., + RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., + RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., + RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., + RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., + RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., + RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., + RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; + RT "Complete sequencing and characterization of 21,243 full-length human + RT cDNAs."; + RL Nat. Genet. 36:40-45(2004). + RN [4] + RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. + RX PubMed=16625196; DOI=10.1038/nature04689; + RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., + RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., + RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., + RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., + RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., + RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., + RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., + RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., + RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., + RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., + RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., + RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., + RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., + RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; + RT "DNA sequence of human chromosome 17 and analysis of rearrangement in + RT the human lineage."; + RL Nature 440:1045-1049(2006). + RN [5] + RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. + RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., + RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., + RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., + RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., + RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., + RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., + RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., + RA Venter J.C.; + RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. + RN [6]
… - RN [4]
+ RN [7]
… - RN [5]
+ RN [8]
… - RN [6]
+ RN [9]
… - RN [7] - RP FUNCTION, AND MUTAGENESIS OF HIS-187; ASP-189 AND HIS-273.
+ RN [10] + RP FUNCTION AS HISTONE DEMETHYLASE, AND MUTAGENESIS OF HIS-187; ASP-189 + RP AND HIS-273.
… - RN [8] - RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
+ RN [11] + RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
… - CC -!- FUNCTION: Arginine demethylase which demethylates histone H3 at - CC 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me). Required for - CC differentiation of multiple organs during embryogenesis. Probably - CC acts as a key regulator of hematopoietic differentiation. Seems to - CC be necessary for the regulation of macrophage cytokine responses.
+ RN [12] + RP FUNCTION AS LYSYL-HYDROXYLASE, COFACTOR, INTERACTION WITH LUC7L2; + RP LUC7L3 AND U2AF2, AND MUTAGENESIS OF HIS-187 AND ASP-189. + RX PubMed=19574390; DOI=10.1126/science.1175865; + RA Webby C.J., Wolf A., Gromak N., Dreger M., Kramer H., Kessler B., + RA Nielsen M.L., Schmitz C., Butler D.S., Yates J.R. III, Delahunty C.M., + RA Hahn P., Lengeling A., Mann M., Proudfoot N.J., Schofield C.J., + RA Boettger A.; + RT "Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated + RT with RNA splicing."; + RL Science 325:90-93(2009). + RN [13] + RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-335 IN COMPLEX WITH NICKEL + RP IONS. + RG Structural genomics consortium (SGC); + RT "Structure of an oxygenase."; + RL Submitted (NOV-2009) to the PDB data bank. + CC -!- FUNCTION: Dioxygenase that can both act as a histone arginine + CC demethylase and a lysyl-hydroxylase. Arginine demethylase which + CC demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at + CC 'Arg-3' (H4R3me), thereby playing a central role in histone code. + CC Also acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on + CC specific lysine residues of target proteins such as U2AF2/U2AF65 + CC and LUC7L2. Acts as a regulator of RNA splicing by mediating 5- + CC hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing + CC activity of U2AF2/U2AF65. Required for differentiation of multiple + CC organs during embryogenesis. Probably acts as a key regulator of + CC hematopoietic differentiation. Seems to be necessary for the + CC regulation of macrophage cytokine responses. + CC -!- COFACTOR: Binds 1 Fe(2+) ion per subunit. + CC -!- SUBUNIT: Interacts with LUC7L2, LUC7L3 and U2AF2/U2AF65.
… - CC -!- INDUCTION: Up-regulated upon cytokine treatment, but not upon TNF- - CC alpha treatment.
+ CC -!- INDUCTION: Up-regulated upon cytokine treatment, but not upon TNF + CC treatment.
… - CC -!- SIMILARITY: Belongs to the PTDSR family.
+ CC -!- SIMILARITY: Belongs to the JMJD6 family.
… + CC -!- SEQUENCE CAUTION: + CC Sequence=AAH47003.1; Type=Erroneous initiation; + CC Sequence=BAA25511.1; Type=Erroneous initiation;
… + DR EMBL; AK021780; BAG51050.1; -; mRNA. + DR EMBL; AK294816; BAG57932.1; -; mRNA. + DR EMBL; AC005837; -; NOT_ANNOTATED_CDS; Genomic_DNA. + DR EMBL; CH471099; EAW89434.1; -; Genomic_DNA.
… - DR RefSeq; NP_001074930.1; -. - DR RefSeq; NP_055982.2; -.
+ DR RefSeq; NP_001074930.1; NM_001081461.1. + DR RefSeq; NP_055982.2; NM_015167.2.
… + DR PDB; 3K2O; X-ray; 1.75 A; A/B=1-335. + DR PDB; 3LD8; X-ray; 2.70 A; A=1-334. + DR PDB; 3LDB; X-ray; 2.70 A; A=1-334. + DR PDBsum; 3K2O; -. + DR PDBsum; 3LD8; -. + DR PDBsum; 3LDB; -. + DR ProteinModelPortal; Q6NYC1; -. + DR SMR; Q6NYC1; 1-335. + DR STRING; Q6NYC1; -.
… - DR Ensembl; ENST00000303996; ENSP00000302916; ENSG00000070495; Homo sapiens. - DR Ensembl; ENST00000344991; ENSP00000345857; ENSG00000070495; Homo sapiens. - DR Ensembl; ENST00000397625; ENSP00000380750; ENSG00000070495; Homo sapiens.
+ DR Ensembl; ENST00000303996; ENSP00000302916; ENSG00000070495. + DR Ensembl; ENST00000445478; ENSP00000394085; ENSG00000070495.
… - DR GeneCards; GC17M072221; -.
+ DR CTD; 23210; -. + DR GeneCards; GC17M074708; -.
… - DR HOVERGEN; Q6NYC1; -. - DR OMA; Q6NYC1; MHRRKKR.
+ DR neXtProt; NX_Q6NYC1; -. + DR PharmGKB; PA162392513; -. + DR eggNOG; prNOG09054; -. + DR GeneTree; ENSGT00530000063579; -. + DR HOGENOM; HBG315636; -. + DR HOVERGEN; HBG054774; -. + DR InParanoid; Q6NYC1; -. + DR OMA; MHRRKKR; -. + DR OrthoDB; EOG4VMFFJ; -.
… + DR Genevestigator; Q6NYC1; -.
… - DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. - DR GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW. - DR GO; GO:0070078; P:histone H3-R2 demethylation; IDA:UniProtKB. - DR GO; GO:0070079; P:histone H4-R3 demethylation; IDA:UniProtKB. - DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
+ DR GO; GO:0042802; F:identical protein binding; IDA:BHF-UCL. + DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. + DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW. + DR GO; GO:0070815; F:peptidyl-lysine 5-dioxygenase activity; IDA:UniProtKB. + DR GO; GO:0070078; P:histone H3-R2 demethylation; IDA:BHF-UCL. + DR GO; GO:0070079; P:histone H4-R3 demethylation; IDA:BHF-UCL. + DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. + DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. + DR GO; GO:0018395; P:peptidyl-lysine hydroxylation to 5-hydroxy-L-lysine; IDA:UniProtKB. + DR GO; GO:0048024; P:regulation of nuclear mRNA splicing, via spliceosome; IMP:UniProtKB. + DR GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW. + DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. + DR GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
… - KW Alternative splicing; Complete proteome; Developmental protein; - KW Differentiation; Dioxygenase; Nucleus; Oxidoreductase. - FT CHAIN 1 403 Histone arginine demethylase JMJD6.
+ KW 3D-structure; Alternative splicing; Chromatin regulator; + KW Complete proteome; Developmental protein; Differentiation; + KW Dioxygenase; Iron; Metal-binding; mRNA processing; mRNA splicing; + KW Nucleus; Oxidoreductase; Transcription; Transcription regulation. + FT CHAIN 1 403 Bifunctional arginine demethylase and + FT lysyl-hydroxylase JMJD6.
… + FT METAL 187 187 Iron; catalytic (Probable). + FT METAL 189 189 Iron; catalytic (Probable). + FT METAL 273 273 Iron; catalytic (Probable). + FT BINDING 184 184 Substrate (By similarity). + FT BINDING 204 204 Substrate (By similarity).
… + FT CONFLICT 136 136 S -> G (in Ref. 3; BAG51050). + FT HELIX 3 16 + FT HELIX 23 27 + FT HELIX 31 34 + FT HELIX 39 41 + FT STRAND 48 50 + FT HELIX 51 53 + FT HELIX 56 62 + FT TURN 63 67 + FT STRAND 70 74 + FT HELIX 81 84 + FT HELIX 87 93 + FT STRAND 98 100 + FT STRAND 111 113 + FT HELIX 114 123 + FT STRAND 132 135 + FT HELIX 143 149 + FT HELIX 154 156 + FT HELIX 160 163 + FT STRAND 173 177 + FT STRAND 194 201 + FT STRAND 203 209 + FT HELIX 215 218 + FT HELIX 232 238 + FT HELIX 240 244 + FT HELIX 250 252 + FT STRAND 255 259 + FT STRAND 264 267 + FT STRAND 272 288 + FT TURN 291 293 + FT HELIX 294 302 + FT HELIX 306 319 + FT HELIX 321 333
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