Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 (EC 1.14.11.-) (Histone arginine demethylase JMJD6) (JmjC domain-containing protein 6) (Jumonji domain-containing protein 6) (Lysyl-hydroxylase JMJD6) (Peptide-lysine 5-dioxygenase JMJD6) (Phosphatidylserine receptor) (Protein PTDSR)

 JMJD6_HUMAN             Reviewed;         403 AA.
Q6NYC1; B3KMN8; B4DGX1; Q86VY0; Q8IUM5; Q9Y4E2;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 133.
RecName: Full=Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6;
EC=1.14.11.-;
AltName: Full=Histone arginine demethylase JMJD6;
AltName: Full=JmjC domain-containing protein 6;
AltName: Full=Jumonji domain-containing protein 6;
AltName: Full=Lysyl-hydroxylase JMJD6;
AltName: Full=Peptide-lysine 5-dioxygenase JMJD6;
AltName: Full=Phosphatidylserine receptor;
Short=Protein PTDSR;
Name=JMJD6; Synonyms=KIAA0585, PTDSR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Stomach cancer;
Izawa M., Takahashi M.;
"Identification of an alternative form of phosphatidylserine
receptor.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"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.";
DNA Res. 5:31-39(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain, and Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
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.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNALS.
PubMed=14729065; DOI=10.1016/j.yexcr.2003.09.023;
Cui P., Qin B., Liu N., Pan G., Pei D.;
"Nuclear localization of the phosphatidylserine receptor protein via
multiple nuclear localization signals.";
Exp. Cell Res. 293:154-163(2004).
[8]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=15072554; DOI=10.1677/jme.0.0320497;
Cao W.M., Murao K., Imachi H., Hiramine C., Abe H., Yu X., Dobashi H.,
Wong N.C.W., Takahara J., Ishida T.;
"Phosphatidylserine receptor cooperates with high-density lipoprotein
receptor in recognition of apoptotic cells by thymic nurse cells.";
J. Mol. Endocrinol. 32:497-505(2004).
[9]
TISSUE SPECIFICITY.
PubMed=15622002;
Koeninger J., Balaz P., Wagner M., Shi X., Cima I., Zimmermann A.,
di Sebastiano P., Buechler M.W., Friess H.;
"Phosphatidylserine receptor in chronic pancreatitis: evidence for a
macrophage independent role.";
Ann. Surg. 241:144-151(2005).
[10]
FUNCTION AS HISTONE DEMETHYLASE, AND MUTAGENESIS OF HIS-187; ASP-189
AND HIS-273.
PubMed=17947579; DOI=10.1126/science.1145801;
Chang B., Chen Y., Zhao Y., Bruick R.K.;
"JMJD6 is a histone arginine demethylase.";
Science 318:444-447(2007).
[11]
FUNCTION AS LYSYL-HYDROXYLASE, COFACTOR, INTERACTION WITH LUC7L2;
LUC7L3 AND U2AF2, AND MUTAGENESIS OF HIS-187 AND ASP-189.
PubMed=19574390; DOI=10.1126/science.1175865;
Webby C.J., Wolf A., Gromak N., Dreger M., Kramer H., Kessler B.,
Nielsen M.L., Schmitz C., Butler D.S., Yates J.R. III, Delahunty C.M.,
Hahn P., Lengeling A., Mann M., Proudfoot N.J., Schofield C.J.,
Boettger A.;
"Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated
with RNA splicing.";
Science 325:90-93(2009).
[12]
SUBCELLULAR LOCATION, RNA-BINDING, AND FUNCTION.
PubMed=21060799; DOI=10.1371/journal.pone.0013769;
Hahn P., Wegener I., Burrells A., Bose J., Wolf A., Erck C.,
Butler D., Schofield C.J., Bottger A., Lengeling A.;
"Analysis of Jmjd6 cellular localization and testing for its
involvement in histone demethylation.";
PLoS ONE 5:E13769-E13769(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
INTERACTION WITH BRD4.
PubMed=21555454; DOI=10.1128/MCB.01341-10;
Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W.,
Howley P.M.;
"The Brd4 extraterminal domain confers transcription activation
independent of pTEFb by recruiting multiple proteins, including
NSD3.";
Mol. Cell. Biol. 31:2641-2652(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-335 IN COMPLEX WITH NICKEL
IONS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF
TYR-131; LYS-204; GLU-231; THR-285 AND ASN-287.
PubMed=20684070; DOI=10.1016/j.jmb.2010.05.054;
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.;
"Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl
hydroxylase JMJD6.";
J. Mol. Biol. 401:211-222(2010).
[17]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-334 IN COMPLEX WITH IRON
IONS AND 2-OXOGLUTARATE, POSSIBLE FUNCTION, AND RNA-BINDING.
PubMed=20679243; DOI=10.1073/pnas.1008832107;
Hong X., Zang J., White J., Wang C., Pan C.H., Zhao R., Murphy R.C.,
Dai S., Henson P., Kappler J.W., Hagman J., Zhang G.;
"Interaction of JMJD6 with single-stranded RNA.";
Proc. Natl. Acad. Sci. U.S.A. 107:14568-14572(2010).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:17947579, ECO:0000269|PubMed:19574390,
ECO:0000269|PubMed:20684070, ECO:0000269|PubMed:21060799}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:19574390};
Note=Binds 1 Fe(2+) ion per subunit.
{ECO:0000269|PubMed:19574390};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=39 uM for 2-oxoglutarate {ECO:0000269|PubMed:20684070};
-!- SUBUNIT: Interacts with LUC7L2, LUC7L3 and U2AF2/U2AF65. Interacts
with BRD4. Interacts with LIAT1 (By similarity).
{ECO:0000250|UniProtKB:Q9ERI5, ECO:0000269|PubMed:19574390,
ECO:0000269|PubMed:20679243, ECO:0000269|PubMed:20684070,
ECO:0000269|PubMed:21555454}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-8464037, EBI-8464037;
O60885:BRD4; NbExp=10; IntAct=EBI-8464037, EBI-723869;
P50750:CDK9; NbExp=5; IntAct=EBI-8464037, EBI-1383449;
Q96NE9:FRMD6; NbExp=3; IntAct=EBI-8464037, EBI-741729;
Q9GZZ1:NAA50; NbExp=5; IntAct=EBI-8464037, EBI-1052523;
Q8NAV1:PRPF38A; NbExp=2; IntAct=EBI-8464037, EBI-715374;
P04637:TP53; NbExp=7; IntAct=EBI-8464037, EBI-366083;
Q01081:U2AF1; NbExp=2; IntAct=EBI-8464037, EBI-632461;
Q9NP64:ZCCHC17; NbExp=2; IntAct=EBI-8464037, EBI-746345;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus, nucleolus.
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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Alpha;
IsoId=Q6NYC1-1; Sequence=Displayed;
Name=2; Synonyms=Beta;
IsoId=Q6NYC1-2; Sequence=VSP_014022, VSP_014023;
Name=3;
IsoId=Q6NYC1-3; Sequence=VSP_014023;
-!- TISSUE SPECIFICITY: 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. {ECO:0000269|PubMed:15072554,
ECO:0000269|PubMed:15622002, ECO:0000269|PubMed:9628581}.
-!- INDUCTION: Up-regulated upon cytokine treatment, but not upon TNF
treatment. {ECO:0000269|PubMed:15072554}.
-!- DOMAIN: The nuclear localization signal motifs are necessary and
sufficient to target it into the nucleus.
-!- SIMILARITY: Belongs to the JMJD6 family. {ECO:0000305}.
-!- 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.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH47003.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAA25511.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB073711; BAC16755.1; -; mRNA.
EMBL; AB011157; BAA25511.1; ALT_INIT; mRNA.
EMBL; AK021780; BAG51050.1; -; mRNA.
EMBL; AK294816; BAG57932.1; -; mRNA.
EMBL; AC005837; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471099; EAW89434.1; -; Genomic_DNA.
EMBL; BC047003; AAH47003.1; ALT_INIT; mRNA.
EMBL; BC066654; AAH66654.1; -; mRNA.
CCDS; CCDS42383.1; -. [Q6NYC1-3]
CCDS; CCDS42384.1; -. [Q6NYC1-1]
RefSeq; NP_001074930.1; NM_001081461.1. [Q6NYC1-3]
RefSeq; NP_055982.2; NM_015167.2. [Q6NYC1-1]
UniGene; Hs.514505; -.
PDB; 3K2O; X-ray; 1.75 A; A/B=2-335.
PDB; 3LD8; X-ray; 2.70 A; A=1-334.
PDB; 3LDB; X-ray; 2.70 A; A=1-334.
PDBsum; 3K2O; -.
PDBsum; 3LD8; -.
PDBsum; 3LDB; -.
ProteinModelPortal; Q6NYC1; -.
SMR; Q6NYC1; -.
BioGrid; 116817; 133.
DIP; DIP-60686N; -.
IntAct; Q6NYC1; 35.
MINT; MINT-3086431; -.
STRING; 9606.ENSP00000394085; -.
iPTMnet; Q6NYC1; -.
PhosphoSitePlus; Q6NYC1; -.
BioMuta; JMJD6; -.
DMDM; 67461014; -.
EPD; Q6NYC1; -.
MaxQB; Q6NYC1; -.
PaxDb; Q6NYC1; -.
PeptideAtlas; Q6NYC1; -.
PRIDE; Q6NYC1; -.
Ensembl; ENST00000397625; ENSP00000380750; ENSG00000070495. [Q6NYC1-1]
Ensembl; ENST00000445478; ENSP00000394085; ENSG00000070495. [Q6NYC1-3]
GeneID; 23210; -.
KEGG; hsa:23210; -.
UCSC; uc002jsn.2; human. [Q6NYC1-1]
CTD; 23210; -.
DisGeNET; 23210; -.
EuPathDB; HostDB:ENSG00000070495.14; -.
GeneCards; JMJD6; -.
HGNC; HGNC:19355; JMJD6.
HPA; CAB004548; -.
HPA; HPA059156; -.
MIM; 604914; gene.
neXtProt; NX_Q6NYC1; -.
OpenTargets; ENSG00000070495; -.
PharmGKB; PA162392513; -.
eggNOG; KOG2130; Eukaryota.
eggNOG; ENOG410XQCR; LUCA.
GeneTree; ENSGT00530000063579; -.
HOGENOM; HOG000265824; -.
HOVERGEN; HBG054774; -.
InParanoid; Q6NYC1; -.
KO; K11323; -.
OrthoDB; EOG091G0AJ6; -.
PhylomeDB; Q6NYC1; -.
TreeFam; TF314988; -.
BRENDA; 1.14.11.4; 2681.
Reactome; R-HSA-3214842; HDMs demethylate histones.
EvolutionaryTrace; Q6NYC1; -.
GeneWiki; JMJD6; -.
GenomeRNAi; 23210; -.
PRO; PR:Q6NYC1; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000070495; -.
CleanEx; HS_JMJD6; -.
ExpressionAtlas; Q6NYC1; baseline and differential.
Genevisible; Q6NYC1; HS.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0032452; F:histone demethylase activity; TAS:Reactome.
GO; GO:0033746; F:histone demethylase activity (H3-R2 specific); IDA:UniProtKB.
GO; GO:0033749; F:histone demethylase activity (H4-R3 specific); IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:BHF-UCL.
GO; GO:0005506; F:iron ion binding; IDA:UniProtKB.
GO; GO:0070815; F:peptidyl-lysine 5-dioxygenase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0004872; F:receptor activity; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; TAS:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:Ensembl.
GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0070078; P:histone H3-R2 demethylation; IDA:BHF-UCL.
GO; GO:0070079; P:histone H4-R3 demethylation; IDA:BHF-UCL.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0042116; P:macrophage activation; IEA:Ensembl.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0018395; P:peptidyl-lysine hydroxylation to 5-hydroxy-L-lysine; IDA:UniProtKB.
GO; GO:0043654; P:recognition of apoptotic cell; IEA:Ensembl.
GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
GO; GO:0033077; P:T cell differentiation in thymus; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR003347; JmjC_dom.
Pfam; PF02373; JmjC; 1.
SMART; SM00558; JmjC; 1.
PROSITE; PS51184; JMJC; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; Developmental protein; Differentiation;
Dioxygenase; Iron; Metal-binding; mRNA processing; mRNA splicing;
Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome;
RNA-binding; Transcription; Transcription regulation.
CHAIN 1 403 Bifunctional arginine demethylase and
lysyl-hydroxylase JMJD6.
/FTId=PRO_0000129369.
DOMAIN 141 305 JmjC. {ECO:0000255|PROSITE-
ProRule:PRU00538}.
MOTIF 6 10 Nuclear localization signal 1.
{ECO:0000269|PubMed:14729065}.
MOTIF 91 95 Nuclear localization signal 2.
{ECO:0000269|PubMed:14729065}.
MOTIF 141 145 Nuclear localization signal 3.
{ECO:0000269|PubMed:14729065}.
MOTIF 167 170 Nuclear localization signal 4.
{ECO:0000269|PubMed:14729065}.
MOTIF 373 378 Nuclear localization signal 5.
{ECO:0000269|PubMed:14729065}.
COMPBIAS 340 365 Ser-rich.
METAL 187 187 Iron; catalytic.
METAL 189 189 Iron; catalytic.
METAL 273 273 Iron; catalytic.
BINDING 184 184 Substrate. {ECO:0000250}.
BINDING 197 197 2-oxoglutarate.
{ECO:0000269|PubMed:20679243}.
BINDING 204 204 Substrate. {ECO:0000250}.
BINDING 285 285 2-oxoglutarate.
{ECO:0000269|PubMed:20679243}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 361 402 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_014022.
VAR_SEQ 403 403 R -> RIRDTCGGRAHP (in isoform 2 and
isoform 3). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:9628581,
ECO:0000303|Ref.1}.
/FTId=VSP_014023.
MUTAGEN 131 131 Y->F: Abolishes 2-oxoglutarate-binding
and enzyme activity.
{ECO:0000269|PubMed:20684070}.
MUTAGEN 187 187 H->A: Loss of catalytic activity; when
associated with A-189 and A-273.
{ECO:0000269|PubMed:17947579,
ECO:0000269|PubMed:19574390}.
MUTAGEN 189 189 D->A: Loss of catalytic activity; when
associated with A-187 and A-273.
{ECO:0000269|PubMed:17947579,
ECO:0000269|PubMed:19574390}.
MUTAGEN 204 204 K->A: Impairs enzyme activity without
affecting 2-oxoglutarate-binding.
{ECO:0000269|PubMed:20684070}.
MUTAGEN 231 231 E->A: Impairs both hydroxylation activity
and 2-oxoglutarate turnover assays.
{ECO:0000269|PubMed:20684070}.
MUTAGEN 273 273 H->A: Loss of catalytic activity; when
associated with A-187 and A-189.
{ECO:0000269|PubMed:17947579}.
MUTAGEN 285 285 T->A: Impairs enzyme activity and 2-
oxoglutarate-binding.
{ECO:0000269|PubMed:20684070}.
MUTAGEN 287 287 N->A: Impairs enzyme activity.
{ECO:0000269|PubMed:20684070}.
CONFLICT 136 136 S -> G (in Ref. 3; BAG51050).
{ECO:0000305}.
HELIX 3 16 {ECO:0000244|PDB:3K2O}.
HELIX 23 27 {ECO:0000244|PDB:3K2O}.
HELIX 31 34 {ECO:0000244|PDB:3K2O}.
HELIX 39 41 {ECO:0000244|PDB:3K2O}.
STRAND 48 50 {ECO:0000244|PDB:3K2O}.
HELIX 51 53 {ECO:0000244|PDB:3K2O}.
HELIX 56 62 {ECO:0000244|PDB:3K2O}.
TURN 63 67 {ECO:0000244|PDB:3K2O}.
STRAND 70 74 {ECO:0000244|PDB:3K2O}.
TURN 75 78 {ECO:0000244|PDB:3K2O}.
HELIX 81 84 {ECO:0000244|PDB:3K2O}.
HELIX 87 93 {ECO:0000244|PDB:3K2O}.
STRAND 98 103 {ECO:0000244|PDB:3K2O}.
STRAND 109 113 {ECO:0000244|PDB:3K2O}.
HELIX 114 123 {ECO:0000244|PDB:3K2O}.
STRAND 132 135 {ECO:0000244|PDB:3K2O}.
HELIX 137 139 {ECO:0000244|PDB:3K2O}.
HELIX 143 149 {ECO:0000244|PDB:3K2O}.
HELIX 154 156 {ECO:0000244|PDB:3K2O}.
HELIX 160 164 {ECO:0000244|PDB:3K2O}.
TURN 166 168 {ECO:0000244|PDB:3K2O}.
STRAND 173 178 {ECO:0000244|PDB:3K2O}.
STRAND 183 187 {ECO:0000244|PDB:3K2O}.
HELIX 190 192 {ECO:0000244|PDB:3K2O}.
STRAND 194 202 {ECO:0000244|PDB:3K2O}.
STRAND 204 209 {ECO:0000244|PDB:3K2O}.
HELIX 215 218 {ECO:0000244|PDB:3K2O}.
HELIX 222 225 {ECO:0000244|PDB:3K2O}.
HELIX 226 228 {ECO:0000244|PDB:3K2O}.
HELIX 232 238 {ECO:0000244|PDB:3K2O}.
HELIX 240 244 {ECO:0000244|PDB:3K2O}.
HELIX 250 252 {ECO:0000244|PDB:3K2O}.
STRAND 255 259 {ECO:0000244|PDB:3K2O}.
STRAND 264 267 {ECO:0000244|PDB:3K2O}.
STRAND 272 279 {ECO:0000244|PDB:3K2O}.
STRAND 281 288 {ECO:0000244|PDB:3K2O}.
TURN 291 293 {ECO:0000244|PDB:3K2O}.
HELIX 294 304 {ECO:0000244|PDB:3K2O}.
HELIX 306 319 {ECO:0000244|PDB:3K2O}.
HELIX 321 333 {ECO:0000244|PDB:3K2O}.
SEQUENCE 403 AA; 46462 MW; 9C9AADA98B24B035 CRC64;
MNHKSKKRIR EAKRSARPEL KDSLDWTRHN YYESFSLSPA AVADNVERAD ALQLSVEEFV
ERYERPYKPV VLLNAQEGWS AQEKWTLERL KRKYRNQKFK CGEDNDGYSV KMKMKYYIEY
MESTRDDSPL YIFDSSYGEH PKRRKLLEDY KVPKFFTDDL FQYAGEKRRP PYRWFVMGPP
RSGTGIHIDP LGTSAWNALV QGHKRWCLFP TSTPRELIKV TRDEGGNQQD EAITWFNVIY
PRTQLPTWPP EFKPLEILQK PGETVFVPGG WWHVVLNLDT TIAITQNFAS STNFPVVWHK
TVRGRPKLSR KWYRILKQEH PELAVLADSV DLQESTGIAS DSSSDSSSSS SSSSSDSDSE
CESGSEGDGT VHRRKKRRTC SMVGNGDTTS QDDCVSKERS SSR


Related products :

Catalog number Product name Quantity
U1916r CLIA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Lysyl-hydroxylase JMJD6 96T
U1916m CLIA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Kiaa0585,Lysyl-hydroxyl 96T
U1916b CLIA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Bos taurus,Bovine,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6,Lysyl 96T
E1916m ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Kiaa0585,Lysyl-hydroxy 96T
E1916r ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Lysyl-hydroxylase JMJD 96T
U1916m CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Kiaa0585,Lysyl-hyd 96T
E1916m ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Kiaa0585,Lysyl-hy 96T
U1916h CLIA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,Homo sapiens,Human,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6,KIAA 96T
U1916h CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,Homo sapiens,Human,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6 96T
E1916h ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,Homo sapiens,Human,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6,KIA 96T
E1916b ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Bos taurus,Bovine,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6,Lysy 96T
E1916h ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,Homo sapiens,Human,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 96T
E1916r ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Lysyl-hydroxylase 96T
U1916r CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,Jmjd6,Jumonji domain-containing protein 6,Lysyl-hydroxylase 96T
U1916b CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Bos taurus,Bovine,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6, 96T
E1916b ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Bos taurus,Bovine,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6 96T
E1916c ELISA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Chicken,Gallus gallus,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing prote 96T
U1916c CLIA kit Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Chicken,Gallus gallus,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protei 96T
U1916c CLIA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Chicken,Gallus gallus,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6,L 96T
E1916c ELISA Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6,Chicken,Gallus gallus,Histone arginine demethylase JMJD6,JmjC domain-containing protein 6,JMJD6,Jumonji domain-containing protein 6, 96T
CSB-EL011954RA Rat Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6(JMJD6) ELISA kit 96T
CSB-EL011954CH Chicken Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6(JMJD6) ELISA kit 96T
CSB-EL011954RA Rat Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6(JMJD6) ELISA kit SpeciesRat 96T
CSB-EL011954HU Human Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6(JMJD6) ELISA kit 96T
CSB-EL011954MO Mouse Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6(JMJD6) ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur