Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 is an enzyme that in humans is encoded by the JMJD6 gene.[5][6]

JMJD6
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesJMJD6, PSR, PTDSR, PTDSR1, arginine demethylase and lysine hydroxylase, jumonji domain containing 6, arginine demethylase and lysine hydroxylase
External IDsOMIM: 604914; MGI: 1858910; HomoloGene: 9046; GeneCards: JMJD6; OMA:JMJD6 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001081461
NM_015167

NM_033398
NM_001363363

RefSeq (protein)

NP_001074930
NP_055982

NP_203971
NP_001350292

Location (UCSC)Chr 17: 76.71 – 76.73 MbChr 11: 116.73 – 116.73 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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This gene encodes a nuclear protein with a JmjC domain. JmjC domain-containing proteins belong to the alpha-ketoglutarate-dependent hydroxylase superfamily. They are predicted to function as protein hydroxylases or histone demethylases. This protein was first identified as a putative phosphatidylserine receptor involved in phagocytosis of apoptotic cells. Subsequent studies suggest that the protein may cross-react with a monoclonal antibody that recognizes the phosphatidylserine receptor and does not directly function in the clearance of apoptotic cells. Multiple transcript variants encoding different isoforms have been found for this gene.[6] On a physiological level JMJD6 has a role in angiogenesis, the process of vessel formation, whereas further roles of JMJD6 in pathophysiological processes were implicated, such as mammary tumorigenesis.[7] Here, elevated JMJD6 level were found in breast cancer associated with aggressiveness and metastasis in mice.[8]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000070495Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000056962Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Vandivier RW, Fadok VA, Hoffmann PR, Bratton DL, Penvari C, Brown KK, Brain JD, Accurso FJ, Henson PM (March 2002). "Elastase-mediated phosphatidylserine receptor cleavage impairs apoptotic cell clearance in cystic fibrosis and bronchiectasis". The Journal of Clinical Investigation. 109 (5): 661–70. doi:10.1172/JCI13572. PMC 150889. PMID 11877474.
  6. ^ a b "Entrez Gene: JMJD6 jumonji domain containing 6".
  7. ^ Boeckel JN, Guarani V, Koyanagi M, Roexe T, Lengeling A, Schermuly RT, Gellert P, Braun T, Zeiher A, Dimmeler S (February 2011). "Jumonji domain-containing protein 6 (Jmjd6) is required for angiogenic sprouting and regulates splicing of VEGF-receptor 1". Proceedings of the National Academy of Sciences of the United States of America. 108 (8): 3276–81. Bibcode:2011PNAS..108.3276B. doi:10.1073/pnas.1008098108. PMC 3044381. PMID 21300889.
  8. ^ Aprelikova O, Chen K, El Touny LH, Brignatz-Guittard C, Han J, Qiu T, Yang HH, Lee MP, Zhu M, Green JE (14 Apr 2016). "The epigenetic modifier JMJD6 is amplified in mammary tumors and cooperates with c-Myc to enhance cellular transformation, tumor progression, and metastasis". Clin Epigenetics. 8 (38): 38. doi:10.1186/s13148-016-0205-6. PMC 4831179. PMID 27081402.

Further reading

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