KDM4B

Lysine (K)-specific demethylase 4B

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
4LXL

Identifiers

Symbols

KDM4B ; JMJD2B; TDRD14B

External IDs

OMIM: 609765 MGI: 2442355 HomoloGene: 27773 IUPHAR: 2676 GeneCards: KDM4B Gene

Gene ontology
Molecular function	• zinc ion binding • dioxygenase activity
Cellular component	• nucleus • nucleoplasm • focal adhesion • cell junction
Biological process	• chromatin organization • transcription, DNA-templated • regulation of transcription, DNA-templated • chromatin modification • oxidation-reduction process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 19:
4.97 – 5.15 Mb

Chr 17:
56.33 – 56.4 Mb

PubMed search

Lysine-specific demethylase 4B is an enzyme that in humans is encoded by the KDM4B gene.^[1]^[2]^[3]

References

↑ Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (May 1999). "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res 5 (6): 355–64. doi:10.1093/dnares/5.6.355. PMID 10048485.
↑ Katoh M, Katoh M (May 2004). "Identification and characterization of JMJD2 family genes in silico". Int J Oncol 24 (6): 1623–8. doi:10.3892/ijo.25.3.759. PMID 15138608.
↑ "Entrez Gene: JMJD2B jumonji domain containing 2B".

Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19.". Nature 428 (6982): 529–35. doi:10.1038/nature02399. PMID 15057824.
Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Gray SG, Iglesias AH, Lizcano F, et al. (2005). "Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein.". J. Biol. Chem. 280 (31): 28507–18. doi:10.1074/jbc.M413687200. PMID 15927959.
Whetstine JR, Nottke A, Lan F, et al. (2006). "Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases.". Cell 125 (3): 467–81. doi:10.1016/j.cell.2006.03.028. PMID 16603238.
Katoh Y, Katoh M (2007). "Comparative integromics on JMJD2A, JMJD2B and JMJD2C: preferential expression of JMJD2C in undifferentiated ES cells.". Int. J. Mol. Med. 20 (2): 269–73. doi:10.3892/ijmm.20.2.269. PMID 17611647.

Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)

1.14.11: 2-oxoglutarate	Prolyl hydroxylase Lysyl hydroxylase

1.14.13: NADH or NADPH	Flavin-containing monooxygenase FMO1 FMO2 FMO3 FMO4 FMO5 Nitric oxide synthase NOS1 NOS2 NOS3 Cholesterol 7 alpha-hydroxylase Methane monooxygenase 3A4 Lanosterol 14 alpha-demethylase 24-hydroxycholesterol 7α-hydroxylase

1.14.14: reduced flavin or flavoprotein	19A1 2D6 2E1

1.14.15: reduced iron-sulfur protein	11B1 11B2 11A1

1.14.16: reduced pteridine (BH4 dependent)	Phenylalanine hydroxylase Tyrosine hydroxylase Tryptophan hydroxylase

1.14.17: reduced ascorbate	Dopamine beta-hydroxylase

1.14.18-19: other	Tyrosinase Stearoyl-CoA desaturase-1

1.14.99 - miscellaneous	Cyclooxygenase Heme oxygenase (HMOX1) Squalene monooxygenase 17A1 21A2

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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KDM4B

References

Further reading