KDM4B

Protein-coding gene in the species Homo sapiens

KDM4B

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
4LXL, 4UC4

Identifiers

Aliases

KDM4B, JMJD2B, TDRD14B, lysine demethylase 4B, MRD65

External IDs

OMIM: 609765; MGI: 2442355; HomoloGene: 27773; GeneCards: KDM4B; OMA:KDM4B - orthologs

Gene location (Human)

Chr.	Chromosome 19 (human)^[1]

Band	19p13.3	Start	4,969,113 bp^[1]
Band	19p13.3	End	5,153,598 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 17 (mouse)^[2]

Band	17\|17 D	Start	56,633,062 bp^[2]
Band	17\|17 D	End	56,709,870 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

dorsal motor nucleus of vagus nerve

corpus epididymis

blood

caput epididymis

inferior olivary nucleus

sural nerve

parotid gland

tendon of biceps brachii

nipple

Skeletal muscle tissue of biceps brachii

Top expressed in

Rostral migratory stream

neural layer of retina

superior frontal gyrus

otic vesicle

primary visual cortex

external carotid artery

dentate gyrus of hippocampal formation granule cell

granulocyte

muscle of thigh

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	oxidoreductase activity dioxygenase activity metal ion binding histone demethylase activity histone H3-methyl-lysine-36 demethylase activity histone H3-methyl-lysine-9 demethylase activity DNA-binding transcription repressor activity, RNA polymerase II-specific chromatin binding methylated histone binding
Cellular component	nucleoplasm nucleus histone methyltransferase complex
Biological process	regulation of transcription, DNA-templated transcription, DNA-templated histone H3-K36 demethylation histone H3-K9 demethylation chromatin organization negative regulation of transcription by RNA polymerase II chromatin remodeling
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


23030


193796

Ensembl


ENSG00000127663


ENSMUSG00000024201

UniProt


O94953


Q91VY5

RefSeq (mRNA)


NM_015015 NM_001370093 NM_001370094


NM_172132 NM_001357909

RefSeq (protein)


NP_055830 NP_001357022 NP_001357023


NP_742144 NP_001344838

Location (UCSC)

Chr 19: 4.97 – 5.15 Mb

Chr 17: 56.63 – 56.71 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Lysine-specific demethylase 4B is an enzyme that in humans is encoded by the KDM4B gene.^[5]^[6]^[7] KDM4B belongs to the alpha-ketoglutarate-dependent hydroxylase superfamily.

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000127663 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000024201 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2004Natur.428..529G. 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. Bibcode:2004PNAS..10112130B. 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. S2CID 14461740.
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.
Deng P, Yuan Q, Cheng Y, et al. (2021). "Loss of KDM4B exacerbates bone-fat imbalance and mesenchymal stromal cell exhaustion in skeletal aging". Cell Stem Cell. 28 (6): 1057–1073.e7. doi:10.1016/j.stem.2021.01.010. PMC 8178178. PMID 33571444.

Oxidoreductases: dioxygenases, including steroid hydroxylases (EC 1.14)

1.14.11: 2-oxoglutarate

1.14.13: NADH or NADPH

1.14.14: reduced flavin or flavoprotein

1.14.15: reduced iron–sulfur protein

1.14.16: reduced pteridine (BH4 dependent)

1.14.17: reduced ascorbate

Dopamine beta-hydroxylase

1.14.18-19: other

1.14.99 - miscellaneous

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)