Oncomodulin 2

OCM2
Identifiers
Aliases	OCM2 , OCM, LOC4951, oncomodulin 2, OM
External IDs	HomoloGene: 130549 GeneCards: OCM2
Gene location (Human)
Chr.	Chromosome 7 (human)
End	97,991,169 bp
RNA expression pattern
	Top expressed in
	bone marrow; ; prefrontal cortex; ; placenta; ; lymph node; ; cell; ; blood; ; monocyte; ; skin of abdomen; ; Brodmann area 9; ; myometrium;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	metal ion binding ; calcium ion binding ;
Cellular component	nucleus ; cytoplasm ;
Biological process	regulation of cytosolic calcium ion concentration ;
	Sources:Amigo / QuickGO
Orthologs
	4951
	n/a
	ENSG00000135175
	n/a
	P0CE71
	n/a
	NM_006188
	n/a
	NP_006179
	n/a
	Wikidata
View/Edit Human

Last updated March 04, 2023

Oncomodulin 2, also known as OCM2, is a human gene that is similar to oncomodulin.^[3]

Oncomodulin is a high-affinity calcium ion-binding protein. It belongs to the superfamily of calmodulin proteins, also known as the EF-hand proteins. Oncomodulin 2 is an oncodevelopmental protein found in early embryonic cells in the placenta and also in tumors.^[3]

Related Research Articles

Oncomodulin is a parvalbumin-family calcium-binding protein expressed and secreted by macrophages.

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Calmodulin 2 is a protein that in humans is encoded by the CALM2 gene.

Calcium/calmodulin-dependent protein kinase type IV is an enzyme that in humans is encoded by the CAMK4 gene.

Calcium/calmodulin-dependent protein kinase type 1 is an enzyme that in humans is encoded by the CAMK1 gene.

Calcium/calmodulin-dependent protein kinase type II delta chain is an enzyme that in humans is encoded by the CAMK2D gene.

Visinin-like protein 1 is a protein that in humans is encoded by the VSNL1 gene.

Interleukin-18-binding protein is a protein that in humans is encoded by the IL18BP gene.

Annexin A3 is a protein that in humans is encoded by the ANXA3 gene.

Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A is an enzyme that in humans is encoded by the PDE1A gene.

Calmodulin-like protein 3 is a protein that in humans is encoded by the CALML3 gene.

Calcium/calmodulin-dependent protein kinase kinase 1 is an enzyme that in humans is encoded by the CAMKK1 gene.

Plasma membrane calcium-transporting ATPase 3 is an enzyme that in humans is encoded by the ATP2B3 gene.

S100 calcium-binding protein G (S100G) is a protein that in humans is encoded by the S100G gene.

Calmodulin-like protein 5 is a protein that in humans is encoded by the CALML5 gene.

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Potassium intermediate/small conductance calcium-activated channel, subfamily N, member 1 , also known as KCNN1 is a human gene encoding the K_Ca2.1 protein.

Myosin light chain kinase 2 also known as MYLK2 is an enzyme which in humans is encoded by the MYLK2 gene.

ParvE101Q is an experimental modification of parvalbumin, designed to delay calcium sequestration in heart muscles to enhance contraction. The protein parvalbumin has EF hand motifs used for calcium binding. EF hands are structural helix-loop-helix protein subunits that have a high affinity for calcium ions, and a moderate affinity for magnesium ions. In muscle, the binding of Ca²⁺ by parvalbumin efficiently sequesters it following contraction. This increases the speed of muscle relaxation, allowing the muscle to contract again sooner. Although parvalbumin is classified as a delayed calcium buffer, it quickly sequesters Ca²⁺, usually before the muscle is done fully contracting. Large amounts of parvalbumin allow rapid contractions of muscles at a high contractile speed with the trade-off of having relatively lower contraction force. This decreased force of contraction is due to the rapid sequestration of Ca²⁺, preventing prolonged contraction which is required for greater force.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000135175 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 "Entrez Gene: OCM oncomodulin".

Pauls TL, Cox JA, Berchtold MW (1996). "The Ca2+(-)binding proteins parvalbumin and oncomodulin and their genes: new structural and functional findings". Biochim. Biophys. Acta. 1306 (1): 39–54. doi:10.1016/0167-4781(95)00221-9. PMID 8611623.
Belkacemi L, Simoneau L, Lafond J (2003). "Calcium-binding proteins: distribution and implication in mammalian placenta". Endocrine. 19 (1): 57–64. doi:10.1385/ENDO:19:1:57. PMID 12583602. S2CID 28802052.
Ritzler JM, Sawhney R, Geurts van Kessel AH, et al. (1992). "The genes for the highly homologous Ca(2+)-binding proteins oncomodulin and parvalbumin are not linked in the human genome". Genomics. 12 (3): 567–72. doi:10.1016/0888-7543(92)90449-3. PMID 1559707.
Palmer EJ, MacManus JP, Mutus B (1990). "Inhibition of glutathione reductase by oncomodulin". Arch. Biochem. Biophys. 277 (1): 149–54. doi:10.1016/0003-9861(90)90563-E. PMID 2306116.
Mutus B, Palmer EJ, MacManus JP (1988). "Disulfide-linked dimer of oncomodulin: comparison to calmodulin". Biochemistry. 27 (15): 5615–22. doi:10.1021/bi00415a033. PMID 3179268.
Gillen MF, Banville D, Rutledge RG, et al. (1987). "A complete complementary DNA for the oncodevelopmental calcium-binding protein, oncomodulin". J. Biol. Chem. 262 (11): 5308–12. doi: 10.1016/S0021-9258(18)61189-5 . PMID 3558395.
MacManus JP, Brewer LM, Whitfield JF (1985). "The widely-distributed tumour protein, oncomodulin, is a normal constituent of human and rodent placentas". Cancer Lett. 27 (2): 145–51. doi:10.1016/0304-3835(85)90103-X. PMID 4005827.
Blum JK, Berchtold MW (1994). "Calmodulin-like effect of oncomodulin on cell proliferation". J. Cell. Physiol. 160 (3): 455–62. doi:10.1002/jcp.1041600308. PMID 8077283. S2CID 25079233.
Föhr UG, Weber BR, Müntener M, et al. (1993). "Human alpha and beta parvalbumins. Structure and tissue-specific expression". Eur. J. Biochem. 215 (3): 719–27. doi: 10.1111/j.1432-1033.1993.tb18084.x . PMID 8354278.
Sakaguchi N, Henzl MT, Thalmann I, et al. (2000). "Oncomodulin is expressed exclusively by outer hair cells in the organ of Corti". J. Histochem. Cytochem. 46 (1): 29–40. doi: 10.1177/002215549804600105 . PMID 9405492.
Sanger Centre, The; Washington University Genome Sequencing Cente, The (1999). "Toward a complete human genome sequence". Genome Res. 8 (11): 1097–108. doi: 10.1101/gr.8.11.1097 . PMID 9847074.
Harrington JJ, Sherf B, Rundlett S, et al. (2001). "Creation of genome-wide protein expression libraries using random activation of gene expression". Nat. Biotechnol. 19 (5): 440–5. doi:10.1038/88107. PMID 11329013. S2CID 25064683.
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.
Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. Bibcode:2003Natur.424..157H. doi: 10.1038/nature01782 . PMID 12853948.
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.
Babini E, Bertini I, Capozzi F, et al. (2005). "Solution structure of human beta-parvalbumin and structural comparison with its paralog alpha-parvalbumin and with their rat orthologs". Biochemistry. 43 (51): 16076–85. doi:10.1021/bi048388o. PMID 15610002.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000135175 - Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-3] 1 2 "Entrez Gene: OCM oncomodulin".

[1]

[2]

[3]

Oncomodulin 2

Related Research Articles

References

Further reading