Oncomodulin 2

OCM2
Identifiers
Aliases	OCM2, OCM, LOC4951, oncomodulin 2, OM
External IDs	MGI: 97401; HomoloGene: 130549; GeneCards: OCM2; OMA:OCM2 - orthologs
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7q21.3 Start 97,984,684 bp[1] End 97,991,169 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5 G2|5 82.85 cM Start 143,956,622 bp[2] End 143,963,488 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in testicle gonad bone marrow prefrontal cortex placenta primary visual cortex lymph node cell blood monocyte Top expressed in ileum jejunum cochlea epithelium of small intestine intestinal villus Ileal epithelium morula blastocyst secondary oocyte primary oocyte More reference expression data BioGPS 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 Species Human Mouse Entrez 4951 18261 Ensembl ENSG00000135175 ENSMUSG00000029618 UniProt P0CE71 P51879 RefSeq (mRNA) NM_006188 NM_033039 RefSeq (protein) NP_006179 NP_149028 Location (UCSC) Chr 7: 97.98 – 97.99 Mb Chr 5: 143.96 – 143.96 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Oncomodulin 2, also known as OCM2, is a human gene that is similar to oncomodulin.^[5]

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.^[5]

References

1. GRCh38: Ensembl release 89: ENSG00000135175 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000029618 – Ensembl, 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. "Entrez Gene: OCM oncomodulin".

Further reading

• 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.