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CALCOCO2
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 3VVV, 3VVW, 4GXL, 4HAN, 2MXP, 4XKL
Identifiers
Aliases	CALCOCO2, NDP52, calcium binding and coiled-coil domain 2
External IDs	OMIM: 604587; HomoloGene: 31339; GeneCards: CALCOCO2; OMA:CALCOCO2 - orthologs
Gene location (Human) Chr. Chromosome 17 (human) Band 17q21.32 Start 48,831,018 bp End 48,866,522 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon gastric mucosa right lung epithelium of colon sural nerve left testis right testis rectum popliteal artery tibial arteries n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding protein homodimerization activity Cellular component cytoplasm perinuclear region of cytoplasm autophagosome autophagosome membrane cytoskeleton membrane cytoplasmic vesicle nucleus intracellular membrane-bounded organelle cytosol Biological process autophagy viral process positive regulation of autophagosome maturation response to interferon-gamma xenophagy Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10241 n/a Ensembl ENSG00000136436 n/a UniProt Q13137 n/a RefSeq (mRNA) NM_001261390 NM_001261391 NM_001261393 NM_001261395 NM_005831 n/a RefSeq (protein) NP_001248319 NP_001248320 NP_001248322 NP_001248324 NP_005822 n/a Location (UCSC) Chr 17: 48.83 – 48.87 Mb n/a PubMed search n/a
Wikidata
View/Edit Human

Calcium-binding and coiled-coil domain-containing protein 2 is a protein that in humans is encoded by the CALCOCO2 gene.

The protein encoded by this gene is a subunit of nuclear domain 10 (ND10) bodies. ND10 bodies are nuclear domains appearing immunohistochemically as ten dots per nucleus. They are believed to be associated with the nuclear matrix on the basis of their resistance to nuclease digestion and salt extraction. ND10 proteins are removed from the nucleus by HSV-1 infection and may have a role in viral life cycles.

CALCOCO2 is an autophagy receptor, and loss of CALCOCO2 in human beta cells has been linked to autophagy-mediated altered insulin granule homeostasis. Thus, mutations in CALCOCO2 have been linked to type 2 diabetes risk.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000136436 – Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. Korioth F, Gieffers C, Maul GG, Frey J (July 1995). "Molecular characterization of NDP52, a novel protein of the nuclear domain 10, which is redistributed upon virus infection and interferon treatment". The Journal of Cell Biology. 130 (1): 1–13. doi:10.1083/jcb.130.1.1. PMC 2120522. PMID 7540613.
4. ^ "Entrez Gene: CALCOCO2 calcium binding and coiled-coil domain 2".
5. Rottner AK, Ye Y, Navarro-Guerrero E, Rajesh V, Pollner A, Bevacqua RJ, et al. (December 2022). "A genome-wide CRISPR screen identifies CALCOCO2 as a regulator of beta cell function influencing type 2 diabetes risk". Nature Genetics. 55 (1): 54–65. doi:10.1038/s41588-022-01261-2. PMC 9839450. PMID 36543916.

Further reading

• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Sternsdorf T, Jensen K, Züchner D, Will H (July 1997). "Cellular localization, expression, and structure of the nuclear dot protein 52". The Journal of Cell Biology. 138 (2): 435–448. doi:10.1083/jcb.138.2.435. PMC 2138200. PMID 9230084.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Florin L, Schäfer F, Sotlar K, Streeck RE, Sapp M (March 2002). "Reorganization of nuclear domain 10 induced by papillomavirus capsid protein L2". Virology. 295 (1): 97–107. doi:10.1006/viro.2002.1360. PMID 12033769.
• Di Y, Li J, Zhang Y, He X, Lu H, Xu D, et al. (June 2003). "HCC-associated protein HCAP1, a variant of GEMIN4, interacts with zinc-finger proteins". Journal of Biochemistry. 133 (6): 713–718. doi:10.1093/jb/mvg091. PMID 12869526.
• Everett RD, Sourvinos G, Leiper C, Clements JB, Orr A (February 2004). "Formation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexes". Journal of Virology. 78 (4): 1903–1917. doi:10.1128/JVI.78.4.1903-1917.2004. PMC 369473. PMID 14747555.
• Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, et al. (July 2004). "Functional proteomics mapping of a human signaling pathway". Genome Research. 14 (7): 1324–1332. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–1178. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Morriswood B, Ryzhakov G, Puri C, Arden SD, Roberts R, Dendrou C, et al. (August 2007). "T6BP and NDP52 are myosin VI binding partners with potential roles in cytokine signalling and cell adhesion". Journal of Cell Science. 120 (Pt 15): 2574–2585. doi:10.1242/jcs.007005. PMC 2621013. PMID 17635994.

External links

• CALCOCO2 human gene location in the UCSC Genome Browser.
• CALCOCO2 human gene details in the UCSC Genome Browser.

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