CDC23

Protein-coding gene in the species Homo sapiens
CDC23
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4UI9, 5A31, 5G05, 5G04

Identifiers
AliasesCDC23, ANAPC8, APC8, CUT23, cell division cycle 23
External IDsOMIM: 603462; MGI: 1098815; HomoloGene: 3426; GeneCards: CDC23; OMA:CDC23 - orthologs
Gene location (Human)
Chromosome 5 (human)
Chr.Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for CDC23
Genomic location for CDC23
Band5q31.2Start138,187,650 bp[1]
End138,213,343 bp[1]
Gene location (Mouse)
Chromosome 18 (mouse)
Chr.Chromosome 18 (mouse)[2]
Chromosome 18 (mouse)
Genomic location for CDC23
Genomic location for CDC23
Band18 B1|18 18.69 cMStart34,764,004 bp[2]
End34,784,788 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • gonad

  • ventricular zone

  • tibia

  • endothelial cell

  • rectum

  • cerebellar hemisphere

  • right hemisphere of cerebellum

  • ovary

  • islet of Langerhans

  • left ovary
Top expressed in
  • genital tubercle

  • tail of embryo

  • ventricular zone

  • mandibular prominence

  • medullary collecting duct

  • superior cervical ganglion

  • maxillary prominence

  • abdominal wall

  • ganglionic eminence

  • renal corpuscle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • ubiquitin-protein transferase activity
  • protein binding
Cellular component
  • nucleoplasm
  • cytosol
  • intracellular anatomical structure
  • anaphase-promoting complex
Biological process
  • ubiquitin-dependent protein catabolic process
  • regulation of exit from mitosis
  • regulation of mitotic metaphase/anaphase transition
  • cell cycle
  • cell division
  • protein K11-linked ubiquitination
  • metaphase
  • anaphase-promoting complex-dependent catabolic process
  • protein ubiquitination
  • mitotic metaphase plate congression
  • mitotic cell cycle
  • regulation of mitotic cell cycle phase transition
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

8697

52563

Ensembl

ENSG00000094880

ENSMUSG00000024370

UniProt

Q9UJX2

Q8BGZ4

RefSeq (mRNA)

NM_004661

NM_178347

RefSeq (protein)

NP_004652

NP_848124

Location (UCSC)Chr 5: 138.19 – 138.21 MbChr 18: 34.76 – 34.78 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Cell division cycle 23 homolog (S. cerevisiae), also known as CDC23, is a protein that, in humans, is encoded by the CDC23 gene.[5]

Function

The CDC23 protein shares strong similarity with Saccharomyces cerevisiae Cdc23, a protein essential for cell cycle progression through the G2/M transition. This protein is a component of anaphase-promoting complex (APC), which is composed of eight protein subunits and highly conserved in eukaryotic cells. APC catalyzes the formation of cyclin B-ubiquitin conjugate that is responsible for the ubiquitin-mediated proteolysis of B-type cyclins. This protein and 3 other members of the APC complex contain the TPR (tetratricopeptide repeat), a protein domain important for protein-protein interaction.[5]

Interactions

CDC23 has been shown to interact with CDC27.[6][7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000094880 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024370 – 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. ^ a b "Entrez Gene: CDC23 cell division cycle 23 homolog (S. cerevisiae)".
  6. ^ Vodermaier HC, Gieffers C, Maurer-Stroh S, Eisenhaber F, Peters JM (Sep 2003). "TPR subunits of the anaphase-promoting complex mediate binding to the activator protein CDH1". Current Biology. 13 (17): 1459–68. Bibcode:2003CBio...13.1459V. doi:10.1016/S0960-9822(03)00581-5. PMID 12956947.
  7. ^ Gmachl M, Gieffers C, Podtelejnikov AV, Mann M, Peters JM (Aug 2000). "The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex". Proceedings of the National Academy of Sciences of the United States of America. 97 (16): 8973–8. Bibcode:2000PNAS...97.8973G. doi:10.1073/pnas.97.16.8973. PMC 16806. PMID 10922056.

External links

Further reading

  • Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Yu H, Peters JM, King RW, Page AM, Hieter P, Kirschner MW (Feb 1998). "Identification of a cullin homology region in a subunit of the anaphase-promoting complex". Science. 279 (5354): 1219–22. Bibcode:1998Sci...279.1219Y. doi:10.1126/science.279.5354.1219. PMID 9469815.
  • Zhao N, Lai F, Fernald AA, Eisenbart JD, Espinosa R, Wang PW, Le Beau MM (Oct 1998). "Human CDC23: cDNA cloning, mapping to 5q31, genomic structure, and evaluation as a candidate tumor suppressor gene in myeloid leukemias". Genomics. 53 (2): 184–90. doi:10.1006/geno.1998.5473. PMID 9790767.
  • Grossberger R, Gieffers C, Zachariae W, Podtelejnikov AV, Schleiffer A, Nasmyth K, Mann M, Peters JM (May 1999). "Characterization of the DOC1/APC10 subunit of the yeast and the human anaphase-promoting complex". The Journal of Biological Chemistry. 274 (20): 14500–7. doi:10.1074/jbc.274.20.14500. PMID 10318877.
  • Gieffers C, Peters BH, Kramer ER, Dotti CG, Peters JM (Sep 1999). "Expression of the CDH1-associated form of the anaphase-promoting complex in postmitotic neurons". Proceedings of the National Academy of Sciences of the United States of America. 96 (20): 11317–22. Bibcode:1999PNAS...9611317G. doi:10.1073/pnas.96.20.11317. PMC 18031. PMID 10500174.
  • Gmachl M, Gieffers C, Podtelejnikov AV, Mann M, Peters JM (Aug 2000). "The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to ubiquitinate substrates of the anaphase-promoting complex". Proceedings of the National Academy of Sciences of the United States of America. 97 (16): 8973–8. Bibcode:2000PNAS...97.8973G. doi:10.1073/pnas.97.16.8973. PMC 16806. PMID 10922056.
  • Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S (Sep 2000). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Reports. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
  • Walker MG (May 2001). "Drug target discovery by gene expression analysis: cell cycle genes". Current Cancer Drug Targets. 1 (1): 73–83. doi:10.2174/1568009013334241. PMID 12188893.
  • Wang Q, Moyret-Lalle C, Couzon F, Surbiguet-Clippe C, Saurin JC, Lorca T, Navarro C, Puisieux A (Mar 2003). "Alterations of anaphase-promoting complex genes in human colon cancer cells". Oncogene. 22 (10): 1486–90. doi:10.1038/sj.onc.1206224. PMID 12629511.
  • Vodermaier HC, Gieffers C, Maurer-Stroh S, Eisenhaber F, Peters JM (Sep 2003). "TPR subunits of the anaphase-promoting complex mediate binding to the activator protein CDH1". Current Biology. 13 (17): 1459–68. Bibcode:2003CBio...13.1459V. doi:10.1016/S0960-9822(03)00581-5. PMID 12956947.
  • Kraft C, Herzog F, Gieffers C, Mechtler K, Hagting A, Pines J, Peters JM (Dec 2003). "Mitotic regulation of the human anaphase-promoting complex by phosphorylation". The EMBO Journal. 22 (24): 6598–609. doi:10.1093/emboj/cdg627. PMC 291822. PMID 14657031.
  • Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12130–5. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
  • Ballif BA, Villén J, Beausoleil SA, Schwartz D, Gygi SP (Nov 2004). "Phosphoproteomic analysis of the developing mouse brain". Molecular & Cellular Proteomics. 3 (11): 1093–101. doi:10.1074/mcp.M400085-MCP200. PMID 15345747.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R (Apr 2006). "Phosphoproteome analysis of the human mitotic spindle". Proceedings of the National Academy of Sciences of the United States of America. 103 (14): 5391–6. Bibcode:2006PNAS..103.5391N. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
  • Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (Oct 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nature Biotechnology. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
  • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.


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