ORC2

Origin recognition complex subunit 2 is a protein that is encoded by the ORC2 (ORC2L) gene in humans.[5][6]

ORC2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesORC2, ORC2L, origin recognition complex subunit 2
External IDsOMIM: 601182 MGI: 1328306 HomoloGene: 4512 GeneCards: ORC2
Orthologs
SpeciesHumanMouse
Entrez

4999

18393

Ensembl

ENSG00000115942

ENSMUSG00000026037

UniProt

Q13416

Q60862

RefSeq (mRNA)

NM_006190

NM_001025378
NM_001271526
NM_008765

RefSeq (protein)

NP_006181

NP_001020549
NP_001258455
NP_032791

Location (UCSC)Chr 2: 200.91 – 200.96 MbChr 1: 58.5 – 58.54 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
Origin recognition complex subunit 2
Identifiers
SymbolORC2
PfamPF04084
InterProIPR007220
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Function

The origin recognition complex (ORC) is a highly conserved six subunits protein complex essential for the initiation of the DNA replication in eukaryotic cells. Studies in yeast demonstrated that ORC binds specifically to origins of replication and serves as a platform for the assembly of additional initiation factors such as Cdc6 and Mcm proteins. The protein encoded by this gene is a subunit of the ORC complex. This protein forms a core complex with ORC3, ORC4, and ORC5. It also interacts with CDC45L and MCM10, which are proteins known to be important for the initiation of DNA replication. This protein has been demonstrated to specifically associate with the origin of replication of Epstein-Barr virus in human cells, and is thought to be required for DNA replication from viral origin of replication.[6]

Interactions

ORC2 has been shown to interact with:

References
  1. GRCh38: Ensembl release 89: ENSG00000115942 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000026037 - 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. Takahara K, Bong M, Brevard R, Eddy RL, Haley LL, Sait SJ, Shows TB, Hoffman GG, Greenspan DS (October 1996). "Mouse and human homologues of the yeast origin of replication recognition complex subunit ORC2 and chromosomal localization of the cognate human gene ORC2L". Genomics. 31 (1): 119–122. doi:10.1006/geno.1996.0018. PMID 8808289.
  6. "Entrez Gene: ORC2L origin recognition complex, subunit 2-like (yeast)".
  7. Kneissl M, Pütter V, Szalay AA, Grummt F (March 2003). "Interaction and assembly of murine pre-replicative complex proteins in yeast and mouse cells". J. Mol. Biol. 327 (1): 111–28. doi:10.1016/s0022-2836(03)00079-2. PMID 12614612.
  8. Méndez J, Stillman B (November 2000). "Chromatin association of human origin recognition complex, cdc6, and minichromosome maintenance proteins during the cell cycle: assembly of prereplication complexes in late mitosis". Mol. Cell. Biol. 20 (22): 8602–12. doi:10.1128/mcb.20.22.8602-8612.2000. PMC 102165. PMID 11046155.
  9. Izumi M, Yanagi K, Mizuno T, Yokoi M, Kawasaki Y, Moon KY, Hurwitz J, Yatagai F, Hanaoka F (December 2000). "The human homolog of Saccharomyces cerevisiae Mcm10 interacts with replication factors and dissociates from nuclease-resistant nuclear structures in G(2) phase". Nucleic Acids Res. 28 (23): 4769–77. doi:10.1093/nar/28.23.4769. PMC 115166. PMID 11095689.
  10. Fujita M, Ishimi Y, Nakamura H, Kiyono T, Tsurumi T (March 2002). "Nuclear organization of DNA replication initiation proteins in mammalian cells". J. Biol. Chem. 277 (12): 10354–61. doi:10.1074/jbc.M111398200. PMID 11779870.
  11. Vashee S, Simancek P, Challberg MD, Kelly TJ (July 2001). "Assembly of the human origin recognition complex". J. Biol. Chem. 276 (28): 26666–73. doi:10.1074/jbc.M102493200. PMID 11323433.
  12. Méndez J, Zou-Yang XH, Kim SY, Hidaka M, Tansey WP, Stillman B (March 2002). "Human origin recognition complex large subunit is degraded by ubiquitin-mediated proteolysis after initiation of DNA replication". Mol. Cell. 9 (3): 481–91. doi:10.1016/s1097-2765(02)00467-7. PMID 11931757.
  13. Dhar SK, Delmolino L, Dutta A (August 2001). "Architecture of the human origin recognition complex". J. Biol. Chem. 276 (31): 29067–71. doi:10.1074/jbc.M103078200. PMID 11395502.
  14. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ (May 2007). "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage". Science. 316 (5828): 1160–6. Bibcode:2007Sci...316.1160M. doi:10.1126/science.1140321. PMID 17525332. S2CID 16648052.
  15. Pinto S, Quintana DG, Smith P, Mihalek RM, Hou ZH, Boynton S, Jones CJ, Hendricks M, Velinzon K, Wohlschlegel JA, Austin RJ, Lane WS, Tully T, Dutta A (May 1999). "latheo encodes a subunit of the origin recognition complex and disrupts neuronal proliferation and adult olfactory memory when mutant". Neuron. 23 (1): 45–54. doi:10.1016/s0896-6273(00)80752-7. PMID 10402192. S2CID 781511.
  16. Quintana DG, Hou Zh, Thome KC, Hendricks M, Saha P, Dutta A (November 1997). "Identification of HsORC4, a member of the human origin of replication recognition complex". J. Biol. Chem. 272 (45): 28247–51. doi:10.1074/jbc.272.45.28247. PMID 9353276.
  17. Quintana DG, Thome KC, Hou Zh, Ligon AH, Morton CC, Dutta A (October 1998). "ORC5L, a new member of the human origin recognition complex, is deleted in uterine leiomyomas and malignant myeloid diseases". J. Biol. Chem. 273 (42): 27137–45. doi:10.1074/jbc.273.42.27137. PMID 9765232.

Further reading
  • PDBe-KB provides an overview of all the structure information available in the PDB for Human Origin recognition complex subunit 2 (ORC2)
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