Host cell factor C1

Host cell factor C1
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsHCFC1 ; CFF; HCF-1; HCF1; HFC1; MRX3; PPP1R89; VCAF
External IDsOMIM: 300019 MGI: 105942 HomoloGene: 3898 GeneCards: HCFC1 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez305415161
EnsemblENSG00000172534ENSMUSG00000031386
UniProtP51610Q61191
RefSeq (mRNA)NM_005334NM_008224
RefSeq (protein)NP_005325NP_032250
Location (UCSC)Chr HG1497_PATCH:
153.12 – 153.14 Mb		Chr X:
73.94 – 73.97 Mb
PubMed search

Host cell factor 1 (HCFC1, HCF1, or HCF-1), also known as VP16-accessory protein,[1] is a protein that in humans is encoded by the HCFC1 gene.[2][3]

Structure

HCF1 is a member of the highly conserved host cell factor family and encodes a protein with five Kelch repeats, a fibronectin-like motif, and six HCF repeats, each of which contains a highly specific cleavage signal. This nuclear transcription coregulator is proteolytically cleaved at one or more of the six possible sites, resulting in the creation of an N-terminal chain and the corresponding C-terminal chain. The final form of this protein consists of noncovalently bound N- and C-terminal chains which interact through electrostatic forces.

Function

HCF1 is involved in control of the cell cycle as well as having regulatory roles in a multitude of processes related to transcription. Additionally, work in model organisms point to HCF1 as being a putative longevity determinant.[4] Alternatively spliced variants that encode different protein isoforms have been described; however, not all variants have been fully characterized.[3]

Mutations in this gene have been linked to disorders of the cobalamine metabolism.[5]

Interactions

Host cell factor C1 has been shown to interact with:

References

  1. ↑ GeneCards entry for HCFC1, http://genecards.org
  2. ↑ Wilson AC, LaMarco K, Peterson MG, Herr W (August 1993). "The VP16 accessory protein HCF is a family of polypeptides processed from a large precursor protein". Cell 74 (1): 115–25. doi:10.1016/0092-8674(93)90299-6. PMID 8392914.
  3. ↑ 3.0 3.1 "Entrez Gene: HCFC1 host cell factor C1 (VP16-accessory protein)".
  4. ↑ Li J, Ebata A, Dong Y, Rizki G, Iwata T, Lee SS (September 2008). "Caenorhabditis elegans HCF-1 functions in longevity maintenance as a DAF-16 regulator". PLoS Biol. 6 (9): e233. doi:10.1371/journal.pbio.0060233. PMC 2553839. PMID 18828672.
  5. ↑ "An X-Linked Cobalamin Disorder Caused by Mutations in Transcriptional Coregulator HCFC1". The American Journal of Human Genetics 93: 506–514. doi:10.1016/j.ajhg.2013.07.022.
  6. ↑ Machida YJ, Machida Y, Vashisht AA, Wohlschlegel JA, Dutta A (December 2009). "The deubiquitinating enzyme BAP1 regulates cell growth via interaction with HCF-1". J. Biol. Chem. 284 (49): 34179–88. doi:10.1074/jbc.M109.046755. PMC 2797188. PMID 19815555.
  7. ↑ Lu R, Yang P, Padmakumar S, Misra V (August 1998). "The herpesvirus transactivator VP16 mimics a human basic domain leucine zipper protein, luman, in its interaction with HCF". J. Virol. 72 (8): 6291–7. PMC 109766. PMID 9658067.
  8. ↑ Freiman RN, Herr W (December 1997). "Viral mimicry: common mode of association with HCF by VP16 and the cellular protein LZIP". Genes Dev. 11 (23): 3122–7. doi:10.1101/gad.11.23.3122. PMC 316754. PMID 9389645.
  9. ↑ Vogel JL, Kristie TM (February 2000). "The novel coactivator C1 (HCF) coordinates multiprotein enhancer formation and mediates transcription activation by GABP". EMBO J. 19 (4): 683–90. doi:10.1093/emboj/19.4.683. PMC 305606. PMID 10675337.
  10. ↑ 10.0 10.1 10.2 10.3 10.4 10.5 10.6 Wysocka J, Myers MP, Laherty CD, Eisenman RN, Herr W (April 2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes Dev. 17 (7): 896–911. doi:10.1101/gad.252103. PMC 196026. PMID 12670868.
  11. ↑ 11.0 11.1 11.2 Yokoyama A, Wang Z, Wysocka J, Sanyal M, Aufiero DJ, Kitabayashi I, Herr W, Cleary ML (July 2004). "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression". Mol. Cell. Biol. 24 (13): 5639–49. doi:10.1128/MCB.24.13.5639-5649.2004. PMC 480881. PMID 15199122.
  12. ↑ Scarr RB, Sharp PA (August 2002). "PDCD2 is a negative regulator of HCF-1 (C1)". Oncogene 21 (34): 5245–54. doi:10.1038/sj.onc.1205647. PMID 12149646.
  13. ↑ La Boissière S, Hughes T, O'Hare P (January 1999). "HCF-dependent nuclear import of VP16". EMBO J. 18 (2): 480–9. doi:10.1093/emboj/18.2.480. PMC 1171141. PMID 9889203.
  14. ↑ Kristie TM, Sharp PA (March 1993). "Purification of the cellular C1 factor required for the stable recognition of the Oct-1 homeodomain by the herpes simplex virus alpha-trans-induction factor (VP16)". J. Biol. Chem. 268 (9): 6525–34. PMID 8454622.
  15. ↑ Ajuh PM, Browne GJ, Hawkes NA, Cohen PT, Roberts SG, Lamond AI (February 2000). "Association of a protein phosphatase 1 activity with the human factor C1 (HCF) complex". Nucleic Acids Res. 28 (3): 678–86. doi:10.1093/nar/28.3.678. PMC 102561. PMID 10637318.
  16. ↑ Gunther M, Laithier M, Brison O (July 2000). "A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening". Mol. Cell. Biochem. 210 (1-2): 131–42. doi:10.1023/A:1007177623283. PMID 10976766.
  17. ↑ Piluso D, Bilan P, Capone JP (November 2002). "Host cell factor-1 interacts with and antagonizes transactivation by the cell cycle regulatory factor Miz-1". J. Biol. Chem. 277 (48): 46799–808. doi:10.1074/jbc.M206226200. PMID 12244100.

Further reading