The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

FAF1  -  Fas (TNFRSF6) associated factor 1

Homo sapiens

Synonyms: CGI-03, FAS-associated factor 1, HFAF1s, UBX domain-containing protein 12, UBX domain-containing protein 3A, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of FAF1

  • Clinical study has revealed that FAF1 is significantly reduced in gastric carcinomas [1].
  • Here, we report the full length human FAF1 cDNA sequence, expression of FAF1 in Escherichia coli and purification and characterization of FAF1 as a substrate for CK2 [2].
  • Additionally, 31 colorectal carcinomas were analyzed for expression of FAF1 [3].
  • Also, the reduction of FAF1 is likely to be specific for gastric cancer, which might be due to the fact that signet ring cells are most frequently found in gastric cancers [3].
  • The aggression profile of patients with Duodenal Peptic Ulcer (DPU) (n = 39) was assessed by means of five self-rating scales (FAF 1, FAF 3, PDS-Extp, PDS-Intp, PDS-Dom) and was compared with a matched normal control group (n = 39) and a psychiatric outpatient sample (n = 67) [4].

High impact information on FAF1

  • These results suggest that hFAF1 binding to ubiquitinated protein and VCP is involved in the ubiquitin-proteasome pathway [5].
  • The overexpression of hFAF1 and a truncated UBA domain inhibited the degradation of ubiquitinated proteins and increased cell death [5].
  • These results suggest that hFAF1 prevents cells from recovery after stress by binding to and inhibiting the chaperone activity of Hsp70 [6].
  • Interaction mapping indicated that the 82-180 sequence of hFAF1 directly binds to the N-terminal region containing sequence 1-120 of Hsc70/Hsp70 [6].
  • NF-kappaB activation induced by tumor necrosis factor (TNF)-alpha, interleukin-1beta, and lipopolysaccharide was also inhibited by FAF1 overexpression [7].

Biological context of FAF1

  • Cell death by overexpression of FAF1 was suppressed significantly in both FADD- and caspase-8-deficient Jurkat cells when compared with that in their parental Jurkat cells [8].
  • In addition, the FAF1 deletion mutant lacking the N terminus where Fas, FADD, and caspase-8 interact protected Jurkat cells from Fas-induced apoptosis demonstrating dominant-negative phenotype [8].
  • Based on the fact that FAF1 is a Fas-binding protein, we asked if FAF1 interacted with other members of the Fas-death-inducing signaling complex (Fas-DISC) such as Fas-associated death domain protein (FADD) and caspase-8 [8].
  • Introduction of antisense FAF1 construct inhibited DEF assembly and chemotherapeutic-induced apoptosis [1].
  • Furthermore, we analyzed putative physiological functions of FAF1 phosphorylation [9].

Anatomical context of FAF1

  • Overexpression of FAF1 in Jurkat cells caused significant apoptotic death [8].
  • By confocal microscopic analysis, both Fas and FAF1 were detected in the cytoplasmic membrane before Fas activation, and in the cytoplasm after Fas activation [8].
  • Not much is known about the function of FAF1, but it has been found that it is able to potentiate Fas-induced apoptosis in cell lines [3].
  • Here, FAF1 was only reduced in 16% of the carcinomas when compared to non-neoplastic colorectal mucosa [3].
  • We found that FAF1 was reduced in 50% (29/58) of the gastric carcinomas analyzed as compared to non-neoplastic gastric mucosa from the same patients [3].

Associations of FAF1 with chemical compounds


Physical interactions of FAF1


Co-localisations of FAF1

  • FADD and caspase-8 colocalized with Fas in Jurkat cells validating the presence of FAF1 in the authentic Fas-DISC [8].

Other interactions of FAF1

  • In the coimmunoprecipitation with an anti-Fas antibody (APO-1) in Jurkat cells, endogenous FAF1 was associated with the precipitates in which caspase-8 was present [8].
  • Human Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathway [5].
  • By employing co-immunoprecipitation and peptide mass fingerprinting using matrix-assisted laser desorption ionization time-of-flight mass spectrometry, we found that hFAF1 binds to the 70-kDa heat shock protein family (Hsc70/Hsp70) [6].
  • Here, we identify Fas-associated factor 1 (FAF1) as a regulatory factor, which is coexpressed with and binds to TRPV1 in sensory neurons [10].
  • The N-terminal region (amino acid 1 approximately 201) including the upstream ubiquitin homology domain of hFAF1 could bind with the death domain of Fas unlike that of qFAF1 whose binding region with Fas could not be determined [12].

Analytical, diagnostic and therapeutic context of FAF1


  1. Fas-associated factor-1 mediates chemotherapeutic-induced apoptosis via death effector filament formation. Park, M.Y., Ryu, S.W., Kim, K.D., Lim, J.S., Lee, Z.W., Kim, E. Int. J. Cancer (2005) [Pubmed]
  2. Phosphorylation of the Fas associated factor FAF1 by protein kinase CK2 and identification of serines 289 and 291 as the in vitro phosphorylation sites. Jensen, H.H., Hjerrild, M., Guerra, B., Larsen, M.R., Højrup, P., Boldyreff, B. Int. J. Biochem. Cell Biol. (2001) [Pubmed]
  3. The pro-apoptotic FAS-associated factor 1 is specifically reduced in human gastric carcinomas. Bjørling-Poulsen, M., Seitz, G., Guerra, B., Issinger, O.G. Int. J. Oncol. (2003) [Pubmed]
  4. Hostile personality characteristics of duodenal ulcer patients. Rubino, I.A., Castiglia, I., Rossi, P., Paoluzi, P. The Italian journal of gastroenterology. (1990) [Pubmed]
  5. Human Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathway. Song, E.J., Yim, S.H., Kim, E., Kim, N.S., Lee, K.J. Mol. Cell. Biol. (2005) [Pubmed]
  6. Human Fas-associated factor 1 interacts with heat shock protein 70 and negatively regulates chaperone activity. Kim, H.J., Song, E.J., Lee, Y.S., Kim, E., Lee, K.J. J. Biol. Chem. (2005) [Pubmed]
  7. Fas-associated factor-1 inhibits nuclear factor-kappaB (NF-kappaB) activity by interfering with nuclear translocation of the RelA (p65) subunit of NF-kappaB. Park, M.Y., Jang, H.D., Lee, S.Y., Lee, K.J., Kim, E. J. Biol. Chem. (2004) [Pubmed]
  8. Fas-associated factor 1, FAF1, is a member of Fas death-inducing signaling complex. Ryu, S.W., Lee, S.J., Park, M.Y., Jun, J.I., Jung, Y.K., Kim, E. J. Biol. Chem. (2003) [Pubmed]
  9. Protein kinase CK2 phosphorylates the Fas-associated factor FAF1 in vivo and influences its transport into the nucleus. Olsen, B.B., Jessen, V., Højrup, P., Issinger, O.G., Boldyreff, B. FEBS Lett. (2003) [Pubmed]
  10. TRPV1 recapitulates native capsaicin receptor in sensory neurons in association with Fas-associated factor 1. Kim, S., Kang, C., Shin, C.Y., Hwang, S.W., Yang, Y.D., Shim, W.S., Park, M.Y., Kim, E., Kim, M., Kim, B.M., Cho, H., Shin, Y., Oh, U. J. Neurosci. (2006) [Pubmed]
  11. Interactions of protein kinase CK2beta subunit within the holoenzyme and with other proteins. Kusk, M., Ahmed, R., Thomsen, B., Bendixen, C., Issinger, O.G., Boldyreff, B. Mol. Cell. Biochem. (1999) [Pubmed]
  12. Identification and characterization of human Fas associated factor 1, hFAF1. Ryu, S.W., Chae, S.K., Lee, K.J., Kim, E. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  13. Fas-associated factor 1 is a negative regulator of PYRIN-containing Apaf-1-like protein 1. Kinoshita, T., Kondoh, C., Hasegawa, M., Imamura, R., Suda, T. Int. Immunol. (2006) [Pubmed]
WikiGenes - Universities