AMFR

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Autocrine motility factor receptor
Identifiers
Symbol(s) AMFR; GP78; RNF45
External IDs OMIM: 603243 MGI1345634 Homologene888
RNA expression pattern

PBB GE AMFR 202203 s at tn.png

PBB GE AMFR 202204 s at tn.png

More reference expression data

Orthologs
Human Mouse
Entrez 267 23802
Ensembl ENSG00000159461 ENSMUSG00000031751
Uniprot Q9UKV5 Q3TCI2
Refseq NM_001144 (mRNA)
NP_001135 (protein)
XM_990903 (mRNA)
XP_995997 (protein)
Location Chr 16: 54.95 - 55.02 Mb Chr 8: 96.86 - 96.9 Mb
Pubmed search [1] [2]

Autocrine motility factor receptor, also known as AMFR, is a human gene.[1]


Autocrine motility factor is a tumor motility-stimulating protein secreted by tumor cells. The protein encoded by this gene is a glycosylated transmembrane protein and a receptor for autocrine motility factor. The receptor, which shows some sequence similarity to tumor protein p53, is localized to the leading and trailing edges of carcinoma cells.[1]


References

Further reading

  • Watanabe H, Carmi P, Hogan V; et al. (1991). "Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor.". J. Biol. Chem. 266 (20): 13442–8. PMID 1649192. 
  • Huang B, Xie Y, Raz A (1995). "Identification of an upstream region that controls the transcription of the human autocrine motility factor receptor.". Biochem. Biophys. Res. Commun. 212 (3): 727–42. PMID 7626106. 
  • Hillier LD, Lennon G, Becker M; et al. (1997). "Generation and analysis of 280,000 human expressed sequence tags.". Genome Res. 6 (9): 807–28. PMID 8889549. 
  • Shimizu K, Tani M, Watanabe H; et al. (1999). "The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein.". FEBS Lett. 456 (2): 295–300. PMID 10456327. 
  • Fang S, Ferrone M, Yang C; et al. (2002). "The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum.". Proc. Natl. Acad. Sci. U.S.A. 98 (25): 14422–7. PMID 11724934. doi:10.1073/pnas.251401598. 
  • Luo Y, Long JM, Lu C; et al. (2002). "A link between maze learning and hippocampal expression of neuroleukin and its receptor gp78.". J. Neurochem. 80 (2): 354–61. PMID 11902125. 
  • Tímár J, Rásó E, Döme B; et al. (2002). "Expression and function of the AMF receptor by human melanoma in experimental and clinical systems.". Clin. Exp. Metastasis. 19 (3): 225–32. PMID 12067203. 
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMID 12477932. doi:10.1073/pnas.242603899. 
  • Liang JS, Kim T, Fang S; et al. (2003). "Overexpression of the tumor autocrine motility factor receptor Gp78, a ubiquitin protein ligase, results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in HepG2 cells.". J. Biol. Chem. 278 (26): 23984–8. PMID 12670940. doi:10.1074/jbc.M302683200. 
  • Takanami I, Takeuchi K (2003). "Autocrine motility factor-receptor gene expression in lung cancer.". Jpn. J. Thorac. Cardiovasc. Surg. 51 (8): 368–73. PMID 12962414. 
  • Ota T, Suzuki Y, Nishikawa T; et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. PMID 14702039. doi:10.1038/ng1285. 
  • Registre M, Goetz JG, St Pierre P; et al. (2004). "The gene product of the gp78/AMFR ubiquitin E3 ligase cDNA is selectively recognized by the 3F3A antibody within a subdomain of the endoplasmic reticulum.". Biochem. Biophys. Res. Commun. 320 (4): 1316–22. PMID 15303277. 
  • Zhong X, Shen Y, Ballar P; et al. (2004). "AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation.". J. Biol. Chem. 279 (44): 45676–84. PMID 15331598. doi:10.1074/jbc.M409034200. 
  • Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. PMID 15489334. doi:10.1101/gr.2596504. 
  • Song BL, Sever N, DeBose-Boyd RA (2005). "Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase.". Mol. Cell. 19 (6): 829–40. PMID 16168377. doi:10.1016/j.molcel.2005.08.009. 
  • Kaynak K, Kara M, Oz B; et al. (2006). "Autocrine motility factor receptor expression implies an unfavourable prognosis in resected stage I pulmonary adenocarcinomas.". Acta Chir. Belg. 105 (4): 378–82. PMID 16184720. 
  • Ye Y, Shibata Y, Kikkert M; et al. (2006). "Inaugural Article: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane.". Proc. Natl. Acad. Sci. U.S.A. 102 (40): 14132–8. PMID 16186510. doi:10.1073/pnas.0505006102. 
  • Chen B, Mariano J, Tsai YC; et al. (2006). "The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site.". Proc. Natl. Acad. Sci. U.S.A. 103 (2): 341–6. PMID 16407162. doi:10.1073/pnas.0506618103. 
  • Haga A, Tanaka N, Funasaka T; et al. (2006). "The autocrine motility factor (AMF) and AMF-receptor combination needs sugar chain recognition ability and interaction using the C-terminal region of AMF.". J. Mol. Biol. 358 (3): 741–53. PMID 16563432. doi:10.1016/j.jmb.2006.02.046. 
  • Shen Y, Ballar P, Fang S (2006). "Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of alpha-1-antitrypsin.". Biochem. Biophys. Res. Commun. 349 (4): 1285–93. PMID 16979136. doi:10.1016/j.bbrc.2006.08.173. 
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