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AMFR

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(Redirected from AMFR (gene))
AMFR
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesAMFR, GP78, RNF45, autocrine motility factor receptor
External IDsOMIM: 603243; MGI: 1345634; HomoloGene: 888; GeneCards: AMFR; OMA:AMFR - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001144
NM_138958
NM_001323511
NM_001323512

NM_011787

RefSeq (protein)

NP_001135
NP_001310440
NP_001310441

NP_035917

Location (UCSC)Chr 16: 56.36 – 56.43 MbChr 8: 94.7 – 94.74 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Autocrine motility factor receptor, isoform 2 is a protein that in humans is encoded by the AMFR gene.[5][6]

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.[6]

Interactions

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AMFR has been shown to interact with Valosin-containing protein.[7][8]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000159461Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031751Ensembl, 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. ^ Watanabe H, Carmi P, Hogan V, Raz T, Silletti S, Nabi IR, Raz A (Aug 1991). "Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor". J Biol Chem. 266 (20): 13442–8. doi:10.1016/S0021-9258(18)98859-9. PMID 1649192.
  6. ^ a b "Entrez Gene: AMFR autocrine motility factor receptor".
  7. ^ Zhong, Xiaoyan; Shen Yuxian; Ballar Petek; Apostolou Andria; Agami Reuven; Fang Shengyun (Oct 2004). "AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation". J. Biol. Chem. 279 (44). United States: 45676–84. doi:10.1074/jbc.M409034200. ISSN 0021-9258. PMID 15331598.
  8. ^ Lee, Joon No; Zhang Xiangyu; Feramisco Jamison D; Gong Yi; Ye Jin (Nov 2008). "Unsaturated fatty acids inhibit proteasomal degradation of Insig-1 at a postubiquitination step". J. Biol. Chem. 283 (48). United States: 33772–83. doi:10.1074/jbc.M806108200. ISSN 0021-9258. PMC 2586246. PMID 18835813.
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Further reading

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