E3 ubiquitin-protein ligase AMFR (Protein name
), AMFR_HUMAN from NCBI database.
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General Annotation
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Antigen Annotation
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Gene name:
AMFR(RNF45);
Protein name:
E3 ubiquitin-protein ligase AMFR;
Alternative:
RING finger protein 45;Autocrine motility factor receptor(AMF receptor);gp78;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Interacts with RNF5. Also forms an ERAD complex containing VCP/p97, NGLY1; PSMC1; SAKS1 AND RAD23B required for coupling retrotranslocation, ubiquitination and deglycosylation (By similarity). Interacts with DRL1. Interacts (through a region distinct from the RING finger) with UBE2G2/UBC7. Component of the VCP/p97-AMFR/gp78 complex that enhances VCP/p97 binding to polyubiquitinated proteins for their degradation by the endoplasmic reticulum-associated degradation (ERAD) pathway. Interacts (via the VIM) with VCP/p97. Interacts (via its membrane domain) with INSIG1; the interaction initiates the sterol-mediated ubiquitination and degradation of HMGCR by the ERAD pathway.
Function:
E3 ubiquitin-protein ligase that mediates the polyubiquitination of a number of proteins such as CD3D, CYP3A4, CFTR and APOB for proteasomal degradation. Component of a VCP/p97-AMFR/gp78 complex that participates in the final step of endoplasmic reticulum-associated degradation (ERAD). The VCP/p97-AMFR/gp78 complex is involved in the sterol-accelerated ERAD degradation of HMGCR through binding to the HMGCR-INSIG complex at the ER membrane and initiating ubiquitination of HMGCR. The ubiquitinated HMGCR is then released from the ER by the complex into the cytosol for subsequent destruction. Also acts as a scaffold protein to assemble a complex that couples ubiquitination, retranslocation and deglycosylation. Mediates tumor invasion and metastasis as a receptor for the GPI/autocrine motility factor.
Subcellular Location:
Endoplasmic reticulum membrane
Multi-pass membrane protein
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Cited for: FUNCTION AS A UBIQUITIN LIGASE;SUBCELLULAR LOCATION;INTERACTION WITH UBE2G2
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Cited for: INTERACTION WITH INSIG1 AND VCP;FUNCTION;MUTAGENESIS OF CYS-356
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 622-640 IN COMPLEX WITH VCP;VIM MOTIF
Vaild Sequence:
