Details for: AMFR

Gene ID: 267

Symbol: AMFR

Ensembl ID: ENSG00000159461

Description: autocrine motility factor receptor

Associated with

Other Information

Genular Protein ID: 2440094864

Symbol: AMFR_HUMAN

Name: E3 ubiquitin-protein ligase AMFR

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 10456327

Title: The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein.

PubMed ID: 10456327

DOI: 10.1016/s0014-5793(99)00966-7

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 7626106

Title: Identification of an upstream region that controls the transcription of the human autocrine motility factor receptor.

PubMed ID: 7626106

DOI: 10.1006/bbrc.1995.2031

PubMed ID: 1649192

Title: Purification of human tumor cell autocrine motility factor and molecular cloning of its receptor.

PubMed ID: 1649192

DOI: 10.1016/s0021-9258(18)98859-9

PubMed ID: 11724934

Title: The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum.

PubMed ID: 11724934

DOI: 10.1073/pnas.251401598

PubMed ID: 12670940

Title: Overexpression of the tumor autocrine motility factor receptor, gp78, a ubiquitin protein ligase (E3), results in increased ubiquitinylation and decreased secretion of apolipoprotein B100 in Hep G2 cells.

PubMed ID: 12670940

DOI: 10.1074/jbc.m302683200

PubMed ID: 16168377

Title: Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase.

PubMed ID: 16168377

DOI: 10.1016/j.molcel.2005.08.009

PubMed ID: 16186510

Title: Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane.

PubMed ID: 16186510

DOI: 10.1073/pnas.0505006102

PubMed ID: 17043353

Title: Sterol-regulated degradation of Insig-1 mediated by the membrane-bound ubiquitin ligase gp78.

PubMed ID: 17043353

DOI: 10.1074/jbc.m608999200

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19103148

Title: CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases.

PubMed ID: 19103148

DOI: 10.1016/j.abb.2008.12.001

PubMed ID: 21636303

Title: A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation.

PubMed ID: 21636303

DOI: 10.1016/j.molcel.2011.05.010

PubMed ID: 22143767

Title: Sterol-induced degradation of HMG CoA reductase depends on interplay of two Insigs and two ubiquitin ligases, gp78 and Trc8.

PubMed ID: 22143767

DOI: 10.1073/pnas.1112831108

PubMed ID: 22728137

Title: RING finger palmitoylation of the endoplasmic reticulum Gp78 E3 ubiquitin ligase.

PubMed ID: 22728137

DOI: 10.1016/j.febslet.2012.06.011

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23223569

Title: Ancient ubiquitous protein-1 mediates sterol-induced ubiquitination of 3-hydroxy-3-methylglutaryl CoA reductase in lipid droplet-associated endoplasmic reticulum membranes.

PubMed ID: 23223569

DOI: 10.1091/mbc.e12-07-0564

PubMed ID: 24424410

Title: USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradation.

PubMed ID: 24424410

DOI: 10.7554/elife.01369

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 29275994

Title: A Proximity Labeling Strategy Provides Insights into the Composition and Dynamics of Lipid Droplet Proteomes.

PubMed ID: 29275994

DOI: 10.1016/j.devcel.2017.11.020

PubMed ID: 28604676

Title: Cholesterol and fatty acids regulate cysteine ubiquitylation of ACAT2 through competitive oxidation.

PubMed ID: 28604676

DOI: 10.1038/ncb3551

PubMed ID: 29184177

Title: Corrigendum: Cholesterol and fatty acids regulate cysteine ubiquitylation of ACAT2 through competitive oxidation.

PubMed ID: 29184177

DOI: 10.1038/ncb3651

PubMed ID: 31073040

Title: LMBR1L regulates lymphopoiesis through Wnt/beta-catenin signaling.

PubMed ID: 31073040

DOI: 10.1126/science.aau0812

PubMed ID: 31953408

Title: Competitive oxidation and ubiquitylation on the evolutionarily conserved cysteine confer tissue-specific stabilization of Insig-2.

PubMed ID: 31953408

DOI: 10.1038/s41467-019-14231-w

PubMed ID: 36593296

Title: Staphylococcal virulence factor HlgB targets the endoplasmic-reticulum-resident E3 ubiquitin ligase AMFR to promote pneumonia.

PubMed ID: 36593296

DOI: 10.1038/s41564-022-01278-7

PubMed ID: 21914798

Title: The structural and functional basis of the p97/valosin-containing protein (VCP)-interacting motif (VIM): mutually exclusive binding of cofactors to the N-terminal domain of p97.

PubMed ID: 21914798

DOI: 10.1074/jbc.m111.274506

PubMed ID: 16959974

Title: The consensus coding sequences of human breast and colorectal cancers.

PubMed ID: 16959974

DOI: 10.1126/science.1133427

Sequence Information:

  • Length: 643
  • Mass: 72996
  • Checksum: 8782324609C0E62A
  • Sequence:
  • MPLLFLERFP WPSLRTYTGL SGLALLGTII SAYRALSQPE AGPGEPDQLT ASLQPEPPAP 
    ARPSAGGPRA RDVAQYLLSD SLFVWVLVNT ACCVLMLVAK LIQCIVFGPL RVSERQHLKD 
    KFWNFIFYKF IFIFGVLNVQ TVEEVVMWCL WFAGLVFLHL MVQLCKDRFE YLSFSPTTPM 
    SSHGRVLSLL VAMLLSCCGL AAVCSITGYT HGMHTLAFMA AESLLVTVRT AHVILRYVIH 
    LWDLNHEGTW EGKGTYVYYT DFVMELTLLS LDLMHHIHML LFGNIWLSMA SLVIFMQLRY 
    LFHEVQRRIR RHKNYLRVVG NMEARFAVAT PEELAVNNDD CAICWDSMQA ARKLPCGHLF 
    HNSCLRSWLE QDTSCPTCRM SLNIADNNRV REEHQGENLD ENLVPVAAAE GRPRLNQHNH 
    FFHFDGSRIA SWLPSFSVEV MHTTNILGIT QASNSQLNAM AHQIQEMFPQ VPYHLVLQDL 
    QLTRSVEITT DNILEGRIQV PFPTQRSDSI RPALNSPVER PSSDQEEGET SAQTERVPLD 
    LSPRLEETLD FGEVEVEPSE VEDFEARGSR FSKSADERQR MLVQRKDELL QQARKRFLNK 
    SSEDDAASES FLPSEGASSD PVTLRRRMLA AAAERRLQKQ QTS

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.