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AMFR (autocrine motility factor receptor)

Written2011-08Yalcin Erzurumlu, Petek Ballar
Ege University, Faculty of Pharmacy, Biochemistry Department, Bornova, 35100, Izmir, Turkey

(Note : for Links provided by Atlas : click)

Identity

Alias_namesautocrine motility factor receptor
autocrine motility factor receptor, E3 ubiquitin protein ligase
Alias_symbol (synonym)RNF45
gp78
HGNC (Hugo) AMFR
LocusID (NCBI) 267
Atlas_Id 627
Location 16q12.2  [Link to chromosome band 16q12]
Location_base_pair Starts at 56395364 and ends at 56459450 bp from pter ( according to hg19-Feb_2009)  [Mapping AMFR.png]
 
  AMFR gene genomic location at chromosome 16q12.2 (minus strand).
Fusion genes
(updated 2016)
AMFR (16q12.2) / ITGAM (16p11.2)AMFR (16q12.2) / PRRC2A (6p21.33)PRRC2A (6p21.33) / AMFR (16q12.2)

DNA/RNA

 
  A. The alignment of AMFR mRNA to its genomic sequence. B. AMFR mRNA and its amino acid coding.
Description The AMFR gene spans 64081 bases on minus strand. The DNA of AMFR consists of 14 exons and the coding sequence starts in the first exon.
Transcription The AMFR gene has two transcripts. One of these transcripts is 2249 bp long and is a processed transcript with no protein product. 3598 bp long second AMFR transcript is a protein coding transcript (accession number: NM_001144). The DNA has been cloned in 1999 (Shimizu et al., 1999).

Protein

 
  A schematic representation of the domain structure.
Description AMFR belongs to the family of RING-Finger ubiquitin ligases. The complete protein contains 643 amino acids. The calculated molecular weight of AMFR is 73,0 kDa.
AMFR was originally isolated as a membrane glycoprotein from murine melanoma cells and was implicated in cell migration (Nabi and Raz, 1987). Subsequently, gp78/AMFR was identified as the tumor autocrine motility factor receptor mediating tumor invasion and metastasis (Nabi et al., 1990). A monoclonal antibody named 3F3A was generated against this protein and first sequence reported for human gp78/AMFR was in 1991 using this antibody (Watanabe et al., 1991). However, the protein product was only 321 amino acids (Watanabe et al., 1991). A sequence giving 643 amino acids protein product was cloned in 1999 (Shimizu et al., 1999).
gp78/AMFR has five to seven transmembrane domains according to different softwares like SACS MEMSAT and SOSUI. The protein has a long cytoplasmic tail composed of around 350 amino acids (Shimizu et al., 1999). Besides conveying E3 activity the multifunctional cytoplasmic tail is responsible for interaction with polyubiquitin, ubiquitin conjugating enzyme, p97/VCP and Ufd1. The RING finger domain of gp78/AMFR residing between amino acids 341 and 383 is a RING-H2 type domain containing two His residues in positions 4 and 5 (Fang et al., 2001). The Cue domain of gp78/AMFR residing between amino acids 456 and 497 is responsible for polyubiquitin binding and has been identified by having homologous sequences of yeast protein Cue1p (Ponting, 2000). The p97/VCP-interacting motif of gp78/AMFR consists of C-terminal amino acid residues between 614-643 and it is sufficient to bind to p97/VCP protein (Ballar et al., 2006). gp78/AMFR binds to its ubiquitin conjugating enzyme via a region called UBE2G2 binding region (G2BR) and this region is resides between amino acids 579 and 600 (Chen et al., 2006). Additionally, gp78/AMFR interacts directly with Ufd1 through residues 383-497 (Cao et al., 2007) and with INSIGs through its transmembrane domains (Song et al., 2005).
Expression gp78/AMFR is relatively ubiquitously expressed in normal human cells, especially highly in liver, heart and lung. Northern blot analysis detected a 3.5-kb AMFR transcript in mouse heart, brain, lung, liver, skeletal muscle, kidney, and testis, but not in spleen (Shimizu et al., 1999). gp78/AMFR is overexpressed in certain malignant tumors and human cancers of the lung, gastrointestinal tract, breast, liver, thymus, and skin (Chiu et al., 2008; Sjöblom et al., 2006; Tsai et al., 2007; Joshi et al., 2010).
Localisation Endoplasmic reticulum membrane, multi-pass transmembrane protein (Fang et al., 2001).
Function In 2001, it has been reported that gp78/AMFR possesses ubiquitin ligase (E3) activity (Fang et al., 2001) and can ubiquitinate both itself and other proteins for proteasomal degradation. gp78/AMFR is a member of multiprotein complex functioning in endoplasmic reticulum associated degradation (ERAD). gp78/AMFR not only functions as an E3 during ERAD but also couples retrotranslocation and deglycosylation to ubiquitination (Ballar et al., 2006; Li et al., 2005).
Homology Homologues have been found in various species like bovine, chimpanzee (99.8 % homology), chicken, zebra fish, rat, C. elegans and mouse. gp78/AMFR shares 94.7 % of homology with murine gp78/AMFR.

Mutations

Somatic D605V mutation has been reported in breast cancer (Sjöblom et al., 2006). Several SNPs have been found in gp78/AMFR gene both at coding regions and at UTRs and introns. See SNP database at NCBI.

Implicated in

Note
Entity Sarcoma metastasis
Note gp78/AMFR targets KAI1, a known metastasis suppressor protein for ubiquitin mediated proteasomal degradation (Tsai et al., 2007). Thus gp78/AMFR has role in metastasis of human sarcoma. Furthermore, a human sarcoma tissue microarray study documents that tumors with low gp78 expression has higher levels of KAI1 and high gp78 level lower KAI1 expression in tumors (Tsai et al., 2007).
  
Entity Breast cancer
Note gp78/AMFR expression in gp78 transgenic mammary glands induces mammary gland hyperplasia, increases duct number and network density and shows down-regulation of KAI1 metastasis suppressor (Joshi et al., 2010). Additionally, gp78/AMFR has been identified as one of the most mutated genes in breast cancer (Sjöblom et al., 2006). Consistently, gp78/AMFR is overexpressed in human breast cancer and is negatively associated with patients' clinical outcome (Jiang et al., 2006).
  
Entity Gastric carcinoma
Note gp78/AMFR expression may be associated with the progression and invasion of gastric carcinoma as well as the prognoses of the patients (Hirono et al., 1996). Furthermore, by using same 3F3A antibody it was reported that gp78/AMFR expression is associated with lymph node metastasis and peritoneal dissemination in gastric carcinoma (Taniguchi et al., 1998).
  
Entity Colorectal cancer
Note gp78/AMFR expression is correlated high incidence of recurrence of the patients with colorectal cancer (Nakamori et al., 1994).
  
Entity Melanoma
Note It was showed by using 3F3A antibody that gp78/AMFR protein expression in human melanoma cell lines correlates to their metastatic potential. While in thin tumors weak/heterogenous gp78/AMFR expression predominated, in thick tumors the strong gp78/AMFR expression profile was predominant (Tímár et al., 2002).
  
Entity Lung cancer
Note Using immunohistochemical staining the gp78/AMFR expression was showed to be associated with histologic type of tumor, mainly in adenocarcinoma (Kara et al., 2001).
  
Entity Hepatocellular carcinoma
Note The expression of gp78/AMFR significantly increased in hepatocellular carcinoma compared with pericarcinomatous liver tissues. Furthermore, there is a strong correlation between AMFR expression and invasion and metastasis of HCC (Wang et al., 2007).
  
Entity Bladder carcinoma
Note While in normal urothelium gp78/AMFR is not expressed, its expression is increased in bladder carcinoma specimens (Otto et al., 1994).
  
Entity Cardiovascular diseases and hypercholesterolemia
Note Accumulation of sterols in ER membranes triggers the binding of HMG CoA reductase, the rate limiting enzyme of cholesterol biosynthesis, to the Insig1-gp78/AMFR complex which is essential for the ubiquitination and proteasomal degradation of HMGCoA-reductase (Goldstein et al., 2006; Jo and DeBose-Boyd, 2010). gp78/AMFR is also the E3 ligase of apolipoprotein B100, the protein component of atherogenic lipoproteins, overproduction of which is a common feature of human dyslipidemia (Liang et al., 2003).
  
Entity Cystic fibrosis
Note gp78/AMFR degrades mutant cystic fibrosis transmembrane conductance regulator (CFTRΔF508) associated with cystic fibrosis (Ballar et al., 2010; Morito et al., 2008).
  
Entity Metabolism and disposition of drugs
Note gp78/AMFR participates in proteasomal degradation of CYP3A4, a dominant human liver cytochrome P450 enzyme functioning in the metabolism and disposition of drugs and responsible for many adverse drug-drug interactions (Kim et al., 2010; Pabarcus et al., 2009).
  
Entity Chronic obstructive pulmonary disease
Note gp78/AMFR expression is increased with the severity of emphysema (Min et al., 2011).
  
Entity Neurodegenerative diseases
Note gp78/AMFR may play a protective role against mutant huntingtin toxicity. Mutant huntingtin hinders polyubiquitin binding to the cue domain of gp78/AMFR and causes aggregation of ligase (Yang et al., 2010). gp78/AMFR also enhances ubiquitination, degradation, suppression of aggregation of mutant SOD1 associated with amyotrophic lateral sclerosis (ALS), and mutant ataxin-3 associated with Machado-Joseph disease. Furthermore, in spinal cords of ALS mice, gp78/AMFR expression is significantly is up-regulated (Ying et al., 2009).
  
Entity Alpha-1-antitrypsin deficiency
Note gp78/AMFR targets mutant ATZ (Z-variant alpha-1-antitrypsin) associated with alpha-1-antitrypsin deficiency for the proteasomal degradation and increases its solubility (Shen et al., 2006).
  

Bibliography

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Ballar P, Ors AU, Yang H, Fang S.
Int J Biochem Cell Biol. 2010 Jan;42(1):167-73. Epub 2009 Oct 12.
PMID 19828134
 
The role of a novel p97/valosin-containing protein-interacting motif of gp78 in endoplasmic reticulum-associated degradation.
Ballar P, Shen Y, Yang H, Fang S.
J Biol Chem. 2006 Nov 17;281(46):35359-68. Epub 2006 Sep 20.
PMID 16987818
 
Ufd1 is a cofactor of gp78 and plays a key role in cholesterol metabolism by regulating the stability of HMG-CoA reductase.
Cao J, Wang J, Qi W, Miao HH, Wang J, Ge L, DeBose-Boyd RA, Tang JJ, Li BL, Song BL.
Cell Metab. 2007 Aug;6(2):115-28.
PMID 17681147
 
The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site.
Chen B, Mariano J, Tsai YC, Chan AH, Cohen M, Weissman AM.
Proc Natl Acad Sci U S A. 2006 Jan 10;103(2):341-6. Epub 2006 Jan 3.
PMID 16407162
 
Autocrine motility factor receptor: a clinical review.
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PMID 18279062
 
The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum.
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Proc Natl Acad Sci U S A. 2001 Dec 4;98(25):14422-7. Epub 2001 Nov 27.
PMID 11724934
 
Protein sensors for membrane sterols.
Goldstein JL, DeBose-Boyd RA, Brown MS.
Cell. 2006 Jan 13;124(1):35-46. (REVIEW)
PMID 16413480
 
Expression of autocrine motility factor receptor correlates with disease progression in human gastric cancer.
Hirono Y, Fushida S, Yonemura Y, Yamamoto H, Watanabe H, Raz A.
Br J Cancer. 1996 Dec;74(12):2003-7.
PMID 8980404
 
Expression of autocrine motility factor (AMF) and its receptor, AMFR, in human breast cancer.
Jiang WG, Raz A, Douglas-Jones A, Mansel RE.
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PMID 16204225
 
Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase.
Jo Y, Debose-Boyd RA.
Crit Rev Biochem Mol Biol. 2010 Jun;45(3):185-98. (REVIEW)
PMID 20482385
 
A role for KAI1 in promotion of cell proliferation and mammary gland hyperplasia by the gp78 ubiquitin ligase.
Joshi B, Li L, Nabi IR.
J Biol Chem. 2010 Mar 19;285(12):8830-9. Epub 2010 Jan 20.
PMID 20089858
 
Autocrine motility factor receptor expression in patients with stage I non-small cell lung cancer.
Kara M, Ohta Y, Tanaka Y, Oda M, Watanabe Y.
Ann Thorac Surg. 2001 Mar;71(3):944-8.
PMID 11269478
 
Liver cytochrome P450 3A ubiquitination in vivo by gp78/autocrine motility factor receptor and C terminus of Hsp70-interacting protein (CHIP) E3 ubiquitin ligases: physiological and pharmacological relevance.
Kim SM, Acharya P, Engel JC, Correia MA.
J Biol Chem. 2010 Nov 12;285(46):35866-77. Epub 2010 Sep 6.
PMID 20819951
 
Multiple modes of interaction of the deglycosylation enzyme, mouse peptide N-glycanase, with the proteasome.
Li G, Zhou X, Zhao G, Schindelin H, Lennarz WJ.
Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):15809-14. Epub 2005 Oct 25.
PMID 16249333
 
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.
Liang JS, Kim T, Fang S, Yamaguchi J, Weissman AM, Fisher EA, Ginsberg HN.
J Biol Chem. 2003 Jun 27;278(26):23984-8. Epub 2003 Apr 1.
PMID 12670940
 
Critical role of proteostasis-imbalance in pathogenesis of COPD and severe emphysema.
Min T, Bodas M, Mazur S, Vij N.
J Mol Med (Berl). 2011 Jun;89(6):577-93. Epub 2011 Feb 12.
PMID 21318260
 
Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508.
Morito D, Hirao K, Oda Y, Hosokawa N, Tokunaga F, Cyr DM, Tanaka K, Iwai K, Nagata K.
Mol Biol Cell. 2008 Apr;19(4):1328-36. Epub 2008 Jan 23.
PMID 18216283
 
Cell shape modulation alters glycosylation of a metastatic melanoma cell-surface antigen.
Nabi IR, Raz A.
Int J Cancer. 1987 Sep 15;40(3):396-402.
PMID 3623718
 
Identification of B16-F1 melanoma autocrine motility-like factor receptor.
Nabi IR, Watanabe H, Raz A.
Cancer Res. 1990 Jan 15;50(2):409-14.
PMID 2153051
 
Expression of autocrine motility factor receptor in colorectal cancer as a predictor for disease recurrence.
Nakamori S, Watanabe H, Kameyama M, Imaoka S, Furukawa H, Ishikawa O, Sasaki Y, Kabuto T, Raz A.
Cancer. 1994 Oct 1;74(7):1855-62.
PMID 8082090
 
Inverse relation of E-cadherin and autocrine motility factor receptor expression as a prognostic factor in patients with bladder carcinomas.
Otto T, Birchmeier W, Schmidt U, Hinke A, Schipper J, Rubben H, Raz A.
Cancer Res. 1994 Jun 15;54(12):3120-3.
PMID 8205527
 
CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligases.
Pabarcus MK, Hoe N, Sadeghi S, Patterson C, Wiertz E, Correia MA.
Arch Biochem Biophys. 2009 Mar 1;483(1):66-74. Epub 2008 Dec 10.
PMID 19103148
 
Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction.
Ponting CP.
Biochem J. 2000 Oct 15;351 Pt 2:527-35.
PMID 11023840
 
Ubiquitin ligase gp78 increases solubility and facilitates degradation of the Z variant of alpha-1-antitrypsin.
Shen Y, Ballar P, Fang S.
Biochem Biophys Res Commun. 2006 Nov 3;349(4):1285-93. Epub 2006 Sep 7.
PMID 16979136
 
The autocrine motility factor receptor gene encodes a novel type of seven transmembrane protein.
Shimizu K, Tani M, Watanabe H, Nagamachi Y, Niinaka Y, Shiroishi T, Ohwada S, Raz A, Yokota J.
FEBS Lett. 1999 Aug 6;456(2):295-300.
PMID 10456327
 
Autocrine motility factor is a growth factor.
Silletti S, Raz A.
Biochem Biophys Res Commun. 1993 Jul 15;194(1):446-57.
PMID 8392842
 
The consensus coding sequences of human breast and colorectal cancers.
Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE.
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PMID 16959974
 
Gp78, a membrane-anchored ubiquitin ligase, associates with Insig-1 and couples sterol-regulated ubiquitination to degradation of HMG CoA reductase.
Song BL, Sever N, DeBose-Boyd RA.
Mol Cell. 2005 Sep 16;19(6):829-40.
PMID 16168377
 
The relation between the growth patterns of gastric carcinoma and the expression of hepatocyte growth factor receptor (c-met), autocrine motility factor receptor, and urokinase-type plasminogen activator receptor.
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Timar J, Raso E, Dome B, Ladanyi A, Banfalvi T, Gilde K, Raz A.
Clin Exp Metastasis. 2002;19(3):225-32.
PMID 12067203
 
The ubiquitin ligase gp78 promotes sarcoma metastasis by targeting KAI1 for degradation.
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Nat Med. 2007 Dec;13(12):1504-9. Epub 2007 Nov 25.
PMID 18037895
 
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PMID 17265125
 
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PMID 1649192
 
Huntingtin interacts with the cue domain of gp78 and inhibits gp78 binding to ubiquitin and p97/VCP.
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PMID 20126661
 
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Citation

This paper should be referenced as such :
Erzurumlu, Y ; Ballar, P
AMFR (autocrine motility factor receptor)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(1):25-29.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/AMFRID627ch16q12.html


External links

Nomenclature
HGNC (Hugo)AMFR   463
Cards
AtlasAMFRID627ch16q12
Entrez_Gene (NCBI)AMFR  267  autocrine motility factor receptor
AliasesGP78; RNF45
GeneCards (Weizmann)AMFR
Ensembl hg19 (Hinxton)ENSG00000159461 [Gene_View]  chr16:56395364-56459450 [Contig_View]  AMFR [Vega]
Ensembl hg38 (Hinxton)ENSG00000159461 [Gene_View]  chr16:56395364-56459450 [Contig_View]  AMFR [Vega]
ICGC DataPortalENSG00000159461
TCGA cBioPortalAMFR
AceView (NCBI)AMFR
Genatlas (Paris)AMFR
WikiGenes267
SOURCE (Princeton)AMFR
Genetics Home Reference (NIH)AMFR
Genomic and cartography
GoldenPath hg19 (UCSC)AMFR  -     chr16:56395364-56459450 -  16q21   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)AMFR  -     16q21   [Description]    (hg38-Dec_2013)
EnsemblAMFR - 16q21 [CytoView hg19]  AMFR - 16q21 [CytoView hg38]
Mapping of homologs : NCBIAMFR [Mapview hg19]  AMFR [Mapview hg38]
OMIM603243   
Gene and transcription
Genbank (Entrez)AA767223 AF124145 AK023874 AK123962 BC017043
RefSeq transcript (Entrez)NM_001144 NM_138958
RefSeq genomic (Entrez)NC_000016 NC_018927 NT_010498 NW_004929402
Consensus coding sequences : CCDS (NCBI)AMFR
Cluster EST : UnigeneHs.295137 [ NCBI ]
CGAP (NCI)Hs.295137
Alternative Splicing GalleryENSG00000159461
Gene ExpressionAMFR [ NCBI-GEO ]   AMFR [ EBI - ARRAY_EXPRESS ]   AMFR [ SEEK ]   AMFR [ MEM ]
Gene Expression Viewer (FireBrowse)AMFR [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)267
GTEX Portal (Tissue expression)AMFR
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9UKV5   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9UKV5  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9UKV5
Splice isoforms : SwissVarQ9UKV5
Catalytic activity : Enzyme6.3.2.- [ Enzyme-Expasy ]   6.3.2.-6.3.2.- [ IntEnz-EBI ]   6.3.2.- [ BRENDA ]   6.3.2.- [ KEGG ]   
PhosPhoSitePlusQ9UKV5
Domaine pattern : Prosite (Expaxy)CUE (PS51140)    ZF_RING_2 (PS50089)   
Domains : Interpro (EBI)CUE    Znf_RING    Znf_RING/FYVE/PHD   
Domain families : Pfam (Sanger)CUE (PF02845)    zf-RING_2 (PF13639)   
Domain families : Pfam (NCBI)pfam02845    pfam13639   
Domain families : Smart (EMBL)CUE (SM00546)  RING (SM00184)  
Conserved Domain (NCBI)AMFR
DMDM Disease mutations267
Blocks (Seattle)AMFR
PDB (SRS)2EJS    2LVN    2LVO    2LVP    2LVQ    2LXH    2LXP    3FSH    3H8K    3TIW    4G3O    4LAD   
PDB (PDBSum)2EJS    2LVN    2LVO    2LVP    2LVQ    2LXH    2LXP    3FSH    3H8K    3TIW    4G3O    4LAD   
PDB (IMB)2EJS    2LVN    2LVO    2LVP    2LVQ    2LXH    2LXP    3FSH    3H8K    3TIW    4G3O    4LAD   
PDB (RSDB)2EJS    2LVN    2LVO    2LVP    2LVQ    2LXH    2LXP    3FSH    3H8K    3TIW    4G3O    4LAD   
Structural Biology KnowledgeBase2EJS    2LVN    2LVO    2LVP    2LVQ    2LXH    2LXP    3FSH    3H8K    3TIW    4G3O    4LAD   
SCOP (Structural Classification of Proteins)2EJS    2LVN    2LVO    2LVP    2LVQ    2LXH    2LXP    3FSH    3H8K    3TIW    4G3O    4LAD   
CATH (Classification of proteins structures)2EJS    2LVN    2LVO    2LVP    2LVQ    2LXH    2LXP    3FSH    3H8K    3TIW    4G3O    4LAD   
SuperfamilyQ9UKV5
Human Protein AtlasENSG00000159461
Peptide AtlasQ9UKV5
HPRD09130
IPIIPI00435690   IPI00423874   IPI00640753   
Protein Interaction databases
DIP (DOE-UCLA)Q9UKV5
IntAct (EBI)Q9UKV5
FunCoupENSG00000159461
BioGRIDAMFR
STRING (EMBL)AMFR
ZODIACAMFR
Ontologies - Pathways
QuickGOQ9UKV5
Ontology : AmiGOprotein polyubiquitination  protein polyubiquitination  Hrd1p ubiquitin ligase ERAD-M complex  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  receptor activity  protein binding  nucleus  endoplasmic reticulum membrane  ubiquitin-dependent protein catabolic process  movement of cell or subcellular component  signal transduction  aging  learning or memory  zinc ion binding  membrane  integral component of membrane  ligase activity  integral component of endoplasmic reticulum membrane  dendrite  growth cone  ER-associated ubiquitin-dependent protein catabolic process  ER-associated ubiquitin-dependent protein catabolic process  ER-associated ubiquitin-dependent protein catabolic process  protein binding, bridging  endoplasmic reticulum unfolded protein response  positive regulation of protein binding  ubiquitin-ubiquitin ligase activity  ERAD pathway  Derlin-1 retrotranslocation complex  protein ubiquitination involved in ubiquitin-dependent protein catabolic process  neuronal cell body  protein complex  perinuclear region of cytoplasm  chaperone binding  protein oligomerization  protein autoubiquitination  ubiquitin protein ligase activity  protein K48-linked ubiquitination  ubiquitin protein ligase activity involved in ERAD pathway  BAT3 complex binding  BAT3 complex binding  ubiquitin-specific protease binding  
Ontology : EGO-EBIprotein polyubiquitination  protein polyubiquitination  Hrd1p ubiquitin ligase ERAD-M complex  ubiquitin-protein transferase activity  ubiquitin-protein transferase activity  receptor activity  protein binding  nucleus  endoplasmic reticulum membrane  ubiquitin-dependent protein catabolic process  movement of cell or subcellular component  signal transduction  aging  learning or memory  zinc ion binding  membrane  integral component of membrane  ligase activity  integral component of endoplasmic reticulum membrane  dendrite  growth cone  ER-associated ubiquitin-dependent protein catabolic process  ER-associated ubiquitin-dependent protein catabolic process  ER-associated ubiquitin-dependent protein catabolic process  protein binding, bridging  endoplasmic reticulum unfolded protein response  positive regulation of protein binding  ubiquitin-ubiquitin ligase activity  ERAD pathway  Derlin-1 retrotranslocation complex  protein ubiquitination involved in ubiquitin-dependent protein catabolic process  neuronal cell body  protein complex  perinuclear region of cytoplasm  chaperone binding  protein oligomerization  protein autoubiquitination  ubiquitin protein ligase activity  protein K48-linked ubiquitination  ubiquitin protein ligase activity involved in ERAD pathway  BAT3 complex binding  BAT3 complex binding  ubiquitin-specific protease binding  
Pathways : KEGGProtein processing in endoplasmic reticulum   
NDEx NetworkAMFR
Atlas of Cancer Signalling NetworkAMFR
Wikipedia pathwaysAMFR
Orthology - Evolution
OrthoDB267
GeneTree (enSembl)ENSG00000159461
Phylogenetic Trees/Animal Genes : TreeFamAMFR
HOVERGENQ9UKV5
HOGENOMQ9UKV5
Homologs : HomoloGeneAMFR
Homology/Alignments : Family Browser (UCSC)AMFR
Gene fusions - Rearrangements
Fusion : MitelmanAMFR/ITGAM [16q12.2/16p11.2]  
Fusion: TCGAAMFR 16q12.2 ITGAM 16p11.2 BRCA
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerAMFR [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)AMFR
dbVarAMFR
ClinVarAMFR
1000_GenomesAMFR 
Exome Variant ServerAMFR
ExAC (Exome Aggregation Consortium)AMFR (select the gene name)
Genetic variants : HAPMAP267
Genomic Variants (DGV)AMFR [DGVbeta]
DECIPHER (Syndromes)16:56395364-56459450  ENSG00000159461
CONAN: Copy Number AnalysisAMFR 
Mutations
ICGC Data PortalAMFR 
TCGA Data PortalAMFR 
Broad Tumor PortalAMFR
OASIS PortalAMFR [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICAMFR  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDAMFR
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch AMFR
DgiDB (Drug Gene Interaction Database)AMFR
DoCM (Curated mutations)AMFR (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)AMFR (select a term)
intoGenAMFR
NCG5 (London)AMFR
Cancer3DAMFR(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM603243   
Orphanet
MedgenAMFR
Genetic Testing Registry AMFR
NextProtQ9UKV5 [Medical]
TSGene267
GENETestsAMFR
Huge Navigator AMFR [HugePedia]
snp3D : Map Gene to Disease267
BioCentury BCIQAMFR
ClinGenAMFR
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD267
Chemical/Pharm GKB GenePA24768
Clinical trialAMFR
Miscellaneous
canSAR (ICR)AMFR (select the gene name)
Other databaseH-invDB
Probes
Litterature
PubMed105 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineAMFR
EVEXAMFR
GoPubMedAMFR
iHOPAMFR
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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