Format

Send to:

Choose Destination

AMFR autocrine motility factor receptor [ Homo sapiens (human) ]

Gene ID: 267, updated on 4-Nov-2018

Summary

Official Symbol
AMFRprovided by HGNC
Official Full Name
autocrine motility factor receptorprovided by HGNC
Primary source
HGNC:HGNC:463
See related
Ensembl:ENSG00000159461 MIM:603243; Vega:OTTHUMG00000133239
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
GP78; RNF45
Summary
This locus encodes a glycosylated transmembrane receptor. Its ligand, autocrine motility factor, is a tumor motility-stimulating protein secreted by tumor cells. The encoded receptor is also a member of the E3 ubiquitin ligase family of proteins. It catalyzes ubiquitination and endoplasmic reticulum-associated degradation of specific proteins. [provided by RefSeq, Feb 2012]
Expression
Ubiquitous expression in testis (RPKM 45.4), kidney (RPKM 36.4) and 25 other tissues See more
Orthologs

Genomic context

See AMFR in Genome Data Viewer
Location:
16q13
Exon count:
17
Annotation release Status Assembly Chr Location
109 current GRCh38.p12 (GCF_000001405.38) 16 NC_000016.10 (56361452..56425538, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 16 NC_000016.9 (56395364..56459450, complement)

Chromosome 16 - NC_000016.10Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC26077 Neighboring gene G protein subunit alpha o1 Neighboring gene microRNA 3935 Neighboring gene nudix hydrolase 21 Neighboring gene 2-oxoglutarate and iron dependent oxygenase domain containing 1 Neighboring gene Bardet-Biedl syndrome 2

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Jun 15 11:32:44 2016

Bibliography

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

Pathways from BioSystems

  • Asparagine N-linked glycosylation, organism-specific biosystem (from REACTOME)
    Asparagine N-linked glycosylation, organism-specific biosystemN-linked glycosylation is the most important form of post-translational modification for proteins synthesized and folded in the Endoplasmic Reticulum (Stanley et al. 2009). An early study in 1999 rev...
  • Calnexin/calreticulin cycle, organism-specific biosystem (from REACTOME)
    Calnexin/calreticulin cycle, organism-specific biosystemThe unfolded protein is recognized by a chaperon protein (calnexin or calreticulin) and the folding process starts. The binding of these protein requires a mono-glucosylated glycan (Caramelo JJ and P...
  • ER Quality Control Compartment (ERQC), organism-specific biosystem (from REACTOME)
    ER Quality Control Compartment (ERQC), organism-specific biosystemProteins that are released from the CNX or CRT complex with folding defects accumulate in a compartment of the ER called ERQC (Kamhi-Nesher et al. 2001). Here, the enzymes UGGG1 or UGGG2 are able to ...
  • Metabolism of proteins, organism-specific biosystem (from REACTOME)
    Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
  • N-glycan trimming in the ER and Calnexin/Calreticulin cycle, organism-specific biosystem (from REACTOME)
    N-glycan trimming in the ER and Calnexin/Calreticulin cycle, organism-specific biosystemAfter being synthesized in the ER membrane the 14-sugars lipid-linked oligosaccharide is co-translationally transferred to an unfolded protein, as described in the previous steps. After this point th...
  • Post-translational protein modification, organism-specific biosystem (from REACTOME)
    Post-translational protein modification, organism-specific biosystemAfter translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the...
  • Protein processing in endoplasmic reticulum, organism-specific biosystem (from KEGG)
    Protein processing in endoplasmic reticulum, organism-specific biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
  • Protein processing in endoplasmic reticulum, conserved biosystem (from KEGG)
    Protein processing in endoplasmic reticulum, conserved biosystemThe endoplasmic reticulum (ER) is a subcellular organelle where proteins are folded with the help of lumenal chaperones. Newly synthesized peptides enter the ER via the sec61 pore and are glycosylate...
  • Sterol Regulatory Element-Binding Proteins (SREBP) signalling, organism-specific biosystem (from WikiPathways)
    Sterol Regulatory Element-Binding Proteins (SREBP) signalling, organism-specific biosystemSterol regulatory element-binding proteins (SREBPs) are membrane-bound proteins that act as transcription factors. They regulate lipid, especially cholesterol, biosynthesis and uptake at a transcript...

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
BAT3 complex binding IDA
Inferred from Direct Assay
more info
PubMed 
BAT3 complex binding IPI
Inferred from Physical Interaction
more info
PubMed 
chaperone binding IPI
Inferred from Physical Interaction
more info
PubMed 
identical protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
metal ion binding IEA
Inferred from Electronic Annotation
more info
 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein binding, bridging IMP
Inferred from Mutant Phenotype
more info
PubMed 
signaling receptor activity IPI
Inferred from Physical Interaction
more info
PubMed 
ubiquitin protein ligase activity IDA
Inferred from Direct Assay
more info
PubMed 
ubiquitin protein ligase activity TAS
Traceable Author Statement
more info
PubMed 
ubiquitin-protein transferase activity IDA
Inferred from Direct Assay
more info
PubMed 
ubiquitin-protein transferase activity IMP
Inferred from Mutant Phenotype
more info
PubMed 
ubiquitin-specific protease binding IPI
Inferred from Physical Interaction
more info
PubMed 
ubiquitin-ubiquitin ligase activity IDA
Inferred from Direct Assay
more info
PubMed 
Process Evidence Code Pubs
aging IEA
Inferred from Electronic Annotation
more info
 
endoplasmic reticulum mannose trimming TAS
Traceable Author Statement
more info
 
endoplasmic reticulum unfolded protein response IMP
Inferred from Mutant Phenotype
more info
PubMed 
learning or memory IEA
Inferred from Electronic Annotation
more info
 
positive regulation of protein binding IMP
Inferred from Mutant Phenotype
more info
PubMed 
protein K48-linked ubiquitination IDA
Inferred from Direct Assay
more info
PubMed 
protein autoubiquitination IDA
Inferred from Direct Assay
more info
PubMed 
protein complex oligomerization IDA
Inferred from Direct Assay
more info
PubMed 
protein folding TAS
Traceable Author Statement
more info
 
protein polyubiquitination IDA
Inferred from Direct Assay
more info
PubMed 
protein polyubiquitination IMP
Inferred from Mutant Phenotype
more info
PubMed 
signal transduction TAS
Traceable Author Statement
more info
PubMed 
ubiquitin-dependent ERAD pathway IC
Inferred by Curator
more info
PubMed 
ubiquitin-dependent ERAD pathway IDA
Inferred from Direct Assay
more info
PubMed 
ubiquitin-dependent ERAD pathway IMP
Inferred from Mutant Phenotype
more info
PubMed 
ubiquitin-dependent ERAD pathway TAS
Traceable Author Statement
more info
PubMed 
ubiquitin-dependent protein catabolic process IMP
Inferred from Mutant Phenotype
more info
PubMed 
Component Evidence Code Pubs
Derlin-1 retrotranslocation complex IDA
Inferred from Direct Assay
more info
PubMed 
Golgi apparatus IDA
Inferred from Direct Assay
more info
 
dendrite IEA
Inferred from Electronic Annotation
more info
 
endoplasmic reticulum IDA
Inferred from Direct Assay
more info
PubMed 
endoplasmic reticulum membrane IDA
Inferred from Direct Assay
more info
PubMed 
endoplasmic reticulum membrane TAS
Traceable Author Statement
more info
 
endoplasmic reticulum quality control compartment IEA
Inferred from Electronic Annotation
more info
 
growth cone IEA
Inferred from Electronic Annotation
more info
 
integral component of endoplasmic reticulum membrane IDA
Inferred from Direct Assay
more info
PubMed 
integral component of membrane NAS
Non-traceable Author Statement
more info
PubMed 
membrane HDA PubMed 
neuronal cell body IEA
Inferred from Electronic Annotation
more info
 
nucleus IEA
Inferred from Electronic Annotation
more info
 
perinuclear region of cytoplasm IDA
Inferred from Direct Assay
more info
PubMed 
protein-containing complex IDA
Inferred from Direct Assay
more info
PubMed 

General protein information

Preferred Names
E3 ubiquitin-protein ligase AMFR
Names
RING finger protein 45
RING-type E3 ubiquitin transferase AMFR
NP_001135.3
NP_001310440.1
NP_001310441.1
XP_005255947.1

NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

  1. NG_047034.1 RefSeqGene

    Range
    5001..69087
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001144.5NP_001135.3  E3 ubiquitin-protein ligase AMFR isoform c

    See identical proteins and their annotated locations for NP_001135.3

    Status: REVIEWED

    Source sequence(s)
    AA767223, AC009102, BC069197, BX345849, BX409690, CA748782
    Consensus CDS
    CCDS10758.1
    UniProtKB/Swiss-Prot
    Q9UKV5
    Related
    ENSP00000290649.5, OTTHUMP00000164316, ENST00000290649.9, OTTHUMT00000256978
    Conserved Domains (3) summary
    cd14421
    Location:458498
    CUE_AMFR; CUE domain found in autocrine motility factor receptor (AMFR) and similar proteins
    cd16455
    Location:339382
    RING-H2_AMFR; RING finger, H2 subclass, found in autocrine motility factor receptor (AMFR) and similar proteins
    cl26329
    Location:86382
    zf-rbx1; RING-H2 zinc finger domain
  2. NM_001323511.1NP_001310440.1  E3 ubiquitin-protein ligase AMFR isoform e

    Status: REVIEWED

    Source sequence(s)
    AA280077, AC009102, AC092140, BC051032, BQ889409, CD642692
    UniProtKB/TrEMBL
    A0A024R6R5
    Conserved Domains (3) summary
    COG5243
    Location:2287
    HRD1; HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones]
    cd14421
    Location:363403
    CUE_AMFR; CUE domain found in autocrine motility factor receptor (AMFR) and similar proteins
    pfam13639
    Location:244284
    zf-RING_2; Ring finger domain
  3. NM_001323512.1NP_001310441.1  E3 ubiquitin-protein ligase AMFR isoform d

    Status: REVIEWED

    Source sequence(s)
    AC009102, BC051032, BC069197, BI766313, CA425340, DB172402, DR005354
    UniProtKB/Swiss-Prot
    Q9UKV5

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109 details...Open this link in a new tab

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38.p12 Primary Assembly

Genomic

  1. NC_000016.10 Reference GRCh38.p12 Primary Assembly

    Range
    56361452..56425538 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_005255890.4XP_005255947.1  E3 ubiquitin-protein ligase AMFR isoform X1

    See identical proteins and their annotated locations for XP_005255947.1

    UniProtKB/TrEMBL
    A0A024R6R5
    Conserved Domains (3) summary
    COG5243
    Location:2287
    HRD1; HRD ubiquitin ligase complex, ER membrane component [Posttranslational modification, protein turnover, chaperones]
    cd14421
    Location:363403
    CUE_AMFR; CUE domain found in autocrine motility factor receptor (AMFR) and similar proteins
    pfam13639
    Location:244284
    zf-RING_2; Ring finger domain

Suppressed Reference Sequence(s)

The following Reference Sequences have been suppressed. Explain

  1. NM_138958.1: Suppressed sequence

    Description
    NM_138958.1: This RefSeq was permanently suppressed because it is a nonsense-mediated mRNA decay (NMD) candidate.
Support Center