Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

Q8N7J2 · AMER2_HUMAN

  • Protein
    APC membrane recruitment protein 2
  • Gene
    AMER2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Negative regulator of the canonical Wnt signaling pathway involved in neuroectodermal patterning. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplasma membrane
Molecular Functionbeta-catenin binding
Molecular Functionphosphatidylinositol-4,5-bisphosphate binding
Biological Processectoderm development
Biological Processnegative regulation of canonical Wnt signaling pathway
Biological Processregulation of canonical Wnt signaling pathway
Biological ProcessWnt signaling pathway

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    APC membrane recruitment protein 2
  • Short names
    Amer2
  • Alternative names
    • Protein FAM123A

Gene names

    • Name
      AMER2
    • Synonyms
      FAM123A

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q8N7J2
  • Secondary accessions
    • Q5RL80
    • Q5VX56
    • Q8N593
    • Q96NN5

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Peripheral membrane protein
Note: Translocates to the cell membrane following binding to PtdIns(4,5)P2.

Keywords

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_036448457in a colorectal cancer sample; somatic mutation
Natural variantVAR_031303659in dbSNP:rs2282406

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 907 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data).

Type
IDPosition(s)Source
Description
ChainPRO_00002818851-671UniProtAPC membrane recruitment protein 2
Modified residue162UniProtPhosphoserine
Modified residue229UniProtPhosphoserine
Modified residue233UniProtPhosphoserine
Modified residue (large scale data)233PRIDEPhosphoserine
Modified residue355UniProtPhosphoserine
Modified residue358UniProtPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with APC.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region1-24Disordered
Region76-358Disordered
Compositional bias153-169Polar residues
Compositional bias172-189Basic and acidic residues
Compositional bias200-215Basic and acidic residues
Compositional bias239-256Basic and acidic residues
Compositional bias296-314Basic and acidic residues
Region391-414Disordered
Region444-598Disordered
Compositional bias470-517Basic and acidic residues
Compositional bias520-536Polar residues
Compositional bias572-587Polar residues

Sequence similarities

Belongs to the Amer family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q8N7J2-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    671
  • Mass (Da)
    69,507
  • Last updated
    2011-06-28 v3
  • MD5 Checksum
    247E5F9BAE6E6398108841A926432208
METSRSRGGGGAVSERGGAGASVGVCRRKAEAGAGTGTLAADMDLHCDCAAETPAAEPPSGKINKAAFKLFKKRKSGGTMPSIFGVKNKGDGKSSGPTGLVRSRTHDGLAEVLVLESGRKEEPRGGGDSGGGGGGRPNPGPPRAAGPGGGSLASSSVAKSHSFFSLLKKNGRSENGKGEPVDASKAGGKQKRGLRGLFSGMRWHRKDKRAKAEAAEGRAPGGGLILPGSLTASLECVKEETPRAAREPEEPSQDAPRDPAGEPAGGEEVPAPADRAPARSCREAEGLAHPGDTGARGEDAAGHRRAEPGPGEVRTAEDASRTGAVPVKTVPLVDSEGGSGRAPAAPDPASVDPPSDPSADRICLMFSDVTSLKSFDSLTGCGDIIADQEEEAGPSCDKHVPGPGKPALSKKNPGVVAYQGGGEEMASPDEVDDTYLQEFWDMLSQTEEQGPEPQEGAAKVAAALETKVVPETPKDTRCVEAAKDASSVKRRRLNRIPIEPHPKEEPKHPEKEQQEGVPNSDEGYWDSTTPGPEEDSSSSGKKAGIPRDSYSGDALYDLYADPDGSPATLPGGKDNEETSSLSRLKPVSPGTITCPLRTPGSLLKDSKIPISIKHLTNLPSSHPVVHQQPSRSEMPRTKIPVSKVLVRRVSNRGLAGTTIRATACHDSAKKL

Q8N7J2-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Sequence caution

The sequence AAH32653.2 differs from that shown. Reason: Erroneous initiation Extended N-terminus.
The sequence AAH41392.1 differs from that shown. Reason: Frameshift
The sequence BAC05288.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for sequence conflict, compositional bias, alternative sequence.

Type
IDPosition(s)Description
Sequence conflict120in Ref. 1; BAB70845
Sequence conflict142in Ref. 3; AAH41392
Compositional bias153-169Polar residues
Compositional bias172-189Basic and acidic residues
Compositional bias200-215Basic and acidic residues
Compositional bias239-256Basic and acidic residues
Alternative sequenceVSP_024089261-379in isoform 2
Sequence conflict265in Ref. 1; BAC05288
Sequence conflict290in Ref. 3; AAH41392
Compositional bias296-314Basic and acidic residues
Sequence conflict442in Ref. 1; BAB70845
Compositional bias470-517Basic and acidic residues
Sequence conflict511in Ref. 3; AAH41392
Compositional bias520-536Polar residues
Compositional bias572-587Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK055049
EMBL· GenBank· DDBJ
BAB70845.1
EMBL· GenBank· DDBJ
mRNA
AK098343
EMBL· GenBank· DDBJ
BAC05288.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AL359757
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC032653
EMBL· GenBank· DDBJ
AAH32653.2
EMBL· GenBank· DDBJ
mRNA Different initiation
BC041392
EMBL· GenBank· DDBJ
AAH41392.1
EMBL· GenBank· DDBJ
mRNA Frameshift

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help