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Q00776 · AP1M1_YEAST

Function

function

Component of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin. AP57 is probably a subunit of the Golgi membrane adaptor.

Miscellaneous

Present with 4420 molecules/cell in log phase SD medium.

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 ComponentAP-1 adaptor complex
Cellular Componentclathrin-coated pit
Cellular Componentclathrin-coated vesicle
Cellular Componentcytosol
Molecular Functionclathrin adaptor activity
Biological ProcessGolgi to vacuole transport
Biological Processintracellular protein transport
Biological Processvesicle targeting, trans-Golgi to endosome
Biological Processvesicle-mediated transport

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    AP-1 complex subunit mu-1-I
  • Alternative names
    • Clathrin assembly protein complex 1 mu-1-I medium chain
    • Clathrin coat assembly protein AP54
    • Clathrin coat-associated protein AP54
    • Golgi adaptor AP-1 54 kDa protein
    • HA1 54 kDa subunit

Gene names

    • Name
      APM1
    • Synonyms
      YAP54
    • ORF names
      P0394
    • Ordered locus names
      YPL259C

Organism names

Accessions

  • Primary accession
    Q00776
  • Secondary accessions
    • D6W3B0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001937781-475AP-1 complex subunit mu-1-I

Proteomic databases

PTM databases

Interaction

Subunit

Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit APL4 and beta-type subunit APL2), a medium adaptin (mu-type subunit APM1) and a small adaptin (sigma-type subunit APS1). AP-1 interacts with clathrin.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY Q00776APL2 P3600010EBI-2624, EBI-2206
BINARY Q00776APS1 P351815EBI-2624, EBI-2612

Complex viewer

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain175-473MHD
Region240-262Disordered

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    475
  • Mass (Da)
    53,874
  • Last updated
    1996-10-01 v2
  • MD5 Checksum
    A0E414E44A5A4FF23E77DB30286EBA42
MASAVYFCDHNGKPLLSRRYRDDIPLSAIDKFPILLSDLEEQSNLIPPCLNHNGLEYLFIQHNDLYVVAIVTSLSANAAAIFTFLHKLVEVLSDYLKTVEEESIRDNFVIIYELLDEVMDYGIPQITETKMLKQYITQKSFKLVKSAKKKRNATRPPVALTNSVSWRPEGITHKKNEAFLDIVESINMLMTQKGQVLRSEIIGDVKVNSKLSGMPDLKLGINDKGIFSKYLDDDTNIPSASATTSDNNTETDKKPSITSSSATNKKKVNIELEDLKFHQCVRLSKFENEKIITFIPPDGKFDLMNYRLSTTIKPLIWCDVNVQVHSNSRIEIHCKAKAQIKRKSTATNVEILIPVPDDADTPTFKYSHGSLKYVPEKSAILWKIRSFPGGKEYSMSAELGLPSISNNEDGNRTMPKSNAEILKGPVQIKFQIPYFTTSGIQVRYLKINEPKLQYKSYPWVRYITQSGDDYTIRLT

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict214in Ref. 1; CAA42828
Sequence conflict216in Ref. 1; CAA42828
Sequence conflict222in Ref. 1; CAA42828
Sequence conflict433in Ref. 1; CAA42828
Sequence conflict440in Ref. 1; CAA42828
Sequence conflict450in Ref. 1; CAA42828

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X60288
EMBL· GenBank· DDBJ
CAA42828.1
EMBL· GenBank· DDBJ
Genomic DNA
Z73615
EMBL· GenBank· DDBJ
CAA97989.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006949
EMBL· GenBank· DDBJ
DAA11176.1
EMBL· GenBank· DDBJ
Genomic DNA

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.
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