P38696 · ARP1_YEAST

Function

function

Core component of the dynactin complex which assists cytoplasmic dynein by increasing its processivity and by regulation of its cargo binding (By similarity).
The dynactin complex is required for the spindle translocation late in anaphase and is involved in a cell wall synthesis checkpoint. ARP1 forms the backbone filament of the dynactin rod structure and serves as the scaffold for the remaining subunits. Required for proper orientation of the mitotic spindle

Miscellaneous

Present with 1580 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 Componentactin cytoskeleton
Cellular Componentcytoplasm
Cellular Componentdynactin complex
Cellular Componentdynein complex
Cellular Componentmembrane
Cellular Componentmicrotubule
Molecular Functionstructural constituent of cytoskeleton
Biological Processactin filament-based movement
Biological Processestablishment of mitotic spindle orientation
Biological Processmitotic spindle orientation checkpoint signaling
Biological Processnuclear migration

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Centractin
  • Alternative names
    • Actin-like protein
    • Actin-related protein 1

Gene names

    • Name
      ARP1
    • Synonyms
      ACT3, ACT5
    • Ordered locus names
      YHR129C

Organism names

Accessions

  • Primary accession
    P38696
  • Secondary accessions
    • D3DL78
    • Q6B1J6

Proteomes

Organism-specific databases

Subcellular Location

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis2Temperature-sensitive; when associated with A-6.
Mutagenesis6Temperature-sensitive; when associated with A-2.
Mutagenesis46Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis; when associated with 48-A-A-49.
Mutagenesis48-49Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis; when associated with A-46.
Mutagenesis73Reduces spindle formation; when associated with A-75.
Mutagenesis75Reduces spindle formation; when associated with A-73.
Mutagenesis79-80Reduces nuclear migration in mitosis.
Mutagenesis84-85Reduces spindle formation. Strongly reduces interaction with JNM1. Reduces nuclear migration in mitosis; when associated with A-87.
Mutagenesis87Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with 84-A-A-85.
Mutagenesis108-109Reduces nuclear migration in mitosis.
Mutagenesis133Lethal. Strongly reduces interaction with JNM1; when associated with A-136.
Mutagenesis136Lethal. Strongly reduces interaction with JNM1; when associated with A-133.
Mutagenesis162Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with A-165.
Mutagenesis165Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with A-162.
Mutagenesis185Temperature-sensitive. Strongly reduces interaction with JNM1; when associated with A-187.
Mutagenesis187Temperature-sensitive. Strongly reduces interaction with JNM1; when associated with A-185.
Mutagenesis214-216Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis. Alters complex assembly; when associated with A-219.
Mutagenesis219Lethal; when associated with 214-A--A-216.
Mutagenesis222-224Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis.
Mutagenesis233-235Reduces spindle formation.
Mutagenesis233-238Temperature-sensitive. Strongly reduces interaction with JNM1.
Mutagenesis236-238Reduces spindle formation.
Mutagenesis251Lethal and dominant cold-sensitive. Reduces nuclear migration in mitosis; when associated with A-254.
Mutagenesis254Lethal and dominant cold-sensitive. Reduces nuclear migration in mitosis; when associated with A-251.
Mutagenesis263-264Reduces spindle formation.
Mutagenesis266Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with A-269.
Mutagenesis269Lethal. Reduces spindle formation. Reduces nuclear migration in mitosis; when associated with A-266.
Mutagenesis294Reduces nuclear migration in mitosis; when associated with A-296 and A-298.
Mutagenesis296Reduces nuclear migration in mitosis; when associated with A-294 and A-298.
Mutagenesis298Reduces nuclear migration in mitosis; when associated with A-294 and A-296.
Mutagenesis321-322Lethal. Strongly reduces interaction with JNM1.
Mutagenesis326Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1; when associated with A-328.
Mutagenesis328Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1; when associated with A-326.
Mutagenesis336Strongly reduces interaction with JNM1; when associated with A-338.
Mutagenesis338Strongly reduces interaction with JNM1; when associated with A-336.
Mutagenesis344-346Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1.
Mutagenesis368-369Reduces nuclear migration in mitosis; when associated with A-371.
Mutagenesis369Lethal. Strongly reduces interaction with JNM1; when associated with A-371.
Mutagenesis371Lethal. Strongly reduces interaction with JNM1; when associated with A-369.
Mutagenesis371Reduces nuclear migration in mitosis; when associated with 368-A-A-369.
Mutagenesis374-375Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1; when associated with A-378.
Mutagenesis378Temperature-sensitive. Reduces nuclear migration in mitosis. Strongly reduces interaction with JNM1; when associated with 374-A-A-375.

Variants

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

The viewer provides 5 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000890661-384Centractin

Proteomic databases

Interaction

Subunit

Self-associates to form an actin-like filament of 8-10 monomers. Component of the dynactin complex composed of at least ARP1, JNM1, NIP100 and ARP10. Dynactin comprises a short rod of the ARP1 filament attached to ARP10 at its pointed-end and probably associated with the capping protein at its barbed-end. The rod is implicated in dynein cargo binding. A sidearm formed by NIP100 projects from the ARP1 filament and is implicated in motor binding (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P38696ARP10 Q045495EBI-2920, EBI-2977
BINARY P38696JNM1 P362247EBI-2920, EBI-9415
BINARY P38696NIP100 P334204EBI-2920, EBI-12049

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Sequence similarities

Belongs to the actin family. ARP1 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    384
  • Mass (Da)
    42,995
  • Last updated
    1995-02-01 v1
  • Checksum
    98EEA90DC9497B81
MDQLSDSYALYNQPVVIDNGSGIIKAGFSGEERPKALEYCLVGNTKYDKVMLEGLQGDTFIGNNAQKLRGLLKLRYPIKHGVVEDWDSMELIWSYVLNEVLQLQNIGEHPLLITEAPMNPLKNREQMAQVLFETFDVSALYVSNPAVLSLYASGRTTGCVVDCGEGYCSTVPIYDGFALPASMMRMDIGGADITEQLQFQLRKSAGVSLFSSSEREIVRTMKEKVCYLAKNIKKEEEKYLQGTQDLISTFKLPDGRCIEVGNDRYRAPEILFSPQIIGLGYDGLSDMCMQSIWKVDLDLRKPLLSSIILSGGTTTLKGFGDRMLWDLEALTKGTSKIKIIAPSERKYTTWIGGSILTGLSTFQRLWTKKSDWLEDSTRVYSNLM

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict3in Ref. 5; AAT93103

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X79811
EMBL· GenBank· DDBJ
CAA56206.1
EMBL· GenBank· DDBJ
Genomic DNA
U10398
EMBL· GenBank· DDBJ
AAB68412.1
EMBL· GenBank· DDBJ
Genomic DNA
AY693084
EMBL· GenBank· DDBJ
AAT93103.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006934
EMBL· GenBank· DDBJ
DAA06822.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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