Q9H1A4 · APC1_HUMAN

  • Protein
    Anaphase-promoting complex subunit 1
  • Gene
    ANAPC1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle (PubMed:18485873).
The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (PubMed:18485873).
The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132).

Pathway

Protein modification; protein ubiquitination.

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 Componentanaphase-promoting complex
Cellular Componentcytosol
Cellular Componentnucleoplasm
Molecular Functionmolecular adaptor activity
Biological Processanaphase-promoting complex-dependent catabolic process
Biological Processcell division
Biological Processmetaphase/anaphase transition of mitotic cell cycle
Biological Processprotein branched polyubiquitination
Biological Processprotein K11-linked ubiquitination
Biological Processprotein K48-linked ubiquitination
Biological Processregulation of meiotic cell cycle
Biological Processregulation of mitotic cell cycle

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Anaphase-promoting complex subunit 1
  • Short names
    APC1
  • Alternative names
    • Cyclosome subunit 1
    • Mitotic checkpoint regulator
    • Testis-specific gene 24 protein

Gene names

    • Name
      ANAPC1
    • Synonyms
      TSG24

Organism names

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

Accessions

  • Primary accession
    Q9H1A4
  • Secondary accessions
    • Q2M3H8
    • Q9BSE6
    • Q9H8D0

Proteomes

Organism-specific databases

Disease & Variants

Involvement in disease

Rothmund-Thomson syndrome 1 (RTS1)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A form of Rothmund-Thomson syndrome, a disorder characterized by sparse hair, eyebrows and eyelashes, juvenile cataracts, and poikiloderma, a genodermatosis presenting with mottled pigmentation, telangiectasia and epidermal atrophy. Additional features are short stature, dysplastic nails, and skeletal and dental abnormalities. RTS1 is an autosomal recessive form not associated with an increased risk of cancer.
  • See also
    MIM:618625

Variants

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

The viewer provides 1,780 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

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

TypeIDPosition(s)SourceDescription
ChainPRO_00002158711-1944UniProtAnaphase-promoting complex subunit 1
Modified residue51UniProtPhosphoserine
Modified residue (large scale data)51PRIDEPhosphoserine
Modified residue60UniProtPhosphoserine
Modified residue (large scale data)60PRIDEPhosphoserine
Modified residue202UniProtPhosphoserine
Modified residue (large scale data)202PRIDEPhosphoserine
Modified residue286UniProtPhosphoserine
Modified residue (large scale data)286PRIDEPhosphoserine
Modified residue291UniProtPhosphothreonine
Modified residue (large scale data)291PRIDEPhosphothreonine
Modified residue (large scale data)297PRIDEPhosphothreonine
Modified residue (large scale data)300PRIDEPhosphoserine
Modified residue (large scale data)309PRIDEPhosphoserine
Modified residue313UniProtPhosphoserine
Modified residue (large scale data)313PRIDEPhosphoserine
Modified residue (large scale data)317PRIDEPhosphoserine
Modified residue (large scale data)333PRIDEPhosphoserine
Modified residue (large scale data)334PRIDEPhosphoserine
Modified residue341UniProtPhosphoserine
Modified residue (large scale data)341PRIDEPhosphoserine
Modified residue343UniProtPhosphoserine
Modified residue (large scale data)343PRIDEPhosphoserine
Modified residue (large scale data)351PRIDEPhosphoserine
Modified residue355UniProtPhosphoserine
Modified residue (large scale data)355PRIDEPhosphoserine
Modified residue362UniProtPhosphoserine
Modified residue (large scale data)362PRIDEPhosphoserine
Modified residue (large scale data)364PRIDEPhosphoserine
Modified residue (large scale data)372PRIDEPhosphoserine
Modified residue373UniProtPhosphoserine
Modified residue377UniProtPhosphoserine
Modified residue (large scale data)377PRIDEPhosphoserine
Modified residue (large scale data)518PRIDEPhosphoserine
Modified residue (large scale data)522PRIDEPhosphoserine
Modified residue (large scale data)524PRIDEPhosphothreonine
Modified residue (large scale data)530PRIDEPhosphothreonine
Modified residue537UniProtPhosphothreonine
Modified residue (large scale data)537PRIDEPhosphothreonine
Modified residue547UniProtPhosphoserine
Modified residue (large scale data)547PRIDEPhosphoserine
Modified residue555UniProtPhosphoserine
Modified residue (large scale data)555PRIDEPhosphoserine
Modified residue (large scale data)563PRIDEPhosphoserine
Modified residue (large scale data)564PRIDEPhosphoserine
Modified residue (large scale data)569PRIDEPhosphoserine
Modified residue571UniProtPhosphotyrosine
Modified residue686UniProtPhosphoserine
Modified residue (large scale data)686PRIDEPhosphoserine
Modified residue688UniProtPhosphoserine
Modified residue (large scale data)688PRIDEPhosphoserine
Modified residue (large scale data)699PRIDEPhosphoserine
Modified residue (large scale data)701PRIDEPhosphothreonine
Modified residue (large scale data)703PRIDEPhosphoserine
Modified residue (large scale data)727PRIDEPhosphoserine
Modified residue (large scale data)731PRIDEPhosphoserine
Modified residue916UniProtPhosphoserine
Modified residue (large scale data)1058PRIDEPhosphoserine
Modified residue (large scale data)1347PRIDEPhosphoserine

Post-translational modification

Phosphorylated. Phosphorylation on Ser-355 occurs specifically during mitosis.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

The mammalian APC/C is composed at least of 14 distinct subunits ANAPC1, ANAPC2, CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10, ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a complex of at least 19 chains with a combined molecular mass of around 1.2 MDa; APC/C interacts with FZR1 and FBXO5.
View interactors in UniProtKB
View CPX-1860 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, repeat.

TypeIDPosition(s)Description
Region305-343Disordered
Region373-396Disordered
Region994-1016Disordered
Repeat1297-1325PC 1
Repeat1366-1404PC 2
Repeat1467-1501PC 3
Repeat1520-1552PC 4

Sequence similarities

Belongs to the APC1 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,944
  • Mass (Da)
    216,500
  • Last updated
    2001-03-01 v1
  • Checksum
    E08B1FE3FC28917E
MSNFYEERTTMIAARDLQEFVPFGRDHCKHHPNALNLQLRQLQPASELWSSDGAAGLVGSLQEVTIHEKQKESWQLRKGVSEIGEDVDYDEELYVAGNMVIWSKGSKSQALAVYKAFTVDSPVQQALWCDFIISQDKSEKAYSSNEVEKCICILQSSCINMHSIEGKDYIASLPFQVANVWPTKYGLLFERSASSHEVPPGSPREPLPTMFSMLHPLDEITPLVCKSGSLFGSSRVQYVVDHAMKIVFLNTDPSIVMTYDAVQNVHSVWTLRRVKSEEENVVLKFSEQGGTPQNVATSSSLTAHLRSLSKGDSPVTSPFQNYSSIHSQSRSTSSPSLHSRSPSISNMAALSRAHSPALGVHSFSGVQRFNISSHNQSPKRHSISHSPNSNSNGSFLAPETEPIVPELCIDHLWTETITNIREKNSQASKVFITSDLCGQKFLCFLVESQLQLRCVKFQESNDKTQLIFGSVTNIPAKDAAPVEKIDTMLVLEGSGNLVLYTGVVRVGKVFIPGLPAPSLTMSNTMPRPSTPLDGVSTPKPLSKLLGSLDEVVLLSPVPELRDSSKLHDSLYNEDCTFQQLGTYIHSIRDPVHNRVTLELSNGSMVRITIPEIATSELVQTCLQAIKFILPKEIAVQMLVKWYNVHSAPGGPSYHSEWNLFVTCLMNMMGYNTDRLAWTRNFDFEGSLSPVIAPKKARPSETGSDDDWEYLLNSDYHQNVESHLLNRSLCLSPSEASQMKDEDFSQNLSLDSSTLLFTHIPAIFFVLHLVYEELKLNTLMGEGICSLVELLVQLARDLKLGPYVDHYYRDYPTLVRTTGQVCTIDPGQTGFMHHPSFFTSEPPSIYQWVSSCLKGEGMPPYPYLPGICERSRLVVLSIALYILGDESLVSDESSQYLTRITIAPQKLQVEQEENRFSFRHSTSVSSLAERLVVWMTNVGFTLRDLETLPFGIALPIRDAIYHCREQPASDWPEAVCLLIGRQDLSKQACEGNLPKGKSVLSSDVPSGTETEEEDDGMNDMNHEVMSLIWSEDLRVQDVRRLLQSAHPVRVNVVQYPELSDHEFIEEKENRLLQLCQRTMALPVGRGMFTLFSYHPVPTEPLPIPKLNLTGRAPPRNTTVDLNSGNIDVPPNMTSWASFHNGVAAGLKIAPASQIDSAWIVYNKPKHAELANEYAGFLMALGLNGHLTKLATLNIHDYLTKGHEMTSIGLLLGVSAAKLGTMDMSITRLLSIHIPALLPPTSTELDVPHNVQVAAVVGIGLVYQGTAHRHTAEVLLAEIGRPPGPEMEYCTDRESYSLAAGLALGMVCLGHGSNLIGMSDLNVPEQLYQYMVGGHRRFQTGMHREKHKSPSYQIKEGDTINVDVTCPGATLALAMIYLKTNNRSIADWLRAPDTMYLLDFVKPEFLLLRTLARCLILWDDILPNSKWVDSNVPQIIRENSISLSEIELPCSEDLNLETLSQAHVYIIAGACLSLGFRFAGSENLSAFNCLHKFAKDFMTYLSAPNASVTGPHNLETCLSVVLLSLAMVMAGSGNLKVLQLCRFLHMKTGGEMNYGFHLAHHMALGLLFLGGGRYSLSTSNSSIAALLCALYPHFPAHSTDNRYHLQALRHLYVLAAEPRLLVPVDVDTNTPCYALLEVTYKGTQWYEQTKEELMAPTLLPELHLLKQIKVKGPRYWELLIDLSKGTQHLKSILSKDGVLYVKLRAGQLSYKEDPMGWQSLLAQTVANRNSEARAFKPETISAFTSDPALLSFAEYFCKPTVNMGQKQEILDLFSSVLYECVTQETPEMLPAYIAMDQAIRRLGRREMSETSELWQIKLVLEFFSSRSHQERLQNHPKRGLFMNSEFLPVVKCTIDNTLDQWLQVGGDMCVHAYLSGQPLEESQLSMLACFLVYHSVPAPQHLPPIGLEGSTSFAELLFKFKQLKMPVRALLRLAPLLLGNPQPMVM

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F8WAS1F8WAS1_HUMANANAPC1149
A0A2R8YF63A0A2R8YF63_HUMANANAPC1259
H0Y564H0Y564_HUMANANAPC11452

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict604in Ref. 3; BAB14687

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ278357
EMBL· GenBank· DDBJ
CAC19484.1
EMBL· GenBank· DDBJ
mRNA
BC005089
EMBL· GenBank· DDBJ
AAH05089.1
EMBL· GenBank· DDBJ
mRNA
BC104902
EMBL· GenBank· DDBJ
AAI04903.1
EMBL· GenBank· DDBJ
mRNA
BC104904
EMBL· GenBank· DDBJ
AAI04905.1
EMBL· GenBank· DDBJ
mRNA
AK023807
EMBL· GenBank· DDBJ
BAB14687.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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