Q9NYG5 · APC11_HUMAN

  • Protein
    Anaphase-promoting complex subunit 11
  • Gene
    ANAPC11
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Together with the cullin protein ANAPC2, constitutes the catalytic 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:11739784, 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:11739784, PubMed:18485873).
The APC/C complex catalyzes assembly of branched 'Lys-11'-/'Lys-48'-linked branched ubiquitin chains on target proteins (PubMed:29033132).
May recruit the E2 ubiquitin-conjugating enzymes to the complex (PubMed:11739784, PubMed:18485873).

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for binding site.

1841020304050607080
MKVKIKCWNGVATWLWVANDENCGICRMAFNGCCPDCKVPGDDCPLVWGQCSHCFHMHCILKWLHAQQVQQHCPMCRQEWKFKE
TypeIDPosition(s)Description
Binding site23Zn2+ 1 (UniProtKB | ChEBI)
Binding site26Zn2+ 1 (UniProtKB | ChEBI)
Binding site34Zn2+ 3 (UniProtKB | ChEBI)
Binding site37Zn2+ 3 (UniProtKB | ChEBI)
Binding site44Zn2+ 3 (UniProtKB | ChEBI)
Binding site51Zn2+ 2 (UniProtKB | ChEBI)
Binding site53Zn2+ 2 (UniProtKB | ChEBI)
Binding site56Zn2+ 1 (UniProtKB | ChEBI)
Binding site58Zn2+ 3 (UniProtKB | ChEBI)
Binding site59Zn2+ 1 (UniProtKB | ChEBI)
Binding site73Zn2+ 2 (UniProtKB | ChEBI)
Binding site76Zn2+ 2 (UniProtKB | ChEBI)

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 Componentnucleolus
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular Functioncullin family protein binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionubiquitin-ubiquitin ligase activity
Molecular Functionzinc ion binding
Biological Processanaphase-promoting complex-dependent catabolic process
Biological Processcell division
Biological Processmitotic cell cycle
Biological Processpositive regulation of mitotic metaphase/anaphase transition
Biological Processprotein branched polyubiquitination
Biological Processprotein K11-linked ubiquitination
Biological Processprotein K48-linked ubiquitination
Biological Processprotein ubiquitination
Biological Processregulation of meiotic cell cycle
Biological Processregulation of mitotic cell cycle
Biological Processubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Anaphase-promoting complex subunit 11
  • Short names
    APC11
  • Alternative names
    • Cyclosome subunit 11
    • Hepatocellular carcinoma-associated RING finger protein

Gene names

    • Name
      ANAPC11
    • ORF names
      HSPC214

Organism names

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

Accessions

  • Primary accession
    Q9NYG5
  • Secondary accessions
    • A8MTT2
    • B7ZW64
    • Q502X9
    • Q9BW64
    • Q9P0R2

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis23Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis26Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis34Slightly reduces autoubiquitination activity; in isoform 1.
Mutagenesis37Slightly reduces autoubiquitination activity; in isoform 1.
Mutagenesis44Slightly reduces autoubiquitination activity; in isoform 1.
Mutagenesis51Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis53Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis56Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis58Slightly reduces autoubiquitination activity; in isoform 1.
Mutagenesis59Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis73Greatly reduces autoubiquitination activity; in isoform 1.
Mutagenesis76Greatly reduces autoubiquitination activity; in isoform 1.

Variants

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

The viewer provides 71 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.

TypeIDPosition(s)Description
ChainPRO_00000557471-84Anaphase-promoting complex subunit 11

Post-translational modification

Auto-ubiquitinated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed at high levels in skeletal muscle and heart; in moderate levels in brain, kidney, and liver; and at low levels in colon, thymus, spleen, small intestine, placenta, lung and peripheral blood leukocyte.

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 (PubMed:10922056, PubMed:25043029, PubMed:26083744).
Interacts with the cullin domain of ANAPC2 (PubMed:11739784).
Interacts with UBE2D2 (PubMed:11739784).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q9NYG5GRN P287993EBI-2130187, EBI-747754
BINARY Q9NYG5PEX1 O439333EBI-2130187, EBI-988601
BINARY Q9NYG5-2BANP Q8N9N5-23EBI-12224467, EBI-11524452
BINARY Q9NYG5-2BEND2 Q8NDZ03EBI-12224467, EBI-954079
BINARY Q9NYG5-2CREB5 Q02930-33EBI-12224467, EBI-10192698
BINARY Q9NYG5-2CRYBA2 P536723EBI-12224467, EBI-750444
BINARY Q9NYG5-2CYSRT1 A8MQ033EBI-12224467, EBI-3867333
BINARY Q9NYG5-2DTX2 Q86UW93EBI-12224467, EBI-740376
BINARY Q9NYG5-2EFEMP1 Q128053EBI-12224467, EBI-536772
BINARY Q9NYG5-2EFEMP2 O959673EBI-12224467, EBI-743414
BINARY Q9NYG5-2FRS3 O435593EBI-12224467, EBI-725515
BINARY Q9NYG5-2GPANK1 O958723EBI-12224467, EBI-751540
BINARY Q9NYG5-2HSD3B7 Q9H2F33EBI-12224467, EBI-3918847
BINARY Q9NYG5-2IQUB Q8NA543EBI-12224467, EBI-10220600
BINARY Q9NYG5-2KRTAP11-1 Q8IUC13EBI-12224467, EBI-1052037
BINARY Q9NYG5-2KRTAP13-2 Q52LG23EBI-12224467, EBI-11953846
BINARY Q9NYG5-2KRTAP19-2 Q3LHN23EBI-12224467, EBI-12196745
BINARY Q9NYG5-2KRTAP3-1 Q9BYR83EBI-12224467, EBI-9996449
BINARY Q9NYG5-2KRTAP3-3 Q9BYR63EBI-12224467, EBI-3957694
BINARY Q9NYG5-2KRTAP6-1 Q3LI643EBI-12224467, EBI-12111050
BINARY Q9NYG5-2KRTAP6-2 Q3LI663EBI-12224467, EBI-11962084
BINARY Q9NYG5-2OXER1 Q8TDS53EBI-12224467, EBI-12813389
BINARY Q9NYG5-2P4HA3 Q7Z4N83EBI-12224467, EBI-10181968
BINARY Q9NYG5-2PRKAA2 P546463EBI-12224467, EBI-1383852
BINARY Q9NYG5-2PRKAB2 O437413EBI-12224467, EBI-1053424
BINARY Q9NYG5-2RBPMS Q93062-33EBI-12224467, EBI-740343
BINARY Q9NYG5-2SPMIP9 Q96LM63EBI-12224467, EBI-743976
BINARY Q9NYG5-2TCEANC Q8N8B7-23EBI-12224467, EBI-11955057
BINARY Q9NYG5-2TLE5 Q08117-23EBI-12224467, EBI-11741437
BINARY Q9NYG5-2WWOX Q9NZC7-53EBI-12224467, EBI-12040603
View interactors in UniProtKB
View CPX-1860 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for zinc finger.

TypeIDPosition(s)Description
Zinc finger34-77RING-type

Domain

The RING-type zinc finger domain coordinates an additional third zinc ion.

Sequence similarities

Belongs to the RING-box family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9NYG5-1

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
    84
  • Mass (Da)
    9,841
  • Last updated
    2000-10-01 v1
  • Checksum
    EACBD5A54FDC11AE
MKVKIKCWNGVATWLWVANDENCGICRMAFNGCCPDCKVPGDDCPLVWGQCSHCFHMHCILKWLHAQQVQQHCPMCRQEWKFKE

Q9NYG5-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 38-84: KVPGDDCPLVWGQCSHCFHMHCILKWLHAQQVQQHCPMCRQEWKFKE → PLHGESISRCLGWCPQPVPVLGGRAHPQVPINTASPTPGQHTGSLMSREESSRSPDPTPPALDQETSSLLRCTSPWCLDHSCDLFGITDQVSADGPRACRQGARRRLPAGVGPVLPLLPHALHPQVAARTAGAAALPHVPPGMEVQGVRPDLALAGGAS

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
J3KSK3J3KSK3_HUMANANAPC11111
A0A087X1B5A0A087X1B5_HUMANANAPC1189
J3QL35J3QL35_HUMANANAPC1144
J3QS46J3QS46_HUMANANAPC1172

Sequence caution

The sequence AAF36134.1 differs from that shown. Reason: Frameshift

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_01234738-84in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF247565
EMBL· GenBank· DDBJ
AAF65816.1
EMBL· GenBank· DDBJ
mRNA
AF247789
EMBL· GenBank· DDBJ
AAL95694.1
EMBL· GenBank· DDBJ
mRNA
AF151048
EMBL· GenBank· DDBJ
AAF36134.1
EMBL· GenBank· DDBJ
mRNA Frameshift
AC145207
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC000607
EMBL· GenBank· DDBJ
AAH00607.2
EMBL· GenBank· DDBJ
mRNA
BC066308
EMBL· GenBank· DDBJ
AAH66308.1
EMBL· GenBank· DDBJ
mRNA
BC095454
EMBL· GenBank· DDBJ
AAH95454.1
EMBL· GenBank· DDBJ
mRNA
BC104641
EMBL· GenBank· DDBJ
AAI04642.1
EMBL· GenBank· DDBJ
mRNA
BC171892
EMBL· GenBank· DDBJ
AAI71892.1
EMBL· GenBank· DDBJ
mRNA
BC171898
EMBL· GenBank· DDBJ
AAI71898.1
EMBL· GenBank· DDBJ
mRNA
BC171899
EMBL· GenBank· DDBJ
AAI71899.1
EMBL· GenBank· DDBJ
mRNA
BC171900
EMBL· GenBank· DDBJ
AAI71900.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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