Q5HY92 · FIGN_HUMAN

  • Protein
    Fidgetin
  • Gene
    FIGN
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

ATP-dependent microtubule severing protein. Severs microtubules along their length and depolymerizes their ends, primarily the minus-end, that may lead to the suppression of microtubule growth from and attachment to centrosomes. Microtubule severing may promote rapid reorganization of cellular microtubule arrays and the release of microtubules from the centrosome following nucleation. Microtubule release from the mitotic spindle poles may allow depolymerization of the microtubule end proximal to the spindle pole, leading to poleward microtubule flux and poleward motion of chromosome.

Features

Showing features for binding site.

1759100200300400500600700
TypeIDPosition(s)Description
Binding site489ATP (UniProtKB | ChEBI)
Binding site529-534ATP (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 Componentcentrosome
Cellular Componentcytoplasm
Cellular Componentmicrotubule
Cellular Componentnuclear matrix
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionmicrotubule severing ATPase activity
Biological Processcell division

Keywords

Enzyme and pathway databases

Community curation (1)

Community annotation

The subsequence LLVQRTEGFSGLDVAHLCQEAVVGPLHAMPATDLSAIMPSQLRPVTYQDFENAFCKIQPSISQKELDMYVEWNKMFGCSQ, which contains the Vps4_C domain, shows transcriptional activator activity in a high-throughput recruitment assay.

SourceSubmission dateContributor
PubMed:333267460000-0002-4108-0575

Names & Taxonomy

Protein names

  • Recommended name
    Fidgetin

Gene names

    • Name
      FIGN

Organism names

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

Accessions

  • Primary accession
    Q5HY92
  • Secondary accessions
    • B3KWM0
    • Q9H6M5
    • Q9NVZ9

Proteomes

Organism-specific databases

Subcellular Location

Nucleus matrix
Note: Localizes to centrosomes throughout mitosis and to the spindle midzone during telophase.

Keywords

Disease & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variantVAR_02761396in dbSNP:rs2231902
Natural variantVAR_027614448in dbSNP:rs2231904
Mutagenesis532Inhibits the ability to sever and depolymerize microtubules.
Natural variantVAR_027615565in dbSNP:rs2231905

Variants

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

The viewer provides 876 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 (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00002507481-759UniProtFidgetin
Modified residue (large scale data)5PRIDEPhosphothreonine
Modified residue400UniProtPhosphothreonine
Modified residue (large scale data)400PRIDEPhosphothreonine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with AKAP8 (via C-terminus).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q5HY92CHERP Q8IWX83EBI-12297985, EBI-2555370
BINARY Q5HY92HGS O149643EBI-12297985, EBI-740220

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region89-111Disordered
Region196-237Disordered
Compositional bias204-234Pro residues
Region258-290Disordered
Compositional bias264-289Pro residues
Compositional bias339-423Polar residues
Region339-457Disordered

Sequence similarities

Belongs to the AAA ATPase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    759
  • Mass (Da)
    82,146
  • Last updated
    2006-10-03 v2
  • Checksum
    68E1C4C8CA66AE2A
MISSTSVYGLKMQWTPEHAQWPEQHFDITSTTRSPAHKVEAYRGHLQRTYQYAWANDDISALTASNLLKKYAEKYSGILEGPVDRPVLSNYSDTPSGLVNGRKNESEPWQPSLNSEAVYPMNCVPDVITASKAGVSSALPPADVSASIGSSPGVASNLTEPSYSSSTCGSHTVPSLHAGLPSQEYAPGYNGSYLHSTYSSQPAPALPSPHPSPLHSSGLLQPPPPPPPPPALVPGYNGTSNLSSYSYPSASYPPQTAVGSGYSPGGAPPPPSAYLPSGIPAPTPLPPTTVPGYTYQGHGLTPIAPSALTNSSASSLKRKAFYMAGQGDMDSSYGNYSYGQQRSTQSPMYRMPDNSISNTNRGNGFDRSAETSSLAFKPTKQLMSSEQQRKFSSQSSRALTPPSYSTAKNSLGSRSSESFGKYTSPVMSEHGDEHRQLLSHPMQGPGLRAATSSNHSVDEQLKNTDTHLIDLVTNEIITQGPPVDWNDIAGLDLVKAVIKEEVLWPVLRSDAFSGLTALPRSILLFGPRGTGKTLLGRCIASQLGATFFKIAGSGLVAKWLGEAEKIIHASFLVARCRQPSVIFVSDIDMLLSSQVNEEHSPVSRMRTEFLMQLDTVLTSAEDQIVVICATSKPEEIDESLRRYFMKRLLIPLPDSTARHQIIVQLLSQHNYCLNDKEFALLVQRTEGFSGLDVAHLCQEAVVGPLHAMPATDLSAIMPSQLRPVTYQDFENAFCKIQPSISQKELDMYVEWNKMFGCSQ

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
B8ZZS6B8ZZS6_HUMANFIGN29

Sequence caution

The sequence AAX81992.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence BAA91590.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAA91590.1 differs from that shown. Reason: Frameshift
The sequence BAB15231.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias204-234Pro residues
Compositional bias264-289Pro residues
Compositional bias339-423Polar residues
Sequence conflict713in Ref. 2; CAI45980

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK001267
EMBL· GenBank· DDBJ
BAA91590.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
AK025747
EMBL· GenBank· DDBJ
BAB15231.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK125324
EMBL· GenBank· DDBJ
BAG54182.1
EMBL· GenBank· DDBJ
mRNA
BX649105
EMBL· GenBank· DDBJ
CAI45980.1
EMBL· GenBank· DDBJ
mRNA
AC093727
EMBL· GenBank· DDBJ
AAX81992.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.

Genome annotation databases

Similar Proteins

Disclaimer

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