Q9D2L9 · F111A_MOUSE

  • Protein
    Serine protease FAM111A
  • Gene
    Fam111a
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    4/5

Function

function

Single-stranded DNA-binding serine protease that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity. DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication and transcription, and which are induced by reactive agents, such as UV light or formaldehyde. Protects replication fork from stalling by removing DPCs, such as covalently trapped topoisomerase 1 (TOP1) adducts on DNA lesion, or poly(ADP-ribose) polymerase 1 (PARP1)-DNA complexes trapped by PARP inhibitors. Required for PCNA loading on replication sites. Promotes S-phase entry and DNA synthesis.

Features

Showing features for site, active site.

161350100150200250300350400450500550600
TypeIDPosition(s)Description
Site331-332Cleavage; by autolysis
Active site383Charge relay system
Active site437Charge relay system
Active site543Charge relay system

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 Componentchromatin
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Functionpeptidase activity
Molecular Functionsingle-stranded DNA binding
Biological ProcessDNA damage response
Biological ProcessDNA replication
Biological Processprotein autoprocessing
Biological Processprotein-DNA covalent cross-linking repair
Biological Processproteolysis
Biological Processreplication fork processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Serine protease FAM111A
  • EC number

Gene names

    • Name
      Fam111a

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • NOD
    • Czech II
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9D2L9
  • Secondary accessions
    • Q3T9N2
    • Q8BLH2
    • Q8CI07
    • Q8VE75
    • Q9CU11

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Chromosome
Cytoplasm
Note: Mainly localizes to nucleus: colocalizes with PCNA on replication sites.

Keywords

PTM/Processing

Features

Showing features for chain, cross-link, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002744081-613Serine protease FAM111A
Cross-link19Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue25Phosphoserine
Cross-link29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link62Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

Post-translational modification

Autocatalytically cleaved; autocatalytic cleavage takes place in trans.

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts (via PIP-box) with PCNA; this interaction is direct.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region1-72Disordered
Compositional bias15-61Basic and acidic residues

Domain

The PIP-box mediates the interaction with PCNA.

Sequence similarities

Belongs to the FAM111 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    613
  • Mass (Da)
    69,949
  • Last updated
    2001-06-01 v1
  • Checksum
    F926114F705A639B
MSCKKRKSQISFNPRKNKKIKDYFSQVPKEEQNDPNTVKVDSKKMPRDITNTRDQRPLSPRKTRQDQTPPLNKKITVTLGVNSRKHKNMKYELTCRETSSLYAALNTLSAVREEVESQKGREMLVCGKEGIEGYLNLGMPVCCIPEGSHVVITFCQCKSKTQENKQFFESQDQASTNYVRFCIHAVGSKRKKILKCGELQKEGNKLCVYGFKGETIRDTLRKDGRFCTFIESDDWKLINDLDTIIENTQPVDELEGKLFQVAAELPKNPRVVSVTQNSGSENRNFHKLEEYIVNEYTTLKEEGKKLRAYIKEKSEKRKKKASLFKVHKEHFGKMTRNSTPVKVVKHLSRVSDSVGFLWWNNNGNAGCATCFVFKELYILTCQHVIASIVGEGIDSSEWANIISQCVKVTFDYEELLPTGDKFFMVKPWFEISDKHLDYAVLELKENGQEVPAGLYHRIRPVPHSGLIYIIGHPEGEKKSIDCCTVVPQSSRRKKCQENFQAREEAGFCFSTSFIHMYTQRSFQEMLHNSDVVTYDTSFFGGSSGSPVFDSNGSLVAMHAAGITCTYQAGVSNIIEFGSIMESIDDHMKQDKYKEWYNTISGNVQNVEMLSIDF

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
D3YYD2D3YYD2_MOUSEFam111a569

Sequence caution

The sequence AAH38020.1 differs from that shown. Reason: Frameshift

Features

Showing features for compositional bias, sequence conflict.

TypeIDPosition(s)Description
Compositional bias15-61Basic and acidic residues
Sequence conflict227-228in Ref. 1; BAE42988
Sequence conflict239-240in Ref. 2; AAH19638
Sequence conflict243in Ref. 2; AAH19638
Sequence conflict272in Ref. 2; AAH19638
Sequence conflict282in Ref. 1; BAE42988
Sequence conflict293in Ref. 2; AAH19638
Sequence conflict301in Ref. 2; AAH19638
Sequence conflict304in Ref. 2; AAH19638
Sequence conflict325in Ref. 1; BAE42988
Sequence conflict330in Ref. 1; BAE42988
Sequence conflict335-336in Ref. 1; BAE42988
Sequence conflict342in Ref. 2; AAH19638
Sequence conflict342-346in Ref. 1; BAE42988
Sequence conflict352in Ref. 1; BAE42988
Sequence conflict356in Ref. 1; BAE42988
Sequence conflict360in Ref. 1; BAE42988
Sequence conflict400in Ref. 1; BAE42988
Sequence conflict413-419in Ref. 1; BAE42988
Sequence conflict435in Ref. 1; BAE42988
Sequence conflict456-459in Ref. 1; BAE42988
Sequence conflict463in Ref. 2; AAH19638
Sequence conflict463-464in Ref. 1; BAE42988
Sequence conflict476in Ref. 1; BAE42988
Sequence conflict480-482in Ref. 1; BAE42988
Sequence conflict489in Ref. 1; BAE42988
Sequence conflict507in Ref. 1; BAE42988
Sequence conflict532in Ref. 1; BAE42988
Sequence conflict572in Ref. 1; BAE42988
Sequence conflict579in Ref. 1; BAE42988
Sequence conflict584-586in Ref. 1; BAE42988
Sequence conflict592in Ref. 1; BAE42988
Sequence conflict599-600in Ref. 1; BAE42988
Sequence conflict604in Ref. 2; AAH19638
Sequence conflict605in Ref. 1; BAE42988
Sequence conflict611-613in Ref. 1; BAE42988

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK018830
EMBL· GenBank· DDBJ
BAB31452.3
EMBL· GenBank· DDBJ
mRNA
AK019499
EMBL· GenBank· DDBJ
BAB31763.1
EMBL· GenBank· DDBJ
mRNA
AK045189
EMBL· GenBank· DDBJ
BAC32254.1
EMBL· GenBank· DDBJ
mRNA
AK172402
EMBL· GenBank· DDBJ
BAE42988.1
EMBL· GenBank· DDBJ
mRNA
BC019638
EMBL· GenBank· DDBJ
AAH19638.1
EMBL· GenBank· DDBJ
mRNA
BC038020
EMBL· GenBank· DDBJ
AAH38020.1
EMBL· GenBank· DDBJ
mRNA Frameshift

Genome annotation databases

Similar Proteins

Disclaimer

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