Q9D2L9 · F111A_MOUSE
- ProteinSerine protease FAM111A
- GeneFam111a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids613 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 331-332 | Cleavage; by autolysis | ||||
Sequence: FG | ||||||
Active site | 383 | Charge relay system | ||||
Sequence: H | ||||||
Active site | 437 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 543 | Charge relay system | ||||
Sequence: S |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | chromatin | |
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | peptidase activity | |
Molecular Function | single-stranded DNA binding | |
Biological Process | DNA damage response | |
Biological Process | DNA replication | |
Biological Process | protein autoprocessing | |
Biological Process | protein-DNA covalent cross-linking repair | |
Biological Process | proteolysis | |
Biological Process | replication fork processing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSerine protease FAM111A
- EC number
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9D2L9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Mainly localizes to nucleus: colocalizes with PCNA on replication sites.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, cross-link, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000274408 | 1-613 | Serine protease FAM111A | |||
Sequence: MSCKKRKSQISFNPRKNKKIKDYFSQVPKEEQNDPNTVKVDSKKMPRDITNTRDQRPLSPRKTRQDQTPPLNKKITVTLGVNSRKHKNMKYELTCRETSSLYAALNTLSAVREEVESQKGREMLVCGKEGIEGYLNLGMPVCCIPEGSHVVITFCQCKSKTQENKQFFESQDQASTNYVRFCIHAVGSKRKKILKCGELQKEGNKLCVYGFKGETIRDTLRKDGRFCTFIESDDWKLINDLDTIIENTQPVDELEGKLFQVAAELPKNPRVVSVTQNSGSENRNFHKLEEYIVNEYTTLKEEGKKLRAYIKEKSEKRKKKASLFKVHKEHFGKMTRNSTPVKVVKHLSRVSDSVGFLWWNNNGNAGCATCFVFKELYILTCQHVIASIVGEGIDSSEWANIISQCVKVTFDYEELLPTGDKFFMVKPWFEISDKHLDYAVLELKENGQEVPAGLYHRIRPVPHSGLIYIIGHPEGEKKSIDCCTVVPQSSRRKKCQENFQAREEAGFCFSTSFIHMYTQRSFQEMLHNSDVVTYDTSFFGGSSGSPVFDSNGSLVAMHAAGITCTYQAGVSNIIEFGSIMESIDDHMKQDKYKEWYNTISGNVQNVEMLSIDF | ||||||
Cross-link | 19 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 25 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 29 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Cross-link | 62 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K |
Post-translational modification
Autocatalytically cleaved; autocatalytic cleavage takes place in trans.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-72 | Disordered | ||||
Sequence: MSCKKRKSQISFNPRKNKKIKDYFSQVPKEEQNDPNTVKVDSKKMPRDITNTRDQRPLSPRKTRQDQTPPLN | ||||||
Compositional bias | 15-61 | Basic and acidic residues | ||||
Sequence: RKNKKIKDYFSQVPKEEQNDPNTVKVDSKKMPRDITNTRDQRPLSPR |
Domain
The PIP-box mediates the interaction with PCNA.
Sequence similarities
Belongs to the FAM111 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length613
- Mass (Da)69,949
- Last updated2001-06-01 v1
- ChecksumF926114F705A639B
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
D3YYD2 | D3YYD2_MOUSE | Fam111a | 569 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 15-61 | Basic and acidic residues | ||||
Sequence: RKNKKIKDYFSQVPKEEQNDPNTVKVDSKKMPRDITNTRDQRPLSPR | ||||||
Sequence conflict | 227-228 | in Ref. 1; BAE42988 | ||||
Sequence: CT → RS | ||||||
Sequence conflict | 239-240 | in Ref. 2; AAH19638 | ||||
Sequence: ND → GN | ||||||
Sequence conflict | 243 | in Ref. 2; AAH19638 | ||||
Sequence: T → S | ||||||
Sequence conflict | 272 | in Ref. 2; AAH19638 | ||||
Sequence: V → A | ||||||
Sequence conflict | 282 | in Ref. 1; BAE42988 | ||||
Sequence: N → K | ||||||
Sequence conflict | 293 | in Ref. 2; AAH19638 | ||||
Sequence: V → M | ||||||
Sequence conflict | 301 | in Ref. 2; AAH19638 | ||||
Sequence: E → K | ||||||
Sequence conflict | 304 | in Ref. 2; AAH19638 | ||||
Sequence: K → E | ||||||
Sequence conflict | 325 | in Ref. 1; BAE42988 | ||||
Sequence: K → E | ||||||
Sequence conflict | 330 | in Ref. 1; BAE42988 | ||||
Sequence: H → Q | ||||||
Sequence conflict | 335-336 | in Ref. 1; BAE42988 | ||||
Sequence: TR → KS | ||||||
Sequence conflict | 342 | in Ref. 2; AAH19638 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 342-346 | in Ref. 1; BAE42988 | ||||
Sequence: KVVKH → TVHEN | ||||||
Sequence conflict | 352 | in Ref. 1; BAE42988 | ||||
Sequence: D → A | ||||||
Sequence conflict | 356 | in Ref. 1; BAE42988 | ||||
Sequence: F → Y | ||||||
Sequence conflict | 360 | in Ref. 1; BAE42988 | ||||
Sequence: N → D | ||||||
Sequence conflict | 400 | in Ref. 1; BAE42988 | ||||
Sequence: N → S | ||||||
Sequence conflict | 413-419 | in Ref. 1; BAE42988 | ||||
Sequence: EELLPTG → KDFPLTK | ||||||
Sequence conflict | 435 | in Ref. 1; BAE42988 | ||||
Sequence: H → D | ||||||
Sequence conflict | 456-459 | in Ref. 1; BAE42988 | ||||
Sequence: HRIR → NGIG | ||||||
Sequence conflict | 463 | in Ref. 2; AAH19638 | ||||
Sequence: H → P | ||||||
Sequence conflict | 463-464 | in Ref. 1; BAE42988 | ||||
Sequence: HS → LG | ||||||
Sequence conflict | 476 | in Ref. 1; BAE42988 | ||||
Sequence: E → G | ||||||
Sequence conflict | 480-482 | in Ref. 1; BAE42988 | ||||
Sequence: IDC → SDG | ||||||
Sequence conflict | 489 | in Ref. 1; BAE42988 | ||||
Sequence: S → G | ||||||
Sequence conflict | 507 | in Ref. 1; BAE42988 | ||||
Sequence: F → C | ||||||
Sequence conflict | 532 | in Ref. 1; BAE42988 | ||||
Sequence: V → I | ||||||
Sequence conflict | 572 | in Ref. 1; BAE42988 | ||||
Sequence: N → S | ||||||
Sequence conflict | 579 | in Ref. 1; BAE42988 | ||||
Sequence: I → T | ||||||
Sequence conflict | 584-586 | in Ref. 1; BAE42988 | ||||
Sequence: DDH → LAN | ||||||
Sequence conflict | 592 | in Ref. 1; BAE42988 | ||||
Sequence: Y → H | ||||||
Sequence conflict | 599-600 | in Ref. 1; BAE42988 | ||||
Sequence: IS → VF | ||||||
Sequence conflict | 604 | in Ref. 2; AAH19638 | ||||
Sequence: Q → E | ||||||
Sequence conflict | 605 | in Ref. 1; BAE42988 | ||||
Sequence: N → D | ||||||
Sequence conflict | 611-613 | in Ref. 1; BAE42988 | ||||
Sequence: IDF → TDS |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |