SCUBA

FAM111A — FAM111 trypsin like peptidase A

FAM111A belongs to a gene co-expression module in 4 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.

FAM111A's module in each cell type

Cell typeModuleShares the module with
CD4⁺ T cellsImmune regulation
Immune regulation
DENND1B, GIT2, GOLGA8A, LPIN1, NLRC3, PPP2R5C, PSD4, RUFY3 +5 moreView in SCUBA
CD8⁺ T cellsS-phase Replication
Cell cycle
ATAD2, CEP152, E2F7, E2F8, ESCO2, NCAPD3, POLQ, STILView in SCUBA
Gamma-delta T cellsMitotic Spindle
Cell cycle
CAPRIN1, CDK5RAP2, CKAP5, CNTRL, DEK, DNMT1, GMPS, HADH +11 more
MacrophagesCentrosome & DNA Repair
Cell cycle
ANKRD13A, BRCA2, CASP2, CBX5, CCDC14, CEP152, CEP78, CKAP5 +34 moreView in SCUBA

About the gene

SynonymsFLJ22794, KIAA1895
Chromosome11: 59142748-59155039
Predicted locationIntracellular
Essential geneNo
Protein classDisease related genes, Human disease related genes, Predicted intracellular proteins
Molecular functionDNA-binding, Hydrolase, Protease
Biological processDNA damage, DNA repair, DNA replication, Host-virus interaction

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. Also acts as a restriction factor for some viruses including SV40 polyomavirus and vaccinia virus. Mechanistically, affects nuclear barrier function during viral replication by mediating the disruption of the nuclear pore complex (NPC) via its protease activity. In turn, interacts with vaccinia virus DNA-binding protein OPG079 in the cytoplasm and promotes its degradation without the need of its protease activity but through autophagy.

Human Protein Atlas · Open Targets · UniProt

Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.