SCUBA

ASF1B — Anti-silencing function 1B histone chaperone

ASF1B belongs to a gene co-expression module in 5 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.

ASF1B's module in each cell type

Cell typeModuleShares the module with
CD19⁺ B cellsReplication Licensing
Cell cycle
CDC6, CDCA5, CDT1, CENPK, CENPU, CLSPN, DNAJC9, FAM111B +5 moreView in SCUBA
CD8⁺ T cellsMitotic Spindle
Cell cycle
CENPN, DDX39A, DTYMK, GGH, HMGB2, HMGN2, LMNB1, STMN1 +3 moreView in SCUBA
Gamma-delta T cellsMitosis Execution
Cell cycle
BUB1, CDCA8, CENPE, CENPF, CKS1B, EZH2, MAD2L1, MKI67 +12 more
Goblet cellsS-phase DNA Replication
Cell cycle
BRCA1, CDC6, CENPU, DHFR, FEN1, MYBL2, PCLAF, TK1 +1 moreView in SCUBA
Hematopoietic progenitor cellsLate S-phase G2 Entry
Cell cycle
CDC45, CDCA5, CENPM, DIAPH3, MND1, MYBL2, PKMYT1, RAD51AP1 +1 more

About the gene

SynonymsFLJ10604
Chromosome19: 14119512-14136613
Predicted locationIntracellular
Essential geneNo
Protein classPredicted intracellular proteins
Molecular functionChaperone, Chromatin regulator, Developmental protein
Biological processDifferentiation, Spermatogenesis, Transcription, Transcription regulation

Function

Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly. Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4): specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' (H3K9me1) and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in the cytosol. Does not participate in replication-independent nucleosome deposition which is mediated by ASF1A and HIRA. Required for gonad development.

Human Protein Atlas · Open Targets · UniProt

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