DCAF1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0016567Biological processprotein ubiquitination
GO_0035212Biological processcell competition in a multicellular organism
GO_0033151Biological processV(D)J recombination
GO_0000122Biological processnegative regulation of transcription by RNA polymerase II
GO_0043687Biological processpost-translational protein modification
GO_0006338Biological processchromatin remodeling
GO_0045732Biological processpositive regulation of protein catabolic process
GO_0030183Biological processB cell differentiation
GO_0005654Cellular componentnucleoplasm
GO_0080008Cellular componentCul4-RING E3 ubiquitin ligase complex
GO_0001650Cellular componentfibrillar center
GO_0008180Cellular componentCOP9 signalosome
GO_0005737Cellular componentcytoplasm
GO_0005634Cellular componentnucleus
GO_1990756Molecular functionubiquitin-like ligase-substrate adaptor activity
GO_0106310Molecular functionprotein serine kinase activity
GO_0030331Molecular functionnuclear estrogen receptor binding
GO_0005524Molecular functionATP binding
GO_1990244Molecular functionhistone H2AT120 kinase activity
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameDCAF1
Protein nameDDB1- and CUL4-associated factor 1 (HIV-1 Vpr-binding protein) (VprBP) (Serine/threonine-protein kinase VPRBP) (EC 2.7.11.1) (Vpr-interacting protein)
SynonymsKIAA0800
VPRBP
RIP
DescriptionFUNCTION: Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2. Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex . The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination. Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition . Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription. H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors . Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 . By acting on TET dioxygenses, essential for oocyte maintenance at the primordial follicle stage, hence essential for female fertility (By similarity). .; FUNCTION: (Microbial infection) In case of infection by HIV-1 virus, it is recruited by HIV-1 Vpr in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to arrest the cell cycle in G2 phase, and also to protect the viral protein from proteasomal degradation by another E3 ubiquitin ligase. The HIV-1 Vpr protein hijacks the CUL4A-RBX1-DDB1-DCAF1/VPRBP complex to promote ubiquitination and degradation of proteins such as TERT and ZIP/ZGPAT. .; FUNCTION: (Microbial infection) In case of infection by HIV-2 virus, it is recruited by HIV-2 Vpx in order to hijack the CUL4A-RBX1-DDB1-DCAF1/VPRBP function leading to enhanced efficiency of macrophage infection and promotion of the replication of cognate primate lentiviruses in cells of monocyte/macrophage lineage. .

AccessionsQ9Y4B6
ENST00000504652.5 [Q9Y4B6-2]
ENST00000423656.5 [Q9Y4B6-1]
ENST00000684031.1 [Q9Y4B6-1]