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IID00392
UniprotQ99549
ProteinM-phase phosphoprotein 8
GeneMPHOSPH8
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
860
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 55-116 Hetero dimer : IID00336Complex
 Evidence X-RAY 3svm A Reference
       Region 3svm A 55-55 disorder
       Region 3svm A 56-115 order
       Region 3svm A 116-116 disorder
Seq 55-116 Hetero dimer : IID00088Complex
 Evidence X-RAY 3qo2 A Reference
       Region 3qo2 A 55-114 order
       Region 3qo2 A 115-116 disorder
 Evidence X-RAY 3qo2 B Reference
       Region 3qo2 B 55-56 disorder
       Region 3qo2 B 57-115 order
       Region 3qo2 B 116-116 disorder
 Evidence X-RAY 3qo2 C Reference
       Region 3qo2 C 55-55 disorder
       Region 3qo2 C 56-114 order
       Region 3qo2 C 115-116 disorder
 Evidence X-RAY 3qo2 D Reference
       Region 3qo2 D 55-55 disorder
       Region 3qo2 D 56-114 order
       Region 3qo2 D 115-116 disorder
Seq 55-116 Hetero octamer : IID00088Complex
 Evidence X-RAY 3r93 A Reference
       Region 3r93 A 55-56 disorder
       Region 3r93 A 57-114 order
       Region 3r93 A 115-116 disorder
 Evidence X-RAY 3r93 B Reference
       Region 3r93 B 55-56 disorder
       Region 3r93 B 57-114 order
       Region 3r93 B 115-116 disorder
 Evidence X-RAY 3r93 C Reference
       Region 3r93 C 55-56 disorder
       Region 3r93 C 57-114 order
       Region 3r93 C 115-116 disorder
 Evidence X-RAY 3r93 D Reference
       Region 3r93 D 55-55 disorder
       Region 3r93 D 56-114 order
       Region 3r93 D 115-116 disorder
Seq 55-116 Monomer :
 Evidence X-RAY 3lwe A Reference
       Region 3lwe A 55-115 order
       Region 3lwe A 116-116 disorder
 Evidence X-RAY 3lwe B Reference
       Region 3lwe B 55-113 order
       Region 3lwe B 114-116 disorder
Seqphosphorylation
    454-454 Phosphothreonine
    51-51 Phosphoserine
    85-85 Phosphoserine
    136-136 Phosphoserine
    138-138 Phosphoserine
    144-144 Phosphothreonine
    149-149 Phosphoserine; by CDK1
    403-403 Phosphoserine
    400-400 Phosphoserine
    392-392 Phosphoserine
    385-385 Phosphothreonine; by CDK1
    334-334 Phosphothreonine; by CDK1
    319-319 Phosphoserine
    279-279 Phosphoserine
    272-272 Phosphoserine
    266-266 Phosphoserine
    192-192 Phosphoserine
    189-189 Phosphoserine
    188-188 Phosphoserine
    164-164 Phosphoserine; by CDK1
Seqacetylation
    1-1 N-acetylmethionine
 
Prediction
NeProc
Disorder 1-61,136-199,228-450
Order 62-135,200-227,451-860
ProS 18-22,28-33,56-61,136-144,241-263,283-285,296-301,353-362,409-416,422-450
AlphaFold
Disorder 1-58,97-97,115-505,507-543,547-550,552-565,589-591,737-741,743-743,745-745,754-762,765-765,767-835,837-848,858-860
Order 59-96,98-114,506-506,544-546,551-551,566-588,592-736,742-742,744-744,746-753,763-764,766-766,836-836,849-857
Pfam Hmmer
PF00385 59-109 7.8e-19
PF00023 666-698 8.7e-09
SEG 26-36 ,151-156 ,163-185 ,205-234 ,253-268
Function
Function in SwissProt
Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression (PubMed:20871592, PubMed:26022416). Mediates recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2 (PubMed:26022416, PubMed:28581500). Binds H3K9me and promotes DNA methylation by recruiting DNMT3A to target CpG sites; these can be situated within the coding region of the gene (PubMed:20871592). Mediates down-regulation of CDH1 expression (PubMed:20871592). Also represses L1 retrotransposons in collaboration with MORC2 and, probably, SETDB1, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression (PubMed:29211708). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA by being recruited by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602).