PPHLN1
entrez
51535
canonical
uniprot
Q8NEY8
canonical
ensembl
ENSG00000134283
resolver
ensp
ENSP00000256678
resolver
ensp
ENSP00000322048
resolver
ensp
ENSP00000338510
resolver
ensp
ENSP00000351066
resolver
ensp
ENSP00000378935
resolver
ensp
ENSP00000378947
resolver
ensp
ENSP00000390681
resolver
ensp
ENSP00000393965
resolver
ensp
ENSP00000449331
resolver
ensp
ENSP00000603433
resolver
ensp
ENSP00000658248
resolver
ensp
ENSP00000658250
resolver
ensp
ENSP00000658251
resolver
ensp
ENSP00000658252
resolver
ensp
ENSP00000658253
resolver
ensp
ENSP00000658254
resolver
ensp
ENSP00000689739
resolver
ensp
ENSP00000689740
resolver
ensp
ENSP00000758566
resolver
ensp
ENSP00000779715
resolver
ensp
ENSP00000790804
resolver
enst
ENST00000256678
resolver
genesymbol
PPHLN1
resolver
hgnc
HGNC:19369
resolver
uniprot
E9PAX8
resolver
uniprot
F8W6A0
resolver
uniprot
Q86YT2
resolver
uniprot
Q8IXN3
resolver
uniprot
Q8TB09
resolver
uniprot
Q96NB9
resolver
uniprot
Q9NXL4
resolver
uniprot
Q9P0P6
resolver
uniprot
Q9P0R9
resolver
uniprot_entry
F8W6A0_HUMAN
resolver
uniprot_entry
PPHLN_HUMAN
resolver
uniprot_sec
E9PAX8
resolver
uniprot_sec
Q86YT2
resolver
uniprot_sec
Q8IXN3
resolver
uniprot_sec
Q8TB09
resolver
uniprot_sec
Q96NB9
resolver
uniprot_sec
Q9NXL4
resolver
uniprot_sec
Q9P0P6
resolver
uniprot_sec
Q9P0R9
resolver
amino_acid_sequence
MWSEGRYEYERIPRERAPPRSHPSDGYNRLVNIVPKKPPLLDRPGEGSYNRYYSHVDYRDYDEGRSFSHDRRSGPPHRGDESGYRWTRDDHSASRQPEYRDMRDGFRRKSFYSSHYARERSPYKRDNTFFRESPVGRKDSPHSRSGSSVSSRSYSPERSKSYSFHQSQHRKSVRPGASYKRQNEGNPERDKERPVQSLKTSRDTSPSSGSAVSSSKVLDKPSRLTEKELAEAASKWAAEKLEKSDESNLPEISEYEAGSTAPLFTDQPEEPESNTTHGIELFEDSQLTTRSKAIASKTKEIEQVYRQDCETFGMVVKMLIEKDPSLEKSIQFALRQNLHEIESAGQTWQQVPPVRNTEMDHDGTPENEGEETAQSAPQPPQAPQPLQPRKKRVRRTTQLRRTTGAPDITWGMLKKTTQEAERILLRTQTPFTPENLFLAMLSVVHCNSRKDVKPENKQ
uniprot
proteins
function
FUNCTION: RNA-binding component of the HUSH complex, a multiprotein complex that mediates epigenetic repression of mobile genetic elements, such as retroviruses and transposable elements (PubMed:15474462, PubMed:17963697, PubMed:26022416, PubMed:32976585, PubMed:39658355). The HUSH complex mainly represses LINE-1 (L1) retrotransposons that are still capable of transposition (PubMed:32976585, PubMed:39658355). The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2, a chromatin remodeler that compacts chromatin (PubMed:26022416). The HUSH complex is also involved in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). Within the HUSH complex, PPHLN1 acts as a mRNA-binding component, which specifically binds nascent transcripts of mobile genetic elements, enabling HUSH-dependent silencing of transcripts (PubMed:39658355). Contributes to the maintenance of the HUSH complex at chromatin (PubMed:26022416, PubMed:39013473). As part of the HUSH2 complex, promotes epigenetic repression of interferon-stimulated genes (PubMed:33144593, PubMed:39013473). May be involved in epithelial differentiation by contributing to epidermal integrity and barrier formation (PubMed:12853457). {ECO:0000269|PubMed:12853457, ECO:0000269|PubMed:15474462, ECO:0000269|PubMed:17963697, ECO:0000269|PubMed:26022416, ECO:0000269|PubMed:30487602, ECO:0000269|PubMed:32976585, ECO:0000269|PubMed:33144593, ECO:0000269|PubMed:39013473, ECO:0000269|PubMed:39658355}.
uniprot
proteins
mass_dalton
52737
uniprot
proteins
mutagenesis
MUTAGEN 319; /note="L->A: In LLI mutant; abolished mRNA-binding and ability to silence mobile elements; when associated with A-326 and A-330."; /evidence="ECO:0000269|PubMed:32976585, ECO:0000269|PubMed:39658355"; MUTAGEN 326; /note="L->A: In LLI mutant; abolished mRNA-binding and ability to silence mobile elements; when associated with A-319 and A-330."; /evidence="ECO:0000269|PubMed:32976585, ECO:0000269|PubMed:39658355"; MUTAGEN 330; /note="I->A: In LLI mutant; abolished mRNA-binding and ability to silence mobile elements; when associated with A-319 and A-326."; /evidence="ECO:0000269|PubMed:32976585, ECO:0000269|PubMed:39658355
uniprot
proteins
post_translational_modification
PTM: Substrate of transglutaminase (in vitro). {ECO:0000269|PubMed:12853457}.
uniprot
proteins
pubmed
11042152
uniprot
proteins
pubmed
12087473
uniprot
proteins
pubmed
12853457
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15474462
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
17963697
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
26022416
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
30487602
uniprot
proteins
pubmed
32976585
uniprot
proteins
pubmed
33144593
uniprot
proteins
pubmed
39013473
uniprot
proteins
pubmed
39489739
uniprot
proteins
pubmed
39658355
uniprot
proteins
sequence_length
458
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12853457, ECO:0000269|PubMed:15474462, ECO:0000269|PubMed:26022416, ECO:0000269|PubMed:39013473, ECO:0000269|PubMed:39489739}. Cytoplasm {ECO:0000269|PubMed:12853457}. Chromosome {ECO:0000269|PubMed:26022416, ECO:0000269|PubMed:39013473, ECO:0000269|PubMed:39489739}. Note=In undifferentiated keratinocytes expressed in speckle-type nuclear granules and at the nuclear membrane, but in the differentiated keratinocytes colocalized with periplakin at the cell periphery and at cell-cell junctions (PubMed:12853457). Localizes to chromatin (PubMed:26022416). {ECO:0000269|PubMed:12853457, ECO:0000269|PubMed:26022416}.
uniprot
proteins