Search Results

Overview

Uniprot IDQ8NEY8
Protein NamePeriphilin-1
Gene NamePPHLN1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
109 MRDGFRRKSFYSSHY
160 SYSPERSKSYSFHQS
180 VRPGASYKRQNEGNP
235 ELAEAASKWAAEKLE
37 LVNIVPKKPPLLDRP

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)

Protein Sequence

10 MWSEGRYEYE 20 RIPRERAPPR 30 SHPSDGYNRL 40 VNIVPKKPPL 50 LDRPGEGSYN 60 RYYSHVDYRD 70 YDEGRSFSHD 80 RRSGPPHRGD 90 ESGYRWTRDD 100 HSASRQPEYR 110 DMRDGFRRKS 120 FYSSHYARER 130 SPYKRDNTFF 140 RESPVGRKDS 150 PHSRSGSSVS 160 SRSYSPERSK 170 SYSFHQSQHR 180 KSVRPGASYK 190 RQNEGNPERD 200 KERPVQSLKT 210 SRDTSPSSGS 220 AVSSSKVLDK 230 PSRLTEKELA 240 EAASKWAAEK 250 LEKSDESNLP 260 EISEYEAGST 270 APLFTDQPEE 280 PESNTTHGIE 290 LFEDSQLTTR 300 SKAIASKTKE 310 IEQVYRQDCE 320 TFGMVVKMLI 330 EKDPSLEKSI 340 QFALRQNLHE 350 IESAGQTWQQ 360 VPPVRNTEMD 370 HDGTPENEGE 380 ETAQSAPQPP 390 QAPQPLQPRK 400 KRVRRTTQLR 410 RTTGAPDITW 420 GMLKKTTQEA 430 ERILLRTQTP 440 FTPENLFLAM 450 LSVVHCNSRK DVKPENKQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0000792 heterochromatin
Cellular Component GO:0140283 HUSH complex
Cellular Component GO:0140286 HUSH2 complex
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003729 mRNA binding
Molecular Function GO:0003723 RNA binding
Biological Process GO:0140719 constitutive heterochromatin formation
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0031424 keratinization
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0045814 negative regulation of gene expression, epigenetic
Biological Process GO:0032480 negative regulation of type I interferon production
Biological Process GO:0097355 protein localization to heterochromatin
Biological Process GO:0141005 transposable element silencing by heterochromatin formation

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.