Search Results

Overview

Uniprot IDQ9NRZ9
Protein NameLymphoid-specific helicase
Gene NameHELLS
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
122 SIDASEEKPVMRKKR
152 EEILSVAKKNKKENE
153 EILSVAKKNKKENED
155 LSVAKKNKKENEDEN
514 RPKRRTRKSINYSKI
520 RKSINYSKIDDFPNE
744 AAKRKLEKLIIHKNH
749 LEKLIIHKNHFKGGQ
753 IIHKNHFKGGQSGLN

Function

ATP-dependent chromatin remodeler that regulates chromatin accessibility, DNA methylation, and histone modifications. It facilitates de novo DNA methylation at repetitive sequences and promotes transcriptional silencing via recruitment of DNA methyltransferases (DNMTs) and histone deacetylases (HDACs), contributing to heterochromatin formation and repression of transposable elements (PubMed:30307408). Also involved in DNA repair by recruiting DNA damage response mediators to double-strand breaks in heterochromatin, promoting homologous recombination via RBBP8/CtIP-dependent end resection (PubMed:22946062, PubMed:31802118). During meiosis, it is recruited by PRDM9 to recombination hotspots, aiding chromatin opening (PubMed:32001511). Through these diverse roles, is crucial for processes such as development, differentiation, and genomic stability (PubMed:22946062, PubMed:31802118). Involved in regulation of the expansion or survival of lymphoid cells (By similarity)

Protein Sequence

10 MPAERPAGSG 20 GSEAPAMVEQ 30 LDTAVITPAM 40 LEEEEQLEAA 50 GLERERKMLE 60 KARMSWDRES 70 TEIRYRRLQH 80 LLEKSNIYSK 90 FLLTKMEQQQ 100 LEEQKKKEKL 110 ERKKESLKVK 120 KGKNSIDASE 130 EKPVMRKKRG 140 REDESYNISE 150 VMSKEEILSV 160 AKKNKKENED 170 ENSSSTNLCV 180 EDLQKNKDSN 190 SIIKDRLSET 200 VRQNTKFFFD 210 PVRKCNGQPV 220 PFQQPKHFTG 230 GVMRWYQVEG 240 MEWLRMLWEN 250 GINGILADEM 260 GLGKTVQCIA 270 TIALMIQRGV 280 PGPFLVCGPL 290 STLPNWMAEF 300 KRFTPDIPTM 310 LYHGTQEERQ 320 KLVRNIYKRK 330 GTLQIHPVVI 340 TSFEIAMRDR 350 NALQHCYWKY 360 LIVDEGHRIK 370 NMKCRLIREL 380 KRFNADNKLL 390 LTGTPLQNNL 400 SELWSLLNFL 410 LPDVFDDLKS 420 FESWFDITSL 430 SETAEDIIAK 440 EREQNVLHML 450 HQILTPFLLR 460 RLKSDVALEV 470 PPKREVVVYA 480 PLSKKQEIFY 490 TAIVNRTIAN 500 MFGSSEKETI 510 ELSPTGRPKR 520 RTRKSINYSK 530 IDDFPNELEK 540 LISQIQPEVD 550 RERAVVEVNI 560 PVESEVNLKL 570 QNIMMLLRKC 580 CNHPYLIEYP 590 IDPVTQEFKI 600 DEELVTNSGK 610 FLILDRMLPE 620 LKKRGHKVLL 630 FSQMTSMLDI 640 LMDYCHLRDF 650 NFSRLDGSMS 660 YSEREKNMHS 670 FNTDPEVFIF 680 LVSTRAGGLG 690 INLTAADTVI 700 IYDSDWNPQS 710 DLQAQDRCHR 720 IGQTKPVVVY 730 RLVTANTIDQ 740 KIVERAAAKR 750 KLEKLIIHKN 760 HFKGGQSGLN 770 LSKNFLDPKE 780 LMELLKSRDY 790 EREIKGSREK 800 VISDKDLELL 810 LDRSDLIDQM 820 NASGPIKEKM 830 GIFKILENSE DSSPECLF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000775 chromosome, centromeric region
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005721 pericentric heterochromatin
Cellular Component GO:0035861 site of double-strand break
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0140658 ATP-dependent chromatin remodeler activity
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0140463 chromatin-protein adaptor activity
Molecular Function GO:0004386 helicase activity
Biological Process GO:0051301 cell division
Biological Process GO:0006346 DNA methylation-dependent constitutive heterochromatin formation
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0006302 double-strand break repair
Biological Process GO:0000724 double-strand break repair via homologous recombination
Biological Process GO:0001822 kidney development
Biological Process GO:0046651 lymphocyte proliferation
Biological Process GO:0044027 negative regulation of gene expression via chromosomal CpG island methylation
Biological Process GO:0031508 pericentric 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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[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] 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.