Search Results

Overview

Uniprot IDQ8WUB8
Protein NamePHD finger protein 10
Gene NamePHF10
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
195 TQKVEASKVPEYIKK
201 SKVPEYIKKAAKKAA
202 KVPEYIKKAAKKAAE
206 YIKKAAKKAAEFNSN
241 QVPQGKYKVLPTERT
365 PKRSVLSKSVPGYKP

Function

Involved in transcription activity regulation by chromatin remodeling. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth (By similarity)

Protein Sequence

10 MAAAAGPGAA 20 LSPRPCDSDP 30 ATPGAQSPKD 40 DNEDNSNDGT 50 QPSKRRRMGS 60 GDSSRSCETS 70 SQDLGFSYYP 80 AENLIEYKWP 90 PDETGEYYML 100 QEQVSEYLGV 110 TSFKRKYPDL 120 ERRDLSHKEK 130 LYLRELNVIT 140 ETQCTLGLTA 150 LRSDEVIDLM 160 IKEYPAKHAE 170 YSVILQEKER 180 QRITDHYKEY 190 SQMQQQNTQK 200 VEASKVPEYI 210 KKAAKKAAEF 220 NSNLNRERME 230 ERRAYFDLQT 240 HVIQVPQGKY 250 KVLPTERTKV 260 SSYPVALIPG 270 QFQEYYKRYS 280 PDELRYLPLN 290 TALYEPPLDP 300 ELPALDSDGD 310 SDDGEDGRGD 320 EKRKNKGTSD 330 SSSGNVSEGE 340 SPPDSQEDSF 350 QGRQKSKDKA 360 ATPRKDGPKR 370 SVLSKSVPGY 380 KPKVIPNAIC 390 GICLKGKESN 400 KKGKAESLIH 410 CSQCENSGHP 420 SCLDMTMELV 430 SMIKTYPWQC 440 MECKTCIICG 450 QPHHEEEMMF 460 CDMCDRGYHT 470 FCVGLGAIPS 480 GRWICDCCQR 490 APPTPRKVGR RGKNSKEG

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0000776 kinetochore
Cellular Component GO:0071564 npBAF complex
Cellular Component GO:0016363 nuclear matrix
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0004402 histone acetyltransferase activity
Molecular Function GO:0003712 transcription coregulator activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006338 chromatin remodeling
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0007399 nervous system development
Biological Process GO:0045597 positive regulation of cell differentiation
Biological Process GO:2000781 positive regulation of double-strand break repair
Biological Process GO:0045663 positive regulation of myoblast differentiation
Biological Process GO:1902459 positive regulation of stem cell population maintenance
Biological Process GO:0045582 positive regulation of T cell differentiation
Biological Process GO:0070316 regulation of G0 to G1 transition
Biological Process GO:2000045 regulation of G1/S transition of mitotic cell cycle
Biological Process GO:0030071 regulation of mitotic metaphase/anaphase transition
Biological Process GO:2000819 regulation of nucleotide-excision repair
Biological Process GO:0006357 regulation of transcription by RNA polymerase II

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] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] 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.

[7] 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.