Search Results

Overview

Uniprot IDQ9ULU4
Protein NameMYND-type zinc finger-containing chromatin reader ZMYND8
Gene NameZMYND8
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1115 ETSAEKSKESGSTLD
1148 SDHSRSNKSSWSSSD
1157 SWSSSDEKRGSTRSD
1172 HNTSTSTKSLLPKES
333 KEIPFSVKKTKSIFN
413 SPKILMSKPVLSGGT
46 TSPIKKKKKPGLLNS
47 SPIKKKKKPGLLNSN
505 LSAPITTKTDKTSTT
508 PITTKTDKTSTTGSI
549 PVPLISPKRQIRSRF
562 RFQLNLDKTIESCKA
8 MDISTRSKDPGSAER
801 ATGSPVKKQRPLLPK
808 KQRPLLPKETAPAVQ
824 VVWNSSSKFQTSSQK
831 KFQTSSQKWHMQKMQ
868 YQTRQAVKAVQQKEI

Function

Chromatin reader that recognizes dual histone modifications such as histone H3.1 dimethylated at 'Lys-36' and histone H4 acetylated at 'Lys-16' (H3.1K36me2-H4K16ac) and histone H3 methylated at 'Lys-4' and histone H4 acetylated at 'Lys-14' (H3K4me1-H3K14ac) (PubMed:26655721, PubMed:27477906, PubMed:31965980, PubMed:36064715). May act as a transcriptional corepressor for KDM5D by recognizing the dual histone signature H3K4me1-H3K14ac (PubMed:27477906). May also act as a transcriptional corepressor for KDM5C and EZH2 (PubMed:33323928). Recognizes acetylated histone H4 and recruits the NuRD chromatin remodeling complex to damaged chromatin for transcriptional repression and double-strand break repair by homologous recombination (PubMed:25593309, PubMed:27732854, PubMed:30134174). Also activates transcription elongation by RNA polymerase II through recruiting the P-TEFb complex to target promoters (PubMed:26655721, PubMed:30134174). Localizes to H3.1K36me2-H4K16ac marks at all-trans-retinoic acid (ATRA)-responsive genes and positively regulates their expression (PubMed:26655721). Promotes neuronal differentiation by associating with regulatory regions within the MAPT gene, to enhance transcription of a protein-coding MAPT isoform and suppress the non-coding MAPT213 isoform (PubMed:30134174, PubMed:35916866, PubMed:36064715). Suppresses breast cancer, and prostate cancer cell invasion and metastasis (PubMed:27477906, PubMed:31965980, PubMed:33323928)

Protein Sequence

10 MDISTRSKDP 20 GSAERTAQKR 30 KFPSPPHSSN 40 GHSPQDTSTS 50 PIKKKKKPGL 60 LNSNNKEQSE 70 LRHGPFYYMK 80 QPLTTDPVDV 90 VPQDGRNDFY 100 CWVCHREGQV 110 LCCELCPRVY 120 HAKCLRLTSE 130 PEGDWFCPEC 140 EKITVAECIE 150 TQSKAMTMLT 160 IEQLSYLLKF 170 AIQKMKQPGT 180 DAFQKPVPLE 190 QHPDYAEYIF 200 HPMDLCTLEK 210 NAKKKMYGCT 220 EAFLADAKWI 230 LHNCIIYNGG 240 NHKLTQIAKV 250 VIKICEHEMN 260 EIEVCPECYL 270 AACQKRDNWF 280 CEPCSNPHPL 290 VWAKLKGFPF 300 WPAKALRDKD 310 GQVDARFFGQ 320 HDRAWVPINN 330 CYLMSKEIPF 340 SVKKTKSIFN 350 SAMQEMEVYV 360 ENIRRKFGVF 370 NYSPFRTPYT 380 PNSQYQMLLD 390 PTNPSAGTAK 400 IDKQEKVKLN 410 FDMTASPKIL 420 MSKPVLSGGT 430 GRRISLSDMP 440 RSPMSTNSSV 450 HTGSDVEQDA 460 EKKATSSHFS 470 ASEESMDFLD 480 KSTASPASTK 490 TGQAGSLSGS 500 PKPFSPQLSA 510 PITTKTDKTS 520 TTGSILNLNL 530 DRSKAEMDLK 540 ELSESVQQQS 550 TPVPLISPKR 560 QIRSRFQLNL 570 DKTIESCKAQ 580 LGINEISEDV 590 YTAVEHSDSE 600 DSEKSDSSDS 610 EYISDDEQKS 620 KNEPEDTEDK 630 EGCQMDKEPS 640 AVKKKPKPTN 650 PVEIKEELKS 660 TSPASEKADP 670 GAVKDKASPE 680 PEKDFSEKAK 690 PSPHPIKDKL 700 KGKDETDSPT 710 VHLGLDSDSE 720 SELVIDLGED 730 HSGREGRKNK 740 KEPKEPSPKQ 750 DVVGKTPPST 760 TVGSHSPPET 770 PVLTRSSAQT 780 SAAGATATTS 790 TSSTVTVTAP 800 APAATGSPVK 810 KQRPLLPKET 820 APAVQRVVWN 830 SSSKFQTSSQ 840 KWHMQKMQRQ 850 QQQQQQQNQQ 860 QQPQSSQGTR 870 YQTRQAVKAV 880 QQKEITQSPS 890 TSTITLVTST 900 QSSPLVTSSG 910 SMSTLVSSVN 920 ADLPIATASA 930 DVAADIAKYT 940 SKMMDAIKGT 950 MTEIYNDLSK 960 NTTGSTIAEI 970 RRLRIEIEKL 980 QWLHQQELSE 990 MKHNLELTMA 1000 EMRQSLEQER 1010 DRLIAEVKKQ 1020 LELEKQQAVD 1030 ETKKKQWCAN 1040 CKKEAIFYCC 1050 WNTSYCDYPC 1060 QQAHWPEHMK 1070 SCTQSATAPQ 1080 QEADAEVNTE 1090 TLNKSSQGSS 1100 SSTQSAPSET 1110 ASASKEKETS 1120 AEKSKESGST 1130 LDLSGSRETP 1140 SSILLGSNQG 1150 SDHSRSNKSS 1160 WSSSDEKRGS 1170 TRSDHNTSTS 1180 TKSLLPKESR LDTFWD

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0043198 dendritic shaft
Cellular Component GO:0043197 dendritic spine
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0090734 site of DNA damage
Molecular Function GO:0140297 DNA-binding transcription factor binding
Molecular Function GO:0140015 histone H3K14ac reader activity
Molecular Function GO:0140109 histone H3K4me1 reader activity
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0003714 transcription corepressor activity
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0000724 double-strand break repair via homologous recombination
Biological Process GO:0098815 modulation of excitatory postsynaptic potential
Biological Process GO:0030336 negative regulation of cell migration
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0007399 nervous system development
Biological Process GO:0060999 positive regulation of dendritic spine development
Biological Process GO:1902952 positive regulation of dendritic spine maintenance
Biological Process GO:0051491 positive regulation of filopodium assembly
Biological Process GO:0032968 positive regulation of transcription elongation by RNA polymerase II
Biological Process GO:0071168 protein localization to chromatin
Biological Process GO:1902897 regulation of postsynaptic density protein 95 clustering

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.