Search Results

Overview

Uniprot ID	Q9Y6X9
Protein Name	ATPase MORC2
Gene Name	MORC2
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
574	KIRQQQEKLEALQKT
580	EKLEALQKTTPIRSQ
643	RPASQPRKAPVISST
713	PREVPSPKVIKTPVV
716	VPSPKVIKTPVVKKT
728	KKTESPIKLSPATPS
767	KRGRFVVKEEKKDSN
819	VTAVEVGKHVVRWKV

Function

ATP-dependent chromatin remodeler essential for epigenetic silencing by the HUSH (human silencing hub) complex (PubMed:28581500, PubMed:29440755, PubMed:32693025). Recruited by HUSH to target site in heterochromatin, the ATPase activity and homodimerization are critical for HUSH-mediated silencing (PubMed:28581500, PubMed:29440755, PubMed:32693025). Represses germ cell-related genes and L1 retrotransposons in collaboration with SETDB1 and the HUSH complex, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression (PubMed:29211708). During DNA damage response, regulates chromatin remodeling through ATP hydrolysis. Upon DNA damage, is phosphorylated by PAK1, both colocalize to chromatin and induce H2AX expression. ATPase activity is required and dependent of phosphorylation by PAK1 and presence of DNA (PubMed:23260667). Recruits histone deacetylases, such as HDAC4, to promoter regions, causing local histone H3 deacetylation and transcriptional repression of genes such as CA9 (PubMed:20110259, PubMed:20225202). Exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY, possibly preventing its dephosphorylation (PubMed:24286864). Together with MPHOSPH8, mediates silencing of protocadherin genes in the nervous system (By similarity)

Protein Sequence

10 MAFTNYSSLN 20 RAQLTFEYLH 30 TNSTTHEFLF 40 GALAELVDNA 50 RDADATRIDI 60 YAERREDLRG 70 GFMLCFLDDG 80 AGMDPSDAAS 90 VIQFGKSAKR 100 TPESTQIGQY 110 GNGLKSGSMR 120 IGKDFILFTK 130 KEDTMTCLFL 140 SRTFHEEEGI 150 DEVIVPLPTW 160 NARTREPVTD 170 NVEKFAIETE 180 LIYKYSPFRT 190 EEEVMTQFMK 200 IPGDSGTLVI 210 IFNLKLMDNG 220 EPELDIISNP 230 RDIQMAETSP 240 EGTKPERRSF 250 RAYAAVLYID 260 PRMRIFIHGH 270 KVQTKRLSCC 280 LYKPRMYKYT 290 SSRFKTRAEQ 300 EVKKAEHVAR 310 IAEEKAREAE 320 SKARTLEVRL 330 GGDLTRDSRV 340 MLRQVQNRAI 350 TLRREADVKK 360 RIKEAKQRAL 370 KEPKELNFVF 380 GVNIEHRDLD 390 GMFIYNCSRL 400 IKMYEKVGPQ 410 LEGGMACGGV 420 VGVVDVPYLV 430 LEPTHNKQDF 440 ADAKEYRHLL 450 RAMGEHLAQY 460 WKDIAIAQRG 470 IIKFWDEFGY 480 LSANWNQPPS 490 SELRYKRRRA 500 MEIPTTIQCD 510 LCLKWRTLPF 520 QLSSVEKDYP 530 DTWVCSMNPD 540 PEQDRCEASE 550 QKQKVPLGTF 560 RKDMKTQEEK 570 QKQLTEKIRQ 580 QQEKLEALQK 590 TTPIRSQADL 600 KKLPLEVTTR 610 PSTEEPVRRP 620 QRPRSPPLPA 630 VIRNAPSRPP 640 SLPTPRPASQ 650 PRKAPVISST 660 PKLPALAARE 670 EASTSRLLQP 680 PEAPRKPANT 690 LVKTASRPAP 700 LVQQLSPSLL 710 PNSKSPREVP 720 SPKVIKTPVV 730 KKTESPIKLS 740 PATPSRKRSV 750 AVSDEEEVEE 760 EAERRKERCK 770 RGRFVVKEEK 780 KDSNELSDSA 790 GEEDSADLKR 800 AQKDKGLHVE 810 VRVNREWYTG 820 RVTAVEVGKH 830 VVRWKVKFDY 840 VPTDTTPRDR 850 WVEKGSEDVR 860 LMKPPSPEHQ 870 SLDTQQEGGE 880 EEVGPVAQQA 890 IAVAEPSTSE 900 CLRIEPDTTA 910 LSTNHETIDL 920 LVQILRNCLR 930 YFLPPSFPIS 940 KKQLSAMNSD 950 ELISFPLKEY 960 FKQYEVGLQN 970 LCNSYQSRAD 980 SRAKASEESL 990 RTSERKLRET 1000 EEKLQKLRTN 1010 IVALLQKVQE 1020 DIDINTDDEL 1030 DAYIEDLITK GD

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005737	cytoplasm
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0000792	heterochromatin
Cellular Component	GO:0016363	nuclear matrix
Cellular Component	GO:0005654	nucleoplasm
Cellular Component	GO:0005634	nucleus
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:0000287	magnesium ion binding
Molecular Function	GO:0042803	protein homodimerization activity
Molecular Function	GO:0008270	zinc ion binding
Biological Process	GO:0006338	chromatin remodeling
Biological Process	GO:0140719	constitutive heterochromatin formation
Biological Process	GO:0006974	DNA damage response
Biological Process	GO:0006631	fatty acid metabolic process
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] 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.

[5] Chao L, Xu Y, Yang Y, Ao X, Liang J. Identification of lactylation-related biomarkers for diagnosis, prognosis, and treatment responsiveness in triple-negative breast cancer.. World J Surg Oncol 24(1):77. 2026 Jan 22. PMID: 41566505.

[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.