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Overview

Uniprot IDP25205
Protein NameDNA replication licensing factor MCM3
Gene NameMCM3
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
152 VHYCPATKKTIERRY
153 HYCPATKKTIERRYS
248 YRCLPGKKGGYTSGT
314 IHGHDYVKKAILCLL
315 HGHDYVKKAILCLLL
435 QGRVTIAKAGIHARL
556 DNLLHGTKKKKEKMV
557 NLLHGTKKKKEKMVS
570 VSAAFMKKYIHVAKI

Function

Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built (PubMed:32453425, PubMed:34694004, PubMed:34700328, PubMed:35585232). The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity (PubMed:32453425). Required for the entry in S phase and for cell division (Probable)

Protein Sequence

10 MAGTVVLDDV 20 ELREAQRDYL 30 DFLDDEEDQG 40 IYQSKVRELI 50 SDNQYRLIVN 60 VNDLRRKNEK 70 RANRLLNNAF 80 EELVAFQRAL 90 KDFVASIDAT 100 YAKQYEEFYV 110 GLEGSFGSKH 120 VSPRTLTSCF 130 LSCVVCVEGI 140 VTKCSLVRPK 150 VVRSVHYCPA 160 TKKTIERRYS 170 DLTTLVAFPS 180 SSVYPTKDEE 190 NNPLETEYGL 200 SVYKDHQTIT 210 IQEMPEKAPA 220 GQLPRSVDVI 230 LDDDLVDKAK 240 PGDRVQVVGT 250 YRCLPGKKGG 260 YTSGTFRTVL 270 IACNVKQMSK 280 DAQPSFSAED 290 IAKIKKFSKT 300 RSKDIFDQLA 310 KSLAPSIHGH 320 DYVKKAILCL 330 LLGGVERDLE 340 NGSHIRGDIN 350 ILLIGDPSVA 360 KSQLLRYVLC 370 TAPRAIPTTG 380 RGSSGVGLTA 390 AVTTDQETGE 400 RRLEAGAMVL 410 ADRGVVCIDE 420 FDKMSDMDRT 430 AIHEVMEQGR 440 VTIAKAGIHA 450 RLNARCSVLA 460 AANPVYGRYD 470 QYKTPMENIG 480 LQDSLLSRFD 490 LLFIMLDQMD 500 PEQDREISDH 510 VLRMHRYRAP 520 GEQDGDAMPL 530 GSAVDILATD 540 DPNFSQEDQQ 550 DTQIYEKHDN 560 LLHGTKKKKE 570 KMVSAAFMKK 580 YIHVAKIIKP 590 VLTQESATYI 600 AEEYSRLRSQ 610 DSMSSDTART 620 SPVTARTLET 630 LIRLATAHAK 640 ARMSKTVDLQ 650 DAEEAVELVQ 660 YAYFKKVLEK 670 EKKRKKRSED 680 ESETEDEEEK 690 SQEDQEQKRK 700 RRKTRQPDAK 710 DGDSYDPYDF 720 SDTEEEMPQV 730 HTPKTADSQE 740 TKESQKVELS 750 ESRLKAFKVA 760 LLDVFREAHA 770 QSIGMNRLTE 780 SINRDSEEPF 790 SSVEIQAALS 800 KMQDDNQVMV SEGIIFLI

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005658 alpha DNA polymerase:primase complex
Biological Process GO:0006271 DNA strand elongation involved in DNA replication
Biological Process GO:0000727 double-strand break repair via break-induced replication
Biological Process GO:1902975 mitotic DNA replication initiation
Biological Process GO:0030174 regulation of DNA-templated DNA replication initiation
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0071162 CMG complex
Cellular Component GO:0042555 MCM complex
Cellular Component GO:0016020 membrane
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0048471 perinuclear region of cytoplasm
Molecular Function GO:0005524 ATP binding
Molecular Function GO:0016887 ATP hydrolysis activity
Molecular Function GO:0003677 DNA binding
Molecular Function GO:0003678 DNA helicase activity
Molecular Function GO:0003697 single-stranded DNA binding
Biological Process GO:0006260 DNA replication
Biological Process GO:0006270 DNA replication initiation

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] 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.

[5] 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.