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Overview

Uniprot IDP49736
Protein NameDNA replication licensing factor MCM2
Gene NameMCM2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
728 KKYIIYAKERVHPKL
896 NKFSHDLKRKMILQQ

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 (PubMed:8175912). Plays a role in terminally differentiated hair cells development of the cochlea and induces cells apoptosis (PubMed:26196677)

Protein Sequence

10 MAESSESFTM 20 ASSPAQRRRG 30 NDPLTSSPGR 40 SSRRTDALTS 50 SPGRDLPPFE 60 DESEGLLGTE 70 GPLEEEEDGE 80 ELIGDGMERD 90 YRAIPELDAY 100 EAEGLALDDE 110 DVEELTASQR 120 EAAERAMRQR 130 DREAGRGLGR 140 MRRGLLYDSD 150 EEDEERPARK 160 RRQVERATED 170 GEEDEEMIES 180 IENLEDLKGH 190 SVREWVSMAG 200 PRLEIHHRFK 210 NFLRTHVDSH 220 GHNVFKERIS 230 DMCKENRESL 240 VVNYEDLAAR 250 EHVLAYFLPE 260 APAELLQIFD 270 EAALEVVLAM 280 YPKYDRITNH 290 IHVRISHLPL 300 VEELRSLRQL 310 HLNQLIRTSG 320 VVTSCTGVLP 330 QLSMVKYNCN 340 KCNFVLGPFC 350 QSQNQEVKPG 360 SCPECQSAGP 370 FEVNMEETIY 380 QNYQRIRIQE 390 SPGKVAAGRL 400 PRSKDAILLA 410 DLVDSCKPGD 420 EIELTGIYHN 430 NYDGSLNTAN 440 GFPVFATVIL 450 ANHVAKKDNK 460 VAVGELTDED 470 VKMITSLSKD 480 QQIGEKIFAS 490 IAPSIYGHED 500 IKRGLALALF 510 GGEPKNPGGK 520 HKVRGDINVL 530 LCGDPGTAKS 540 QFLKYIEKVS 550 SRAIFTTGQG 560 ASAVGLTAYV 570 QRHPVSREWT 580 LEAGALVLAD 590 RGVCLIDEFD 600 KMNDQDRTSI 610 HEAMEQQSIS 620 ISKAGIVTSL 630 QARCTVIAAA 640 NPIGGRYDPS 650 LTFSENVDLT 660 EPIISRFDIL 670 CVVRDTVDPV 680 QDEMLARFVV 690 GSHVRHHPSN 700 KEEEGLANGS 710 AAEPAMPNTY 720 GVEPLPQEVL 730 KKYIIYAKER 740 VHPKLNQMDQ 750 DKVAKMYSDL 760 RKESMATGSI 770 PITVRHIESM 780 IRMAEAHARI 790 HLRDYVIEDD 800 VNMAIRVMLE 810 SFIDTQKFSV 820 MRSMRKTFAR 830 YLSFRRDNNE 840 LLLFILKQLV 850 AEQVTYQRNR 860 FGAQQDTIEV 870 PEKDLVDKAR 880 QINIHNLSAF 890 YDSELFRMNK 900 FSHDLKRKMI LQQF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0000781 chromosome, telomeric region
Cellular Component GO:0071162 CMG complex
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0042555 MCM complex
Cellular Component GO:0005664 nuclear origin of replication recognition complex
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:0003677 DNA binding
Molecular Function GO:0003678 DNA helicase activity
Molecular Function GO:0003688 DNA replication origin binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0042393 histone binding
Molecular Function GO:0003697 single-stranded DNA binding
Molecular Function GO:0008270 zinc ion binding
Biological Process GO:0006915 apoptotic process
Biological Process GO:0090102 cochlea development
Biological Process GO:0006260 DNA replication
Biological Process GO:0006270 DNA replication initiation
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

Reference

[1] 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.

[2] 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.