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Overview

Uniprot IDP31350
Protein NameRibonucleoside-diphosphate reductase subunit M2
Gene NameRRM2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
206 TMPCVKKKADWALRW
46 GTRVLASKTARRIFQ

Function

Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling

Protein Sequence

10 MLSLRVPLAP 20 ITDPQQLQLS 30 PLKGLSLVDK 40 ENTPPALSGT 50 RVLASKTARR 60 IFQEPTEPKT 70 KAAAPGVEDE 80 PLLRENPRRF 90 VIFPIEYHDI 100 WQMYKKAEAS 110 FWTAEEVDLS 120 KDIQHWESLK 130 PEERYFISHV 140 LAFFAASDGI 150 VNENLVERFS 160 QEVQITEARC 170 FYGFQIAMEN 180 IHSEMYSLLI 190 DTYIKDPKER 200 EFLFNAIETM 210 PCVKKKADWA 220 LRWIGDKEAT 230 YGERVVAFAA 240 VEGIFFSGSF 250 ASIFWLKKRG 260 LMPGLTFSNE 270 LISRDEGLHC 280 DFACLMFKHL 290 VHKPSEERVR 300 EIIINAVRIE 310 QEFLTEALPV 320 KLIGMNCTLM 330 KQYIEFVADR 340 LMLELGFSKV 350 FRVENPFDFM 360 ENISLEGKTN 370 FFEKRVGEYQ 380 RMGVMSSPTE NSFTLDADF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005971 ribonucleoside-diphosphate reductase complex
Molecular Function GO:0008199 ferric iron binding
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0036175 ribonucleoside-diphosphate reductase activity, glutaredoxin disulfide as acceptor
Molecular Function GO:0004748 ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor
Biological Process GO:0009265 2'-deoxyribonucleotide biosynthetic process
Biological Process GO:0009263 deoxyribonucleotide biosynthetic process
Biological Process GO:0006281 DNA repair
Biological Process GO:1900087 positive regulation of G1/S transition of mitotic cell cycle
Biological Process GO:0051290 protein heterotetramerization
Biological Process GO:0009185 ribonucleoside diphosphate metabolic process

Reference

[1] 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.

[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.