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Overview

Uniprot IDP35249
Protein NameReplication factor C subunit 4
Gene NameRFC4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
13 KGTSISTKPPLTKDR
18 STKPPLTKDRGVAAS
6 **MQAFLKGTSISTK

Function

Subunit of the replication factor C (RFC) complex which acts during elongation of primed DNA templates by DNA polymerases delta and epsilon, and is necessary for ATP-dependent loading of proliferating cell nuclear antigen (PCNA) onto primed DNA. The RFC4 subunit probably functions as a scaffold on which the other complex components can assemble

Protein Sequence

10 MQAFLKGTSI 20 STKPPLTKDR 30 GVAASAGSSG 40 ENKKAKPVPW 50 VEKYRPKCVD 60 EVAFQEEVVA 70 VLKKSLEGAD 80 LPNLLFYGPP 90 GTGKTSTILA 100 AARELFGPEL 110 FRLRVLELNA 120 SDERGIQVVR 130 EKVKNFAQLT 140 VSGSRSDGKP 150 CPPFKIVILD 160 EADSMTSAAQ 170 AALRRTMEKE 180 SKTTRFCLIC 190 NYVSRIIEPL 200 TSRCSKFRFK 210 PLSDKIQQQR 220 LLDIAKKENV 230 KISDEGIAYL 240 VKVSEGDLRK 250 AITFLQSATR 260 LTGGKEITEK 270 VITDIAGVIP 280 AEKIDGVFAA 290 CQSGSFDKLE 300 AVVKDLIDEG 310 HAATQLVNQL 320 HDVVVENNLS 330 DKQKSIITEK 340 LAEVDKCLAD 350 GADEHLQLIS 360 LCATVMQQLS QNC

Gene Ontology

Classification GO ID Description
Cellular Component GO:0031390 Ctf18 RFC-like complex
Cellular Component GO:0005663 DNA replication factor C complex
Cellular Component GO:0031391 Elg1 RFC-like 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:0019899 enzyme binding
Biological Process GO:0006281 DNA repair
Biological Process GO:0006260 DNA replication
Biological Process GO:0000076 DNA replication checkpoint signaling
Biological Process GO:0006271 DNA strand elongation involved in DNA replication
Biological Process GO:0006261 DNA-templated DNA replication
Biological Process GO:1900264 positive regulation of DNA-directed DNA polymerase activity

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] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[4] 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.

[5] 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.

[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.