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Overview

Uniprot IDP35251
Protein NameReplication factor C subunit 1
Gene NameRFC1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
187 KMVASKRKELSQNTD
260 SVQANLSKAEKHKYP
294 QSKYESSKESQQHSK
301 KESQQHSKSSADKIG
306 HSKSSADKIGEVSSP
318 SSPKASSKLAIMKRK
339 EIEPVASKRKENAIK
346 KRKENAIKLKGETKT
5 ***MDIRKFFGVIPS
509 KLERTPQKNVQGKRK
568 EETSGDSKARNLADD
634 KHAAKFGKFSGKDDG
638 KFGKFSGKDDGSSFK
88 NAKKPPEKLPVSSKP

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 (PubMed:9488738). This subunit binds to the primer-template junction. Binds the PO-B transcription element as well as other GA rich DNA sequences. Can bind single- or double-stranded DNA

Protein Sequence

10 MDIRKFFGVI 20 PSGKKLVSET 30 VKKNEKTKSD 40 EETLKAKKGI 50 KEIKVNSSRK 60 EDDFKQKQPS 70 KKKRIIYDSD 80 SESEETLQVK 90 NAKKPPEKLP 100 VSSKPGKISR 110 QDPVTYISET 120 DEEDDFMCKK 130 AASKSKENGR 140 STNSHLGTSN 150 MKKNEENTKT 160 KNKPLSPIKL 170 TPTSVLDYFG 180 TGSVQRSNKK 190 MVASKRKELS 200 QNTDESGLND 210 EAIAKQLQLD 220 EDAELERQLH 230 EDEEFARTLA 240 MLDEEPKTKK 250 ARKDTEAGET 260 FSSVQANLSK 270 AEKHKYPHKV 280 KTAQVSDERK 290 SYSPRKQSKY 300 ESSKESQQHS 310 KSSADKIGEV 320 SSPKASSKLA 330 IMKRKEESSY 340 KEIEPVASKR 350 KENAIKLKGE 360 TKTPKKTKSS 370 PAKKESVSPE 380 DSEKKRTNYQ 390 AYRSYLNREG 400 PKALGSKEIP 410 KGAENCLEGL 420 IFVITGVLES 430 IERDEAKSLI 440 ERYGGKVTGN 450 VSKKTNYLVM 460 GRDSGQSKSD 470 KAAALGTKII 480 DEDGLLNLIR 490 TMPGKKSKYE 500 IAVETEMKKE 510 SKLERTPQKN 520 VQGKRKISPS 530 KKESESKKSR 540 PTSKRDSLAK 550 TIKKETDVFW 560 KSLDFKEQVA 570 EETSGDSKAR 580 NLADDSSENK 590 VENLLWVDKY 600 KPTSLKTIIG 610 QQGDQSCANK 620 LLRWLRNWQK 630 SSSEDKKHAA 640 KFGKFSGKDD 650 GSSFKAALLS 660 GPPGVGKTTT 670 ASLVCQELGY 680 SYVELNASDT 690 RSKSSLKAIV 700 AESLNNTSIK 710 GFYSNGAASS 720 VSTKHALIMD 730 EVDGMAGNED 740 RGGIQELIGL 750 IKHTKIPIIC 760 MCNDRNHPKI 770 RSLVHYCFDL 780 RFQRPRVEQI 790 KGAMMSIAFK 800 EGLKIPPPAM 810 NEIILGANQD 820 IRQVLHNLSM 830 WCARSKALTY 840 DQAKADSHRA 850 KKDIKMGPFD 860 VARKVFAAGE 870 ETAHMSLVDK 880 SDLFFHDYSI 890 APLFVQENYI 900 HVKPVAAGGD 910 MKKHLMLLSR 920 AADSICDGDL 930 VDSQIRSKQN 940 WSLLPAQAIY 950 ASVLPGELMR 960 GYMTQFPTFP 970 SWLGKHSSTG 980 KHDRIVQDLA 990 LHMSLRTYSS 1000 KRTVNMDYLS 1010 LLRDALVQPL 1020 TSQGVDGVQD 1030 VVALMDTYYL 1040 MKEDFENIME 1050 ISSWGGKPSP 1060 FSKLDPKVKA 1070 AFTRAYNKEA 1080 HLTPYSLQAI 1090 KASRHSTSPS 1100 LDSEYNEELN 1110 EDDSQSDEKD 1120 QDAIETDAMI 1130 KKKTKSSKPS 1140 KPEKDKEPRK GKGKSSKK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005663 DNA replication factor C complex
Cellular Component GO:0031391 Elg1 RFC-like complex
Cellular Component GO:0070062 extracellular exosome
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:0003689 DNA clamp loader activity
Molecular Function GO:0061860 DNA clamp unloader activity
Molecular Function GO:0140297 DNA-binding transcription factor binding
Molecular Function GO:0003690 double-stranded DNA binding
Molecular Function GO:0008047 enzyme activator activity
Molecular Function GO:0019904 protein domain specific binding
Molecular Function GO:0043565 sequence-specific DNA binding
Biological Process GO:0006281 DNA repair
Biological Process GO:0006261 DNA-templated DNA replication
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:0007004 telomere maintenance via telomerase

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] 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.

[5] 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.

[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.