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Overview

Uniprot ID	Q9Y508
Protein Name	E3 ubiquitin-protein ligase RNF114
Gene Name	RNF114
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
126	EGVKATIKDASLQPR

Function

E3 ubiquitin-protein ligase that promotes the ubiquitination of various substrates (PubMed:23645206, PubMed:25165885). In turn, participates in the regulation of many biological processes including cell cycle, apoptosis, osteoclastogenesis as well as innate or adaptive immunity (PubMed:25165885, PubMed:28708287). Acts as a negative regulator of NF-kappa-B-dependent transcription by promoting the ubiquitination and stabilization of the NF-kappa-B inhibitor TNFAIP3 (PubMed:25165885). May promote the ubiquitination of TRAF6 as well (PubMed:28708287). Also acts as a negative regulator of T-cell activation (PubMed:25165885). Inhibits cellular dsRNA responses and interferon production by targeting MAVS component for proteasomal degradation (PubMed:25165885). Ubiquitinates the CDK inhibitor CDKN1A leading to its degradationand probably also CDKN1B and CDKN1C (PubMed:23645206). This activity stimulates cell cycle G1-to-S phase transition and suppresses cellular senescence. May play a role in spermatogenesis

Protein Sequence

10 MAAQQRDCGG 20 AAQLAGPAAE 30 ADPLGRFTCP 40 VCLEVYEKPV 50 QVPCGHVFCS 60 ACLQECLKPK 70 KPVCGVCRSA 80 LAPGVRAVEL 90 ERQIESTETS 100 CHGCRKNFFL 110 SKIRSHVATC 120 SKYQNYIMEG 130 VKATIKDASL 140 QPRNVPNRYT 150 FPCPYCPEKN 160 FDQEGLVEHC 170 KLFHSTDTKS 180 VVCPICASMP 190 WGDPNYRSAN 200 FREHIQRRHR 210 FSYDTFVDYD 220 VDEEDMMNQV LQRSIIDQ

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0005634	nucleus
Molecular Function	GO:0061630	ubiquitin protein ligase activity
Molecular Function	GO:0008270	zinc ion binding
Biological Process	GO:0030154	cell differentiation
Biological Process	GO:0000209	protein polyubiquitination
Biological Process	GO:0007283	spermatogenesis
Biological Process	GO:0006511	ubiquitin-dependent protein catabolic 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.