Q96BH1A8K0D6Q53HQ5Q9H874RNF25_HUMANE3 ubiquitin-protein ligase RNF252.3.2.27RING finger protein 25RING finger protein AO7RNF25Homo sapiensHumanEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomoComplete sequencing and characterization of 21,243 full-length human cDNAs.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]Generation and annotation of the DNA sequences of human chromosomes 2 and 4.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]RING finger protein AO7 supports NF-kappaB-mediated transcription by interacting with the transactivation domain of the p65 subunit.FUNCTIONSUBCELLULAR LOCATIONINTERACTION WITH RELAMUTAGENESIS OF CYS-159 AND CYS-161Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Initial characterization of the human central proteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Toward a comprehensive characterization of a human cancer cell phosphoproteome.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]An extended conformation of the RWD domain of human RING finger protein 25.STRUCTURE BY NMR OF 10-134An E3 ligase network engages GCN1 to promote the degradation of translation factors on stalled ribosomes.FUNCTIONCATALYTIC ACTIVITYPATHWAYDrug-induced eRF1 degradation promotes readthrough and reveals a new branch of ribosome quality control.FUNCTIONCATALYTIC ACTIVITYPATHWAYMUTAGENESIS OF 135-CYS--CYS-138RNF14-dependent atypical ubiquitylation promotes translation-coupled resolution of RNA-protein crosslinks.FUNCTIONInsights into ubiquitination from the unique clamp-like binding of the RING E3 AO7 to the E2 UbcH5B.X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 126-258 IN COMPLEX WITH ZN(2+) AND UBE2D2CATALYTIC ACTIVITYPATHWAYINTERACTION WITH UBE2D2AUTOUBIQUITINATIONMUTAGENESIS OF ILE-137; TYR-165; PRO-199; TYR-242 AND GLN-245E3 ubiquitin-protein ligase that plays a key role in the RNF14-RNF25 translation quality control pathway, a pathway that takes place when a ribosome has stalled during translation, and which promotes ubiquitination and degradation of translation factors on stalled ribosomes (PubMed:36638793, PubMed:37651229, PubMed:37951216). Catalyzes ubiquitination of RPS27A in response to ribosome collisions, promoting activation of RNF14 (PubMed:36638793). RNF25 catalyzes ubiquitination of other ribosomal proteins on stalled ribosomes, such as RPL0, RPL1, RPL12, RPS13 and RPS17 (PubMed:36638793). Also involved in ubiquitination and degradation of stalled ETF1/eRF1 (PubMed:36638793, PubMed:37651229). Independently of its function in the response to stalled ribosomes, mediates ubiquitination and subsequent proteasomal degradation of NKD2 (By similarity). May also stimulate transcription mediated by NF-kappa-B via its interaction with RELA/p65 (PubMed:12748188).S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.Protein modification; protein ubiquitination.Interacts with UBE2D2, and may also interact with UBE2E1 and UBE2E3 (PubMed:26475854). Interacts with RELA/p65 (PubMed:12748188).Q96BH1Q4G0X4false3Q96BH1Q6FHY5false3Q96BH1Q969F2false2Q96BH1O60260-5false3Q96BH1P51668false5Q96BH1P62837false3Q96BH1P61077false5Q96BH1Q9Y2X8false3Q96BH1P51965false3Q96BH1Q969T4false3CytoplasmUbiquitinated; autoubiquitinated.Belongs to the RNF25 family.3D-structureCytoplasmMetal-bindingPhosphoproteinReference proteomeTransferaseUbl conjugationUbl conjugation pathwayZincZinc-fingerZn(2+)Zn(2+)Zn(2+)Zn(2+)Zn(2+)Zn(2+)Zn(2+)Zn(2+)CVICSVISIACSCSYAPAYAQAHRPSMAASASAAAGEEDWVLPSEVEVLESIYLDELQVIKGNGRTSPWEIYITLHPATAEDQDSQYVCFTLVLQVPAEYPHEVPQISIRNPRGLSDEQIHTILQVLGHVAKAGLGTAMLYELIEKGKEILTDNNIPHGQCVICLYGFQEKEAFTKTPCYHYFHCHCLARYIQHMEQELKAQGQEQEQERQHATTKQKAVGVQCPVCREPLVYDLASLKAAPEPQQPMELYQPSAESLRQQEERKRLYQRQQERGGIIDLEAERNRYFISLQQPPAPAEPESAVDVSKGSQPPSTLAAELSTSPAVQSTLPPPLPVATQHICEKIPGTRSNQQRLGETQKAMLDPPKPSRGPWRQPERRHPKGGECHAPKGTRDTQELPPPEGPLKEPMDLKPEPHSQGVEGPPQEKGPGSWQGPPPRRTRDCVRWERSKGRTPGSSYPRLPRGQGAYRPGTRRESLGLESKDGS
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