RNF34_HUMAN
ID RNF34_HUMAN Reviewed; 372 AA.
AC Q969K3; B7Z933; Q8NG47; Q9H6W8;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=E3 ubiquitin-protein ligase RNF34 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:25012219, ECO:0000269|Ref.13};
DE AltName: Full=Caspase regulator CARP1 {ECO:0000305};
DE AltName: Full=Caspases-8 and -10-associated RING finger protein 1 {ECO:0000303|PubMed:15069192};
DE Short=CARP-1 {ECO:0000303|PubMed:15069192};
DE AltName: Full=FYVE-RING finger protein Momo {ECO:0000250|UniProtKB:Q6AYH3};
DE AltName: Full=Human RING finger homologous to inhibitor of apoptosis protein {ECO:0000303|PubMed:12118383};
DE Short=hRFI {ECO:0000303|PubMed:12118383};
DE AltName: Full=RING finger protein 34 {ECO:0000312|HGNC:HGNC:17297};
DE AltName: Full=RING finger protein RIFF {ECO:0000303|Ref.2};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF34 {ECO:0000305};
GN Name=RNF34 {ECO:0000312|HGNC:HGNC:17297};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP CLEAVAGE BY CASPASE-3, AND TISSUE SPECIFICITY.
RX PubMed=12118383; DOI=10.1038/sj.onc.1205627;
RA Sasaki S., Nakamura T., Arakawa H., Mori M., Watanabe T., Nagawa H.,
RA Croce C.M.;
RT "Isolation and characterization of a novel gene, hRFI, preferentially
RT expressed in esophageal cancer.";
RL Oncogene 21:5024-5030(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Olsson P.-A., Lindholm D.;
RT "Cloning of RIFF, a novel RING finger FYVE finger protein expressed in
RT human fetal brain.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Kanbe D., Araki K., Nawa H.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, INTERACTION WITH CASP8 AND CASP10, MUTAGENESIS OF HIS-342,
RP PROTEOLYTIC DEGRADATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15069192; DOI=10.1073/pnas.0307459101;
RA McDonald E.R. III, El-Deiry W.S.;
RT "Suppression of caspase-8- and -10-associated RING proteins results in
RT sensitization to death ligands and inhibition of tumor cell growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6170-6175(2004).
RN [9]
RP FUNCTION.
RX PubMed=15897238; DOI=10.1158/1535-7163.mct-05-0020;
RA Konishi T., Sasaki S., Watanabe T., Kitayama J., Nagawa H.;
RT "Overexpression of hRFI (human RING finger homologous to inhibitor of
RT apoptosis protein type) inhibits death receptor-mediated apoptosis in
RT colorectal cancer cells.";
RL Mol. Cancer Ther. 4:743-750(2005).
RN [10]
RP FUNCTION, AND INTERACTION WITH P53/TP53.
RX PubMed=17121812; DOI=10.1074/jbc.m610793200;
RA Yang W., Rozan L.M., McDonald E.R. III, Navaraj A., Liu J.J., Matthew E.M.,
RA Wang W., Dicker D.T., El-Deiry W.S.;
RT "CARPs are ubiquitin ligases that promote MDM2-independent p53 and phospho-
RT p53ser20 degradation.";
RL J. Biol. Chem. 282:3273-3281(2007).
RN [11]
RP FUNCTION, AND INTERACTION WITH MDM2 AND P53/TP53.
RX PubMed=18382127; DOI=10.4161/cc.7.5.5701;
RA Yang W., Dicker D.T., Chen J., El-Deiry W.S.;
RT "CARPs enhance p53 turnover by degrading 14-3-3sigma and stabilizing
RT MDM2.";
RL Cell Cycle 7:670-682(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP FUNCTION, INTERACTION WITH RIPK1, AND PATHWAY.
RX DOI=10.1016/j.cub.2008.11.041;
RA Liao W., Fujita K., Xiao Q., Tchikov V., Yang W., Gunsor M., Garfield S.,
RA Goldsmith P., El-Deiry W.S., Schuetze S., Srinivasula S.M.;
RT "Response: CARP1 regulates induction of NF-kappaB by TNFalpha.";
RL Curr. Biol. 19:R17-R19(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP FUNCTION, INTERACTION WITH PPARGC1A, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF CYS-328.
RX PubMed=22064484; DOI=10.1128/mcb.05674-11;
RA Wei P., Pan D., Mao C., Wang Y.X.;
RT "RNF34 is a cold-regulated E3 ubiquitin ligase for PGC-1alpha and modulates
RT brown fat cell metabolism.";
RL Mol. Cell. Biol. 32:266-275(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-254, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP FUNCTION, AND INTERACTION WITH NOD1.
RX PubMed=25012219; DOI=10.1159/000362972;
RA Zhang R., Zhao J., Song Y., Wang X., Wang L., Xu J., Song C., Liu F.;
RT "The E3 ligase RNF34 is a novel negative regulator of the NOD1 pathway.";
RL Cell. Physiol. Biochem. 33:1954-1962(2014).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that regulates several biological
CC processes through the ubiquitin-mediated proteasomal degradation of
CC various target proteins. Ubiquitinates the caspases CASP8 and CASP10,
CC promoting their proteasomal degradation, to negatively regulate cell
CC death downstream of death domain receptors in the extrinsic pathway of
CC apoptosis (PubMed:15069192). May mediate 'Lys-48'-linked
CC polyubiquitination of RIPK1 and its subsequent proteasomal degradation
CC thereby indirectly regulating the tumor necrosis factor-mediated
CC signaling pathway (Ref.13). Negatively regulates p53/TP53 through its
CC direct ubiquitination and targeting to proteasomal degradation
CC (PubMed:17121812). Indirectly, may also negatively regulate p53/TP53
CC through ubiquitination and degradation of SFN (PubMed:18382127).
CC Mediates PPARGC1A proteasomal degradation probably through
CC ubiquitination thereby indirectly regulating the metabolism of brown
CC fat cells (PubMed:22064484). Possibly involved in innate immunity,
CC through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent
CC proteasomal degradation (PubMed:25012219).
CC {ECO:0000269|PubMed:12118383, ECO:0000269|PubMed:15069192,
CC ECO:0000269|PubMed:15897238, ECO:0000269|PubMed:17121812,
CC ECO:0000269|PubMed:22064484, ECO:0000269|PubMed:25012219,
CC ECO:0000269|Ref.13, ECO:0000303|PubMed:18382127}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:25012219,
CC ECO:0000269|Ref.13};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|Ref.13}.
CC -!- SUBUNIT: Interacts with CASP8 and CASP10. Interacts (via RING-type zinc
CC finger) with PPARGC1A. Interacts with NOD1. Interacts with p53/TP53;
CC involved in p53/TP53 ubiquitination. Interacts (via RING-type zinc
CC finger) with MDM2; the interaction stabilizes MDM2.
CC {ECO:0000269|PubMed:12118383, ECO:0000269|PubMed:15069192,
CC ECO:0000269|PubMed:17121812, ECO:0000269|PubMed:18382127,
CC ECO:0000269|PubMed:22064484, ECO:0000269|PubMed:25012219, ECO:0000305}.
CC -!- INTERACTION:
CC Q969K3; Q92624: APPBP2; NbExp=3; IntAct=EBI-2340642, EBI-743771;
CC Q969K3; Q14790: CASP8; NbExp=3; IntAct=EBI-2340642, EBI-78060;
CC Q969K3; P02489: CRYAA; NbExp=3; IntAct=EBI-2340642, EBI-6875961;
CC Q969K3; G5E9A7: DMWD; NbExp=3; IntAct=EBI-2340642, EBI-10976677;
CC Q969K3; Q01658: DR1; NbExp=3; IntAct=EBI-2340642, EBI-750300;
CC Q969K3; O14908-2: GIPC1; NbExp=3; IntAct=EBI-2340642, EBI-25913156;
CC Q969K3; Q53GS7: GLE1; NbExp=3; IntAct=EBI-2340642, EBI-1955541;
CC Q969K3; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-2340642, EBI-1054873;
CC Q969K3; Q92876: KLK6; NbExp=3; IntAct=EBI-2340642, EBI-2432309;
CC Q969K3; Q9BZ23-2: PANK2; NbExp=3; IntAct=EBI-2340642, EBI-25929070;
CC Q969K3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2340642, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15069192};
CC Peripheral membrane protein {ECO:0000305}. Endomembrane system
CC {ECO:0000250|UniProtKB:Q6AYH3}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q6AYH3}. Nucleus {ECO:0000269|PubMed:22064484}.
CC Nucleus speckle {ECO:0000269|PubMed:12118383}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:15069192}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q969K3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969K3-2; Sequence=VSP_038341;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, liver,
CC skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis,
CC ovary, colon and leukocytes. {ECO:0000269|PubMed:12118383,
CC ECO:0000269|PubMed:15069192}.
CC -!- DOMAIN: The RING-type zinc finger is required for the ubiquitination of
CC target proteins. {ECO:0000303|PubMed:25012219}.
CC -!- DOMAIN: The FYVE-type zinc finger domain is required for localization
CC and may confer affinity for cellular compartments enriched in
CC phosphatidylinositol 5-phosphate and phosphatidylinositol 3-phosphate
CC phospholipids. {ECO:0000303|PubMed:15069192}.
CC -!- PTM: Autoubiquitinated (in vitro). {ECO:0000250|UniProtKB:Q6AYH3}.
CC -!- PTM: Proteolytically cleaved by caspases upon induction of apoptosis by
CC TNF. {ECO:0000269|PubMed:12118383}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH14169.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AB084914; BAC11802.1; -; mRNA.
DR EMBL; AF306709; AAK51328.1; -; mRNA.
DR EMBL; AY098934; AAM29180.1; -; mRNA.
DR EMBL; AK304366; BAH14169.1; ALT_SEQ; mRNA.
DR EMBL; AK025439; BAB15132.1; -; mRNA.
DR EMBL; BT007283; AAP35947.1; -; mRNA.
DR EMBL; CR457342; CAG33623.1; -; mRNA.
DR EMBL; BC007826; AAH07826.1; -; mRNA.
DR CCDS; CCDS31915.1; -. [Q969K3-1]
DR CCDS; CCDS9221.1; -. [Q969K3-2]
DR RefSeq; NP_001243787.1; NM_001256858.1.
DR RefSeq; NP_079402.2; NM_025126.3. [Q969K3-1]
DR RefSeq; NP_919247.1; NM_194271.2. [Q969K3-2]
DR AlphaFoldDB; Q969K3; -.
DR SMR; Q969K3; -.
DR BioGRID; 123169; 45.
DR IntAct; Q969K3; 33.
DR MINT; Q969K3; -.
DR STRING; 9606.ENSP00000376258; -.
DR iPTMnet; Q969K3; -.
DR PhosphoSitePlus; Q969K3; -.
DR BioMuta; RNF34; -.
DR DMDM; 74760679; -.
DR EPD; Q969K3; -.
DR jPOST; Q969K3; -.
DR MassIVE; Q969K3; -.
DR MaxQB; Q969K3; -.
DR PaxDb; Q969K3; -.
DR PeptideAtlas; Q969K3; -.
DR PRIDE; Q969K3; -.
DR ProteomicsDB; 75779; -. [Q969K3-1]
DR ProteomicsDB; 75780; -. [Q969K3-2]
DR Antibodypedia; 31576; 305 antibodies from 33 providers.
DR DNASU; 80196; -.
DR Ensembl; ENST00000361234.10; ENSP00000355137.5; ENSG00000170633.17. [Q969K3-1]
DR Ensembl; ENST00000392465.7; ENSP00000376258.3; ENSG00000170633.17. [Q969K3-2]
DR GeneID; 80196; -.
DR KEGG; hsa:80196; -.
DR MANE-Select; ENST00000361234.10; ENSP00000355137.5; NM_025126.4; NP_079402.2.
DR UCSC; uc001uak.3; human. [Q969K3-1]
DR CTD; 80196; -.
DR DisGeNET; 80196; -.
DR GeneCards; RNF34; -.
DR HGNC; HGNC:17297; RNF34.
DR HPA; ENSG00000170633; Low tissue specificity.
DR MIM; 608299; gene.
DR neXtProt; NX_Q969K3; -.
DR OpenTargets; ENSG00000170633; -.
DR PharmGKB; PA34436; -.
DR VEuPathDB; HostDB:ENSG00000170633; -.
DR eggNOG; KOG4275; Eukaryota.
DR GeneTree; ENSGT00390000012719; -.
DR HOGENOM; CLU_041431_1_0_1; -.
DR InParanoid; Q969K3; -.
DR OMA; CRICCDA; -.
DR OrthoDB; 666874at2759; -.
DR PhylomeDB; Q969K3; -.
DR TreeFam; TF325195; -.
DR PathwayCommons; Q969K3; -.
DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q969K3; -.
DR SIGNOR; Q969K3; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 80196; 17 hits in 1121 CRISPR screens.
DR ChiTaRS; RNF34; human.
DR GeneWiki; RNF34; -.
DR GenomeRNAi; 80196; -.
DR Pharos; Q969K3; Tbio.
DR PRO; PR:Q969K3; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q969K3; protein.
DR Bgee; ENSG00000170633; Expressed in secondary oocyte and 189 other tissues.
DR ExpressionAtlas; Q969K3; baseline and differential.
DR Genevisible; Q969K3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0070417; P:cellular response to cold; IEA:Ensembl.
DR GO; GO:2001271; P:negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:UniProtKB.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:UniProtKB.
DR GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:2000374; P:regulation of oxygen metabolic process; ISS:UniProtKB.
DR GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cell membrane; Cytoplasm; Membrane;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..372
FT /note="E3 ubiquitin-protein ligase RNF34"
FT /id="PRO_0000056072"
FT DOMAIN 115..134
FT /note="SAP 1"
FT DOMAIN 264..278
FT /note="SAP 2"
FT ZN_FING 56..107
FT /note="FYVE-type"
FT ZN_FING 325..360
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 194..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..240
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 232..233
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000269|PubMed:12118383"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99KR6"
FT VAR_SEQ 1
FT /note="M -> MR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12118383,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_038341"
FT MUTAGEN 328
FT /note="C->A: Loss of E3 ubiquitin protein ligase activity."
FT /evidence="ECO:0000303|PubMed:22064484"
FT MUTAGEN 342
FT /note="H->A: Loss of E3 ubiquitin protein ligase activity."
FT /evidence="ECO:0000269|PubMed:15069192"
FT CONFLICT 183
FT /note="Y -> C (in Ref. 4; BAB15132)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="N -> D (in Ref. 4; BAB15132)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="I -> V (in Ref. 4; BAB15132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 372 AA; 41641 MW; C044B83BD8591FFA CRC64;
MKAGATSMWA SCCGLLNEVM GTGAVRGQQS AFAGATGPFR FTPNPEFSTY PPAATEGPNI
VCKACGLSFS VFRKKHVCCD CKKDFCSVCS VLQENLRRCS TCHLLQETAF QRPQLMRLKV
KDLRQYLILR NIPIDTCREK EDLVDLVLCH HGLGSEDDMD TSSLNSSRSQ TSSFFTRSFF
SNYTAPSATM SSFQGELMDG DQTSRSGVPA QVQSEITSAN TEDDDDDDDE DDDDEEENAE
DRNPGLSKER VRASLSDLSS LDDVEGMSVR QLKEILARNF VNYSGCCEKW ELVEKVNRLY
KENEENQKSY GERLQLQDEE DDSLCRICMD AVIDCVLLEC GHMVTCTKCG KRMSECPICR
QYVVRAVHVF KS
