RNF34_MOUSE
ID RNF34_MOUSE Reviewed; 376 AA.
AC Q99KR6; Q3UV45;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=E3 ubiquitin-protein ligase RNF34 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q969K3};
DE AltName: Full=Phafin-1 {ECO:0000312|EMBL:AAL30770.1};
DE AltName: Full=RING finger protein 34 {ECO:0000312|MGI:MGI:2153340};
DE AltName: Full=RING-type E3 ubiquitin transferase RNF34 {ECO:0000305};
GN Name=Rnf34 {ECO:0000312|MGI:MGI:2153340};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Hong W.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Bone, Bone marrow, Corpora quadrigemina, Head, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-260, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND INDUCTION.
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).
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. May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and
CC its subsequent proteasomal degradation thereby indirectly regulating
CC the tumor necrosis factor-mediated signaling pathway. Negatively
CC regulates p53/TP53 through its direct ubiquitination and targeting to
CC proteasomal degradation. Indirectly, may also negatively regulate
CC p53/TP53 through ubiquitination and degradation of SFN. Mediates
CC PPARGC1A proteasomal degradation probably through ubiquitination
CC thereby indirectly regulating the metabolism of brown fat cells
CC (PubMed:22064484). Possibly involved in innate immunity, through 'Lys-
CC 48'-linked polyubiquitination of NOD1 and its subsequent proteasomal
CC degradation. {ECO:0000250|UniProtKB:Q969K3,
CC ECO:0000269|PubMed:22064484}.
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:0000250|UniProtKB:Q969K3};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q969K3}.
CC -!- SUBUNIT: Interacts with CASP8 and CASP10. Interacts with p53/TP53;
CC involved in p53/TP53 ubiquitination. Interacts (via RING-type zinc
CC finger) with MDM2; the interaction stabilizes MDM2. Interacts (via
CC RING-type zinc finger) with PPARGC1A. Interacts with NOD1.
CC {ECO:0000250|UniProtKB:Q969K3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q969K3};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q969K3}.
CC Endomembrane system {ECO:0000250|UniProtKB:Q6AYH3}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q6AYH3}. Nucleus
CC {ECO:0000250|UniProtKB:Q969K3}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q969K3}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q969K3}.
CC -!- INDUCTION: Down-regulated in response to cold exposure.
CC {ECO:0000269|PubMed:22064484}.
CC -!- DOMAIN: The RING-type zinc finger is required for the ubiquitination of
CC target proteins. {ECO:0000250|UniProtKB:Q969K3}.
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:0000250|UniProtKB:Q969K3}.
CC -!- PTM: Autoubiquitinated (in vitro). {ECO:0000250|UniProtKB:Q6AYH3}.
CC -!- PTM: Proteolytically cleaved by caspases upon induction of apoptosis by
CC TNF. {ECO:0000250|UniProtKB:Q969K3}.
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DR EMBL; AF434815; AAL30770.1; -; mRNA.
DR EMBL; AK045696; BAC32461.1; -; mRNA.
DR EMBL; AK046274; BAC32666.1; -; mRNA.
DR EMBL; AK046381; BAC32697.1; -; mRNA.
DR EMBL; AK077221; BAC36693.1; -; mRNA.
DR EMBL; AK132330; BAE21109.1; -; mRNA.
DR EMBL; AK137606; BAE23428.1; -; mRNA.
DR EMBL; AK150976; BAE30005.1; -; mRNA.
DR EMBL; AK159753; BAE35344.1; -; mRNA.
DR EMBL; BC004042; AAH04042.1; -; mRNA.
DR CCDS; CCDS19656.1; -.
DR RefSeq; NP_085041.1; NM_030564.1.
DR AlphaFoldDB; Q99KR6; -.
DR SMR; Q99KR6; -.
DR STRING; 10090.ENSMUSP00000031434; -.
DR iPTMnet; Q99KR6; -.
DR PhosphoSitePlus; Q99KR6; -.
DR EPD; Q99KR6; -.
DR jPOST; Q99KR6; -.
DR MaxQB; Q99KR6; -.
DR PaxDb; Q99KR6; -.
DR PeptideAtlas; Q99KR6; -.
DR PRIDE; Q99KR6; -.
DR ProteomicsDB; 300500; -.
DR Antibodypedia; 31576; 305 antibodies from 33 providers.
DR DNASU; 80751; -.
DR Ensembl; ENSMUST00000031434; ENSMUSP00000031434; ENSMUSG00000029474.
DR GeneID; 80751; -.
DR KEGG; mmu:80751; -.
DR UCSC; uc008zmn.1; mouse.
DR CTD; 80196; -.
DR MGI; MGI:2153340; Rnf34.
DR VEuPathDB; HostDB:ENSMUSG00000029474; -.
DR eggNOG; KOG4275; Eukaryota.
DR GeneTree; ENSGT00390000012719; -.
DR HOGENOM; CLU_041431_1_0_1; -.
DR InParanoid; Q99KR6; -.
DR OMA; NEANHRT; -.
DR OrthoDB; 1361306at2759; -.
DR PhylomeDB; Q99KR6; -.
DR TreeFam; TF325195; -.
DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 80751; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Rnf34; mouse.
DR PRO; PR:Q99KR6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q99KR6; protein.
DR Bgee; ENSMUSG00000029474; Expressed in animal zygote and 255 other tissues.
DR ExpressionAtlas; Q99KR6; baseline and differential.
DR Genevisible; Q99KR6; MM.
DR GO; GO:0005737; C:cytoplasm; ISS: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; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0070417; P:cellular response to cold; IMP:UniProtKB.
DR GO; GO:2001271; P:negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; ISS:UniProtKB.
DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB.
DR GO; GO:1901797; P:negative regulation of signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0035872; P:nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:2000374; P:regulation of oxygen metabolic process; IMP:UniProtKB.
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 Apoptosis; Cell membrane; Cytoplasm; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..376
FT /note="E3 ubiquitin-protein ligase RNF34"
FT /id="PRO_0000056073"
FT DOMAIN 115..134
FT /note="SAP 1"
FT DOMAIN 268..282
FT /note="SAP 2"
FT ZN_FING 56..107
FT /note="FYVE-type"
FT ZN_FING 329..364
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 216..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..245
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 236..237
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:Q969K3"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969K3"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 376 AA; 42030 MW; FE4AB65DAE9381BC CRC64;
MKAGATSMWA SCCGLLNEVM GTGAVRGQQA GFPGSTGPFR FTPSSDFPTY PPAATEGPNI
VCKACGLSFS VFRKKHVCCD CKKDFCSLCS VSQENLRRCS TCHLLQETAF QRPQLMRLKV
KDLRQYLLLR NIPTDTCREK EDLVDLVLCH RGLGSGDDLD SSSLNSSRSQ TSSFFTQSLF
SNYTPPSATV SSFQGELMDR DGAFRSEVLA QVQSEIASAN TDDDDDDDDD DDDDEDDDDE
QEEEEQNPGL SKKKARASLS DLSSLEEVEG MSVRQLKEIL ARNFVNYSGC CEKWELVEKV
NRLYKENEEN QKSYGERMQL QDEEDDSLCR ICMDAVIDCV LLECGHMVTC TKCGKRMSEC
PICRQYVVRA VHVFKS
