RNF38_MOUSE
ID RNF38_MOUSE Reviewed; 464 AA.
AC Q8BI21; Q6P5B1;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=E3 ubiquitin-protein ligase RNF38 {ECO:0000305};
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 38;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF38 {ECO:0000305};
GN Name=Rnf38 {ECO:0000312|MGI:MGI:1920719};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-464.
RC STRAIN=C57BL/6J; TISSUE=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).
CC -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase able to ubiquitinate
CC p53/TP53 which promotes its relocalization to discrete foci associated
CC with PML nuclear bodies. Exhibits preference for UBE2D2 as a E2 enzyme.
CC {ECO:0000250}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26547.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. Chimeric cDNA originating from chromosomes 1 and 4.; Evidence={ECO:0000305};
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DR EMBL; AL732563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL805952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060730; AAH60730.1; -; mRNA.
DR EMBL; BC062976; AAH62976.1; -; mRNA.
DR EMBL; AK029650; BAC26547.1; ALT_SEQ; mRNA.
DR CCDS; CCDS18122.1; -.
DR RefSeq; NP_780410.2; NM_175201.5.
DR AlphaFoldDB; Q8BI21; -.
DR SMR; Q8BI21; -.
DR STRING; 10090.ENSMUSP00000095702; -.
DR iPTMnet; Q8BI21; -.
DR PhosphoSitePlus; Q8BI21; -.
DR PaxDb; Q8BI21; -.
DR PRIDE; Q8BI21; -.
DR Antibodypedia; 2887; 89 antibodies from 21 providers.
DR DNASU; 73469; -.
DR Ensembl; ENSMUST00000098098; ENSMUSP00000095702; ENSMUSG00000035696.
DR GeneID; 73469; -.
DR KEGG; mmu:73469; -.
DR UCSC; uc008srs.2; mouse.
DR CTD; 152006; -.
DR MGI; MGI:1920719; Rnf38.
DR VEuPathDB; HostDB:ENSMUSG00000035696; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000156228; -.
DR InParanoid; Q8BI21; -.
DR OMA; PPMIQAC; -.
DR OrthoDB; 1570520at2759; -.
DR PhylomeDB; Q8BI21; -.
DR TreeFam; TF325756; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 73469; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Rnf38; mouse.
DR PRO; PR:Q8BI21; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BI21; protein.
DR Bgee; ENSMUSG00000035696; Expressed in animal zygote and 267 other tissues.
DR ExpressionAtlas; Q8BI21; baseline and differential.
DR Genevisible; Q8BI21; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0036126; C:sperm flagellum; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..464
FT /note="E3 ubiquitin-protein ligase RNF38"
FT /id="PRO_0000056079"
FT ZN_FING 412..453
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 6..20
FT /note="Bipartite nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 64..79
FT /note="Bipartite nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT COMPBIAS 36..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 52168 MW; A67EE0DCAC8101A2 CRC64;
MRESEDSPSP KRQRLSHSVF DYTSASPAPS PPMRPWEMTS NRQPPSVRPN QHHFSGERCN
TPARNRRSPP VRRQRGRRER LSRHNSISQD ENYHHLPYAQ QQAIEEPRAF HPPNVSPRLL
HPAAHPPQQN AVMVDIHDQL HQGTVPVSYT VTTVAPHGLP LCTGQHIPAC STQQVPGCSV
VFSGQHLPVC SVPPPMLQAC SVQHLPVPYA AFPPLISSDP FLIHPPHLSP HHPPHLPPPG
QFVPFQTQQS RSPLQRIENE VELLGEHLQV GSFTYPPSAH PPTLPPSAPL QFLTHDPLHQ
EVSFGVPYPP FMPRRLTGRS RYRSQQPMPP PPYHPSLLPY VLSMLPVPPA VGPTFSFELD
VEDGEVENYE ALLNLAERLG EAKPRGLTKA DIEQLPSYRF NPSNHQSEQT LCVVCMCDFE
SRQLLRVLPC NHEFHAKCVD KWLKGNRTCP ICRADASEVH RDSE
