TRI39_MOUSE
ID TRI39_MOUSE Reviewed; 488 AA.
AC Q9ESN2; Q8BPR5; Q8K0F7;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM39;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 23;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM39 {ECO:0000305};
DE AltName: Full=Testis-abundant finger protein;
DE AltName: Full=Tripartite motif-containing protein 39;
GN Name=Trim39; Synonyms=Rnf23, Tfp;
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] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11006080; DOI=10.1006/bbrc.2000.3380;
RA Orimo A., Yamagishi T., Tominaga N., Yamauchi Y., Hishinuma T., Okada K.,
RA Suzuki M., Sato M., Nogi Y., Suzuki H., Inoue S., Yoshimura K., Shimizu Y.,
RA Muramatsu M.;
RT "Molecular cloning of testis-abundant finger protein/ring finger protein 23
RT (RNF23), a novel RING-B box-coiled coil-B30.2 protein on the class I region
RT of the human MHC.";
RL Biochem. Biophys. Res. Commun. 276:45-51(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Eye;
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] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase (By similarity). May facilitate
CC apoptosis by inhibiting APC/C-Cdh1-mediated poly-ubiquitination and
CC subsequent proteasome-mediated degradation of the pro-apoptotic protein
CC MOAP1 (By similarity). Regulates the G1/S transition of the cell cycle
CC and DNA damage-induced G2 arrest by stabilizing CDKN1A/p21 (By
CC similarity). Positively regulates CDKN1A/p21 stability by competing
CC with DTL for CDKN1A/p21 binding, therefore disrupting DCX(DTL) E3
CC ubiquitin ligase complex-mediated CDKN1A/p21 ubiquitination and
CC degradation (By similarity). {ECO:0000250|UniProtKB:Q9HCM9}.
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 -!- SUBUNIT: Interacts with MOAP1 (By similarity). Interacts with CDKN1A
CC (By similarity). {ECO:0000250|UniProtKB:Q9HCM9}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9HCM9}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9HCM9}. Nucleus {ECO:0000250|UniProtKB:Q9HCM9}.
CC Note=Found predominantly in the cytosol. Partial shift from the cytosol
CC to the mitochondria when colocalized with MOAP1. Colocalizes with
CC CDKN1A in the nucleus. {ECO:0000250|UniProtKB:Q9HCM9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9ESN2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ESN2-2; Sequence=VSP_012065;
CC Name=3;
CC IsoId=Q9ESN2-3; Sequence=VSP_012063, VSP_012064;
CC -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q9HCM9}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AB046382; BAB16375.1; -; mRNA.
DR EMBL; AK053507; BAC35409.1; -; mRNA.
DR EMBL; BC031540; AAH31540.1; -; mRNA.
DR CCDS; CCDS37611.1; -. [Q9ESN2-1]
DR RefSeq; NP_077788.2; NM_024468.2.
DR RefSeq; XP_006525235.1; XM_006525172.3.
DR AlphaFoldDB; Q9ESN2; -.
DR BMRB; Q9ESN2; -.
DR SMR; Q9ESN2; -.
DR STRING; 10090.ENSMUSP00000109336; -.
DR PhosphoSitePlus; Q9ESN2; -.
DR MaxQB; Q9ESN2; -.
DR PaxDb; Q9ESN2; -.
DR PRIDE; Q9ESN2; -.
DR ProteomicsDB; 298298; -. [Q9ESN2-1]
DR ProteomicsDB; 298299; -. [Q9ESN2-2]
DR ProteomicsDB; 298300; -. [Q9ESN2-3]
DR DNASU; 79263; -.
DR GeneID; 79263; -.
DR KEGG; mmu:79263; -.
DR CTD; 56658; -.
DR MGI; MGI:1890659; Trim39.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q9ESN2; -.
DR OrthoDB; 423686at2759; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 79263; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Trim39; mouse.
DR PRO; PR:Q9ESN2; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9ESN2; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd13745; SPRY_PRY_TRIM39; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR035033; PRY/SPRY_TRIM39.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Apoptosis; Coiled coil; Cytoplasm; Metal-binding;
KW Mitochondrion; Nucleus; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..488
FT /note="E3 ubiquitin-protein ligase TRIM39"
FT /id="PRO_0000056258"
FT DOMAIN 289..484
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 29..70
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 102..143
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 268..307
FT /note="Interaction with CDKN1A"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM9"
FT REGION 359..488
FT /note="Interaction with CDKN1A"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM9"
FT COILED 181..250
FT /evidence="ECO:0000255"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 261..264
FT /note="DVKS -> KLCA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012063"
FT VAR_SEQ 265..488
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012064"
FT VAR_SEQ 307
FT /note="A -> APLWLLPPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012065"
FT CONFLICT 11
FT /note="A -> T (in Ref. 2; BAC35409)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 488 AA; 56369 MW; 8CEC3E584541F9A2 CRC64;
MAETSLLEAG ASAASTAAAL ENLQVEASCS VCLEYLKEPV IIECGHNFCK ACITRWWEDL
ERDFPCPVCR KTSRYRSLRP NRQLGSMVEI AKQLQTVKRK IRDESLCSQH HEPLSLFCYE
DQEAVCLICA ISHTHRPHTV VPMDDATQEY KEKLQKCLEP LEQKLQEITC CKASEEKKPG
ELKRLVESRR QQILKEFEEL HRRLDEEQQT LLSRLEEEEQ DILQRLRENA AHLGDRRRDL
AHLAAEVEGK CLQSGFEMLK DVKSTLEKCE KVKTMEVTSV SIELEKNFSN FPRQYFALRK
ILKQLIADVT LDPETAHPNL VLSEDRKSVK FVETRLRDLP DTPQRFTFYP CVLATEGFTS
GRHYWEVEVG DKTHWAVGVC RDSVSRKGEL TPLPETGYWR VRLWNGDKYA ATTTPFTPLH
IKVKPKRVGI FLDYEAGTLS FYNVTDRSHI YTFTDTFTEK LWPLFYPGIR AGRKNAAPLT
IRPPTDWE
