TRI32_MOUSE
ID TRI32_MOUSE Reviewed; 655 AA.
AC Q8CH72; Q8K055;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM32;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q13049};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM32 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 32;
GN Name=Trim32;
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], FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION,
RP TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Testis;
RX PubMed=14578165; DOI=10.1093/carcin/bgh003;
RA Horn E.J., Albor A., Liu Y., El-Hizawi S., Vanderbeek G.E., Babcock M.,
RA Bowden G.T., Hennings H., Lozano G., Weinberg W.C., Kulesz-Martin M.;
RT "RING protein Trim32 associated with skin carcinogenesis has anti-apoptotic
RT and E3-ubiquitin ligase properties.";
RL Carcinogenesis 25:157-167(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PIAS4.
RX PubMed=16816390; DOI=10.1074/jbc.m601655200;
RA Albor A., El-Hizawi S., Horn E.J., Laederich M., Frosk P., Wrogemann K.,
RA Kulesz-Martin M.;
RT "The interaction of Piasy with Trim32, an E3-ubiquitin ligase mutated in
RT limb-girdle muscular dystrophy type 2H, promotes Piasy degradation and
RT regulates UVB-induced keratinocyte apoptosis through NFkappaB.";
RL J. Biol. Chem. 281:25850-25866(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 AND SER-337, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Has an E3 ubiquitin ligase activity (PubMed:14578165,
CC PubMed:16816390). Ubiquitinates DTNBP1 (dysbindin) and promotes its
CC degradation (By similarity). May ubiquitinate BBS2 (By similarity).
CC Ubiquitinates PIAS4/PIASY and promotes its degradation in keratinocytes
CC treated with UVB and TNF-alpha (PubMed:14578165, PubMed:16816390)Also
CC acts as a regulator of autophagy by mediating formation of unanchored
CC 'Lys-63'-linked polyubiquitin chains that activate ULK1: interaction
CC with AMBRA1 is required for ULK1 activation (By similarity).
CC {ECO:0000250|UniProtKB:Q13049, ECO:0000269|PubMed:14578165,
CC ECO:0000269|PubMed:16816390}.
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:Q13049};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q13049}.
CC -!- SUBUNIT: It self-associates (By similarity). Interacts with DTNBP1 (By
CC similarity). Interacts with PIAS4/PIASY upon treatment with UVB and
CC TNF-alpha (PubMed:16816390). Interacts with AMBRA1; promoting
CC activation of ULK1 through unanchored 'Lys-63'-linked polyubiquitin
CC chains (By similarity). {ECO:0000250|UniProtKB:Q13049,
CC ECO:0000269|PubMed:16816390}.
CC -!- INTERACTION:
CC Q8CH72; Q8CJG1: Ago1; NbExp=2; IntAct=EBI-773837, EBI-2291996;
CC Q8CH72; P01108: Myc; NbExp=2; IntAct=EBI-773837, EBI-1183114;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14578165,
CC ECO:0000269|PubMed:16816390}. Note=Localized in cytoplasmic bodies,
CC often located around the nucleus. {ECO:0000250|UniProtKB:Q13049}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. High expression in brain.
CC {ECO:0000269|PubMed:14578165}.
CC -!- INDUCTION: By interferon alpha/UVB treatment.
CC {ECO:0000269|PubMed:14578165}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:14578165}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF347694; AAO13297.1; -; mRNA.
DR EMBL; AL691456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034104; AAH34104.1; -; mRNA.
DR CCDS; CCDS18270.1; -.
DR RefSeq; NP_001155254.1; NM_001161782.1.
DR RefSeq; NP_444314.2; NM_053084.2.
DR RefSeq; XP_006538298.1; XM_006538235.1.
DR RefSeq; XP_006538299.1; XM_006538236.3.
DR RefSeq; XP_006538300.1; XM_006538237.1.
DR RefSeq; XP_006538301.1; XM_006538238.1.
DR AlphaFoldDB; Q8CH72; -.
DR SMR; Q8CH72; -.
DR BioGRID; 213691; 29.
DR IntAct; Q8CH72; 9.
DR STRING; 10090.ENSMUSP00000062277; -.
DR iPTMnet; Q8CH72; -.
DR PhosphoSitePlus; Q8CH72; -.
DR EPD; Q8CH72; -.
DR MaxQB; Q8CH72; -.
DR PaxDb; Q8CH72; -.
DR PRIDE; Q8CH72; -.
DR ProteomicsDB; 259317; -.
DR Antibodypedia; 15684; 212 antibodies from 32 providers.
DR DNASU; 69807; -.
DR Ensembl; ENSMUST00000050850; ENSMUSP00000062277; ENSMUSG00000051675.
DR Ensembl; ENSMUST00000107366; ENSMUSP00000102989; ENSMUSG00000051675.
DR GeneID; 69807; -.
DR KEGG; mmu:69807; -.
DR UCSC; uc008thq.2; mouse.
DR CTD; 22954; -.
DR MGI; MGI:1917057; Trim32.
DR VEuPathDB; HostDB:ENSMUSG00000051675; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160949; -.
DR HOGENOM; CLU_423860_0_0_1; -.
DR InParanoid; Q8CH72; -.
DR OMA; VADRGNC; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q8CH72; -.
DR TreeFam; TF331018; -.
DR Reactome; R-MMU-3134975; Regulation of innate immune responses to cytosolic DNA.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 69807; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Trim32; mouse.
DR PRO; PR:Q8CH72; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8CH72; protein.
DR Bgee; ENSMUSG00000051675; Expressed in dorsomedial nucleus of hypothalamus and 256 other tissues.
DR ExpressionAtlas; Q8CH72; baseline and differential.
DR Genevisible; Q8CH72; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005863; C:striated muscle myosin thick filament; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0017022; F:myosin binding; IPI:MGI.
DR GO; GO:0043621; F:protein self-association; ISS:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; IDA:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0031369; F:translation initiation factor binding; IPI:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISS:BHF-UCL.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:BHF-UCL.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007014; P:actin ubiquitination; IDA:MGI.
DR GO; GO:0061564; P:axon development; IMP:MGI.
DR GO; GO:0045444; P:fat cell differentiation; IEP:BHF-UCL.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEP:BHF-UCL.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISS:BHF-UCL.
DR GO; GO:1902173; P:negative regulation of keratinocyte apoptotic process; NAS:BHF-UCL.
DR GO; GO:0032897; P:negative regulation of viral transcription; ISO:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0045787; P:positive regulation of cell cycle; ISS:BHF-UCL.
DR GO; GO:0030307; P:positive regulation of cell growth; ISS:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
DR GO; GO:2000147; P:positive regulation of cell motility; IDA:BHF-UCL.
DR GO; GO:1903886; P:positive regulation of chemokine (C-C motif) ligand 20 production; IMP:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:1903883; P:positive regulation of interleukin-17-mediated signaling pathway; IMP:MGI.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IDA:BHF-UCL.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:BHF-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:BHF-UCL.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISS:BHF-UCL.
DR GO; GO:0051155; P:positive regulation of striated muscle cell differentiation; IMP:MGI.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IMP:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IMP:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IDA:BHF-UCL.
DR GO; GO:0034612; P:response to tumor necrosis factor; IDA:BHF-UCL.
DR GO; GO:0009411; P:response to UV; IDA:BHF-UCL.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:BHF-UCL.
DR Gene3D; 2.120.10.30; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR001258; NHL_repeat.
DR InterPro; IPR027370; Znf-RING_LisH.
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; PF01436; NHL; 3.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS51125; NHL; 5.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..655
FT /note="E3 ubiquitin-protein ligase TRIM32"
FT /id="PRO_0000056247"
FT REPEAT 360..403
FT /note="NHL 1"
FT REPEAT 417..460
FT /note="NHL 2"
FT REPEAT 461..501
FT /note="NHL 3"
FT REPEAT 564..607
FT /note="NHL 4"
FT REPEAT 608..648
FT /note="NHL 5"
FT ZN_FING 21..66
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 96..139
FT /note="B box-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 327..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..198
FT /evidence="ECO:0000255"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 124
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 MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13049"
FT CONFLICT 169
FT /note="A -> V (in Ref. 1; AAO13297)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 655 AA; 72057 MW; 32C01387DA7E9224 CRC64;
MAAAAAASHL NLDALREVLE CPICMESFTE EQLRPKLLHC GHTICRQCLE KLLASSINGV
RCPFCSKITR ITSLTQLTDN LTVLKIIDTA GLSEAVGLLM CRGCGRRLPR QFCRSCGVVL
CEPCREADHQ PPGHCTLPVK EAAEERRRDF GEKLTRLREL TGELQRRKAA LEGVSRDLQA
RYKAVLQEYG HEERRIQEEL ARSRKFFTGS LAEVEKSNSQ VVEEQSYLLN IAEVQAVSRC
DYFLAKIKQA DVALLEETAD EEEPELTASL PRELTLQDVE LLKVGHVGPL QIGQAVKKPR
TVNMEDSWAG EEGAASSASA SVTFREMDMS PEEVAPSPRA SPAKQRSSEA ASGIQQCLFL
KKMGAKGSTP GMFNLPVSLY VTSQSEVLVA DRGNYRIQVF NRKGFLKEIR RSPSGIDSFV
LSFLGADLPN LTPLSVAMNC HGLIGVTDSY DNSLKVYTMD GHCVACHRSQ LSKPWGITAL
PSGQFVVTDV EGGKLWCFTV DRGAGVVKYS CLCSAVRPKF VTCDAEGTVY FTQGLGLNVE
NRQNEHHLEG GFSIGSVGPD GQLGRQISHF FSENEDFRCI AGMCVDARGD LIVADSSRKE
ILHFPKGGGY SVLIREGLTC PVGIALTPKG QLLVLDCWDH CVKIYSYHLR RYSTP
