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E3 ubiquitin-protein ligase TRIM32 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM32) (Tripartite motif-containing protein 32)

 TRI32_MOUSE             Reviewed;         655 AA.
Q8CH72; Q8K055;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 2.
30-AUG-2017, entry version 133.
RecName: Full=E3 ubiquitin-protein ligase TRIM32;
EC=2.3.2.27;
AltName: Full=RING-type E3 ubiquitin transferase TRIM32 {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 32;
Name=Trim32;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
UBIQUITINATION.
TISSUE=Testis;
PubMed=14578165; DOI=10.1093/carcin/bgh003;
Horn E.J., Albor A., Liu Y., El-Hizawi S., Vanderbeek G.E.,
Babcock M., Bowden G.T., Hennings H., Lozano G., Weinberg W.C.,
Kulesz-Martin M.;
"RING protein Trim32 associated with skin carcinogenesis has anti-
apoptotic and E3-ubiquitin ligase properties.";
Carcinogenesis 25:157-167(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Retina;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PIAS4.
PubMed=16816390; DOI=10.1074/jbc.M601655200;
Albor A., El-Hizawi S., Horn E.J., Laederich M., Frosk P.,
Wrogemann K., Kulesz-Martin M.;
"The interaction of Piasy with Trim32, an E3-ubiquitin ligase mutated
in limb-girdle muscular dystrophy type 2H, promotes Piasy degradation
and regulates UVB-induced keratinocyte apoptosis through NFkappaB.";
J. Biol. Chem. 281:25850-25866(2006).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 AND SER-337, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Has an E3 ubiquitin ligase activity. Ubiquitinates
DTNBP1 (dysbindin). May ubiquitinate BBS2 (By similarity).
Ubiquitinates PIAS4/PIASY and promotes its degradation in
keratinocytes treated with UVB and TNF-alpha. {ECO:0000250,
ECO:0000269|PubMed:14578165, ECO:0000269|PubMed:16816390}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with DTNBP1 (By similarity). It self-associates
(By similarity). Interacts with PIAS4/PIASY upon treatment with
UVB and TNF-alpha. {ECO:0000250, ECO:0000269|PubMed:16816390}.
-!- INTERACTION:
Q8CJG1:Ago1; NbExp=2; IntAct=EBI-773837, EBI-2291996;
P01108:Myc; NbExp=2; IntAct=EBI-773837, EBI-1183114;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14578165,
ECO:0000269|PubMed:16816390}. Note=Localized in cytoplasmic
bodies, usually concentrated around the nucleus.
-!- TISSUE SPECIFICITY: Ubiquitous. High expression in brain.
-!- INDUCTION: By interferon alpha/UVB treatment.
-!- PTM: Ubiquitinated. {ECO:0000269|PubMed:14578165}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF347694; AAO13297.1; -; mRNA.
EMBL; AL691456; CAD62276.1; -; Genomic_DNA.
EMBL; BC034104; AAH34104.1; -; mRNA.
CCDS; CCDS18270.1; -.
RefSeq; NP_001155254.1; NM_001161782.1.
RefSeq; NP_444314.2; NM_053084.2.
RefSeq; XP_006538298.1; XM_006538235.1.
RefSeq; XP_006538299.1; XM_006538236.3.
RefSeq; XP_006538300.1; XM_006538237.1.
RefSeq; XP_006538301.1; XM_006538238.1.
UniGene; Mm.22786; -.
ProteinModelPortal; Q8CH72; -.
SMR; Q8CH72; -.
BioGrid; 213691; 21.
IntAct; Q8CH72; 10.
STRING; 10090.ENSMUSP00000062277; -.
iPTMnet; Q8CH72; -.
PhosphoSitePlus; Q8CH72; -.
EPD; Q8CH72; -.
MaxQB; Q8CH72; -.
PaxDb; Q8CH72; -.
PRIDE; Q8CH72; -.
Ensembl; ENSMUST00000050850; ENSMUSP00000062277; ENSMUSG00000051675.
Ensembl; ENSMUST00000107366; ENSMUSP00000102989; ENSMUSG00000051675.
GeneID; 69807; -.
KEGG; mmu:69807; -.
UCSC; uc008thq.2; mouse.
CTD; 22954; -.
MGI; MGI:1917057; Trim32.
eggNOG; ENOG410ITFD; Eukaryota.
eggNOG; ENOG410XRCH; LUCA.
GeneTree; ENSGT00890000139359; -.
HOGENOM; HOG000120114; -.
HOVERGEN; HBG060344; -.
InParanoid; Q8CH72; -.
KO; K10607; -.
OMA; CITGMCV; -.
OrthoDB; EOG091G0KUF; -.
PhylomeDB; Q8CH72; -.
TreeFam; TF331018; -.
Reactome; R-MMU-3134975; Regulation of innate immune responses to cytosolic DNA.
UniPathway; UPA00143; -.
PRO; PR:Q8CH72; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000051675; -.
ExpressionAtlas; Q8CH72; baseline and differential.
Genevisible; Q8CH72; MM.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0017022; F:myosin binding; IPI:MGI.
GO; GO:0043621; F:protein self-association; ISS:BHF-UCL.
GO; GO:0003723; F:RNA binding; IDA:BHF-UCL.
GO; GO:0031369; F:translation initiation factor binding; IPI:MGI.
GO; GO:0043130; F:ubiquitin binding; ISS:BHF-UCL.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:BHF-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IMP:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0007014; P:actin ubiquitination; IDA:MGI.
GO; GO:0061564; P:axon development; IMP:MGI.
GO; GO:0045444; P:fat cell differentiation; IEP:BHF-UCL.
GO; GO:0045087; P:innate immune response; ISO:MGI.
GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:MGI.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEP:BHF-UCL.
GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISS:BHF-UCL.
GO; GO:1902173; P:negative regulation of keratinocyte apoptotic process; NAS:BHF-UCL.
GO; GO:1902187; P:negative regulation of viral release from host cell; ISO:MGI.
GO; GO:0032897; P:negative regulation of viral transcription; ISO:MGI.
GO; GO:0045787; P:positive regulation of cell cycle; ISS:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; ISS:BHF-UCL.
GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
GO; GO:2000147; P:positive regulation of cell motility; IDA:BHF-UCL.
GO; GO:1903886; P:positive regulation of chemokine (C-C motif) ligand 20 production; IMP:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:1903883; P:positive regulation of interleukin-17-mediated signaling pathway; IMP:MGI.
GO; GO:0050769; P:positive regulation of neurogenesis; IDA:BHF-UCL.
GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:BHF-UCL.
GO; GO:0045862; P:positive regulation of proteolysis; ISS:BHF-UCL.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:0051155; P:positive regulation of striated muscle cell differentiation; IMP:MGI.
GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IMP:MGI.
GO; GO:0000209; P:protein polyubiquitination; IMP:MGI.
GO; GO:0016567; P:protein ubiquitination; IDA:BHF-UCL.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:BHF-UCL.
GO; GO:0034612; P:response to tumor necrosis factor; IDA:BHF-UCL.
GO; GO:0009411; P:response to UV; IDA:BHF-UCL.
GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
Gene3D; 2.120.10.30; -; 2.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR001258; NHL_repeat.
InterPro; IPR013017; NHL_repeat_subgr.
InterPro; IPR033569; TRIM32.
InterPro; IPR027370; Znf-RING_LisH.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
PANTHER; PTHR24103:SF430; PTHR24103:SF430; 1.
Pfam; PF01436; NHL; 3.
Pfam; PF13445; zf-RING_UBOX; 1.
SMART; SM00336; BBOX; 1.
SMART; SM00184; RING; 1.
PROSITE; PS51125; NHL; 5.
PROSITE; PS50119; ZF_BBOX; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Cytoplasm; Metal-binding;
Phosphoprotein; Reference proteome; Repeat; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 655 E3 ubiquitin-protein ligase TRIM32.
/FTId=PRO_0000056247.
REPEAT 360 403 NHL 1.
REPEAT 417 460 NHL 2.
REPEAT 461 501 NHL 3.
REPEAT 564 607 NHL 4.
REPEAT 608 648 NHL 5.
ZN_FING 21 66 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
ZN_FING 96 139 B box-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00024}.
COILED 139 198 {ECO:0000255}.
COMPBIAS 2 7 Poly-Ala.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 341 341 Phosphoserine.
{ECO:0000250|UniProtKB:Q13049}.
CONFLICT 169 169 A -> V (in Ref. 1; AAO13297).
{ECO:0000305}.
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


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