TRI32_HUMAN
ID TRI32_HUMAN Reviewed; 653 AA.
AC Q13049; Q9NQP8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 223.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM32;
DE EC=2.3.2.27 {ECO:0000269|PubMed:19349376, ECO:0000269|PubMed:31123703};
DE AltName: Full=72 kDa Tat-interacting protein;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM32 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 32;
DE AltName: Full=Zinc finger protein HT2A;
GN Name=TRIM32; Synonyms=HT2A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION (MICROBIAL INFECTION).
RX PubMed=7778269; DOI=10.1006/viro.1995.1266;
RA Fridell R.A., Harding L.S., Bogerd H.P., Cullen B.R.;
RT "Identification of a novel human zinc finger protein that specifically
RT interacts with the activation domain of lentiviral Tat proteins.";
RL Virology 209:347-357(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 PROTEIN SEQUENCE OF 2-15; 51-60; 70-101; 205-238; 248-282; 345-359;
RP 467-500; 587-596 AND 605-613, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP FUNCTION AS AN E3 UBIQUITIN-PROTEIN LIGASE, CATALYTIC ACTIVITY, PATHWAY,
RP UBIQUITINATION, SELF-ASSOCIATION, AND INTERACTION WITH DTNBP1.
RX PubMed=19349376; DOI=10.1093/hmg/ddp167;
RA Locke M., Tinsley C.L., Benson M.A., Blake D.J.;
RT "TRIM32 is an E3 ubiquitin ligase for dysbindin.";
RL Hum. Mol. Genet. 18:2344-2358(2009).
RN [7]
RP FUNCTION.
RX PubMed=22500027; DOI=10.1074/jbc.m112.341487;
RA Zhang Q., Yu D., Seo S., Stone E.M., Sheffield V.C.;
RT "Intrinsic protein-protein interaction-mediated and chaperonin-assisted
RT sequential assembly of stable Bardet-Biedl syndrome protein complex, the
RT BBSome.";
RL J. Biol. Chem. 287:20625-20635(2012).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-339, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [9]
RP INTERACTION WITH S.TYPHIMURIUM SSEK3 (MICROBIAL INFECTION).
RX PubMed=26394407; DOI=10.1371/journal.pone.0138529;
RA Yang Z., Soderholm A., Lung T.W., Giogha C., Hill M.M., Brown N.F.,
RA Hartland E., Teasdale R.D.;
RT "SseK3 is a Salmonella effector that binds TRIM32 and modulates the host's
RT NF-kappaB signalling activity.";
RL PLoS ONE 10:e0138529-e0138529(2015).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH AMBRA1, AND
RP MUTAGENESIS OF CYS-39.
RX PubMed=31123703; DOI=10.1126/sciadv.aau8857;
RA Di Rienzo M., Antonioli M., Fusco C., Liu Y., Mari M., Orhon I., Refolo G.,
RA Germani F., Corazzari M., Romagnoli A., Ciccosanti F., Mandriani B.,
RA Pellico M.T., De La Torre R., Ding H., Dentice M., Neri M., Ferlini A.,
RA Reggiori F., Kulesz-Martin M., Piacentini M., Merla G., Fimia G.M.;
RT "Autophagy induction in atrophic muscle cells requires ULK1 activation by
RT TRIM32 through unanchored K63-linked polyubiquitin chains.";
RL Sci. Adv. 5:eaau8857-eaau8857(2019).
RN [11]
RP STRUCTURE BY NMR OF 10-84.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RING domain of the tripartite motif protein
RT 32.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [12]
RP VARIANT LGMDR8 ASN-487, AND TISSUE SPECIFICITY.
RX PubMed=11822024; DOI=10.1086/339083;
RA Frosk P., Weiler T., Nylen E., Sudha T., Greenberg C.R., Morgan K.,
RA Fujiwara T.M., Wrogemann K.;
RT "Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32,
RT a putative E3-ubiquitin-ligase gene.";
RL Am. J. Hum. Genet. 70:663-672(2002).
RN [13]
RP VARIANT BBS11 SER-130.
RX PubMed=16606853; DOI=10.1073/pnas.0600158103;
RA Chiang A.P., Beck J.S., Yen H.-J., Tayeh M.K., Scheetz T.E.,
RA Swiderski R.E., Nishimura D.Y., Braun T.A., Kim K.-Y.A., Huang J.,
RA Elbedour K., Carmi R., Slusarski D.C., Casavant T.L., Stone E.M.,
RA Sheffield V.C.;
RT "Homozygosity mapping with SNP arrays identifies TRIM32, an E3 ubiquitin
RT ligase, as a Bardet-Biedl syndrome gene (BBS11).";
RL Proc. Natl. Acad. Sci. U.S.A. 103:6287-6292(2006).
RN [14]
RP VARIANTS LGMDR8 HIS-394 AND ASP-588 DEL.
RX PubMed=17994549; DOI=10.1002/humu.20633;
RA Saccone V., Palmieri M., Passamano L., Piluso G., Meroni G., Politano L.,
RA Nigro V.;
RT "Mutations that impair interaction properties of TRIM32 associated with
RT limb-girdle muscular dystrophy 2H.";
RL Hum. Mutat. 29:240-247(2008).
RN [15]
RP VARIANT GLN-299.
RX PubMed=21344540; DOI=10.1002/humu.21480;
RA Deveault C., Billingsley G., Duncan J.L., Bin J., Theal R., Vincent A.,
RA Fieggen K.J., Gerth C., Noordeh N., Traboulsi E.I., Fishman G.A.,
RA Chitayat D., Knueppel T., Millan J.M., Munier F.L., Kennedy D.,
RA Jacobson S.G., Innes A.M., Mitchell G.A., Boycott K., Heon E.;
RT "BBS genotype-phenotype assessment of a multiethnic patient cohort calls
RT for a revision of the disease definition.";
RL Hum. Mutat. 32:610-619(2011).
CC -!- FUNCTION: Has an E3 ubiquitin ligase activity (PubMed:19349376,
CC PubMed:31123703). Ubiquitinates DTNBP1 (dysbindin) and promotes its
CC degradation (PubMed:19349376). May ubiquitinate BBS2 (PubMed:22500027).
CC Ubiquitinates PIAS4/PIASY and promotes its degradation in keratinocytes
CC treated with UVB and TNF-alpha (By similarity). Also acts as a
CC regulator of autophagy by mediating formation of unanchored 'Lys-63'-
CC linked polyubiquitin chains that activate ULK1: interaction with AMBRA1
CC is required for ULK1 activation (PubMed:31123703).
CC {ECO:0000250|UniProtKB:Q8CH72, ECO:0000269|PubMed:19349376,
CC ECO:0000269|PubMed:22500027, ECO:0000269|PubMed:31123703}.
CC -!- FUNCTION: (Microbial infection) May play a significant role in
CC mediating the biological activity of the HIV-1 Tat protein in vivo
CC (PubMed:7778269). Binds specifically to the activation domain of HIV-1
CC Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo
CC (PubMed:7778269). {ECO:0000269|PubMed:7778269}.
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:0000269|PubMed:19349376,
CC ECO:0000269|PubMed:31123703};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:19349376, ECO:0000269|PubMed:31123703}.
CC -!- SUBUNIT: It self-associates (PubMed:19349376). Interacts with DTNBP1
CC (PubMed:19349376). Interacts with PIAS4/PIASY upon treatment with UVB
CC and TNF-alpha (By similarity). Interacts with AMBRA1; promoting
CC activation of ULK1 through unanchored 'Lys-63'-linked polyubiquitin
CC chains (PubMed:31123703). {ECO:0000250|UniProtKB:Q8CH72,
CC ECO:0000269|PubMed:19349376, ECO:0000269|PubMed:31123703}.
CC -!- SUBUNIT: (Microbial infection) Interacts with S.typhimurium protein
CC SseK3; SseK3 does not glycosylate TRIM32.
CC {ECO:0000269|PubMed:26394407}.
CC -!- INTERACTION:
CC Q13049; Q9NYB9: ABI2; NbExp=6; IntAct=EBI-742790, EBI-743598;
CC Q13049; Q9NYB9-2: ABI2; NbExp=8; IntAct=EBI-742790, EBI-11096309;
CC Q13049; P54253: ATXN1; NbExp=5; IntAct=EBI-742790, EBI-930964;
CC Q13049; Q8N3C7: CLIP4; NbExp=6; IntAct=EBI-742790, EBI-5655540;
CC Q13049; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-742790, EBI-398977;
CC Q13049; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-742790, EBI-781551;
CC Q13049; Q8N9I5: FADS6; NbExp=3; IntAct=EBI-742790, EBI-3943864;
CC Q13049; P55040: GEM; NbExp=3; IntAct=EBI-742790, EBI-744104;
CC Q13049; O60478: GPR137B; NbExp=3; IntAct=EBI-742790, EBI-18945347;
CC Q13049; O60725: ICMT; NbExp=3; IntAct=EBI-742790, EBI-11721771;
CC Q13049; Q7L273: KCTD9; NbExp=6; IntAct=EBI-742790, EBI-4397613;
CC Q13049; P80188: LCN2; NbExp=3; IntAct=EBI-742790, EBI-11911016;
CC Q13049; Q9H8S9: MOB1A; NbExp=3; IntAct=EBI-742790, EBI-748229;
CC Q13049; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-742790, EBI-741158;
CC Q13049; O76083: PDE9A; NbExp=10; IntAct=EBI-742790, EBI-742764;
CC Q13049; O76083-2: PDE9A; NbExp=10; IntAct=EBI-742790, EBI-11524542;
CC Q13049; O76083-4: PDE9A; NbExp=3; IntAct=EBI-742790, EBI-16433425;
CC Q13049; Q9HAT8: PELI2; NbExp=3; IntAct=EBI-742790, EBI-448407;
CC Q13049; Q8WV60: PTCD2; NbExp=3; IntAct=EBI-742790, EBI-12154567;
CC Q13049; Q06124: PTPN11; NbExp=5; IntAct=EBI-742790, EBI-297779;
CC Q13049; O14966: RAB29; NbExp=3; IntAct=EBI-742790, EBI-372165;
CC Q13049; Q9UI14: RABAC1; NbExp=10; IntAct=EBI-742790, EBI-712367;
CC Q13049; P11684: SCGB1A1; NbExp=8; IntAct=EBI-742790, EBI-7797649;
CC Q13049; O00560: SDCBP; NbExp=7; IntAct=EBI-742790, EBI-727004;
CC Q13049; Q5T7P8-2: SYT6; NbExp=6; IntAct=EBI-742790, EBI-10246152;
CC Q13049; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-742790, EBI-11955057;
CC Q13049; Q13049: TRIM32; NbExp=5; IntAct=EBI-742790, EBI-742790;
CC Q13049; Q9C035: TRIM5; NbExp=2; IntAct=EBI-742790, EBI-924214;
CC Q13049; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-742790, EBI-9090990;
CC Q13049; P61088: UBE2N; NbExp=3; IntAct=EBI-742790, EBI-1052908;
CC Q13049; Q5VVX9: UBE2U; NbExp=4; IntAct=EBI-742790, EBI-2130181;
CC Q13049; Q13404: UBE2V1; NbExp=4; IntAct=EBI-742790, EBI-1050671;
CC Q13049; Q9UMX0: UBQLN1; NbExp=7; IntAct=EBI-742790, EBI-741480;
CC Q13049; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-742790, EBI-10173939;
CC Q13049; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-742790, EBI-947187;
CC Q13049; Q9NRR5: UBQLN4; NbExp=3; IntAct=EBI-742790, EBI-711226;
CC Q13049; B3KPU6; NbExp=3; IntAct=EBI-742790, EBI-10175879;
CC Q13049; Q99J34: Irak1; Xeno; NbExp=2; IntAct=EBI-742790, EBI-6117042;
CC Q13049; PRO_0000449633 [P0DTD1]: rep; Xeno; NbExp=4; IntAct=EBI-742790, EBI-25492395;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19349376}.
CC Note=Localized in cytoplasmic bodies, often located around the nucleus.
CC {ECO:0000269|PubMed:19349376}.
CC -!- TISSUE SPECIFICITY: Spleen, thymus, prostate, testis, ovary, intestine,
CC colon and skeletal muscle. {ECO:0000269|PubMed:11822024}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:19349376}.
CC -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 8
CC (LGMDR8) [MIM:254110]: An autosomal recessive degenerative myopathy
CC characterized by pelvic girdle, shoulder girdle and quadriceps muscle
CC weakness. Clinical phenotype and severity are highly variable. Disease
CC progression is slow and most patients remain ambulatory into the sixth
CC decade of life. {ECO:0000269|PubMed:11822024,
CC ECO:0000269|PubMed:17994549}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Bardet-Biedl syndrome 11 (BBS11) [MIM:615988]: A syndrome
CC characterized by usually severe pigmentary retinopathy, early-onset
CC obesity, polydactyly, hypogenitalism, renal malformation and
CC intellectual disability. Secondary features include diabetes mellitus,
CC hypertension and congenital heart disease. Bardet-Biedl syndrome
CC inheritance is autosomal recessive, but three mutated alleles (two at
CC one locus, and a third at a second locus) may be required for clinical
CC manifestation of some forms of the disease.
CC {ECO:0000269|PubMed:16606853}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. It has been suggested
CC that TRIM32 might be the E3 ubiquitin ligase for BBS2, a component of
CC the BBSome complex involved in ciliogenesis, that is ubiquitinated and
CC degraded by the proteasome (PubMed:22500027).
CC {ECO:0000269|PubMed:22500027}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Leiden Muscular Dystrophy pages; Note=TRIM32;
CC URL="https://www.dmd.nl/trim32_home.html";
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DR EMBL; U18543; AAA86474.1; -; mRNA.
DR EMBL; AL133284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003154; AAH03154.1; -; mRNA.
DR CCDS; CCDS6817.1; -.
DR RefSeq; NP_001093149.1; NM_001099679.1.
DR RefSeq; NP_036342.2; NM_012210.3.
DR RefSeq; XP_005251870.1; XM_005251813.3.
DR RefSeq; XP_011516700.1; XM_011518398.2.
DR RefSeq; XP_016869975.1; XM_017014486.1.
DR PDB; 2CT2; NMR; -; A=10-84.
DR PDB; 5FEY; X-ray; 2.23 A; A/B=7-93.
DR PDBsum; 2CT2; -.
DR PDBsum; 5FEY; -.
DR AlphaFoldDB; Q13049; -.
DR SMR; Q13049; -.
DR BioGRID; 116608; 194.
DR CORUM; Q13049; -.
DR IntAct; Q13049; 71.
DR MINT; Q13049; -.
DR STRING; 9606.ENSP00000408292; -.
DR iPTMnet; Q13049; -.
DR PhosphoSitePlus; Q13049; -.
DR BioMuta; TRIM32; -.
DR DMDM; 20178303; -.
DR EPD; Q13049; -.
DR jPOST; Q13049; -.
DR MassIVE; Q13049; -.
DR MaxQB; Q13049; -.
DR PaxDb; Q13049; -.
DR PeptideAtlas; Q13049; -.
DR PRIDE; Q13049; -.
DR ProteomicsDB; 59123; -.
DR Antibodypedia; 15684; 212 antibodies from 32 providers.
DR DNASU; 22954; -.
DR Ensembl; ENST00000373983.2; ENSP00000363095.1; ENSG00000119401.11.
DR Ensembl; ENST00000450136.2; ENSP00000408292.1; ENSG00000119401.11.
DR GeneID; 22954; -.
DR KEGG; hsa:22954; -.
DR MANE-Select; ENST00000450136.2; ENSP00000408292.1; NM_012210.4; NP_036342.2.
DR UCSC; uc004bjw.3; human.
DR CTD; 22954; -.
DR DisGeNET; 22954; -.
DR GeneCards; TRIM32; -.
DR GeneReviews; TRIM32; -.
DR HGNC; HGNC:16380; TRIM32.
DR HPA; ENSG00000119401; Low tissue specificity.
DR MalaCards; TRIM32; -.
DR MIM; 254110; phenotype.
DR MIM; 602290; gene.
DR MIM; 615988; phenotype.
DR neXtProt; NX_Q13049; -.
DR OpenTargets; ENSG00000119401; -.
DR Orphanet; 110; Bardet-Biedl syndrome.
DR Orphanet; 1878; TRIM32-related limb-girdle muscular dystrophy R8.
DR PharmGKB; PA38130; -.
DR VEuPathDB; HostDB:ENSG00000119401; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160949; -.
DR HOGENOM; CLU_423860_0_0_1; -.
DR InParanoid; Q13049; -.
DR OMA; VADRGNC; -.
DR OrthoDB; 489543at2759; -.
DR PhylomeDB; Q13049; -.
DR TreeFam; TF331018; -.
DR PathwayCommons; Q13049; -.
DR Reactome; R-HSA-3134975; Regulation of innate immune responses to cytosolic DNA.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q13049; -.
DR SIGNOR; Q13049; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 22954; 13 hits in 1116 CRISPR screens.
DR ChiTaRS; TRIM32; human.
DR EvolutionaryTrace; Q13049; -.
DR GeneWiki; TRIM32; -.
DR GenomeRNAi; 22954; -.
DR Pharos; Q13049; Tbio.
DR PRO; PR:Q13049; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q13049; protein.
DR Bgee; ENSG00000119401; Expressed in stromal cell of endometrium and 175 other tissues.
DR ExpressionAtlas; Q13049; baseline and differential.
DR Genevisible; Q13049; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0005863; C:striated muscle myosin thick filament; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017022; F:myosin binding; ISS:BHF-UCL.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:BHF-UCL.
DR GO; GO:0030957; F:Tat protein binding; TAS:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0031369; F:translation initiation factor binding; ISS:BHF-UCL.
DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007014; P:actin ubiquitination; IEA:Ensembl.
DR GO; GO:0061564; P:axon development; IEA:Ensembl.
DR GO; GO:0045444; P:fat cell differentiation; ISS:BHF-UCL.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:BHF-UCL.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IDA:BHF-UCL.
DR GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProtKB.
DR GO; GO:0045787; P:positive regulation of cell cycle; IDA:BHF-UCL.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:2000147; P:positive regulation of cell motility; ISS:BHF-UCL.
DR GO; GO:1903886; P:positive regulation of chemokine (C-C motif) ligand 20 production; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:1903883; P:positive regulation of interleukin-17-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0050769; P:positive regulation of neurogenesis; ISS:BHF-UCL.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:BHF-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; ISS:BHF-UCL.
DR GO; GO:0045862; P:positive regulation of proteolysis; IDA:BHF-UCL.
DR GO; GO:0051155; P:positive regulation of striated muscle cell differentiation; IEA:Ensembl.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:BHF-UCL.
DR GO; GO:0016567; P:protein ubiquitination; IDA:BHF-UCL.
DR GO; GO:0034612; P:response to tumor necrosis factor; ISS:BHF-UCL.
DR GO; GO:0009411; P:response to UV; ISS:BHF-UCL.
DR GO; GO:0044790; P:suppression of viral release by host; IDA:UniProtKB.
DR GO; GO:0001894; P:tissue homeostasis; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
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 3D-structure; Acetylation; Bardet-Biedl syndrome; Ciliopathy; Coiled coil;
KW Cytoplasm; Direct protein sequencing; Disease variant;
KW Intellectual disability; Limb-girdle muscular dystrophy; Metal-binding;
KW Obesity; Phosphoprotein; Reference proteome; Repeat; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..653
FT /note="E3 ubiquitin-protein ligase TRIM32"
FT /id="PRO_0000056246"
FT REPEAT 358..401
FT /note="NHL 1"
FT REPEAT 415..458
FT /note="NHL 2"
FT REPEAT 459..499
FT /note="NHL 3"
FT REPEAT 562..605
FT /note="NHL 4"
FT REPEAT 606..646
FT /note="NHL 5"
FT ZN_FING 20..65
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 103..133
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 138..197
FT /evidence="ECO:0000255"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CH72"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 130
FT /note="P -> S (in BBS11; dbSNP:rs111033571)"
FT /evidence="ECO:0000269|PubMed:16606853"
FT /id="VAR_038807"
FT VARIANT 257
FT /note="T -> R (in dbSNP:rs3747834)"
FT /id="VAR_038808"
FT VARIANT 299
FT /note="R -> Q (in a patient with Bardet-Biedl syndrome;
FT unknown pathological significance; dbSNP:rs766439806)"
FT /evidence="ECO:0000269|PubMed:21344540"
FT /id="VAR_066295"
FT VARIANT 394
FT /note="R -> H (in LGMDR8; dbSNP:rs121434447)"
FT /evidence="ECO:0000269|PubMed:17994549"
FT /id="VAR_042939"
FT VARIANT 408
FT /note="R -> C (in dbSNP:rs3747835)"
FT /id="VAR_038809"
FT VARIANT 487
FT /note="D -> N (in LGMDR8; dbSNP:rs111033570)"
FT /evidence="ECO:0000269|PubMed:11822024"
FT /id="VAR_018725"
FT VARIANT 588
FT /note="Missing (in LGMDR8)"
FT /evidence="ECO:0000269|PubMed:17994549"
FT /id="VAR_042940"
FT MUTAGEN 39
FT /note="C->S: Abolished E3 ubiquitin ligase activity and
FT ability to activate ULK1."
FT /evidence="ECO:0000269|PubMed:31123703"
FT CONFLICT 27
FT /note="F -> I (in Ref. 1; AAA86474)"
FT /evidence="ECO:0000305"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:5FEY"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:5FEY"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:5FEY"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2CT2"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:5FEY"
FT HELIX 45..51
FT /evidence="ECO:0007829|PDB:5FEY"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5FEY"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:2CT2"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:2CT2"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:5FEY"
SQ SEQUENCE 653 AA; 71989 MW; D83B1595CA8378FD CRC64;
MAAAAASHLN LDALREVLEC PICMESFTEE QLRPKLLHCG HTICRQCLEK LLASSINGVR
CPFCSKITRI TSLTQLTDNL TVLKIIDTAG LSEAVGLLMC RSCGRRLPRQ FCRSCGLVLC
EPCREADHQP PGHCTLPVKE AAEERRRDFG EKLTRLRELM GELQRRKAAL EGVSKDLQAR
YKAVLQEYGH EERRVQDELA RSRKFFTGSL AEVEKSNSQV VEEQSYLLNI AEVQAVSRCD
YFLAKIKQAD VALLEETADE EEPELTASLP RELTLQDVEL LKVGHVGPLQ IGQAVKKPRT
VNVEDSWAME ATASAASTSV TFREMDMSPE EVVASPRASP AKQRGPEAAS NIQQCLFLKK
MGAKGSTPGM FNLPVSLYVT SQGEVLVADR GNYRIQVFTR KGFLKEIRRS PSGIDSFVLS
FLGADLPNLT PLSVAMNCQG LIGVTDSYDN SLKVYTLDGH CVACHRSQLS KPWGITALPS
GQFVVTDVEG GKLWCFTVDR GSGVVKYSCL CSAVRPKFVT CDAEGTVYFT QGLGLNLENR
QNEHHLEGGF SIGSVGPDGQ LGRQISHFFS ENEDFRCIAG MCVDARGDLI VADSSRKEIL
HFPKGGGYSV LIREGLTCPV GIALTPKGQL LVLDCWDHCI KIYSYHLRRY STP
