TRI52_HUMAN
ID TRI52_HUMAN Reviewed; 297 AA.
AC Q96A61; L0CQ38; Q59G66;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM52;
DE EC=2.3.2.27 {ECO:0000269|PubMed:27667714};
DE AltName: Full=RING finger protein 102;
DE AltName: Full=Tripartite motif-containing protein 52;
GN Name=TRIM52; Synonyms=RNF102;
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] (ISOFORM 1).
RX PubMed=24158625; DOI=10.1093/gbe/evt163;
RA Malfavon-Borja R., Sawyer S.L., Wu L.I., Emerman M., Malik H.S.;
RT "An evolutionary screen highlights canonical and noncanonical candidate
RT antiviral genes within the primate TRIM gene family.";
RL Genome Biol. Evol. 5:2141-2154(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [7]
RP UBIQUITINATION.
RX PubMed=20596523; DOI=10.1371/journal.pone.0011332;
RA Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B.,
RA Spruck C.;
RT "Development and validation of a method for profiling post-translational
RT modification activities using protein microarrays.";
RL PLoS ONE 5:E11332-E11332(2010).
RN [8]
RP FUNCTION AS E3 UBIQUITIN-PROTEIN LIGASE, FUNCTION (MICROBIAL FUNCTION),
RP CATALYTIC ACTIVITY, AUTOUBIQUITINATION, DOMAIN RING-TYPE ZINC FINGER,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH JAPANESE ENCEPHALITIS VIRUS
RP (MICROBIAL INFECTION).
RX PubMed=27667714; DOI=10.1038/srep33698;
RA Fan W., Wu M., Qian S., Zhou Y., Chen H., Li X., Qian P.;
RT "TRIM52 inhibits Japanese Encephalitis Virus replication by degrading the
RT viral NS2A.";
RL Sci. Rep. 6:33698-33698(2016).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DOMAIN RING-TYPE ZINC FINGER,
RP AND UBIQUITINATION.
RX PubMed=28073078; DOI=10.1016/j.molimm.2017.01.003;
RA Fan W., Liu T., Li X., Zhou Y., Wu M., Cui X., Chen H., Qian P.;
RT "TRIM52: A nuclear TRIM protein that positively regulates the nuclear
RT factor-kappa B signaling pathway.";
RL Mol. Immunol. 82:114-122(2017).
RN [10]
RP INDUCTION, PROTEASOMAL DEGRADATION, AND REGION.
RX PubMed=31133683; DOI=10.1038/s41598-019-44359-0;
RA Hacker K., Benke S., Agerer B., Scinicariello S., Budroni V.,
RA Versteeg G.A.;
RT "A repetitive acidic region contributes to the extremely rapid degradation
RT of the cell-context essential protein TRIM52.";
RL Sci. Rep. 9:7901-7901(2019).
CC -!- FUNCTION: E3 ubiquitin-protein ligase (PubMed:27667714). Positively
CC regulates the NF-kappa-B signaling pathway (PubMed:27667714,
CC PubMed:28073078). {ECO:0000269|PubMed:27667714,
CC ECO:0000269|PubMed:28073078}.
CC -!- FUNCTION: (Microbial infection) Exhibits antiviral activity against
CC Japanese encephalitis virus (JEV). Ubiquitinates the viral non-
CC structural protein 2 (NS2A) and targets it for proteasome-mediated
CC degradation. {ECO:0000269|PubMed:27667714}.
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:27667714};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: (Microbial infection) Interacts with Japanese encephalitis
CC virus non-structural protein 2 (NS2A); mediates the ubiquitination of
CC NS2A, targeting it for proteasome-mediated degradation.
CC {ECO:0000269|PubMed:27667714}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28073078}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:27667714}. Nucleus
CC {ECO:0000269|PubMed:27667714, ECO:0000269|PubMed:28073078}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96A61-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96A61-2; Sequence=VSP_060452, VSP_060453;
CC -!- INDUCTION: Up-regulated by Golgi stress-inducing agents such nigericin,
CC trichostatin, tetoposide, campothecin and brefeldin A
CC (PubMed:31133683). Up-regulated by IL1B/interleukin-1 beta and
CC TNFA/TNF-alpha (PubMed:28073078). {ECO:0000269|PubMed:28073078,
CC ECO:0000269|PubMed:31133683}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for its E3
CC ubiquitin-protein ligase activity, ability to positively regulate the
CC NF-kappa-B signaling pathway and its antiviral activity.
CC {ECO:0000269|PubMed:27667714, ECO:0000269|PubMed:28073078}.
CC -!- PTM: Autoubiquitinated (PubMed:27667714). Polyubiquitinated
CC (PubMed:20596523, PubMed:27667714). Undergoes extremely rapid
CC proteolytic degradation by the proteasome (PubMed:31133683).
CC {ECO:0000269|PubMed:20596523, ECO:0000269|PubMed:27667714,
CC ECO:0000269|PubMed:31133683}.
CC -!- MISCELLANEOUS: Arose via a partial duplication of the TRIM41 gene,
CC followed by independent loss or pseudogenization of TRIM52 in multiple
CC mammalian and primate lineages. {ECO:0000305|PubMed:24158625}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92480.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; JX896146; AGA17664.1; -; mRNA.
DR EMBL; AK054802; BAB70809.1; -; mRNA.
DR EMBL; AB209243; BAD92480.1; ALT_INIT; mRNA.
DR EMBL; AC008443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471165; EAW53704.1; -; Genomic_DNA.
DR EMBL; BC007372; AAH07372.1; -; mRNA.
DR CCDS; CCDS4467.1; -. [Q96A61-1]
DR RefSeq; NP_116154.1; NM_032765.3. [Q96A61-1]
DR AlphaFoldDB; Q96A61; -.
DR SMR; Q96A61; -.
DR BioGRID; 124301; 130.
DR IntAct; Q96A61; 9.
DR STRING; 9606.ENSP00000483005; -.
DR iPTMnet; Q96A61; -.
DR PhosphoSitePlus; Q96A61; -.
DR BioMuta; TRIM52; -.
DR DMDM; 47606198; -.
DR MassIVE; Q96A61; -.
DR PaxDb; Q96A61; -.
DR PeptideAtlas; Q96A61; -.
DR PRIDE; Q96A61; -.
DR ProteomicsDB; 75922; -.
DR Antibodypedia; 29763; 44 antibodies from 13 providers.
DR DNASU; 84851; -.
DR Ensembl; ENST00000611618.1; ENSP00000483005.1; ENSG00000183718.6. [Q96A61-1]
DR GeneID; 84851; -.
DR KEGG; hsa:84851; -.
DR UCSC; uc003mnp.4; human. [Q96A61-1]
DR CTD; 84851; -.
DR DisGeNET; 84851; -.
DR GeneCards; TRIM52; -.
DR HGNC; HGNC:19024; TRIM52.
DR HPA; ENSG00000183718; Low tissue specificity.
DR MIM; 619265; gene.
DR neXtProt; NX_Q96A61; -.
DR OpenTargets; ENSG00000183718; -.
DR PharmGKB; PA134943216; -.
DR VEuPathDB; HostDB:ENSG00000183718; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154294; -.
DR HOGENOM; CLU_013137_6_2_1; -.
DR InParanoid; Q96A61; -.
DR OMA; SIHSKAY; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q96A61; -.
DR PathwayCommons; Q96A61; -.
DR SignaLink; Q96A61; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 84851; 27 hits in 1108 CRISPR screens.
DR ChiTaRS; TRIM52; human.
DR GenomeRNAi; 84851; -.
DR Pharos; Q96A61; Tdark.
DR PRO; PR:Q96A61; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q96A61; protein.
DR Bgee; ENSG00000183718; Expressed in buccal mucosa cell and 182 other tissues.
DR Genevisible; Q96A61; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
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; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
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 Alternative splicing; Antiviral defense; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway;
KW Zinc; Zinc-finger.
FT CHAIN 1..297
FT /note="E3 ubiquitin-protein ligase TRIM52"
FT /id="PRO_0000056280"
FT ZN_FING 20..62
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 222..263
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 72..167
FT /note="Important for rapid proteolytic degradation by the
FT proteasome"
FT /evidence="ECO:0000269|PubMed:31133683"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 272..286
FT /note="EIKLETTLVGILQIE -> VREMRECGGMKGVER (in isoform 2)"
FT /id="VSP_060452"
FT VAR_SEQ 287..297
FT /note="Missing (in isoform 2)"
FT /id="VSP_060453"
FT CONFLICT 130
FT /note="Missing (in Ref. 3; BAD92480)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 34653 MW; 13381ED57BDCC6AB CRC64;
MAGYATTPSP MQTLQEEAVC AICLDYFKDP VSISCGHNFC RGCVTQLWSK EDEEDQNEEE
DEWEEEEDEE AVGAMDGWDG SIREVLYRGN ADEELFQDQD DDELWLGDSG ITNWDNVDYM
WDEEEEEEEE DQDYYLGGLR PDLRIDVYRE EEILEAYDED EDEELYPDIH PPPSLPLPGQ
FTCPQCRKSF TRRSFRPNLQ LANMVQIIRQ MCPTPYRGNR SNDQGMCFKH QEALKLFCEV
DKEAICVVCR ESRSHKQHSV LPLEEVVQEY QEIKLETTLV GILQIEQESI HSKAYNQ
