ID   TRI60_HUMAN             Reviewed;         471 AA.
AC   Q495X7; Q8NA35;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   24-JAN-2024, entry version 133.
DE   RecName: Full=Tripartite motif-containing protein 60;
DE   AltName: Full=RING finger protein 129;
DE   AltName: Full=RING finger protein 33;
GN   Name=TRIM60; Synonyms=RNF129, RNF33;
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 [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   FUNCTION.
RX   PubMed=33184450; DOI=10.1038/s41423-020-00564-w;
RA   Gu Z., Chen X., Yang W., Qi Y., Yu H., Wang X., Gong Y., Chen Q., Zhong B.,
RA   Dai L., Qi S., Zhang Z., Zhang H., Hu H.;
RT   "The SUMOylation of TAB2 mediated by TRIM60 inhibits MAPK/NF-kappaB
RT   activation and the innate immune response.";
RL   Cell. Mol. Immunol. 18:1981-1994(2021).
CC   -!- FUNCTION: E3 SUMO-protein ligase that mediates SUMOylation of TAB2
CC       leading to inhibition of NF-kappa-B and MAPK pathways by suppressing
CC       the TRAF6/TAB2/TAK1 complex. {ECO:0000269|PubMed:33184450}.
CC   -!- INTERACTION:
CC       Q495X7; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-13576620, EBI-739832;
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR   EMBL; AK093201; BAC04093.1; -; mRNA.
DR   EMBL; BC100983; AAI00984.1; -; mRNA.
DR   EMBL; BC100984; AAI00985.1; -; mRNA.
DR   EMBL; BC100985; AAI00986.1; -; mRNA.
DR   EMBL; BC100986; AAI00987.1; -; mRNA.
DR   CCDS; CCDS3808.1; -.
DR   RefSeq; NP_001244954.1; NM_001258025.1.
DR   RefSeq; NP_689833.1; NM_152620.2.
DR   RefSeq; XP_011529985.1; XM_011531683.2.
DR   AlphaFoldDB; Q495X7; -.
DR   SMR; Q495X7; -.
DR   BioGRID; 127931; 5.
DR   IntAct; Q495X7; 1.
DR   STRING; 9606.ENSP00000497401; -.
DR   iPTMnet; Q495X7; -.
DR   PhosphoSitePlus; Q495X7; -.
DR   SwissPalm; Q495X7; -.
DR   BioMuta; TRIM60; -.
DR   DMDM; 114154820; -.
DR   MassIVE; Q495X7; -.
DR   PaxDb; 9606-ENSP00000421142; -.
DR   PeptideAtlas; Q495X7; -.
DR   Antibodypedia; 28289; 54 antibodies from 15 providers.
DR   DNASU; 166655; -.
DR   Ensembl; ENST00000341062.6; ENSP00000343765.5; ENSG00000176979.14.
DR   Ensembl; ENST00000508504.1; ENSP00000426496.1; ENSG00000176979.14.
DR   Ensembl; ENST00000512596.6; ENSP00000421142.1; ENSG00000176979.14.
DR   Ensembl; ENST00000647760.1; ENSP00000497401.1; ENSG00000176979.14.
DR   GeneID; 166655; -.
DR   KEGG; hsa:166655; -.
DR   MANE-Select; ENST00000512596.6; ENSP00000421142.1; NM_152620.3; NP_689833.1.
DR   UCSC; uc003iqy.2; human.
DR   AGR; HGNC:21162; -.
DR   CTD; 166655; -.
DR   DisGeNET; 166655; -.
DR   GeneCards; TRIM60; -.
DR   HGNC; HGNC:21162; TRIM60.
DR   HPA; ENSG00000176979; Group enriched (placenta, testis).
DR   MIM; 619416; gene.
DR   neXtProt; NX_Q495X7; -.
DR   OpenTargets; ENSG00000176979; -.
DR   PharmGKB; PA134909634; -.
DR   VEuPathDB; HostDB:ENSG00000176979; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000155329; -.
DR   HOGENOM; CLU_013137_0_3_1; -.
DR   InParanoid; Q495X7; -.
DR   OMA; GNKPKWT; -.
DR   OrthoDB; 3453019at2759; -.
DR   PhylomeDB; Q495X7; -.
DR   TreeFam; TF338674; -.
DR   PathwayCommons; Q495X7; -.
DR   SignaLink; Q495X7; -.
DR   SIGNOR; Q495X7; -.
DR   BioGRID-ORCS; 166655; 11 hits in 1180 CRISPR screens.
DR   ChiTaRS; TRIM60; human.
DR   GenomeRNAi; 166655; -.
DR   Pharos; Q495X7; Tdark.
DR   PRO; PR:Q495X7; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q495X7; Protein.
DR   Bgee; ENSG00000176979; Expressed in primordial germ cell in gonad and 6 other cell types or tissues.
DR   ExpressionAtlas; Q495X7; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0140082; F:SUMO-ubiquitin ligase activity; IDA:UniProt.
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:1901223; P:negative regulation of non-canonical NF-kappaB signal transduction; IDA:UniProt.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   CDD; cd19791; Bbox2_TRIM60-like; 1.
DR   CDD; cd16607; RING-HC_TRIM60-like_C-IV; 1.
DR   CDD; cd15828; SPRY_PRY_TRIM60; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR035786; SPRY/PRY_TRIM60.
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   PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR   PANTHER; PTHR24103:SF304; TRIPARTITE MOTIF-CONTAINING PROTEIN 60; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF15227; zf-C3HC4_4; 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; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 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   1: Evidence at protein level;
KW   Coiled coil; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..471
FT                   /note="Tripartite motif-containing protein 60"
FT                   /id="PRO_0000249189"
FT   DOMAIN          277..470
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         16..57
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         92..133
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   COILED          171..223
FT                   /evidence="ECO:0000255"
FT   BINDING         97
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         100
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         125
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   CONFLICT        445
FT                   /note="T -> I (in Ref. 2; AAI00986)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   471 AA;  55114 MW;  6E1E8986BBFC9238 CRC64;
     MEFVTALVNL QEESSCPICL EYLKDPVTIN CGHNFCRSCL SVSWKDLDDT FPCPVCRFCF
     PYKSFRRNPQ LRNLTEIAKQ LQIRRSKRKR QKENAMCEKH NQFLTLFCVK DLEILCTQCS
     FSTKHQKHYI CPIKKAASYH REILEGSLEP LRNNIERVEK VIILQGSKSV ELKKKVEYKR
     EEINSEFEQI RLFLQNEQEM ILRQIQDEEM NILAKLNENL VELSDYVSTL KHLLREVEGK
     SVQSNLELLT QAKSMHHKYQ NLKCPELFSF RLTKYGFSLP PQYSGLDRII KPFQVDVILD
     LNTAHPQLLV SEDRKAVRYE RKKRNICYDP RRFYVCPAVL GSQRFSSGRH YWEVEVGNKP
     KWILGVCQDC LLRNWQDQPS VLGGFWAIGR YMKSGYVASG PKTTQLLPVV KPSKIGIFLD
     YELGDLSFYN MNDRSILYTF NDCFTEAVWP YFYTGTDSEP LKICSVSDSE R
//