TRI23_HUMAN
ID TRI23_HUMAN Reviewed; 574 AA.
AC P36406; Q9BZY4; Q9BZY5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM23;
DE EC=2.3.2.27;
DE AltName: Full=ADP-ribosylation factor domain-containing protein 1;
DE AltName: Full=GTP-binding protein ARD-1;
DE AltName: Full=RING finger protein 46;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM23 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 23;
GN Name=TRIM23; Synonyms=ARD1, ARFD1, RNF46;
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 ALPHA).
RX PubMed=8473324; DOI=10.1016/s0021-9258(18)52945-8;
RA Mishima K., Tsuchiya M., Nightingale M.S., Moss J., Vaughan M.;
RT "ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-
RT terminal ADP-ribosylation factor domain.";
RL J. Biol. Chem. 268:8801-8807(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC TISSUE=Brain;
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 SUBCELLULAR LOCATION.
RX PubMed=9671726; DOI=10.1073/pnas.95.15.8613;
RA Vitale N., Horiba K., Ferrans V.J., Moss J., Vaughan M.;
RT "Localization of ADP-ribosylation factor domain protein 1 (ARD1) in
RT lysosomes and Golgi apparatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8613-8618(1998).
RN [5]
RP INTERACTION WITH PSCD1, AND MUTAGENESIS OF THR-418 AND LYS-458.
RX PubMed=10748148; DOI=10.1074/jbc.m909642199;
RA Vitale N., Pacheco-Rodriguez G., Ferrans V.J., Riemenschneider W., Moss J.,
RA Vaughan M.;
RT "Specific functional interaction of human cytohesin-1 and ADP-ribosylation
RT factor domain protein (ARD1).";
RL J. Biol. Chem. 275:21331-21339(2000).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF CYS-34 AND HIS-53.
RX PubMed=15684077; DOI=10.1073/pnas.0409800102;
RA Vichi A., Payne D.M., Pacheco-Rodriguez G., Moss J., Vaughan M.;
RT "E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation
RT factor domain protein 1).";
RL Proc. Natl. Acad. Sci. U.S.A. 102:1945-1950(2005).
RN [7]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL144.
RX PubMed=19176615; DOI=10.1128/jvi.02072-08;
RA Poole E., Groves I., MacDonald A., Pang Y., Alcami A., Sinclair J.;
RT "Identification of TRIM23 as a cofactor involved in the regulation of NF-
RT kappaB by human cytomegalovirus.";
RL J. Virol. 83:3581-3590(2009).
RN [8]
RP FUNCTION, INTERACTION WITH TBK1 AND SQSTM1, AND SUBCELLULAR LOCATION.
RX PubMed=28871090; DOI=10.1038/s41564-017-0017-2;
RA Sparrer K.M.J., Gableske S., Zurenski M.A., Parker Z.M., Full F.,
RA Baumgart G.J., Kato J., Pacheco-Rodriguez G., Liang C., Pornillos O.,
RA Moss J., Vaughan M., Gack M.U.;
RT "TRIM23 mediates virus-induced autophagy via activation of TBK1.";
RL Nat. Microbiol. 2:1543-1557(2017).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 1-123, SUBUNIT, INTERACTION WITH
RP UBE2D2, AND DOMAIN.
RX PubMed=28681414; DOI=10.1002/prot.25348;
RA Dawidziak D.M., Sanchez J.G., Wagner J.M., Ganser-Pornillos B.K.,
RA Pornillos O.;
RT "Structure and catalytic activation of the TRIM23 RING E3 ubiquitin
RT ligase.";
RL Proteins 85:1957-1961(2017).
CC -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase. Plays an essential
CC role in autophagy activation during viral infection. Mechanistically,
CC activates TANK-binding kinase 1/TBK1 by facilitating its dimerization
CC and ability to phosphorylate the selective autophagy receptor SQSTM1.
CC In order to achieve this function, TRIM23 mediates 'Lys-27'-linked
CC auto-ubiquitination of its ADP-ribosylation factor (ARF) domain to
CC induce its GTPase activity and its recruitment to autophagosomes
CC (PubMed:28871090). {ECO:0000269|PubMed:15684077,
CC ECO:0000269|PubMed:28871090}.
CC -!- FUNCTION: (Microbial infection) Mediates TRAF6 auto-ubiquitination in
CC the presence of human cytomegalovirus protein UL144, resulting in the
CC virally controlled activation of NF-kappa-B stimulation at early times
CC of HCMV infection. {ECO:0000269|PubMed:15684077}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. Interacts with PSCD1. Interacts with UBE2D2
CC (PubMed:28681414). Interacts with TBK1 (via N-terminal kinase domain)
CC and p62/SQSTM1. {ECO:0000269|PubMed:10748148,
CC ECO:0000269|PubMed:28681414, ECO:0000269|PubMed:28871090}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC protein UL144; this interaction might cause autoubiquitination of
CC TRAF6, leading to NF-kappa-B activation. {ECO:0000269|PubMed:19176615}.
CC -!- INTERACTION:
CC P36406; A0A0S2Z3G1: ACTN4; NbExp=3; IntAct=EBI-740098, EBI-16430749;
CC P36406; Q96IX9: ANKRD36BP1; NbExp=3; IntAct=EBI-740098, EBI-744859;
CC P36406; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-740098, EBI-14493093;
CC P36406; Q9Y2T2: AP3M1; NbExp=3; IntAct=EBI-740098, EBI-2371151;
CC P36406; P29972: AQP1; NbExp=6; IntAct=EBI-740098, EBI-745213;
CC P36406; Q8N6T3: ARFGAP1; NbExp=3; IntAct=EBI-740098, EBI-716933;
CC P36406; Q9NR81: ARHGEF3; NbExp=5; IntAct=EBI-740098, EBI-10312733;
CC P36406; Q8N5M1: ATPAF2; NbExp=7; IntAct=EBI-740098, EBI-1166928;
CC P36406; P54253: ATXN1; NbExp=6; IntAct=EBI-740098, EBI-930964;
CC P36406; Q99933: BAG1; NbExp=5; IntAct=EBI-740098, EBI-1030678;
CC P36406; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-740098, EBI-1012434;
CC P36406; Q0VDD7: BRME1; NbExp=4; IntAct=EBI-740098, EBI-741210;
CC P36406; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-740098, EBI-739879;
CC P36406; Q9H7E9: C8orf33; NbExp=3; IntAct=EBI-740098, EBI-715389;
CC P36406; Q9H257: CARD9; NbExp=4; IntAct=EBI-740098, EBI-751319;
CC P36406; P55212: CASP6; NbExp=3; IntAct=EBI-740098, EBI-718729;
CC P36406; Q9HC52: CBX8; NbExp=3; IntAct=EBI-740098, EBI-712912;
CC P36406; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-740098, EBI-10961312;
CC P36406; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-740098, EBI-10247802;
CC P36406; Q86WR0: CCDC25; NbExp=3; IntAct=EBI-740098, EBI-2690264;
CC P36406; Q86Y33: CDC20B; NbExp=3; IntAct=EBI-740098, EBI-10260504;
CC P36406; Q6P1J9: CDC73; NbExp=3; IntAct=EBI-740098, EBI-930143;
CC P36406; Q01850: CDR2; NbExp=6; IntAct=EBI-740098, EBI-1181367;
CC P36406; Q96M91: CFAP53; NbExp=3; IntAct=EBI-740098, EBI-742422;
CC P36406; P10606: COX5B; NbExp=5; IntAct=EBI-740098, EBI-1053725;
CC P36406; Q9UBL6-2: CPNE7; NbExp=3; IntAct=EBI-740098, EBI-12012272;
CC P36406; Q02930-3: CREB5; NbExp=3; IntAct=EBI-740098, EBI-10192698;
CC P36406; Q16527: CSRP2; NbExp=3; IntAct=EBI-740098, EBI-2959737;
CC P36406; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-740098, EBI-5453285;
CC P36406; O95715: CXCL14; NbExp=3; IntAct=EBI-740098, EBI-2798068;
CC P36406; O43602: DCX; NbExp=3; IntAct=EBI-740098, EBI-8646694;
CC P36406; Q14565: DMC1; NbExp=3; IntAct=EBI-740098, EBI-930865;
CC P36406; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-740098, EBI-9679045;
CC P36406; Q92608: DOCK2; NbExp=3; IntAct=EBI-740098, EBI-448771;
CC P36406; Q96CJ1: EAF2; NbExp=3; IntAct=EBI-740098, EBI-1245604;
CC P36406; Q08426: EHHADH; NbExp=3; IntAct=EBI-740098, EBI-2339219;
CC P36406; O15371: EIF3D; NbExp=3; IntAct=EBI-740098, EBI-353818;
CC P36406; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-740098, EBI-744099;
CC P36406; O95208-2: EPN2; NbExp=3; IntAct=EBI-740098, EBI-12135243;
CC P36406; Q8N2X6: EXOC3-AS1; NbExp=3; IntAct=EBI-740098, EBI-749333;
CC P36406; Q9BQ89: FAM110A; NbExp=6; IntAct=EBI-740098, EBI-1752811;
CC P36406; Q8N9E0: FAM133A; NbExp=6; IntAct=EBI-740098, EBI-10268158;
CC P36406; Q96PV7-2: FAM193B; NbExp=3; IntAct=EBI-740098, EBI-10292648;
CC P36406; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-740098, EBI-1384254;
CC P36406; Q86YD7: FAM90A1; NbExp=6; IntAct=EBI-740098, EBI-6658203;
CC P36406; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-740098, EBI-10244131;
CC P36406; P22607: FGFR3; NbExp=3; IntAct=EBI-740098, EBI-348399;
CC P36406; Q8NFF5-2: FLAD1; NbExp=3; IntAct=EBI-740098, EBI-11526128;
CC P36406; C0H5X2: FLJ38668; NbExp=3; IntAct=EBI-740098, EBI-10176227;
CC P36406; A0A0S2Z4D9: GAD1; NbExp=3; IntAct=EBI-740098, EBI-16430771;
CC P36406; P23769: GATA2; NbExp=4; IntAct=EBI-740098, EBI-2806671;
CC P36406; P55040: GEM; NbExp=7; IntAct=EBI-740098, EBI-744104;
CC P36406; Q9NZ52-2: GGA3; NbExp=3; IntAct=EBI-740098, EBI-12075758;
CC P36406; Q8NEA9: GMCL2; NbExp=3; IntAct=EBI-740098, EBI-745707;
CC P36406; O95872: GPANK1; NbExp=7; IntAct=EBI-740098, EBI-751540;
CC P36406; Q92917: GPKOW; NbExp=4; IntAct=EBI-740098, EBI-746309;
CC P36406; Q14957: GRIN2C; NbExp=3; IntAct=EBI-740098, EBI-8285963;
CC P36406; P06396: GSN; NbExp=3; IntAct=EBI-740098, EBI-351506;
CC P36406; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-740098, EBI-11956675;
CC P36406; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-740098, EBI-2514791;
CC P36406; O14964: HGS; NbExp=3; IntAct=EBI-740098, EBI-740220;
CC P36406; O00291: HIP1; NbExp=3; IntAct=EBI-740098, EBI-473886;
CC P36406; P09067: HOXB5; NbExp=6; IntAct=EBI-740098, EBI-3893317;
CC P36406; P01112: HRAS; NbExp=3; IntAct=EBI-740098, EBI-350145;
CC P36406; P04792: HSPB1; NbExp=3; IntAct=EBI-740098, EBI-352682;
CC P36406; Q9UBY9: HSPB7; NbExp=3; IntAct=EBI-740098, EBI-739361;
CC P36406; Q14005-2: IL16; NbExp=3; IntAct=EBI-740098, EBI-17178971;
CC P36406; Q8NA54: IQUB; NbExp=7; IntAct=EBI-740098, EBI-10220600;
CC P36406; Q15040: JOSD1; NbExp=3; IntAct=EBI-740098, EBI-2510602;
CC P36406; O75564-2: JRK; NbExp=3; IntAct=EBI-740098, EBI-17181882;
CC P36406; Q92993: KAT5; NbExp=3; IntAct=EBI-740098, EBI-399080;
CC P36406; O60333-2: KIF1B; NbExp=3; IntAct=EBI-740098, EBI-10975473;
CC P36406; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-740098, EBI-2125614;
CC P36406; Q9P2K6: KLHL42; NbExp=6; IntAct=EBI-740098, EBI-739890;
CC P36406; P02538: KRT6A; NbExp=8; IntAct=EBI-740098, EBI-702198;
CC P36406; O95678: KRT75; NbExp=3; IntAct=EBI-740098, EBI-2949715;
CC P36406; Q01546: KRT76; NbExp=3; IntAct=EBI-740098, EBI-2952745;
CC P36406; Q14657: LAGE3; NbExp=3; IntAct=EBI-740098, EBI-1052105;
CC P36406; P13473-2: LAMP2; NbExp=3; IntAct=EBI-740098, EBI-21591415;
CC P36406; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-740098, EBI-726510;
CC P36406; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-740098, EBI-10274069;
CC P36406; O00214: LGALS8; NbExp=4; IntAct=EBI-740098, EBI-740058;
CC P36406; Q96FQ7: LINC00526; NbExp=3; IntAct=EBI-740098, EBI-10286106;
CC P36406; P25791: LMO2; NbExp=3; IntAct=EBI-740098, EBI-739696;
CC P36406; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-740098, EBI-11742507;
CC P36406; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-740098, EBI-739832;
CC P36406; Q8NDC4: MORN4; NbExp=6; IntAct=EBI-740098, EBI-10269566;
CC P36406; Q9BYD3: MRPL4; NbExp=3; IntAct=EBI-740098, EBI-721368;
CC P36406; Q9BRJ2: MRPL45; NbExp=3; IntAct=EBI-740098, EBI-2514313;
CC P36406; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-740098, EBI-10699187;
CC P36406; Q6P444: MTFR2; NbExp=3; IntAct=EBI-740098, EBI-10252703;
CC P36406; Q9P2K5-2: MYEF2; NbExp=3; IntAct=EBI-740098, EBI-10318831;
CC P36406; P52179-2: MYOM1; NbExp=3; IntAct=EBI-740098, EBI-12010196;
CC P36406; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-740098, EBI-744402;
CC P36406; Q15742: NAB2; NbExp=3; IntAct=EBI-740098, EBI-8641936;
CC P36406; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-740098, EBI-11746523;
CC P36406; Q9HC98: NEK6; NbExp=4; IntAct=EBI-740098, EBI-740364;
CC P36406; Q9UMS0: NFU1; NbExp=3; IntAct=EBI-740098, EBI-725252;
CC P36406; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-740098, EBI-12025760;
CC P36406; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-740098, EBI-741158;
CC P36406; O43809: NUDT21; NbExp=3; IntAct=EBI-740098, EBI-355720;
CC P36406; Q9NPJ8: NXT2; NbExp=3; IntAct=EBI-740098, EBI-752122;
CC P36406; O43189: PHF1; NbExp=4; IntAct=EBI-740098, EBI-530034;
CC P36406; O75928: PIAS2; NbExp=3; IntAct=EBI-740098, EBI-348555;
CC P36406; O00459: PIK3R2; NbExp=3; IntAct=EBI-740098, EBI-346930;
CC P36406; P78337: PITX1; NbExp=4; IntAct=EBI-740098, EBI-748265;
CC P36406; Q99569: PKP4; NbExp=3; IntAct=EBI-740098, EBI-726447;
CC P36406; Q9HB19: PLEKHA2; NbExp=3; IntAct=EBI-740098, EBI-4401947;
CC P36406; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-740098, EBI-10320765;
CC P36406; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-740098, EBI-11956563;
CC P36406; Q13356: PPIL2; NbExp=3; IntAct=EBI-740098, EBI-7705988;
CC P36406; Q5SWA1: PPP1R15B; NbExp=3; IntAct=EBI-740098, EBI-2815482;
CC P36406; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-740098, EBI-2557469;
CC P36406; Q99633: PRPF18; NbExp=3; IntAct=EBI-740098, EBI-2798416;
CC P36406; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-740098, EBI-1567797;
CC P36406; P25786: PSMA1; NbExp=5; IntAct=EBI-740098, EBI-359352;
CC P36406; P20618: PSMB1; NbExp=3; IntAct=EBI-740098, EBI-372273;
CC P36406; Q9BTL3: RAMAC; NbExp=6; IntAct=EBI-740098, EBI-744023;
CC P36406; P62826: RAN; NbExp=3; IntAct=EBI-740098, EBI-286642;
CC P36406; Q9UKA8: RCAN3; NbExp=3; IntAct=EBI-740098, EBI-9091952;
CC P36406; Q8N443: RIBC1; NbExp=3; IntAct=EBI-740098, EBI-10265323;
CC P36406; Q13671: RIN1; NbExp=3; IntAct=EBI-740098, EBI-366017;
CC P36406; Q63HN8-6: RNF213; NbExp=3; IntAct=EBI-740098, EBI-10248548;
CC P36406; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-740098, EBI-16428950;
CC P36406; Q7L4I2-2: RSRC2; NbExp=3; IntAct=EBI-740098, EBI-10256202;
CC P36406; Q14D33: RTP5; NbExp=3; IntAct=EBI-740098, EBI-10217913;
CC P36406; Q96T51-2: RUFY1; NbExp=3; IntAct=EBI-740098, EBI-12192715;
CC P36406; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-740098, EBI-748391;
CC P36406; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-740098, EBI-747035;
CC P36406; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-740098, EBI-10308083;
CC P36406; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-740098, EBI-747107;
CC P36406; P12236: SLC25A6; NbExp=3; IntAct=EBI-740098, EBI-356254;
CC P36406; Q9H0W8: SMG9; NbExp=6; IntAct=EBI-740098, EBI-2872322;
CC P36406; O95863: SNAI1; NbExp=7; IntAct=EBI-740098, EBI-1045459;
CC P36406; O43623: SNAI2; NbExp=3; IntAct=EBI-740098, EBI-9876238;
CC P36406; P14678-2: SNRPB; NbExp=3; IntAct=EBI-740098, EBI-372475;
CC P36406; P08579: SNRPB2; NbExp=3; IntAct=EBI-740098, EBI-1053651;
CC P36406; Q13573: SNW1; NbExp=3; IntAct=EBI-740098, EBI-632715;
CC P36406; O60504: SORBS3; NbExp=6; IntAct=EBI-740098, EBI-741237;
CC P36406; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-740098, EBI-742688;
CC P36406; B7ZLI8: STK19; NbExp=3; IntAct=EBI-740098, EBI-10176124;
CC P36406; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-740098, EBI-10175576;
CC P36406; Q9BSH4: TACO1; NbExp=3; IntAct=EBI-740098, EBI-747797;
CC P36406; Q13148: TARDBP; NbExp=3; IntAct=EBI-740098, EBI-372899;
CC P36406; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-740098, EBI-10172380;
CC P36406; Q9NU19: TBC1D22B; NbExp=8; IntAct=EBI-740098, EBI-8787464;
CC P36406; Q15560: TCEA2; NbExp=3; IntAct=EBI-740098, EBI-710310;
CC P36406; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-740098, EBI-11955057;
CC P36406; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-740098, EBI-11139477;
CC P36406; O43247-2: TEX33; NbExp=3; IntAct=EBI-740098, EBI-12093053;
CC P36406; Q0P5Q0: TMSB4X; NbExp=3; IntAct=EBI-740098, EBI-10226570;
CC P36406; P21580: TNFAIP3; NbExp=6; IntAct=EBI-740098, EBI-527670;
CC P36406; Q13077: TRAF1; NbExp=3; IntAct=EBI-740098, EBI-359224;
CC P36406; P36406: TRIM23; NbExp=7; IntAct=EBI-740098, EBI-740098;
CC P36406; Q0P6H7: TRIM29; NbExp=3; IntAct=EBI-740098, EBI-10226710;
CC P36406; Q14134: TRIM29; NbExp=4; IntAct=EBI-740098, EBI-702370;
CC P36406; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-740098, EBI-5235829;
CC P36406; Q9BYV6: TRIM55; NbExp=2; IntAct=EBI-740098, EBI-2341179;
CC P36406; Q12815: TROAP; NbExp=5; IntAct=EBI-740098, EBI-2349743;
CC P36406; Q7Z6J9: TSEN54; NbExp=3; IntAct=EBI-740098, EBI-2559824;
CC P36406; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-740098, EBI-9053916;
CC P36406; Q86UY0: TXNDC5; NbExp=3; IntAct=EBI-740098, EBI-2825190;
CC P36406; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-740098, EBI-10180829;
CC P36406; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-740098, EBI-741480;
CC P36406; O75604: USP2; NbExp=3; IntAct=EBI-740098, EBI-743272;
CC P36406; Q9Y2K6: USP20; NbExp=3; IntAct=EBI-740098, EBI-2511991;
CC P36406; Q9BRU9: UTP23; NbExp=3; IntAct=EBI-740098, EBI-5457544;
CC P36406; Q99990: VGLL1; NbExp=3; IntAct=EBI-740098, EBI-11983165;
CC P36406; Q64LD2: WDR25; NbExp=3; IntAct=EBI-740098, EBI-744560;
CC P36406; O76024: WFS1; NbExp=3; IntAct=EBI-740098, EBI-720609;
CC P36406; Q05516: ZBTB16; NbExp=3; IntAct=EBI-740098, EBI-711925;
CC P36406; Q9P1Z0: ZBTB4; NbExp=3; IntAct=EBI-740098, EBI-2564133;
CC P36406; Q53FD0: ZC2HC1C; NbExp=3; IntAct=EBI-740098, EBI-740767;
CC P36406; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-740098, EBI-14104088;
CC P36406; Q8N6M9: ZFAND2A; NbExp=3; IntAct=EBI-740098, EBI-3921109;
CC P36406; P17024: ZNF20; NbExp=3; IntAct=EBI-740098, EBI-717634;
CC P36406; P15622-3: ZNF250; NbExp=3; IntAct=EBI-740098, EBI-10177272;
CC P36406; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-740098, EBI-347633;
CC P36406; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-740098, EBI-740727;
CC P36406; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-740098, EBI-17269964;
CC P36406; Q8TBZ8: ZNF564; NbExp=6; IntAct=EBI-740098, EBI-10273713;
CC P36406; Q9P0T4: ZNF581; NbExp=8; IntAct=EBI-740098, EBI-745520;
CC P36406; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-740098, EBI-6427977;
CC P36406; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-740098, EBI-16429014;
CC P36406; A0A0S2Z6P0: ZNF688; NbExp=3; IntAct=EBI-740098, EBI-16429989;
CC P36406; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-740098, EBI-5667516;
CC P36406; P09022: Hoxa1; Xeno; NbExp=2; IntAct=EBI-740098, EBI-3957603;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28871090}.
CC Endomembrane system {ECO:0000269|PubMed:9671726}. Golgi apparatus
CC membrane {ECO:0000269|PubMed:9671726}. Lysosome membrane
CC {ECO:0000269|PubMed:9671726}. Note=Membrane-associated with the Golgi
CC complex and lysosomal structures.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Alpha;
CC IsoId=P36406-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=P36406-2; Sequence=VSP_000296;
CC Name=Gamma;
CC IsoId=P36406-3; Sequence=VSP_000297;
CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3
CC ubiquitin ligase activity. This domain is catalytically active as a
CC dimer. {ECO:0000269|PubMed:28681414}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the small GTPase
CC superfamily. Arf family. {ECO:0000305}.
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DR EMBL; L04510; AAA35940.1; -; mRNA.
DR EMBL; AF230397; AAG50176.1; -; mRNA.
DR EMBL; AF230398; AAG50177.1; -; mRNA.
DR EMBL; AF230399; AAG50178.1; -; mRNA.
DR EMBL; BC022510; AAH22510.1; -; mRNA.
DR CCDS; CCDS3986.1; -. [P36406-3]
DR CCDS; CCDS3987.1; -. [P36406-1]
DR CCDS; CCDS43322.1; -. [P36406-2]
DR PIR; A46054; A46054.
DR RefSeq; NP_001647.1; NM_001656.3. [P36406-1]
DR RefSeq; NP_150230.1; NM_033227.2. [P36406-2]
DR RefSeq; NP_150231.1; NM_033228.2. [P36406-3]
DR RefSeq; XP_016864933.1; XM_017009444.1. [P36406-2]
DR PDB; 5VZV; X-ray; 1.81 A; A/B/C=1-123.
DR PDB; 5VZW; X-ray; 2.28 A; F/G=1-123.
DR PDBsum; 5VZV; -.
DR PDBsum; 5VZW; -.
DR AlphaFoldDB; P36406; -.
DR SMR; P36406; -.
DR BioGRID; 106868; 243.
DR CORUM; P36406; -.
DR IntAct; P36406; 232.
DR MINT; P36406; -.
DR STRING; 9606.ENSP00000231524; -.
DR iPTMnet; P36406; -.
DR PhosphoSitePlus; P36406; -.
DR BioMuta; TRIM23; -.
DR DMDM; 543839; -.
DR EPD; P36406; -.
DR jPOST; P36406; -.
DR MassIVE; P36406; -.
DR MaxQB; P36406; -.
DR PaxDb; P36406; -.
DR PeptideAtlas; P36406; -.
DR PRIDE; P36406; -.
DR ProteomicsDB; 55200; -. [P36406-1]
DR ProteomicsDB; 55201; -. [P36406-2]
DR ProteomicsDB; 55202; -. [P36406-3]
DR Antibodypedia; 11584; 266 antibodies from 32 providers.
DR DNASU; 373; -.
DR Ensembl; ENST00000231524.14; ENSP00000231524.9; ENSG00000113595.15. [P36406-1]
DR Ensembl; ENST00000274327.11; ENSP00000274327.7; ENSG00000113595.15. [P36406-3]
DR Ensembl; ENST00000381018.7; ENSP00000370406.3; ENSG00000113595.15. [P36406-2]
DR GeneID; 373; -.
DR KEGG; hsa:373; -.
DR MANE-Select; ENST00000231524.14; ENSP00000231524.9; NM_001656.4; NP_001647.1.
DR UCSC; uc003jtw.4; human. [P36406-1]
DR CTD; 373; -.
DR DisGeNET; 373; -.
DR GeneCards; TRIM23; -.
DR HGNC; HGNC:660; TRIM23.
DR HPA; ENSG00000113595; Low tissue specificity.
DR MIM; 601747; gene.
DR neXtProt; NX_P36406; -.
DR OpenTargets; ENSG00000113595; -.
DR PharmGKB; PA24943; -.
DR VEuPathDB; HostDB:ENSG00000113595; -.
DR eggNOG; KOG0070; Eukaryota.
DR eggNOG; KOG4185; Eukaryota.
DR GeneTree; ENSGT00940000158562; -.
DR HOGENOM; CLU_033905_0_0_1; -.
DR InParanoid; P36406; -.
DR OMA; WHIQGSS; -.
DR OrthoDB; 1362554at2759; -.
DR PhylomeDB; P36406; -.
DR TreeFam; TF320703; -.
DR BRENDA; 2.3.2.27; 2681.
DR PathwayCommons; P36406; -.
DR SignaLink; P36406; -.
DR SIGNOR; P36406; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 373; 14 hits in 1121 CRISPR screens.
DR GeneWiki; TRIM23; -.
DR GenomeRNAi; 373; -.
DR Pharos; P36406; Tbio.
DR PRO; PR:P36406; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P36406; protein.
DR Bgee; ENSG00000113595; Expressed in cerebellar vermis and 188 other tissues.
DR ExpressionAtlas; P36406; baseline and differential.
DR Genevisible; P36406; HS.
DR GO; GO:0000139; C:Golgi membrane; IDA:HGNC-UCL.
DR GO; GO:0005765; C:lysosomal membrane; IDA:HGNC-UCL.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0019003; F:GDP binding; IDA:HGNC-UCL.
DR GO; GO:0005525; F:GTP binding; IDA:HGNC-UCL.
DR GO; GO:0003924; F:GTPase activity; IDA:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:HGNC-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:HGNC-UCL.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR024156; Small_GTPase_ARF.
DR InterPro; IPR006689; Small_GTPase_ARF/SAR.
DR InterPro; IPR027370; Znf-RING_LisH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11711; PTHR11711; 1.
DR Pfam; PF00025; Arf; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR PRINTS; PR00328; SAR1GTPBP.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00184; RING; 1.
DR SMART; SM00178; SAR; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51417; ARF; 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 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Golgi apparatus; GTP-binding; Host-virus interaction; Immunity;
KW Innate immunity; Lysosome; Membrane; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..574
FT /note="E3 ubiquitin-protein ligase TRIM23"
FT /id="PRO_0000207483"
FT ZN_FING 31..76
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 122..168
FT /note="B box-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 390..574
FT /note="ARF-like"
FT COILED 352..379
FT /evidence="ECO:0000255"
FT BINDING 411..418
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 454..458
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 513..516
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT VAR_SEQ 541..574
FT /note="WYIQGCDARSGMGLYEGLDWLSRQLVAAGVLDVA -> CFSDNM (in
FT isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_000297"
FT VAR_SEQ 551..574
FT /note="GMGLYEGLDWLSRQLVAAGVLDVA -> VFQIICDQYTGKEVVTEKG (in
FT isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_000296"
FT VARIANT 480
FT /note="D -> N (in dbSNP:rs34046496)"
FT /id="VAR_048320"
FT MUTAGEN 34
FT /note="C->A: Loss of E3 ubiquitin-protein ligase activity."
FT /evidence="ECO:0000269|PubMed:15684077"
FT MUTAGEN 53
FT /note="H->A: Loss of E3 ubiquitin-protein ligase activity."
FT /evidence="ECO:0000269|PubMed:15684077"
FT MUTAGEN 418
FT /note="T->N: Maintains GTPase activity. Increases
FT interaction with PSCD1."
FT /evidence="ECO:0000269|PubMed:10748148"
FT MUTAGEN 458
FT /note="K->I: Suppresses GTPase activity. Decreases
FT interaction with PSCD1."
FT /evidence="ECO:0000269|PubMed:10748148"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:5VZV"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:5VZV"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:5VZV"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5VZV"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:5VZV"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5VZV"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:5VZV"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:5VZV"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:5VZV"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:5VZV"
SQ SEQUENCE 574 AA; 64067 MW; CB85923B29BF0320 CRC64;
MATLVVNKLG AGVDSGRQGS RGTAVVKVLE CGVCEDVFSL QGDKVPRLLL CGHTVCHDCL
TRLPLHGRAI RCPFDRQVTD LGDSGVWGLK KNFALLELLE RLQNGPIGQY GAAEESIGIS
GESIIRCDED EAHLASVYCT VCATHLCSEC SQVTHSTKTL AKHRRVPLAD KPHEKTMCSQ
HQVHAIEFVC LEEGCQTSPL MCCVCKEYGK HQGHKHSVLE PEANQIRASI LDMAHCIRTF
TEEISDYSRK LVGIVQHIEG GEQIVEDGIG MAHTEHVPGT AENARSCIRA YFYDLHETLC
RQEEMALSVV DAHVREKLIW LRQQQEDMTI LLSEVSAACL HCEKTLQQDD CRVVLAKQEI
TRLLETLQKQ QQQFTEVADH IQLDASIPVT FTKDNRVHIG PKMEIRVVTL GLDGAGKTTI
LFKLKQDEFM QPIPTIGFNV ETVEYKNLKF TIWDVGGKHK LRPLWKHYYL NTQAVVFVVD
SSHRDRISEA HSELAKLLTE KELRDALLLI FANKQDVAGA LSVEEITELL SLHKLCCGRS
WYIQGCDARS GMGLYEGLDW LSRQLVAAGV LDVA
