TRI39_HUMAN
ID TRI39_HUMAN Reviewed; 518 AA.
AC Q9HCM9; Q5STG3; Q5STG4; Q76BL3; Q8IYT9; Q96IB6;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM39;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 23;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM39 {ECO:0000305};
DE AltName: Full=Testis-abundant finger protein;
DE AltName: Full=Tripartite motif-containing protein 39;
GN Name=TRIM39; Synonyms=RNF23, TFP;
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).
RC TISSUE=Testis;
RX PubMed=11006080; DOI=10.1006/bbrc.2000.3380;
RA Orimo A., Yamagishi T., Tominaga N., Yamauchi Y., Hishinuma T., Okada K.,
RA Suzuki M., Sato M., Nogi Y., Suzuki H., Inoue S., Yoshimura K., Shimizu Y.,
RA Muramatsu M.;
RT "Molecular cloning of testis-abundant finger protein/ring finger protein 23
RT (RNF23), a novel RING-B box-coiled coil-B30.2 protein on the class I region
RT of the human MHC.";
RL Biochem. Biophys. Res. Commun. 276:45-51(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Shiina T., Ota M., Katsuyama Y., Hashimoto N., Siamak B., Inoko H.;
RT "Genome diversity in HLA: a new strategy for detection of genetic
RT polymorphisms in expressed genes within the HLA class III and class I
RT regions.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Peripheral blood leukocyte;
RX PubMed=16702430; DOI=10.1534/genetics.106.057034;
RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M.,
RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K.,
RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A.,
RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T.,
RA Inoko H., Bahram S.;
RT "Rapid evolution of major histocompatibility complex class I genes in
RT primates generates new disease alleles in humans via hitchhiking
RT diversity.";
RL Genetics 173:1555-1570(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon, and Testis;
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 [9]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP MOAP1.
RX PubMed=19100260; DOI=10.1016/j.yexcr.2008.11.021;
RA Lee S.S., Fu N.Y., Sukumaran S.K., Wan K.F., Wan Q., Yu V.C.;
RT "TRIM39 is a MOAP-1-binding protein that stabilizes MOAP-1 through
RT inhibition of its poly-ubiquitination process.";
RL Exp. Cell Res. 315:1313-1325(2009).
RN [10]
RP FUNCTION, AND AUTOUBIQUITINATION.
RX PubMed=22529100; DOI=10.1083/jcb.201111141;
RA Huang N.J., Zhang L., Tang W., Chen C., Yang C.S., Kornbluth S.;
RT "The Trim39 ubiquitin ligase inhibits APC/CCdh1-mediated degradation of the
RT Bax activator MOAP-1.";
RL J. Cell Biol. 197:361-367(2012).
RN [11]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), FUNCTION (ISOFORMS 1 AND 2),
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND INTERACTION WITH CDKN1A
RP (ISOFORMS 1 AND 2).
RX PubMed=23213251; DOI=10.1073/pnas.1214156110;
RA Zhang L., Mei Y., Fu N.Y., Guan L., Xie W., Liu H.H., Yu C.D., Yin Z.,
RA Yu V.C., You H.;
RT "TRIM39 regulates cell cycle progression and DNA damage responses via
RT stabilizing p21.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:20937-20942(2012).
RN [12]
RP FUNCTION (ISOFORM 2), AND INTERACTION WITH CACTIN (ISOFORM 2).
RX PubMed=26363554; DOI=10.1007/s00018-015-2040-x;
RA Suzuki M., Watanabe M., Nakamaru Y., Takagi D., Takahashi H., Fukuda S.,
RA Hatakeyama S.;
RT "TRIM39 negatively regulates the NFkappaB-mediated signaling pathway
RT through stabilization of Cactin.";
RL Cell. Mol. Life Sci. 73:1085-1101(2016).
RN [13]
RP STRUCTURE BY NMR OF 104-143.
RG RIKEN structural genomics initiative (RSGI);
RT "One sequence two fold ? correct fold of the ZF-B-box domain from human
RT tripartite motif protein 39.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: [Isoform 1]: E3 ubiquitin-protein ligase (PubMed:22529100).
CC May facilitate apoptosis by inhibiting APC/C-Cdh1-mediated poly-
CC ubiquitination and subsequent proteasome-mediated degradation of the
CC pro-apoptotic protein MOAP1 (PubMed:19100260, PubMed:22529100).
CC Regulates the G1/S transition of the cell cycle and DNA damage-induced
CC G2 arrest by stabilizing CDKN1A/p21 (PubMed:23213251). Positively
CC regulates CDKN1A/p21 stability by competing with DTL for CDKN1A/p21
CC binding, therefore disrupting DCX(DTL) E3 ubiquitin ligase complex-
CC mediated CDKN1A/p21 ubiquitination and degradation (PubMed:23213251).
CC {ECO:0000269|PubMed:19100260, ECO:0000269|PubMed:22529100,
CC ECO:0000269|PubMed:23213251}.
CC -!- FUNCTION: [Isoform 2]: Regulates the G1/S transition of the cell cycle
CC and DNA damage-induced G2 arrest by stabilizing CDKN1A/p21
CC (PubMed:23213251). Positively regulates CDKN1A/p21 stability by
CC competing with DTL for CDKN1A/p21 binding, therefore disrupting
CC DCX(DTL) E3 ubiquitin ligase complex-mediated CDKN1A/p21 ubiquitination
CC and degradation (PubMed:23213251). Negatively regulates the canonical
CC NF-kappa-B signaling pathway via stabilization of CACTIN in an
CC ubiquitination-independent manner (PubMed:26363554).
CC {ECO:0000269|PubMed:23213251, ECO:0000269|PubMed:26363554}.
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: Isoform 1 interacts with MOAP1 (PubMed:19100260). Isoform 1
CC and isoform 2 interact with CDKN1A (PubMed:23213251). Isoform 2
CC interacts (via domain B box-type) with CACTIN (PubMed:26363554).
CC {ECO:0000269|PubMed:19100260, ECO:0000269|PubMed:23213251,
CC ECO:0000269|PubMed:26363554}.
CC -!- INTERACTION:
CC Q9HCM9; P24863: CCNC; NbExp=4; IntAct=EBI-739510, EBI-395261;
CC Q9HCM9; B2R886: DC-UbP; NbExp=3; IntAct=EBI-739510, EBI-10175550;
CC Q9HCM9; Q96GG9: DCUN1D1; NbExp=4; IntAct=EBI-739510, EBI-740086;
CC Q9HCM9; Q14689-6: DIP2A; NbExp=3; IntAct=EBI-739510, EBI-10233719;
CC Q9HCM9; Q14240: EIF4A2; NbExp=4; IntAct=EBI-739510, EBI-73473;
CC Q9HCM9; Q14240-2: EIF4A2; NbExp=3; IntAct=EBI-739510, EBI-10232522;
CC Q9HCM9; O15197-2: EPHB6; NbExp=3; IntAct=EBI-739510, EBI-10182490;
CC Q9HCM9; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-739510, EBI-739832;
CC Q9HCM9; Q9BS40: LXN; NbExp=3; IntAct=EBI-739510, EBI-1044504;
CC Q9HCM9; Q9BUE0: MED18; NbExp=3; IntAct=EBI-739510, EBI-394640;
CC Q9HCM9; P16333: NCK1; NbExp=2; IntAct=EBI-739510, EBI-389883;
CC Q9HCM9; Q9UNA4: POLI; NbExp=4; IntAct=EBI-739510, EBI-741774;
CC Q9HCM9; O43395: PRPF3; NbExp=4; IntAct=EBI-739510, EBI-744322;
CC Q9HCM9; P60900: PSMA6; NbExp=3; IntAct=EBI-739510, EBI-357793;
CC Q9HCM9; O00233: PSMD9; NbExp=4; IntAct=EBI-739510, EBI-750973;
CC Q9HCM9; Q6P9E2: RECK; NbExp=3; IntAct=EBI-739510, EBI-10253121;
CC Q9HCM9; A2RU48: SMCO3; NbExp=3; IntAct=EBI-739510, EBI-10173195;
CC Q9HCM9; Q9Y577: TRIM17; NbExp=8; IntAct=EBI-739510, EBI-743894;
CC Q9HCM9; P19474: TRIM21; NbExp=4; IntAct=EBI-739510, EBI-81290;
CC Q9HCM9; Q9HCM9: TRIM39; NbExp=6; IntAct=EBI-739510, EBI-739510;
CC Q9HCM9; Q5I0X7: TTC32; NbExp=3; IntAct=EBI-739510, EBI-8636434;
CC Q9HCM9; Q9BSL1: UBAC1; NbExp=3; IntAct=EBI-739510, EBI-749370;
CC Q9HCM9; P51668: UBE2D1; NbExp=6; IntAct=EBI-739510, EBI-743540;
CC Q9HCM9; P61077: UBE2D3; NbExp=6; IntAct=EBI-739510, EBI-348268;
CC Q9HCM9; Q9Y2X8: UBE2D4; NbExp=5; IntAct=EBI-739510, EBI-745527;
CC Q9HCM9; Q96LR5: UBE2E2; NbExp=6; IntAct=EBI-739510, EBI-2129763;
CC Q9HCM9; Q969T4: UBE2E3; NbExp=5; IntAct=EBI-739510, EBI-348496;
CC Q9HCM9; P61086: UBE2K; NbExp=3; IntAct=EBI-739510, EBI-473850;
CC Q9HCM9; Q9HAC8: UBTD1; NbExp=4; IntAct=EBI-739510, EBI-745871;
CC Q9HCM9; Q04323: UBXN1; NbExp=3; IntAct=EBI-739510, EBI-1058647;
CC Q9HCM9; Q9BZV1: UBXN6; NbExp=5; IntAct=EBI-739510, EBI-1993899;
CC Q9HCM9; Q8IZQ1-2: WDFY3; NbExp=3; IntAct=EBI-739510, EBI-10264625;
CC Q9HCM9; Q969J2: ZKSCAN4; NbExp=3; IntAct=EBI-739510, EBI-2818641;
CC Q9HCM9; P17031: ZNF26; NbExp=4; IntAct=EBI-739510, EBI-2841331;
CC Q9HCM9; A8K2R3; NbExp=3; IntAct=EBI-739510, EBI-9977437;
CC Q9HCM9-2; Q96GG9: DCUN1D1; NbExp=7; IntAct=EBI-11523450, EBI-740086;
CC Q9HCM9-2; O15197-2: EPHB6; NbExp=5; IntAct=EBI-11523450, EBI-10182490;
CC Q9HCM9-2; Q14353: GAMT; NbExp=5; IntAct=EBI-11523450, EBI-3909086;
CC Q9HCM9-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11523450, EBI-739832;
CC Q9HCM9-2; Q9BUE0: MED18; NbExp=3; IntAct=EBI-11523450, EBI-394640;
CC Q9HCM9-2; Q8N3F0: MTURN; NbExp=3; IntAct=EBI-11523450, EBI-11980301;
CC Q9HCM9-2; O43395: PRPF3; NbExp=8; IntAct=EBI-11523450, EBI-744322;
CC Q9HCM9-2; P60900: PSMA6; NbExp=5; IntAct=EBI-11523450, EBI-357793;
CC Q9HCM9-2; P20618: PSMB1; NbExp=3; IntAct=EBI-11523450, EBI-372273;
CC Q9HCM9-2; P54725: RAD23A; NbExp=3; IntAct=EBI-11523450, EBI-746453;
CC Q9HCM9-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-11523450, EBI-396669;
CC Q9HCM9-2; P19474: TRIM21; NbExp=3; IntAct=EBI-11523450, EBI-81290;
CC Q9HCM9-2; Q9HCM9-2: TRIM39; NbExp=3; IntAct=EBI-11523450, EBI-11523450;
CC Q9HCM9-2; P51668: UBE2D1; NbExp=5; IntAct=EBI-11523450, EBI-743540;
CC Q9HCM9-2; P62837: UBE2D2; NbExp=5; IntAct=EBI-11523450, EBI-347677;
CC Q9HCM9-2; P61077: UBE2D3; NbExp=5; IntAct=EBI-11523450, EBI-348268;
CC Q9HCM9-2; Q9Y2X8: UBE2D4; NbExp=7; IntAct=EBI-11523450, EBI-745527;
CC Q9HCM9-2; Q96LR5: UBE2E2; NbExp=8; IntAct=EBI-11523450, EBI-2129763;
CC Q9HCM9-2; Q969T4: UBE2E3; NbExp=3; IntAct=EBI-11523450, EBI-348496;
CC Q9HCM9-2; P61086: UBE2K; NbExp=8; IntAct=EBI-11523450, EBI-473850;
CC Q9HCM9-2; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-11523450, EBI-607755;
CC Q9HCM9-2; Q9HAC8: UBTD1; NbExp=5; IntAct=EBI-11523450, EBI-745871;
CC Q9HCM9-2; Q9BZV1: UBXN6; NbExp=3; IntAct=EBI-11523450, EBI-1993899;
CC Q9HCM9-2; O94888: UBXN7; NbExp=3; IntAct=EBI-11523450, EBI-1993627;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytosol
CC {ECO:0000269|PubMed:19100260}. Mitochondrion
CC {ECO:0000269|PubMed:19100260}. Nucleus {ECO:0000269|PubMed:23213251}.
CC Note=Found predominantly in the cytosol. Partial shift from the cytosol
CC to the mitochondria when colocalized with MOAP1. Colocalizes with
CC CDKN1A in the nucleus. {ECO:0000269|PubMed:19100260,
CC ECO:0000269|PubMed:23213251}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:23213251}. Note=Colocalizes with CDKN1A in the
CC nucleus. {ECO:0000269|PubMed:23213251}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=TIM39alpha {ECO:0000303|PubMed:23213251};
CC IsoId=Q9HCM9-1; Sequence=Displayed;
CC Name=2; Synonyms=TIM39beta {ECO:0000303|PubMed:23213251};
CC IsoId=Q9HCM9-2; Sequence=VSP_005755;
CC -!- TISSUE SPECIFICITY: Ubiquitous; highly expressed in brain, heart,
CC kidney, liver, skeletal muscle, spleen and testis.
CC {ECO:0000269|PubMed:19100260}.
CC -!- PTM: Autoubiquitinated. {ECO:0000269|PubMed:22529100}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AB046381; BAB16374.1; -; mRNA.
DR EMBL; BT007370; AAP36034.1; -; mRNA.
DR EMBL; AB110937; BAD13703.1; -; Genomic_DNA.
DR EMBL; AK292512; BAF85201.1; -; mRNA.
DR EMBL; AB110938; BAD13704.1; -; Genomic_DNA.
DR EMBL; AB202089; BAE78608.1; -; Genomic_DNA.
DR EMBL; AL662832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL662795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL773535; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX248580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX927214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03283.1; -; Genomic_DNA.
DR EMBL; CH471081; EAX03284.1; -; Genomic_DNA.
DR EMBL; BC007661; AAH07661.1; -; mRNA.
DR EMBL; BC034985; AAH34985.1; -; mRNA.
DR CCDS; CCDS34377.1; -. [Q9HCM9-1]
DR CCDS; CCDS34378.1; -. [Q9HCM9-2]
DR PIR; JC7387; JC7387.
DR RefSeq; NP_067076.2; NM_021253.3. [Q9HCM9-1]
DR RefSeq; NP_742013.1; NM_172016.2. [Q9HCM9-2]
DR PDB; 2DID; NMR; -; A=104-143.
DR PDB; 2DIF; NMR; -; A=104-143.
DR PDB; 2ECJ; NMR; -; A=19-69.
DR PDBsum; 2DID; -.
DR PDBsum; 2DIF; -.
DR PDBsum; 2ECJ; -.
DR AlphaFoldDB; Q9HCM9; -.
DR BMRB; Q9HCM9; -.
DR SMR; Q9HCM9; -.
DR BioGRID; 121170; 119.
DR IntAct; Q9HCM9; 79.
DR MINT; Q9HCM9; -.
DR STRING; 9606.ENSP00000365844; -.
DR iPTMnet; Q9HCM9; -.
DR PhosphoSitePlus; Q9HCM9; -.
DR BioMuta; TRIM39; -.
DR DMDM; 56405385; -.
DR EPD; Q9HCM9; -.
DR jPOST; Q9HCM9; -.
DR MassIVE; Q9HCM9; -.
DR MaxQB; Q9HCM9; -.
DR PaxDb; Q9HCM9; -.
DR PeptideAtlas; Q9HCM9; -.
DR PRIDE; Q9HCM9; -.
DR ProteomicsDB; 81768; -. [Q9HCM9-1]
DR ProteomicsDB; 81769; -. [Q9HCM9-2]
DR Antibodypedia; 34966; 280 antibodies from 30 providers.
DR DNASU; 56658; -.
DR Ensembl; ENST00000376656.8; ENSP00000365844.4; ENSG00000204599.15. [Q9HCM9-1]
DR Ensembl; ENST00000376659.9; ENSP00000365847.5; ENSG00000204599.15. [Q9HCM9-2]
DR Ensembl; ENST00000383601.6; ENSP00000373095.2; ENSG00000206495.12. [Q9HCM9-2]
DR Ensembl; ENST00000383602.6; ENSP00000373096.2; ENSG00000206495.12. [Q9HCM9-1]
DR Ensembl; ENST00000383603.8; ENSP00000373097.4; ENSG00000206495.12. [Q9HCM9-2]
DR Ensembl; ENST00000396547.5; ENSP00000379796.1; ENSG00000204599.15. [Q9HCM9-1]
DR Ensembl; ENST00000396548.5; ENSP00000379797.1; ENSG00000204599.15. [Q9HCM9-2]
DR Ensembl; ENST00000396551.8; ENSP00000379800.3; ENSG00000204599.15. [Q9HCM9-2]
DR Ensembl; ENST00000400644.5; ENSP00000383486.1; ENSG00000206495.12. [Q9HCM9-2]
DR Ensembl; ENST00000413715.5; ENSP00000411949.1; ENSG00000224994.10. [Q9HCM9-1]
DR Ensembl; ENST00000414015.6; ENSP00000401071.2; ENSG00000224994.10. [Q9HCM9-2]
DR Ensembl; ENST00000419790.6; ENSP00000401184.2; ENSG00000229929.10. [Q9HCM9-2]
DR Ensembl; ENST00000424575.5; ENSP00000409902.1; ENSG00000230308.10. [Q9HCM9-1]
DR Ensembl; ENST00000426469.5; ENSP00000397043.1; ENSG00000229929.10. [Q9HCM9-1]
DR Ensembl; ENST00000430502.5; ENSP00000398956.1; ENSG00000232839.10. [Q9HCM9-2]
DR Ensembl; ENST00000431272.6; ENSP00000396986.2; ENSG00000230308.10. [Q9HCM9-2]
DR Ensembl; ENST00000433900.6; ENSP00000389852.2; ENSG00000232839.10. [Q9HCM9-2]
DR Ensembl; ENST00000438076.5; ENSP00000389198.1; ENSG00000232839.10. [Q9HCM9-2]
DR Ensembl; ENST00000438859.5; ENSP00000411582.1; ENSG00000226437.10. [Q9HCM9-2]
DR Ensembl; ENST00000440117.5; ENSP00000392130.1; ENSG00000224994.10. [Q9HCM9-2]
DR Ensembl; ENST00000443109.5; ENSP00000414525.1; ENSG00000229929.10. [Q9HCM9-2]
DR Ensembl; ENST00000445206.5; ENSP00000391917.1; ENSG00000226437.10. [Q9HCM9-1]
DR Ensembl; ENST00000446397.5; ENSP00000412743.1; ENSG00000230308.10. [Q9HCM9-2]
DR Ensembl; ENST00000449318.5; ENSP00000404904.1; ENSG00000224994.10. [Q9HCM9-2]
DR Ensembl; ENST00000450778.6; ENSP00000387445.2; ENSG00000226437.10. [Q9HCM9-2]
DR Ensembl; ENST00000451132.5; ENSP00000394353.1; ENSG00000226437.10. [Q9HCM9-2]
DR Ensembl; ENST00000451715.5; ENSP00000398355.1; ENSG00000232839.10. [Q9HCM9-1]
DR Ensembl; ENST00000452705.5; ENSP00000415259.1; ENSG00000229929.10. [Q9HCM9-2]
DR Ensembl; ENST00000458607.5; ENSP00000404340.1; ENSG00000230308.10. [Q9HCM9-2]
DR Ensembl; ENST00000547030.3; ENSP00000449847.1; ENSG00000224994.10. [Q9HCM9-1]
DR Ensembl; ENST00000548002.1; ENSP00000447835.1; ENSG00000232839.10. [Q9HCM9-1]
DR Ensembl; ENST00000549841.3; ENSP00000448572.1; ENSG00000230308.10. [Q9HCM9-1]
DR Ensembl; ENST00000550282.5; ENSP00000449272.1; ENSG00000206495.12. [Q9HCM9-1]
DR Ensembl; ENST00000552337.2; ENSP00000450288.1; ENSG00000226437.10. [Q9HCM9-1]
DR Ensembl; ENST00000552520.2; ENSP00000448462.1; ENSG00000229929.10. [Q9HCM9-1]
DR GeneID; 56658; -.
DR KEGG; hsa:56658; -.
DR MANE-Select; ENST00000396551.9; ENSP00000379800.3; NM_001369521.2; NP_001356450.1. [Q9HCM9-2]
DR UCSC; uc003nqb.4; human. [Q9HCM9-1]
DR CTD; 56658; -.
DR DisGeNET; 56658; -.
DR GeneCards; TRIM39; -.
DR HGNC; HGNC:10065; TRIM39.
DR HPA; ENSG00000204599; Low tissue specificity.
DR MIM; 605700; gene.
DR neXtProt; NX_Q9HCM9; -.
DR OpenTargets; ENSG00000204599; -.
DR PharmGKB; PA35535; -.
DR VEuPathDB; HostDB:ENSG00000204599; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154126; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q9HCM9; -.
DR OMA; QLIAPLW; -.
DR PhylomeDB; Q9HCM9; -.
DR TreeFam; TF342569; -.
DR PathwayCommons; Q9HCM9; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9HCM9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 56658; 8 hits in 1116 CRISPR screens.
DR ChiTaRS; TRIM39; human.
DR EvolutionaryTrace; Q9HCM9; -.
DR GenomeRNAi; 56658; -.
DR Pharos; Q9HCM9; Tbio.
DR PRO; PR:Q9HCM9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9HCM9; protein.
DR Bgee; ENSG00000204599; Expressed in granulocyte and 101 other tissues.
DR ExpressionAtlas; Q9HCM9; baseline and differential.
DR Genevisible; Q9HCM9; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:1902806; P:regulation of cell cycle G1/S phase transition; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd13745; SPRY_PRY_TRIM39; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 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; IPR035033; PRY/SPRY_TRIM39.
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 Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 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; SSF49899; SSF49899; 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 3D-structure; Alternative splicing; Apoptosis; Cell cycle; Coiled coil;
KW Cytoplasm; Metal-binding; Mitochondrion; Nucleus; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..518
FT /note="E3 ubiquitin-protein ligase TRIM39"
FT /id="PRO_0000056257"
FT DOMAIN 319..514
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 29..70
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 102..143
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 268..337
FT /note="Interaction with CDKN1A"
FT /evidence="ECO:0000269|PubMed:23213251"
FT REGION 389..518
FT /note="Interaction with CDKN1A"
FT /evidence="ECO:0000269|PubMed:23213251"
FT COILED 181..250
FT /evidence="ECO:0000255"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 129
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 269..298
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_005755"
FT CONFLICT 137
FT /note="A -> P (in Ref. 1; BAB16374)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="E -> K (in Ref. 3; BAD13703)"
FT /evidence="ECO:0000305"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2ECJ"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:2ECJ"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:2DID"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:2DID"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2DID"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:2DID"
FT TURN 134..137
FT /evidence="ECO:0007829|PDB:2DID"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2DID"
SQ SEQUENCE 518 AA; 59690 MW; 2F946F518B217153 CRC64;
MAETSLLEAG ASAASTAAAL ENLQVEASCS VCLEYLKEPV IIECGHNFCK ACITRWWEDL
ERDFPCPVCR KTSRYRSLRP NRQLGSMVEI AKQLQAVKRK IRDESLCPQH HEALSLFCYE
DQEAVCLICA ISHTHRAHTV VPLDDATQEY KEKLQKCLEP LEQKLQEITR CKSSEEKKPG
ELKRLVESRR QQILREFEEL HRRLDEEQQV LLSRLEEEEQ DILQRLRENA AHLGDKRRDL
AHLAAEVEGK CLQSGFEMLK DVKSTLEKNI PRKFGGSLST ICPRDHKALL GLVKEINRCE
KVKTMEVTSV SIELEKNFSN FPRQYFALRK ILKQLIADVT LDPETAHPNL VLSEDRKSVK
FVETRLRDLP DTPRRFTFYP CVLATEGFTS GRHYWEVEVG DKTHWAVGVC RDSVSRKGEL
TPLPETGYWR VRLWNGDKYA ATTTPFTPLH IKVKPKRVGI FLDYEAGTLS FYNVTDRSHI
YTFTDTFTEK LWPLFYPGIR AGRKNAAPLT IRPPTDWE
