TRI37_HUMAN
ID TRI37_HUMAN Reviewed; 964 AA.
AC O94972; A8K0V9; A8K8U4; A8MZ79; B4DGZ3; F8WEE6; Q7Z3E6; Q8IYF7; Q8WYF7;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM37 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000269|PubMed:15885686};
DE AltName: Full=Mulibrey nanism protein {ECO:0000303|PubMed:10888877};
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM37 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 37 {ECO:0000305};
GN Name=TRIM37 {ECO:0000312|HGNC:HGNC:7523};
GN Synonyms=KIAA0898, MUL {ECO:0000303|PubMed:10888877},
GN POB1 {ECO:0000303|PubMed:12754710};
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).
RA Wu G., Couch F.J.;
RT "Gene POB1 is amplified and overexpressed in human breast cancer.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-108.
RC TISSUE=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 [8]
RP INVOLVEMENT IN MUL, AND TISSUE SPECIFICITY.
RX PubMed=10888877; DOI=10.1038/77053;
RA Avela K., Lipsanen-Nyman M., Idanheimo N., Seemanova E., Rosengren S.,
RA Makela T.P., Perheentupa J., Chapelle A.D., Lehesjoki A.E.;
RT "Gene encoding a new RING-B-box-coiled-coil protein is mutated in mulibrey
RT nanism.";
RL Nat. Genet. 25:298-301(2000).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11938494; DOI=10.1086/340256;
RA Kallijarvi J., Avela K., Lipsanen-Nyman M., Ulmanen I., Lehesjoki A.E.;
RT "The TRIM37 gene encodes a peroxisomal RING-B-box-coiled-coil protein:
RT classification of mulibrey nanism as a new peroxisomal disorder.";
RL Am. J. Hum. Genet. 70:1215-1228(2002).
RN [10]
RP INVOLVEMENT IN MUL.
RX PubMed=12754710; DOI=10.1002/humu.10220;
RA Jagiello P., Hammans C., Wieczorek S., Arning L., Stefanski A., Strehl H.,
RA Epplen J.T., Gencik M.;
RT "A novel splice site mutation in the TRIM37 gene causes mulibrey nanism in
RT a Turkish family with phenotypic heterogeneity.";
RL Hum. Mutat. 21:630-635(2003).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AUTOUBIQUITINATION, MUTAGENESIS OF
RP 35-CYS-CYS-36, PATHWAY, VARIANT MUL PRO-76, AND CHARACTERIZATION OF
RP VARIANTS MUL PRO-76 AND MUL VAL-322.
RX PubMed=15885686; DOI=10.1016/j.yexcr.2005.04.001;
RA Kallijaervi J., Lahtinen U., Haemaelaeinen R., Lipsanen-Nyman M.,
RA Palvimo J.J., Lehesjoki A.-E.;
RT "TRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3
RT ligase.";
RL Exp. Cell Res. 308:146-155(2005).
RN [12]
RP TISSUE SPECIFICITY.
RX PubMed=16310976; DOI=10.1016/j.gene.2005.08.008;
RA Hamalainen R.H., Joensuu T., Kallijarvi J., Lehesjoki A.E.;
RT "Characterisation of the mulibrey nanism-associated TRIM37 gene:
RT transcription initiation, promoter region and alternative splicing.";
RL Gene 366:180-188(2006).
RN [13]
RP INVOLVEMENT IN MUL.
RX PubMed=17551331; DOI=10.1097/mcd.0b013e3280f6d00b;
RA Doganc T., Yuksel Konuk B.E., Alpan N., Konuk O., Hamalainen R.H.,
RA Lehesjoki A.E., Tekin M.;
RT "A novel mutation in TRIM37 is associated with mulibrey nanism in a Turkish
RT boy.";
RL Clin. Dysmorphol. 16:173-176(2007).
RN [14]
RP INVOLVEMENT IN MUL.
RX PubMed=21865362; DOI=10.1210/jc.2011-1493;
RA Karlberg S., Toppari J., Karlberg N., Nurmio M., Karikoski R., Jalanko H.,
RA Lipsanen-Nyman M.;
RT "Testicular failure and male infertility in the monogenic Mulibrey nanism
RT disorder.";
RL J. Clin. Endocrinol. Metab. 96:3399-3407(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23769972; DOI=10.1016/j.devcel.2013.05.016;
RA Balestra F.R., Strnad P., Fluckiger I., Gonczy P.;
RT "Discovering regulators of centriole biogenesis through siRNA-based
RT functional genomics in human cells.";
RL Dev. Cell 25:555-571(2013).
RN [17]
RP INVOLVEMENT IN MUL.
RX PubMed=23385855; DOI=10.1007/s00431-013-1962-2;
RA Kumpf M., Hamalainen R.H., Hofbeck M., Baden W.;
RT "Refractory congestive heart failure following delayed pericardectomy in a
RT 12-year-old child with Mulibrey nanism due to a novel mutation in TRIM37.";
RL Eur. J. Pediatr. 172:1415-1418(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [19]
RP FUNCTION.
RX PubMed=24317724; DOI=10.1099/vir.0.057653-0;
RA Tabah A.A., Tardif K., Mansky L.M.;
RT "Anti-HIV-1 activity of Trim 37.";
RL J. Gen. Virol. 95:960-967(2014).
RN [20]
RP FUNCTION, PATHWAY, SUBUNIT, INDUCTION, AND MUTAGENESIS OF CYS-18.
RX PubMed=25470042; DOI=10.1038/nature13955;
RA Bhatnagar S., Gazin C., Chamberlain L., Ou J., Zhu X., Tushir J.S.,
RA Virbasius C.M., Lin L., Zhu L.J., Wajapeyee N., Green M.R.;
RT "TRIM37 is a new histone H2A ubiquitin ligase and breast cancer
RT oncoprotein.";
RL Nature 516:116-120(2014).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 1-90.
RG Northeast structural genomics consortium (NESG);
RT "E3 ubiquitin-protein ligase ring domain from human hr4604d.";
RL Submitted (MAR-2010) to the PDB data bank.
RN [22]
RP VARIANT MUL VAL-322, AND CHARACTERIZATION OF VARIANT MUL VAR-322.
RX PubMed=15108285; DOI=10.1002/humu.9233;
RA Haemaelaeinen R.H., Avela K., Lambert J.A., Kallijaervi J., Eyaid W.,
RA Gronau J., Ignaszewski A.P., McFadden D., Sorge G., Lipsanen-Nyman M.,
RA Lehesjoki A.E.;
RT "Novel mutations in the TRIM37 gene in Mulibrey Nanism.";
RL Hum. Mutat. 23:522-522(2004).
RN [23]
RP VARIANT MUL SER-109, AND CHARACTERIZATION OF VARIANT MUL SER-109.
RX PubMed=17100991; DOI=10.1111/j.1399-0004.2006.00700.x;
RA Haemaelaeinen R.H., Mowat D., Gabbett M.T., O'brien T.A., Kallijaervi J.,
RA Lehesjoki A.-E.;
RT "Wilms' tumor and novel TRIM37 mutations in an Australian patient with
RT mulibrey nanism.";
RL Clin. Genet. 70:473-479(2006).
RN [24]
RP VARIANT ARG-432.
RX PubMed=26697951; DOI=10.1002/ajmg.a.37515;
RA Rohena L., Lawson M., Guzman E., Ganapathi M., Cho M.T., Haverfield E.,
RA Anyane-Yeboa K.;
RT "FTO variant associated with malformation syndrome.";
RL Am. J. Med. Genet. A 170:1023-1028(2016).
CC -!- FUNCTION: E3 ubiquitin-protein ligase required to prevent centriole
CC reduplication (PubMed:15885686, PubMed:23769972). Probably acts by
CC ubiquitinating positive regulators of centriole reduplication
CC (PubMed:23769972). Mediates monoubiquitination of 'Lys-119' of histone
CC H2A (H2AK119Ub), a specific tag for epigenetic transcriptional
CC repression: associates with some Polycomb group (PcG) multiprotein
CC PRC2-like complex and mediates repression of target genes
CC (PubMed:25470042). Has anti-HIV activity (PubMed:24317724).
CC {ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:23769972,
CC ECO:0000269|PubMed:24317724, ECO:0000269|PubMed:25470042}.
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:15885686};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:25470042}.
CC -!- SUBUNIT: Associates with the PRC2/EED-EZH2 complex.
CC {ECO:0000269|PubMed:25470042}.
CC -!- INTERACTION:
CC O94972; P29972: AQP1; NbExp=3; IntAct=EBI-741602, EBI-745213;
CC O94972; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-741602, EBI-16429430;
CC O94972; O15169: AXIN1; NbExp=3; IntAct=EBI-741602, EBI-710484;
CC O94972; Q13895: BYSL; NbExp=9; IntAct=EBI-741602, EBI-358049;
CC O94972; Q86Y33: CDC20B; NbExp=3; IntAct=EBI-741602, EBI-10260504;
CC O94972; Q86Y33-5: CDC20B; NbExp=3; IntAct=EBI-741602, EBI-11983537;
CC O94972; O00311: CDC7; NbExp=3; IntAct=EBI-741602, EBI-374980;
CC O94972; Q8IVW4: CDKL3; NbExp=3; IntAct=EBI-741602, EBI-3919850;
CC O94972; P53618: COPB1; NbExp=4; IntAct=EBI-741602, EBI-359063;
CC O94972; Q2TBE0: CWF19L2; NbExp=6; IntAct=EBI-741602, EBI-5453285;
CC O94972; P26196: DDX6; NbExp=3; IntAct=EBI-741602, EBI-351257;
CC O94972; O60941-5: DTNB; NbExp=3; IntAct=EBI-741602, EBI-11984733;
CC O94972; Q8IYY4: DZIP1L; NbExp=3; IntAct=EBI-741602, EBI-10264440;
CC O94972; Q14241: ELOA; NbExp=3; IntAct=EBI-741602, EBI-742350;
CC O94972; O95990-3: FAM107A; NbExp=3; IntAct=EBI-741602, EBI-10192902;
CC O94972; Q3B820: FAM161A; NbExp=3; IntAct=EBI-741602, EBI-719941;
CC O94972; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-741602, EBI-742802;
CC O94972; Q92993: KAT5; NbExp=3; IntAct=EBI-741602, EBI-399080;
CC O94972; Q96EZ8: MCRS1; NbExp=4; IntAct=EBI-741602, EBI-348259;
CC O94972; Q96T60: PNKP; NbExp=4; IntAct=EBI-741602, EBI-1045072;
CC O94972; O43663: PRC1; NbExp=3; IntAct=EBI-741602, EBI-741137;
CC O94972; Q9Y272: RASD1; NbExp=3; IntAct=EBI-741602, EBI-740818;
CC O94972; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-741602, EBI-16428950;
CC O94972; P32969: RPL9P9; NbExp=3; IntAct=EBI-741602, EBI-358122;
CC O94972; P28702-3: RXRB; NbExp=3; IntAct=EBI-741602, EBI-16429492;
CC O94972; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-741602, EBI-748391;
CC O94972; Q9Y2D8: SSX2IP; NbExp=4; IntAct=EBI-741602, EBI-2212028;
CC O94972; Q96C24: SYTL4; NbExp=3; IntAct=EBI-741602, EBI-747142;
CC O94972; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-741602, EBI-11955057;
CC O94972; P57075: UBASH3A; NbExp=3; IntAct=EBI-741602, EBI-2105393;
CC O94972; O43167: ZBTB24; NbExp=3; IntAct=EBI-741602, EBI-744471;
CC O94972; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-741602, EBI-2682299;
CC O94972; Q86UD4: ZNF329; NbExp=3; IntAct=EBI-741602, EBI-7233259;
CC O94972; Q8TAU3: ZNF417; NbExp=4; IntAct=EBI-741602, EBI-740727;
CC O94972; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-741602, EBI-6427977;
CC O94972; A8K932; NbExp=3; IntAct=EBI-741602, EBI-10174671;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:15885686}. Peroxisome
CC {ECO:0000269|PubMed:11938494}. Note=Found in vesicles of the
CC peroxisome. Aggregates as aggresomes, a perinuclear region where
CC certain misfolded or aggregated proteins are sequestered for
CC proteasomal degradation. {ECO:0000269|PubMed:15885686}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=TRIM37a {ECO:0000303|PubMed:16310976}, TRIM37b
CC {ECO:0000303|PubMed:16310976};
CC IsoId=O94972-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94972-2; Sequence=VSP_011919, VSP_011920;
CC Name=3;
CC IsoId=O94972-3; Sequence=VSP_057468;
CC -!- TISSUE SPECIFICITY: Ubiquitous (PubMed:10888877). Highly expressed in
CC testis, while it is weakly expressed in other tissues
CC (PubMed:16310976). {ECO:0000269|PubMed:10888877,
CC ECO:0000269|PubMed:16310976}.
CC -!- INDUCTION: Overexpressed in a number of breast cancer cell lines.
CC {ECO:0000269|PubMed:25470042}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:15885686}.
CC -!- DISEASE: Mulibrey nanism (MUL) [MIM:253250]: An autosomal recessive
CC growth disorder characterized by severe growth failure of prenatal
CC onset, constrictive pericardium and progressive cardiomyopathy, facial
CC dysmorphism, and failure of sexual maturation. Additional clinical
CC features include hepatomegaly, muscle hypotonia, J-shaped sella
CC turcica, yellowish dots in the ocular fundi, hypoplasia of various
CC endocrine glands, insulin resistance with type 2 diabetes, and an
CC increased risk for Wilms' tumor. {ECO:0000269|PubMed:10888877,
CC ECO:0000269|PubMed:12754710, ECO:0000269|PubMed:15108285,
CC ECO:0000269|PubMed:15885686, ECO:0000269|PubMed:17100991,
CC ECO:0000269|PubMed:17551331, ECO:0000269|PubMed:21865362,
CC ECO:0000269|PubMed:23385855}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Acts as a proto-oncogene via its ability to
CC monoubiquinate 'Lys-119' of histone H2A (H2AK119Ub): overexpressed in a
CC number of breast cancers and promotes transformation of cells by
CC mediating silencing of tumor suppressor genes (PubMed:25470042).
CC {ECO:0000269|PubMed:25470042}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74921.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TRIM37ID42703ch17q23.html";
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DR EMBL; AF213365; AAL36460.1; -; mRNA.
DR EMBL; AB020705; BAA74921.1; ALT_INIT; mRNA.
DR EMBL; AK289674; BAF82363.1; -; mRNA.
DR EMBL; AK294850; BAG57954.1; -; mRNA.
DR EMBL; AK292459; BAF85148.1; -; mRNA.
DR EMBL; BX537955; CAD97922.1; -; mRNA.
DR EMBL; AC005207; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC036154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC100832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94425.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94426.1; -; Genomic_DNA.
DR EMBL; BC036012; AAH36012.1; -; mRNA.
DR CCDS; CCDS32694.1; -. [O94972-1]
DR CCDS; CCDS45746.1; -. [O94972-1]
DR CCDS; CCDS82174.1; -. [O94972-3]
DR RefSeq; NP_001005207.1; NM_001005207.3. [O94972-1]
DR RefSeq; NP_001307916.1; NM_001320987.1. [O94972-3]
DR RefSeq; NP_001307919.1; NM_001320990.1. [O94972-2]
DR RefSeq; NP_056109.1; NM_015294.4. [O94972-1]
DR PDB; 3LRQ; X-ray; 2.29 A; A/B/C/D=1-90.
DR PDBsum; 3LRQ; -.
DR AlphaFoldDB; O94972; -.
DR SMR; O94972; -.
DR BioGRID; 110678; 631.
DR DIP; DIP-34437N; -.
DR IntAct; O94972; 85.
DR MINT; O94972; -.
DR STRING; 9606.ENSP00000262294; -.
DR GlyGen; O94972; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; O94972; -.
DR PhosphoSitePlus; O94972; -.
DR BioMuta; TRIM37; -.
DR EPD; O94972; -.
DR jPOST; O94972; -.
DR MassIVE; O94972; -.
DR MaxQB; O94972; -.
DR PaxDb; O94972; -.
DR PeptideAtlas; O94972; -.
DR PRIDE; O94972; -.
DR ProteomicsDB; 31814; -.
DR ProteomicsDB; 50590; -. [O94972-1]
DR ProteomicsDB; 50591; -. [O94972-2]
DR Antibodypedia; 31047; 232 antibodies from 29 providers.
DR DNASU; 4591; -.
DR Ensembl; ENST00000262294.12; ENSP00000262294.7; ENSG00000108395.14. [O94972-1]
DR Ensembl; ENST00000393065.6; ENSP00000376784.2; ENSG00000108395.14. [O94972-3]
DR Ensembl; ENST00000393066.7; ENSP00000376785.3; ENSG00000108395.14. [O94972-1]
DR GeneID; 4591; -.
DR KEGG; hsa:4591; -.
DR MANE-Select; ENST00000262294.12; ENSP00000262294.7; NM_015294.6; NP_056109.1.
DR UCSC; uc002iwy.5; human. [O94972-1]
DR UCSC; uc010woc.3; human.
DR CTD; 4591; -.
DR DisGeNET; 4591; -.
DR GeneCards; TRIM37; -.
DR HGNC; HGNC:7523; TRIM37.
DR HPA; ENSG00000108395; Tissue enhanced (testis).
DR MalaCards; TRIM37; -.
DR MIM; 253250; phenotype.
DR MIM; 605073; gene.
DR neXtProt; NX_O94972; -.
DR OpenTargets; ENSG00000108395; -.
DR Orphanet; 2576; Mulibrey nanism.
DR PharmGKB; PA35497; -.
DR VEuPathDB; HostDB:ENSG00000108395; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00410000025800; -.
DR HOGENOM; CLU_011183_0_0_1; -.
DR InParanoid; O94972; -.
DR OMA; XYEYRVE; -.
DR OrthoDB; 128089at2759; -.
DR PhylomeDB; O94972; -.
DR TreeFam; TF351092; -.
DR PathwayCommons; O94972; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O94972; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 4591; 236 hits in 1114 CRISPR screens.
DR ChiTaRS; TRIM37; human.
DR EvolutionaryTrace; O94972; -.
DR GeneWiki; TRIM37; -.
DR GenomeRNAi; 4591; -.
DR Pharos; O94972; Tbio.
DR PRO; PR:O94972; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O94972; protein.
DR Bgee; ENSG00000108395; Expressed in endothelial cell and 203 other tissues.
DR ExpressionAtlas; O94972; baseline and differential.
DR Genevisible; O94972; HS.
DR GO; GO:0016235; C:aggresome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; IPI:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI: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:0070842; P:aggresome assembly; IDA:UniProtKB.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IDA:UniProtKB.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; IDA:UniProtKB.
DR GO; GO:0046600; P:negative regulation of centriole replication; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; 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 CDD; cd03773; MATH_TRIM37; 1.
DR Gene3D; 2.60.210.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR002083; MATH/TRAF_dom.
DR InterPro; IPR008974; TRAF-like.
DR InterPro; IPR037299; TRIM37_MATH.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00917; MATH; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00061; MATH; 1.
DR PROSITE; PS50144; MATH; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Dwarfism; Metal-binding; Peroxisome; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Repressor; Transcription; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..964
FT /note="E3 ubiquitin-protein ligase TRIM37"
FT /id="PRO_0000056254"
FT DOMAIN 276..403
FT /note="MATH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00129"
FT ZN_FING 15..55
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 90..132
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT REGION 477..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 132..234
FT /evidence="ECO:0000255"
FT COILED 419..450
FT /evidence="ECO:0000255"
FT COILED 673..700
FT /evidence="ECO:0000255"
FT COMPBIAS 490..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..122
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_011919"
FT VAR_SEQ 8..41
FT /note="Missing (in isoform 3)"
FT /id="VSP_057468"
FT VAR_SEQ 899..937
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_011920"
FT VARIANT 76
FT /note="L -> P (in MUL; decreased ubiquitination and
FT abolishes the formation of perinuclear aggregates;
FT dbSNP:rs386834004)"
FT /evidence="ECO:0000269|PubMed:15885686"
FT /id="VAR_060217"
FT VARIANT 108
FT /note="T -> A (in dbSNP:rs17853504)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_060218"
FT VARIANT 109
FT /note="C -> S (in MUL; no effect on E3 ubiquitin-protein
FT ligase activity; dbSNP:rs121908391)"
FT /evidence="ECO:0000269|PubMed:17100991"
FT /id="VAR_060219"
FT VARIANT 322
FT /note="G -> V (in MUL; no effect on ubiquitination but
FT affects subcellular localization; dbSNP:rs386834009)"
FT /evidence="ECO:0000269|PubMed:15108285,
FT ECO:0000269|PubMed:15885686"
FT /id="VAR_060220"
FT VARIANT 432
FT /note="Q -> R (in dbSNP:rs1458302547)"
FT /evidence="ECO:0000269|PubMed:26697951"
FT /id="VAR_075470"
FT VARIANT 838
FT /note="V -> I (in dbSNP:rs7222388)"
FT /id="VAR_052142"
FT MUTAGEN 18
FT /note="C->R: Abolishes ability to monoubiquitinate 'Lys-
FT 119' of histone H2A (H2AK119Ub)."
FT /evidence="ECO:0000269|PubMed:25470042"
FT MUTAGEN 35..36
FT /note="CC->SS: Reduces ubiquitination and abolishes the
FT formation of perinuclear aggregates."
FT /evidence="ECO:0000269|PubMed:15885686"
FT CONFLICT 620
FT /note="I -> M (in Ref. 3; BAF85148)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="D -> A (in Ref. 1; AAL36460)"
FT /evidence="ECO:0000305"
FT CONFLICT 916
FT /note="E -> G (in Ref. 2; BAG57954)"
FT /evidence="ECO:0000305"
FT HELIX 1..12
FT /evidence="ECO:0007829|PDB:3LRQ"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:3LRQ"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:3LRQ"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:3LRQ"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:3LRQ"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:3LRQ"
FT TURN 52..54
FT /evidence="ECO:0007829|PDB:3LRQ"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3LRQ"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:3LRQ"
SQ SEQUENCE 964 AA; 107906 MW; C0F08D5A5DC3B5AC CRC64;
MDEQSVESIA EVFRCFICME KLRDARLCPH CSKLCCFSCI RRWLTEQRAQ CPHCRAPLQL
RELVNCRWAE EVTQQLDTLQ LCSLTKHEEN EKDKCENHHE KLSVFCWTCK KCICHQCALW
GGMHGGHTFK PLAEIYEQHV TKVNEEVAKL RRRLMELISL VQEVERNVEA VRNAKDERVR
EIRNAVEMMI ARLDTQLKNK LITLMGQKTS LTQETELLES LLQEVEHQLR SCSKSELISK
SSEILMMFQQ VHRKPMASFV TTPVPPDFTS ELVPSYDSAT FVLENFSTLR QRADPVYSPP
LQVSGLCWRL KVYPDGNGVV RGYYLSVFLE LSAGLPETSK YEYRVEMVHQ SCNDPTKNII
REFASDFEVG ECWGYNRFFR LDLLANEGYL NPQNDTVILR FQVRSPTFFQ KSRDQHWYIT
QLEAAQTSYI QQINNLKERL TIELSRTQKS RDLSPPDNHL SPQNDDALET RAKKSACSDM
LLEGGPTTAS VREAKEDEED EEKIQNEDYH HELSDGDLDL DLVYEDEVNQ LDGSSSSASS
TATSNTEEND IDEETMSGEN DVEYNNMELE EGELMEDAAA AGPAGSSHGY VGSSSRISRR
THLCSAATSS LLDIDPLILI HLLDLKDRSS IENLWGLQPR PPASLLQPTA SYSRKDKDQR
KQQAMWRVPS DLKMLKRLKT QMAEVRCMKT DVKNTLSEIK SSSAASGDMQ TSLFSADQAA
LAACGTENSG RLQDLGMELL AKSSVANCYI RNSTNKKSNS PKPARSSVAG SLSLRRAVDP
GENSRSKGDC QTLSEGSPGS SQSGSRHSSP RALIHGSIGD ILPKTEDRQC KALDSDAVVV
AVFSGLPAVE KRRKMVTLGA NAKGGHLEGL QMTDLENNSE TGELQPVLPE GASAAPEEGM
SSDSDIECDT ENEEQEEHTS VGGFHDSFMV MTQPPDEDTH SSFPDGEQIG PEDLSFNTDE
NSGR
