TRI37_MOUSE
ID TRI37_MOUSE Reviewed; 961 AA.
AC Q6PCX9; Q5SX31; Q8CHC5;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM37 {ECO:0000305};
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:O94972};
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|MGI:MGI:2153072};
GN Synonyms=Kiaa0898 {ECO:0000303|PubMed:12465718};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 TISSUE SPECIFICITY.
RX PubMed=16514549; DOI=10.1007/s00418-006-0162-9;
RA Kallijarvi J., Hamalainen R.H., Karlberg N., Sainio K., Lehesjoki A.E.;
RT "Tissue expression of the mulibrey nanism-associated Trim37 protein in
RT embryonic and adult mouse tissues.";
RL Histochem. Cell Biol. 126:325-334(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, AND PATHWAY.
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase required to prevent centriole
CC reduplication (By similarity). Probably acts by ubiquitinating positive
CC regulators of centriole reduplication (By similarity). Mediates
CC monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), a specific
CC tag for epigenetic transcriptional repression: associates with some
CC Polycomb group (PcG) multiprotein PRC2-like complex and mediates
CC repression of target genes (PubMed:25470042).
CC {ECO:0000250|UniProtKB:O94972, 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:0000250|UniProtKB:O94972};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:25470042}.
CC -!- SUBUNIT: Associates with the PRC2/EED-EZH2 complex.
CC {ECO:0000250|UniProtKB:O94972}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O94972}. Peroxisome
CC {ECO:0000250|UniProtKB:O94972}. 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:0000250|UniProtKB:O94972}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and brain. In embryonic
CC tissues, expressed in epithelia, including ducts of the developing
CC pancreas, epithelium of the midgut and nasal epithelium. In adult,
CC detected in the central and peripheral nervous systems, including
CC enteric ganglia, retina and the adrenal medulla (at protein level).
CC {ECO:0000269|PubMed:16514549}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:O94972}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41455.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB093271; BAC41455.1; ALT_INIT; Transcribed_RNA.
DR EMBL; AK140822; BAE24489.1; -; mRNA.
DR EMBL; BC058678; AAH58678.1; -; mRNA.
DR EMBL; BC059070; AAH59070.1; -; mRNA.
DR CCDS; CCDS25210.1; -.
DR RefSeq; NP_932104.1; NM_197987.2.
DR AlphaFoldDB; Q6PCX9; -.
DR SMR; Q6PCX9; -.
DR BioGRID; 213018; 2.
DR STRING; 10090.ENSMUSP00000049057; -.
DR iPTMnet; Q6PCX9; -.
DR PhosphoSitePlus; Q6PCX9; -.
DR EPD; Q6PCX9; -.
DR MaxQB; Q6PCX9; -.
DR PaxDb; Q6PCX9; -.
DR PRIDE; Q6PCX9; -.
DR ProteomicsDB; 298217; -.
DR Antibodypedia; 31047; 232 antibodies from 29 providers.
DR DNASU; 68729; -.
DR Ensembl; ENSMUST00000041282; ENSMUSP00000049057; ENSMUSG00000018548.
DR GeneID; 68729; -.
DR KEGG; mmu:68729; -.
DR UCSC; uc007ktm.2; mouse.
DR CTD; 4591; -.
DR MGI; MGI:2153072; Trim37.
DR VEuPathDB; HostDB:ENSMUSG00000018548; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00410000025800; -.
DR HOGENOM; CLU_011183_0_0_1; -.
DR InParanoid; Q6PCX9; -.
DR OMA; XYEYRVE; -.
DR OrthoDB; 128089at2759; -.
DR PhylomeDB; Q6PCX9; -.
DR TreeFam; TF351092; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 68729; 8 hits in 74 CRISPR screens.
DR ChiTaRS; Trim37; mouse.
DR PRO; PR:Q6PCX9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6PCX9; protein.
DR Bgee; ENSMUSG00000018548; Expressed in spermatocyte and 268 other tissues.
DR ExpressionAtlas; Q6PCX9; baseline and differential.
DR Genevisible; Q6PCX9; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0035098; C:ESC/E(Z) complex; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0005164; F:tumor necrosis factor receptor binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0070842; P:aggresome assembly; ISO:MGI.
DR GO; GO:0035518; P:histone H2A monoubiquitination; IMP:UniProtKB.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; IMP:UniProtKB.
DR GO; GO:0046600; P:negative regulation of centriole replication; ISS:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
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 Acetylation; Coiled coil; Cytoplasm; Metal-binding; Peroxisome;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..961
FT /note="E3 ubiquitin-protein ligase TRIM37"
FT /id="PRO_0000056255"
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 447..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..961
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 COMPBIAS 491..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..809
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:0000250|UniProtKB:O94972"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94972"
FT CONFLICT 227..232
FT /note="Missing (in Ref. 1; BAC41455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 961 AA; 107660 MW; 85629CEFE0A1D6EA 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 NRQNDTVILR FQVRSPTFFQ KCRDQHWYIT
QLEAAQTGYI QQINNLKERL TIELSRTQKS RDLSPPDNHL SPQNDDSPET RTKKAGSCSD
MLLEGGPTCA SVRETKEDED EEEKIQNEDY HHELSDGDLD LDLVGEDEVN HLDGSSSSAS
STATSNTEEN DIDEETMSGE NDVEYNSMEL EEGELMEDAA AAGPPGSSHS YVGASSRMSR
RTHLCSAATS SLLDIDPLIL IHLLDLKDRS SMENLWGLQP RPSASLLQPT ASYSRKDKDQ
RKQQAMWRVP SDLKMLKRLK TQMAEVRCMK TDVKTTLSDI KGSSVASTDM QTNLFCADQA
ALTTCGPENS GRLQDLGMEL LAKSSVAGCY IRNPTNKKNS PKSARAIAGS LSLRRAVDSG
ENSRSKGDCQ VLAEGSSGSS QSGSRHSSPR ALTHGIIGDL LPKSEDRQCK ALDSDAVVVA
VFNGLPTVEK RRKMVTLGTN AKGGRLEGMQ MADLESHSEA GEVQPTLPEG ASAAPEEGMS
SDSDIECDTE NEEQEEHTSM GAFNDPFLAQ PPDEDSHSSF PDGEQIDPEN LHFNPDEGGG
R
