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E3 ubiquitin-protein ligase TRIM37 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM37) (Tripartite motif-containing protein 37)

 TRI37_MOUSE             Reviewed;         961 AA.
Q6PCX9; Q5SX31; Q8CHC5;
23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
12-SEP-2018, entry version 132.
RecName: Full=E3 ubiquitin-protein ligase TRIM37 {ECO:0000305};
EC=2.3.2.27 {ECO:0000250|UniProtKB:O94972};
AltName: Full=RING-type E3 ubiquitin transferase TRIM37 {ECO:0000305};
AltName: Full=Tripartite motif-containing protein 37 {ECO:0000305};
Name=Trim37 {ECO:0000312|MGI:MGI:2153072};
Synonyms=Kiaa0898 {ECO:0000303|PubMed:12465718};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=12465718; DOI=10.1093/dnares/9.5.179;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
I. The complete nucleotide sequences of 100 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 9:179-188(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Head;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
TISSUE SPECIFICITY.
PubMed=16514549; DOI=10.1007/s00418-006-0162-9;
Kallijarvi J., Hamalainen R.H., Karlberg N., Sainio K.,
Lehesjoki A.E.;
"Tissue expression of the mulibrey nanism-associated Trim37 protein in
embryonic and adult mouse tissues.";
Histochem. Cell Biol. 126:325-334(2006).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
FUNCTION, AND PATHWAY.
PubMed=25470042; DOI=10.1038/nature13955;
Bhatnagar S., Gazin C., Chamberlain L., Ou J., Zhu X., Tushir J.S.,
Virbasius C.M., Lin L., Zhu L.J., Wajapeyee N., Green M.R.;
"TRIM37 is a new histone H2A ubiquitin ligase and breast cancer
oncoprotein.";
Nature 516:116-120(2014).
-!- FUNCTION: E3 ubiquitin-protein ligase required to prevent
centriole reduplication (By similarity). Probably acts by
ubiquitinating positive regulators of centriole reduplication (By
similarity). Mediates monoubiquitination of 'Lys-119' of histone
H2A (H2AK119Ub), a specific tag for epigenetic transcriptional
repression: associates with some Polycomb group (PcG) multiprotein
PRC2-like complex and mediates repression of target genes
(PubMed:25470042). {ECO:0000250|UniProtKB:O94972,
ECO:0000269|PubMed:25470042}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000250|UniProtKB:O94972}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000269|PubMed:25470042}.
-!- SUBUNIT: Associates with the PRC2/EED-EZH2 complex.
{ECO:0000250|UniProtKB:O94972}.
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:O94972}. Peroxisome
{ECO:0000250|UniProtKB:O94972}. Note=Found in vesicles of the
peroxisome. Aggregates as aggresomes, a perinuclear region where
certain misfolded or aggregated proteins are sequestered for
proteasomal degradation. {ECO:0000250|UniProtKB:O94972}.
-!- TISSUE SPECIFICITY: Highly expressed in testis and brain. In
embryonic tissues, expressed in epithelia, including ducts of the
developing pancreas, epithelium of the midgut and nasal
epithelium. In adult, detected in the central and peripheral
nervous systems, including enteric ganglia, retina and the adrenal
medulla (at protein level). {ECO:0000269|PubMed:16514549}.
-!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:O94972}.
-!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC41455.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB093271; BAC41455.1; ALT_INIT; Transcribed_RNA.
EMBL; AK140822; BAE24489.1; -; mRNA.
EMBL; BC058678; AAH58678.1; -; mRNA.
EMBL; BC059070; AAH59070.1; -; mRNA.
CCDS; CCDS25210.1; -.
RefSeq; NP_932104.1; NM_197987.2.
UniGene; Mm.17436; -.
ProteinModelPortal; Q6PCX9; -.
SMR; Q6PCX9; -.
STRING; 10090.ENSMUSP00000049057; -.
iPTMnet; Q6PCX9; -.
PhosphoSitePlus; Q6PCX9; -.
MaxQB; Q6PCX9; -.
PaxDb; Q6PCX9; -.
PRIDE; Q6PCX9; -.
Ensembl; ENSMUST00000041282; ENSMUSP00000049057; ENSMUSG00000018548.
GeneID; 68729; -.
KEGG; mmu:68729; -.
UCSC; uc007ktm.2; mouse.
CTD; 4591; -.
MGI; MGI:2153072; Trim37.
eggNOG; ENOG410ITG1; Eukaryota.
eggNOG; ENOG410YSD5; LUCA.
GeneTree; ENSGT00410000025800; -.
HOGENOM; HOG000013010; -.
HOVERGEN; HBG057591; -.
InParanoid; Q6PCX9; -.
KO; K10608; -.
OMA; TQMAEVR; -.
OrthoDB; EOG091G01C1; -.
PhylomeDB; Q6PCX9; -.
TreeFam; TF351092; -.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
ChiTaRS; Trim37; mouse.
PRO; PR:Q6PCX9; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000018548; Expressed in 303 organ(s), highest expression level in testis.
CleanEx; MM_TRIM37; -.
ExpressionAtlas; Q6PCX9; baseline and differential.
Genevisible; Q6PCX9; MM.
GO; GO:0016235; C:aggresome; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0035098; C:ESC/E(Z) complex; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005777; C:peroxisome; ISO:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0005164; F:tumor necrosis factor receptor binding; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0070842; P:aggresome assembly; ISO:MGI.
GO; GO:0035518; P:histone H2A monoubiquitination; IMP:UniProtKB.
GO; GO:0036353; P:histone H2A-K119 monoubiquitination; IMP:UniProtKB.
GO; GO:0046600; P:negative regulation of centriole replication; ISS:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
CDD; cd00021; BBOX; 1.
CDD; cd03773; MATH_TRIM37; 1.
Gene3D; 2.60.210.10; -; 1.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR003649; Bbox_C.
InterPro; IPR002083; MATH/TRAF_dom.
InterPro; IPR008974; TRAF-like.
InterPro; IPR037299; TRIM37_MATH.
InterPro; IPR000315; Znf_B-box.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00917; MATH; 1.
Pfam; PF00643; zf-B_box; 1.
SMART; SM00502; BBC; 1.
SMART; SM00336; BBOX; 1.
SMART; SM00061; MATH; 1.
SUPFAM; SSF49599; SSF49599; 1.
PROSITE; PS50144; MATH; 1.
PROSITE; PS50119; ZF_BBOX; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm; Metal-binding;
Peroxisome; Phosphoprotein; Reference proteome; Transferase;
Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 961 E3 ubiquitin-protein ligase TRIM37.
/FTId=PRO_0000056255.
DOMAIN 276 403 MATH. {ECO:0000255|PROSITE-
ProRule:PRU00129}.
ZN_FING 15 55 RING-type; degenerate.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
ZN_FING 90 132 B box-type. {ECO:0000255|PROSITE-
ProRule:PRU00024}.
COILED 132 234 {ECO:0000255}.
COILED 419 450 {ECO:0000255}.
COMPBIAS 535 541 Poly-Ser.
COMPBIAS 579 582 Poly-Ala.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:O94972}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000250|UniProtKB:O94972}.
CONFLICT 227 232 Missing (in Ref. 1; BAC41455).
{ECO:0000305}.
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


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