ID TRI13_MOUSE Reviewed; 407 AA.
AC Q9CYB0; A6H6L2; Q8CEV0; Q923J0; Q925P1; Q99PQ0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 161.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM13;
DE EC=2.3.2.27;
DE AltName: Full=Putative tumor suppressor RFP2;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM13 {ECO:0000305};
DE AltName: Full=Ret finger protein 2;
DE AltName: Full=Tripartite motif-containing protein 13;
GN Name=Trim13; Synonyms=Rfp2;
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 [GENOMIC DNA].
RA Borodina T.A., Baranova A.V.;
RT "Genomic organization of the murine Rfp2 gene.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and 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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-134.
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-228.
RX PubMed=11161783; DOI=10.1006/geno.2000.6386;
RA Kapanadze B., Makeeva N., Corcoran M., Jareborg N., Hammarsund M.,
RA Baranova A., Zabarovsky E., Vorontsova O., Merup M., Gahrton G.,
RA Jansson M., Yankovsky N., Einhorn S., Oscier D., Grander D., Sangfelt O.;
RT "Comparative sequence analysis of a region on human chromosome 13q14,
RT frequently deleted in B-cell chronic lymphocytic leukemia, and its
RT homologous region on mouse chromosome 14.";
RL Genomics 70:327-334(2000).
CC -!- FUNCTION: Endoplasmic reticulum (ER) membrane anchored E3 ligase
CC involved in the retrotranslocation and turnover of membrane and
CC secretory proteins from the ER through a set of processes named ER-
CC associated degradation (ERAD). This process acts on misfolded proteins
CC as well as in the regulated degradation of correctly folded proteins.
CC Enhances ionizing radiation-induced p53/TP53 stability and apoptosis
CC via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity
CC through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-
CC induced autophagy, and may act as a tumor suppressor. Also plays a role
CC in innate immune response by stimulating NF-kappa-B activity in the
CC TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked
CC polyubiquitination chain resulting in NF-kappa-B activation.
CC Participates as well in T-cell receptor-mediated NF-kappa-B activation.
CC In the presence of TNF, modulates the IKK complex by regulating
CC IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B.
CC {ECO:0000250|UniProtKB:O60858}.
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:O60858};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:O60858}.
CC -!- SUBUNIT: Interacts (via C-terminal domain) with VCP. Interacts with
CC AKT1; the interaction ubiquitinates AKT1 and leads to its proteasomal
CC degradation. Interacts with MDM2; the interaction ubiquitinates AKT1
CC and leads to its proteasomal degradation. Interacts with p62/SQSTM1.
CC Interacts with TRAF6. Interacts with IKBKG/NEMO.
CC {ECO:0000250|UniProtKB:O60858}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O60858}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:O60858}. Note=Concentrates and colocalizes with
CC p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum.
CC {ECO:0000250|UniProtKB:O60858}.
CC -!- DOMAIN: The coiled-coil domain is required for the induction of
CC autophagy during endoplasmic reticulum (ER) stress.
CC {ECO:0000250|UniProtKB:O60858}.
CC -!- DOMAIN: The RING-type zinc finger is required for auto-
CC polyubiquitination. {ECO:0000250|UniProtKB:O60858}.
CC -!- DOMAIN: The C-terminal transmembrane domain is indispensable for the
CC localization to the ER. {ECO:0000250|UniProtKB:O60858}.
CC -!- PTM: Auto-ubiquitinated; requires the RING-type zinc finger. Auto-
CC polyubiquitination leads to proteasomal degradation.
CC {ECO:0000250|UniProtKB:O60858}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AY033605; AAK56791.1; -; Genomic_DNA.
DR EMBL; AK013959; BAC25419.1; -; mRNA.
DR EMBL; AK017850; BAB30973.1; -; mRNA.
DR EMBL; CH466535; EDL36095.1; -; Genomic_DNA.
DR EMBL; CH466535; EDL36096.1; -; Genomic_DNA.
DR EMBL; BC138576; AAI38577.1; -; mRNA.
DR EMBL; BC145915; AAI45916.1; -; mRNA.
DR EMBL; AF220129; AAG53502.1; -; mRNA.
DR EMBL; AF302839; AAK51689.1; -; Genomic_DNA.
DR CCDS; CCDS27186.1; -.
DR RefSeq; NP_001157692.1; NM_001164220.1.
DR RefSeq; NP_075722.1; NM_023233.3.
DR RefSeq; XP_006519455.1; XM_006519392.2.
DR AlphaFoldDB; Q9CYB0; -.
DR SMR; Q9CYB0; -.
DR BioGRID; 211583; 3.
DR STRING; 10090.ENSMUSP00000128509; -.
DR iPTMnet; Q9CYB0; -.
DR PhosphoSitePlus; Q9CYB0; -.
DR SwissPalm; Q9CYB0; -.
DR EPD; Q9CYB0; -.
DR MaxQB; Q9CYB0; -.
DR PaxDb; 10090-ENSMUSP00000128509; -.
DR PeptideAtlas; Q9CYB0; -.
DR ProteomicsDB; 258971; -.
DR Antibodypedia; 638; 255 antibodies from 27 providers.
DR DNASU; 66597; -.
DR Ensembl; ENSMUST00000039562.8; ENSMUSP00000045009.7; ENSMUSG00000035235.14.
DR Ensembl; ENSMUST00000165015.9; ENSMUSP00000128509.2; ENSMUSG00000035235.14.
DR GeneID; 66597; -.
DR KEGG; mmu:66597; -.
DR UCSC; uc007ufy.2; mouse.
DR AGR; MGI:1913847; -.
DR CTD; 10206; -.
DR MGI; MGI:1913847; Trim13.
DR VEuPathDB; HostDB:ENSMUSG00000035235; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159715; -.
DR HOGENOM; CLU_053708_0_0_1; -.
DR InParanoid; Q9CYB0; -.
DR OMA; NLQVNYS; -.
DR OrthoDB; 5383069at2759; -.
DR PhylomeDB; Q9CYB0; -.
DR TreeFam; TF331669; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 66597; 0 hits in 75 CRISPR screens.
DR PRO; PR:Q9CYB0; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9CYB0; Protein.
DR Bgee; ENSMUSG00000035235; Expressed in animal zygote and 257 other cell types or tissues.
DR Genevisible; Q9CYB0; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0061659; F:ubiquitin-like protein ligase activity; ISS:UniProtKB.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0032897; P:negative regulation of viral transcription; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:MGI.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR CDD; cd19767; Bbox2_TRIM13_C-XI; 1.
DR CDD; cd16762; RING-HC_TRIM13_C-V; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR027370; Znf-RING_euk.
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 PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR PANTHER; PTHR24103:SF609; E3 UBIQUITIN-PROTEIN LIGASE TRIM13; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Endoplasmic reticulum; Immunity; Innate immunity; Membrane;
KW Metal-binding; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..407
FT /note="E3 ubiquitin-protein ligase TRIM13"
FT /id="PRO_0000056029"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 10..58
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 89..131
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 172..200
FT /evidence="ECO:0000255"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 97
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 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT CONFLICT 47
FT /note="W -> R (in Ref. 2; BAC25419)"
FT /evidence="ECO:0000305"
FT CONFLICT 140..142
FT /note="NAF -> KCL (in Ref. 1; AAK56791)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="F -> L (in Ref. 1; AAK56791)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="F -> V (in Ref. 6; AAK51689)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="Q -> QKLQ (in Ref. 6; AAK51689)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="S -> C (in Ref. 6; AAK51689)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="D -> E (in Ref. 6; AAK51689)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="Q -> H (in Ref. 6; AAK51689)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 46958 MW; 2D147B68767BBF62 CRC64;
MELLEEDLTC PICCSLFDDP RVLPCSHNFC KKCLEGLLEG NVRNSLWRPS PFKCPTCRKE
TSATGVNSLQ VNYSLKGIVE KYNKIKISPK MPVCKGHLGQ PLNIFCVTDM QLICGICATR
GEHTKHVFSS IEDAYAREKN AFESLFQSFE TWRRGDALSR LDTLETNKRK ALQLLTKDSD
KVKEFFEKLQ HTLDQKKNEI LSDFETMKLA VMQTYDPEIN KINTILQEQR MAFNIAEAFK
DVSEPIIFLQ QMQEFREKIK VIKETPLPHS NLPTSPLMKN FDTSQWGDIK LVDVDKLSLP
QDTGVFTSKI PWYPYLLLMM VVLLGLLIFF GPTVFLEWSP LDELATWKDY LSSFNSYLTK
SADFIEQSVF YWEQMTDGFF IFGERVKNVS LVALNNVAEF ICKYKLL
//
