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TRI13_MOUSE
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   03-AUG-2022, entry version 153.
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; 2.
DR   STRING; 10090.ENSMUSP00000128509; -.
DR   iPTMnet; Q9CYB0; -.
DR   PhosphoSitePlus; Q9CYB0; -.
DR   EPD; Q9CYB0; -.
DR   MaxQB; Q9CYB0; -.
DR   PaxDb; Q9CYB0; -.
DR   PeptideAtlas; Q9CYB0; -.
DR   PRIDE; Q9CYB0; -.
DR   ProteomicsDB; 258971; -.
DR   Antibodypedia; 638; 238 antibodies from 27 providers.
DR   DNASU; 66597; -.
DR   Ensembl; ENSMUST00000039562; ENSMUSP00000045009; ENSMUSG00000035235.
DR   Ensembl; ENSMUST00000165015; ENSMUSP00000128509; ENSMUSG00000035235.
DR   GeneID; 66597; -.
DR   KEGG; mmu:66597; -.
DR   UCSC; uc007ufy.2; mouse.
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; 635534at2759; -.
DR   PhylomeDB; Q9CYB0; -.
DR   TreeFam; TF331669; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 66597; 0 hits in 70 CRISPR screens.
DR   PRO; PR:Q9CYB0; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q9CYB0; protein.
DR   Bgee; ENSMUSG00000035235; Expressed in animal zygote and 253 other 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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; IBA:GO_Central.
DR   GO; GO:0032897; P:negative regulation of viral transcription; IEA:Ensembl.
DR   GO; GO:0010942; P:positive regulation of cell death; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; ISS:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
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:0010332; P:response to gamma radiation; ISS:UniProtKB.
DR   GO; GO:0044790; P:suppression of viral release by host; IEA:Ensembl.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR027370; Znf-RING_LisH.
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; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00184; RING; 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
 
 
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