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TRI60_MOUSE
ID   TRI60_MOUSE             Reviewed;         466 AA.
AC   Q8VI40; Q3UX74;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Tripartite motif-containing protein 60;
DE   AltName: Full=RING finger protein 33;
GN   Name=Trim60; Synonyms=2czf45, Rnf33;
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 [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6J X DBA/2;
RX   PubMed=11424210; DOI=10.1002/mrd.1029;
RA   Choo K.-B., Chen H.-H., Cheng W.T.K., Chang H.-S., Wang M.;
RT   "In silico mining of EST databases for novel pre-implantation embryo-
RT   specific zinc finger protein genes.";
RL   Mol. Reprod. Dev. 59:249-255(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=12160726; DOI=10.1006/geno.2002.6808;
RA   Chen H.-H., Liu T.Y.-C., Li H., Choo K.-B.;
RT   "Use of a common promoter by two juxtaposed and intronless mouse early
RT   embryonic genes, Rnf33 and Rnf35: implications in zygotic gene
RT   expression.";
RL   Genomics 80:140-143(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
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).
CC   -!- INTERACTION:
CC       Q8VI40; P28741: Kif3a; NbExp=5; IntAct=EBI-6395249, EBI-6169413;
CC       Q8VI40; Q61771: Kif3b; NbExp=3; IntAct=EBI-6395249, EBI-6395332;
CC   -!- DEVELOPMENTAL STAGE: Expressed exclusively in embryos before or up to
CC       the 8-cell stage. {ECO:0000269|PubMed:11424210}.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR   EMBL; AF290197; AAL40186.1; -; mRNA.
DR   EMBL; AY063497; AAL58549.1; -; Genomic_DNA.
DR   EMBL; AK135841; BAE22689.1; -; mRNA.
DR   CCDS; CCDS22331.1; -.
DR   RefSeq; NP_694737.1; NM_153097.2.
DR   AlphaFoldDB; Q8VI40; -.
DR   SMR; Q8VI40; -.
DR   IntAct; Q8VI40; 2.
DR   STRING; 10090.ENSMUSP00000040299; -.
DR   iPTMnet; Q8VI40; -.
DR   PhosphoSitePlus; Q8VI40; -.
DR   PaxDb; Q8VI40; -.
DR   PRIDE; Q8VI40; -.
DR   Antibodypedia; 28289; 47 antibodies from 14 providers.
DR   DNASU; 234329; -.
DR   Ensembl; ENSMUST00000048565; ENSMUSP00000040299; ENSMUSG00000053490.
DR   GeneID; 234329; -.
DR   KEGG; mmu:234329; -.
DR   UCSC; uc009lve.2; mouse.
DR   CTD; 166655; -.
DR   MGI; MGI:2387430; Trim60.
DR   VEuPathDB; HostDB:ENSMUSG00000053490; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000155329; -.
DR   HOGENOM; CLU_013137_0_3_1; -.
DR   InParanoid; Q8VI40; -.
DR   OMA; CYNPRRF; -.
DR   OrthoDB; 423686at2759; -.
DR   PhylomeDB; Q8VI40; -.
DR   TreeFam; TF342569; -.
DR   BioGRID-ORCS; 234329; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Trim60; mouse.
DR   PRO; PR:Q8VI40; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8VI40; protein.
DR   Bgee; ENSMUSG00000053490; Expressed in animal zygote and 21 other tissues.
DR   Genevisible; Q8VI40; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   CDD; cd15828; SPRY_PRY_TRIM60; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR003879; Butyrophylin_SPRY.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR006574; PRY.
DR   InterPro; IPR035786; SPRY/PRY_TRIM60.
DR   InterPro; IPR003877; SPRY_dom.
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; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..466
FT                   /note="Tripartite motif-containing protein 60"
FT                   /id="PRO_0000249190"
FT   DOMAIN          272..462
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         15..56
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   ZN_FING         91..132
FT                   /note="B box-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   COILED          171..223
FT                   /evidence="ECO:0000255"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         99
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT   BINDING         118
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   CONFLICT        226
FT                   /note="V -> F (in Ref. 3; BAE22689)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   466 AA;  54199 MW;  63774639F7DEB96D CRC64;
     MDSTALKILQ DKCICYICSD FMEDPVTSRC GHNFCFACLR LLWDDLQGNI FCPVCQTPFP
     PKSFSRNYQF RNMTETIRLL QKRQSKRKRQ EEHTVCPKHD QPLVLFCVRD RDVLCTQCSL
     SVEHQGHYTC PIKKASSYHR KVLESAIATL KFGVKQVEEK LAVQHRRVLG LREEAQYQKI
     EIRYEIGQIK LFLQSEYEAH LNESHMEELR SFSELNGYLE TLLDHVSTAK DLLKEVEAIH
     ERSDVTLLRA YHKLQNLKSP KPWLFRTKQY GLSLPAQYSG LSRIIKQFQA DVTFDRDTAH
     PQLVISEDRK SVFYKEAWPC VCASPQKFHL WPALLGCKGF DSGRQYWEVK VGDKPRWTLG
     VCQAHFSGDW SNQSSGFWAI GRYAENSYVT YGPLRTEFLP VVRPSKVGIF LDYELGELSF
     YNMNDRSLLY TFRNSFTSTL WPYFYIGTDS ESLEILTHPT PDTGSY
 
 
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