TRI66_MOUSE
ID TRI66_MOUSE Reviewed; 1242 AA.
AC Q924W6; E9QKN7; Q5SEK4;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Tripartite motif-containing protein 66;
DE AltName: Full=Transcriptional intermediary factor 1 delta;
GN Name=Trim66; Synonyms=Tif1d;
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], AND ALTERNATIVE SPLICING (ISOFORM 2).
RX PubMed=11528127; DOI=10.1159/000056999;
RA Amid C., Bahr A., Mujica A., Sampson N., Bikar S.E., Winterpacht A.,
RA Zabel B., Hankeln T., Schmidt E.R.;
RT "Comparative genomic sequencing reveals a strikingly similar architecture
RT of a conserved syntenic region on human chromosome 11p15.3 (including gene
RT ST5) and mouse chromosome 7.";
RL Cytogenet. Cell Genet. 93:284-290(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, MOTIF, INTERACTION WITH CBX5, CBX1 AND CBX3,
RP MUTAGENESIS OF VAL-889 AND LEU-891, AND SUBCELLULAR LOCATION.
RX PubMed=15322135; DOI=10.1074/jbc.m404779200;
RA Khetchoumian K., Teletin M., Mark M., Lerouge T., Cervino M.,
RA Oulad-Abdelghani M., Chambon P., Losson R.;
RT "TIF1delta, a novel HP1-interacting member of the transcriptional
RT intermediary factor 1 (TIF1) family expressed by elongating spermatids.";
RL J. Biol. Chem. 279:48329-48341(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: May function as transcription repressor; The repressive
CC effects are mediated, at least in part, by recruitment of deacetylase
CC activity. May play a role as negative regulator of postmeiotic genes
CC acting through CBX3 complex formation and centromere association.
CC {ECO:0000269|PubMed:15322135}.
CC -!- SUBUNIT: Can form homodimers and heterodimers. Interacts with CBX5,
CC CBX1 and CBX3 via PxVxL motif. {ECO:0000269|PubMed:15322135}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15322135}. Note=Forms
CC discrete foci within the centromeric chromocenter and surrounding
CC nucleoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q924W6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q924W6-2; Sequence=VSP_026555, VSP_026556;
CC -!- TISSUE SPECIFICITY: Predominant in testis, specifically in elongating
CC spermatids. {ECO:0000269|PubMed:15322135}.
CC -!- DEVELOPMENTAL STAGE: No significant expression in testis of 2- or 3-
CC week-old mouse, but clear detection at the age of 4 weeks.
CC {ECO:0000269|PubMed:15322135}.
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DR EMBL; AJ307670; CAC38114.1; -; Genomic_DNA.
DR EMBL; AY572455; AAS78677.1; -; mRNA.
DR EMBL; AC124457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS40082.1; -. [Q924W6-1]
DR RefSeq; NP_862901.3; NM_181853.4. [Q924W6-1]
DR RefSeq; XP_006508022.1; XM_006507959.1. [Q924W6-1]
DR RefSeq; XP_006508023.1; XM_006507960.2. [Q924W6-1]
DR RefSeq; XP_006508024.1; XM_006507961.3. [Q924W6-1]
DR RefSeq; XP_006508025.1; XM_006507962.1. [Q924W6-1]
DR RefSeq; XP_011240137.1; XM_011241835.2. [Q924W6-1]
DR AlphaFoldDB; Q924W6; -.
DR SMR; Q924W6; -.
DR BioGRID; 236997; 4.
DR STRING; 10090.ENSMUSP00000102352; -.
DR iPTMnet; Q924W6; -.
DR PhosphoSitePlus; Q924W6; -.
DR PaxDb; Q924W6; -.
DR PRIDE; Q924W6; -.
DR ProteomicsDB; 259328; -. [Q924W6-1]
DR ProteomicsDB; 259329; -. [Q924W6-2]
DR Antibodypedia; 5888; 26 antibodies from 11 providers.
DR DNASU; 330627; -.
DR Ensembl; ENSMUST00000033339; ENSMUSP00000033339; ENSMUSG00000031026. [Q924W6-1]
DR GeneID; 330627; -.
DR KEGG; mmu:330627; -.
DR UCSC; uc012fsa.1; mouse. [Q924W6-1]
DR CTD; 9866; -.
DR MGI; MGI:2152406; Trim66.
DR VEuPathDB; HostDB:ENSMUSG00000031026; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000159240; -.
DR HOGENOM; CLU_005817_1_0_1; -.
DR InParanoid; Q924W6; -.
DR BioGRID-ORCS; 330627; 0 hits in 78 CRISPR screens.
DR PRO; PR:Q924W6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q924W6; protein.
DR Bgee; ENSMUSG00000031026; Expressed in olfactory epithelium and 71 other tissues.
DR ExpressionAtlas; Q924W6; baseline and differential.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0010369; C:chromocenter; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR003649; Bbox_C.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR037372; Trim66.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45915:SF7; PTHR45915:SF7; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Bromodomain; Coiled coil; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1242
FT /note="Tripartite motif-containing protein 66"
FT /id="PRO_0000220376"
FT DOMAIN 1084..1156
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 1..46
FT /note="B box-type 1; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 60..101
FT /note="B box-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT ZN_FING 996..1043
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 376..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1182..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 130..200
FT /evidence="ECO:0000255"
FT MOTIF 887..891
FT /note="PxVxL motif"
FT COMPBIAS 393..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..480
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 8
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 29
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 97..98
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026555"
FT VAR_SEQ 794..825
FT /note="MESEDCTRFSDSVGQGPTASSLDGPKDLAIPS -> V (in isoform
FT 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026556"
FT MUTAGEN 889
FT /note="V->A: Drastic decrease of CBX5, CBX1 and CBX3
FT binding; When associated with A-891."
FT /evidence="ECO:0000269|PubMed:15322135"
FT MUTAGEN 891
FT /note="L->A: Drastic decrease of CBX5, CBX1 and CBX3
FT binding; When associated with A-889."
FT /evidence="ECO:0000269|PubMed:15322135"
FT CONFLICT 43
FT /note="L -> I (in Ref. 2; AAS78677)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="P -> S (in Ref. 2; AAS78677)"
FT /evidence="ECO:0000305"
FT CONFLICT 879
FT /note="A -> T (in Ref. 2; AAS78677)"
FT /evidence="ECO:0000305"
FT CONFLICT 919
FT /note="N -> S (in Ref. 2; AAS78677)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1242 AA; 136766 MW; 98606ACB8BA70243 CRC64;
MARNCSECKE KRAAHILCTY CNRWLCSSCT EEHRHVPAPG GPLFARAQKG SSGVNGGSGD
FALYCPLHTQ EVLKLFCETC DVLTCHSCLM VEHKEHRCRH VEEVLQNQRM LLESVTSQVA
HKKSSLQTSA KQIEDRIFEV KHQHRKVENQ IKMAKMVLMN ELNKQANGLI EELEGITNER
KRKLEQQLQS IMVLNRQFEH VQNFINWAVC SKSSVPFLFS KELIVFQMQR LLETRCNTDP
GSPWSIRFTW EPNFWTKQLA SLGCITTEGG QLTRADAAAA SYGSLQGQPS FYQSHQAPMA
QQEALSHPSH KFQSPALCSS SVCCSHCSPV SPSLKGQVPP PSIHPAHSFR QPSEMVPHQL
GSLQCSTLLP REKELACSPH PPKLMQPWLE PQPPAEQEST SQRPGPQLVS QPVCIVPPQD
VQPGAHAQPT IQTPSIQVQL GHHQKLKLSH FQQQPQQQPP PPPPPPPPPQ HAPPPLPPSQ
HLASSQHESP PGPACSQNVD IMHHKFELEE MQKDLELLLQ AQQPSLQLSQ TKSPQHLQQT
IVGQINYIVR QPAPVQSQSQ EETLQVTEEP PAPEGPKPAL PVDKNTAAPL PQTSGEETPH
SVPPVDGTSQ HSSPNVVRKH ATSVSIMGFS NTVEMELSST RLARTIEPQI HRVSSLTAAP
THTIPSLLSG PPQTVSSLMS VSNHAMPSLT ASHLQPVPNL VRGTFQSTSN LRGDSSQAIT
GLASNHSQAG PSLMSGHTQA APSLATCPLQ GMPPVSDVHV EPRSVSSPGS GPAAESLGTR
DGAESSLGNA LCKMESEDCT RFSDSVGQGP TASSLDGPKD LAIPSELEEP INLSVKKPFL
APVINTSTAL QQYRNPKEYE NFEQGALELD TKENSDIRAI SSEPKIPYVR LERLKICAAS
SGEMPVFKLK PQKNSQDGNF LLVIECGTES SSMSIKVSQN SLPDASQGPG LGGRKVTVTS
LTGQQPQEVE STSEEHRLIP RAPGAKKNTP APIENEDFCA VCINGGELLC CDRCPKVYHL
SCHVPALLSF PGGEWVCTLC RSLTQPEMEY DCENARYGHP GVRVLPGLSM YDQKKCEKLV
LSLCCNSLSL PFHEPVSPLA RHYYQIIKRP MDLSIIRRKL QKKDPAHYTT PEEVVSDVRL
MFWNCAKFNY PDSEVAEAGR CLEVFFEGWL KEIYPDKCFA QPQQEDSDSE DVSGESGCST
PQGFPWPPYM QEGIQPKRRR RHMENEKTKR VSFRLANSIS QV
