TRI66_HUMAN
ID TRI66_HUMAN Reviewed; 1216 AA.
AC O15016; Q9BQQ4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 4.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Tripartite motif-containing protein 66;
GN Name=TRIM66; Synonyms=C11orf29, KIAA0298;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
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 [LARGE SCALE MRNA] OF 1-868 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP SEQUENCE REVISION.
RA Nagase T., Ishikawa K., Seki N., Nakajima D., Ohira M., Miyajima N.,
RA Kotani H., Nomura N., Ohara O.;
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Can form homodimers and heterodimers. Interacts with CBX5,
CC CBX1 and CBX3 via PxVxL motif (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Forms discrete foci within the
CC centromeric chromocenter and surrounding nucleoplasm. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15016-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15016-2; Sequence=VSP_038386;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20758.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ400879; CAC35389.1; -; Genomic_DNA.
DR EMBL; AB002296; BAA20758.2; ALT_FRAME; mRNA.
DR EMBL; AC091053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_055633.1; NM_014818.1. [O15016-1]
DR PDB; 6IET; X-ray; 2.10 A; A=968-1160.
DR PDB; 6IEU; X-ray; 1.79 A; A=968-1160.
DR PDBsum; 6IET; -.
DR PDBsum; 6IEU; -.
DR AlphaFoldDB; O15016; -.
DR SMR; O15016; -.
DR BioGRID; 115199; 200.
DR IntAct; O15016; 2.
DR STRING; 9606.ENSP00000384876; -.
DR ChEMBL; CHEMBL4296267; -.
DR iPTMnet; O15016; -.
DR PhosphoSitePlus; O15016; -.
DR BioMuta; TRIM66; -.
DR EPD; O15016; -.
DR jPOST; O15016; -.
DR MassIVE; O15016; -.
DR PaxDb; O15016; -.
DR PeptideAtlas; O15016; -.
DR PRIDE; O15016; -.
DR ProteomicsDB; 48372; -. [O15016-1]
DR ProteomicsDB; 48373; -. [O15016-2]
DR Antibodypedia; 5888; 26 antibodies from 11 providers.
DR DNASU; 9866; -.
DR GeneID; 9866; -.
DR KEGG; hsa:9866; -.
DR UCSC; uc010rbo.2; human. [O15016-1]
DR CTD; 9866; -.
DR DisGeNET; 9866; -.
DR GeneCards; TRIM66; -.
DR HGNC; HGNC:29005; TRIM66.
DR HPA; ENSG00000166436; Low tissue specificity.
DR MIM; 612000; gene.
DR neXtProt; NX_O15016; -.
DR PharmGKB; PA134954583; -.
DR VEuPathDB; HostDB:ENSG00000166436; -.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_005817_1_0_1; -.
DR InParanoid; O15016; -.
DR OrthoDB; 756911at2759; -.
DR PhylomeDB; O15016; -.
DR PathwayCommons; O15016; -.
DR SignaLink; O15016; -.
DR BioGRID-ORCS; 9866; 1 hit in 271 CRISPR screens.
DR ChiTaRS; TRIM66; human.
DR GenomeRNAi; 9866; -.
DR Pharos; O15016; Tbio.
DR PRO; PR:O15016; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O15016; protein.
DR Genevisible; O15016; HS.
DR GO; GO:0016235; C:aggresome; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 3D-structure; Alternative splicing; Bromodomain; Coiled coil;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1216
FT /note="Tripartite motif-containing protein 66"
FT /id="PRO_0000220375"
FT DOMAIN 1056..1128
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 970..1017
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 438..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 130..200
FT /evidence="ECO:0000255"
FT MOTIF 860..864
FT /note="PxVxL motif"
FT COMPBIAS 438..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..485
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..626
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1205
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:0000303|PubMed:9205841"
FT /id="VSP_038386"
FT TURN 974..976
FT /evidence="ECO:0007829|PDB:6IEU"
FT STRAND 980..984
FT /evidence="ECO:0007829|PDB:6IEU"
FT STRAND 986..989
FT /evidence="ECO:0007829|PDB:6IEU"
FT TURN 994..996
FT /evidence="ECO:0007829|PDB:6IEU"
FT STRAND 997..999
FT /evidence="ECO:0007829|PDB:6IEU"
FT HELIX 1012..1014
FT /evidence="ECO:0007829|PDB:6IEU"
FT HELIX 1044..1059
FT /evidence="ECO:0007829|PDB:6IEU"
FT HELIX 1061..1066
FT /evidence="ECO:0007829|PDB:6IEU"
FT STRAND 1074..1076
FT /evidence="ECO:0007829|PDB:6IEU"
FT HELIX 1077..1080
FT /evidence="ECO:0007829|PDB:6IEU"
FT HELIX 1087..1093
FT /evidence="ECO:0007829|PDB:6IEU"
FT HELIX 1105..1122
FT /evidence="ECO:0007829|PDB:6IEU"
FT HELIX 1128..1147
FT /evidence="ECO:0007829|PDB:6IEU"
SQ SEQUENCE 1216 AA; 134663 MW; 5E0F4953230617D1 CRC64;
MARNCSECKE KRAAHILCTY CNRWLCSSCT EEHRHSPVPG GPFFPRAQKG SPGVNGGPGD
FTLYCPLHTQ EVLKLFCETC DMLTCHSCLV VEHKEHRCRH VEEVLQNQRM LLEGVTTQVA
HKKSSLQTSA KQIEDRIFEV KHQHRKVENQ IKMAKMVLMN ELNKQANGLI EELEGITNER
KRKLEQQLQS IMVLNRQFEH VQNFINWAVC SKTSVPFLFS KELIVFQMQR LLETSCNTDP
GSPWSIRFTW EPNFWTKQLA SLGCITTEGG QMSRADAPAY GGLQGSSPFY QSHQSPVAQQ
EALSHPSHKF QSPAVCSSSV CCSHCSPVSP SLKGQVPPPS IHPAHSFRQP PEMVPQQLGS
LQCSALLPRE KELACSPHPP KLLQPWLETQ PPVEQESTSQ RLGQQLTSQP VCIVPPQDVQ
QGAHAQPTLQ TPSIQVQFGH HQKLKLSHFQ QQPQQQLPPP PPPLPHPPPP LPPPPQQPHP
PLPPSQHLAS SQHESPPGPA CSQNMDIMHH KFELEEMQKD LELLLQAQQP SLQLSQTKSP
QHLQQTIVGQ INYIVRQPAP VQSQSQEETL QATDEPPASQ GSKPALPLDK NTAAALPQAS
GEETPLSVPP VDSTIQHSSP NVVRKHSTSL SIMGFSNTLE MELSSTRLER PLEPQIQSVS
NLTAGAPQAV PSLLSAPPKM VSSLTSVQNQ AMPSLTTSHL QTVPSLVHST FQSMPNLISD
SPQAMASLAS DHPQAGPSLM SGHTQAVPSL ATCPLQSIPP VSDMQPETGS SSSSGRTSGS
LCPRDGADPS LENALCKVKL EEPINLSVKK PPLAPVVSTS TALQQYQNPK ECENFEQGAL
ELDAKENQSI RAFNSEHKIP YVRLERLKIC AASSGEMPVF KLKPQKNDQD GSFLLIIECG
TESSSMSIKV SQDRLSEATQ APGLEGRKVT VTSLAGQRPP EVEGTSPEEH RLIPRTPGAK
KGPPAPIENE DFCAVCLNGG ELLCCDRCPK VFHLSCHVPA LLSFPGGEWV CTLCRSLTQP
EMEYDCENAC YNQPGMRASP GLSMYDQKKC EKLVLSLCCN NLSLPFHEPV SPLARHYYQI
IKRPMDLSII RRKLQKKDPA HYTTPEEVVS DVRLMFWNCA KFNYPDSEVA EAGRCLEVFF
EGWLKEIYPE KRFAQPRQED SDSEEVSSES GCSTPQGFPW PPYMQEGIQP KRRRRHMENE
RAKRMSFRLA NSISQV
