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Database: UniProt
Entry: A0A3Q2I2V4_HORSE
LinkDB: A0A3Q2I2V4_HORSE
Original site: A0A3Q2I2V4_HORSE 
ID   A0A3Q2I2V4_HORSE        Unreviewed;      1050 AA.
AC   A0A3Q2I2V4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 2.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Tripartite motif containing 24 {ECO:0000313|Ensembl:ENSECAP00000041480.2};
GN   Name=TRIM24 {ECO:0000313|Ensembl:ENSECAP00000041480.2,
GN   ECO:0000313|VGNC:VGNC:24497};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000041480.2, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000041480.2, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000041480.2,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000041480.2}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000041480.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q2I2V4; -.
DR   Ensembl; ENSECAT00000052478.2; ENSECAP00000041480.2; ENSECAG00000021957.4.
DR   VGNC; VGNC:24497; TRIM24.
DR   GeneTree; ENSGT00940000159863; -.
DR   InParanoid; A0A3Q2I2V4; -.
DR   OMA; AIKQWQV; -.
DR   Proteomes; UP000002281; Chromosome 4.
DR   Bgee; ENSECAG00000021957; Expressed in inner cell mass and 23 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q2I2V4; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR   GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005726; C:perichromatin fibrils; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0034056; F:estrogen response element binding; IEA:Ensembl.
DR   GO; GO:0070577; F:lysine-acetylated histone binding; IEA:Ensembl.
DR   GO; GO:0016922; F:nuclear receptor binding; IEA:Ensembl.
DR   GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR   GO; GO:0004672; F:protein kinase activity; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
DR   GO; GO:0071391; P:cellular response to estrogen stimulus; IEA:Ensembl.
DR   GO; GO:0050673; P:epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR   GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; IEA:Ensembl.
DR   GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd19845; Bbox1_TIF1a_C-VI; 1.
DR   CDD; cd19828; Bbox2_TIF1a_C-VI; 1.
DR   CDD; cd05502; Bromo_tif1_like; 1.
DR   CDD; cd15622; PHD_TIF1alpha; 1.
DR   CDD; cd16764; RING-HC_TIF1alpha; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR   PANTHER; PTHR45915:SF4; TRANSCRIPTION INTERMEDIARY FACTOR 1-ALPHA; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 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.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00024}.
FT   DOMAIN          56..131
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          158..211
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          218..259
FT                   /note="B box-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50119"
FT   DOMAIN          826..873
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          932..987
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          476..552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          770..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          328..355
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        436..456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        499..525
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..549
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        648..671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        680..706
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..806
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1050 AA;  116581 MW;  FDEC393EE78DD0BB CRC64;
     MEVAVEKAAT AAAAASAAAA GGPSAAPSGE NEAESRQGPD SERGGEAARL NLLDTCAVCH
     QNIQSRTPKL LPCLHSFCQR CLPAPQRYLM LSAPLLGSAE TPPPVPAPGS PGSGSSPFAT
     QVGVIRCPVC SQECAERHII DNFFVKDTTE VPSSTVEKSN QVCTSCEDNA EANGFCVECV
     EWLCKTCIRA HQRVKFTKDH TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK
     LTCRDCQLLE HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKFTGNQ IQNRIIEVNQ
     NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA GLSKQLEHVM
     HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT NNTIQFHCDP SFWAQNIINL
     GSLVIEDKES QPHMPKQNPV VEQNSQPPGG LSSNQLSKFP TQISLAQLRL QHMQQQVMAQ
     RQQVQRRPAP VGLPNPRMQG PIQQPSISHQ QPPPRLINFQ NHSPKPNGPV LPPHPQQLRY
     PPNQSMPRPA IKPNPLQMAF LAQQAIKQWQ ISSGQAAPST ANSTSSTPSS PTITSAAGYD
     GKAFGSPMID LSSPVGGSYN LPSLPDIDCS STIMLDNIVR KDTSIDHGQP RPPSNRTVQS
     PNSSVPSPGL AGPVTMTSVH PPIRSPSASS VGSRGSSGSS SKPAGADSTH KVPVVMLEPI
     RIKQENSGPP ENYDFPVVIV KQESDEESRP QNTNYPRSIL TSLLLNSSQS SASEESVLRS
     DAPDSTGDQP GLQQENSSNG KSEWLDASQK SPLHVGETRK EDDPNEDWCA VCQNGGELLC
     CEKCPKVFHL SCHVPTLANF PSGEWICTFC RDLSKPEVEY DCDAPSHNSE KKKTEGLVKL
     TPIDKRKCER LLLFLYCHEM SLAFQDPVPL TVPDYYKIIK NPMDLSTIKK RLQEDYSMYT
     KPEDFVADFR LIFQNCAEFN EPDSEVANAG IKLESYFEEL LKNLYPEKRF PKLEFRNESE
     DNKFSDDSDD DFVQPRKKRL KSIEERQLLK
//
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