ID A0A452RLB6_URSAM Unreviewed; 1021 AA.
AC A0A452RLB6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Tripartite motif containing 24 {ECO:0000313|Ensembl:ENSUAMP00000019899.1};
GN Name=TRIM24 {ECO:0000313|Ensembl:ENSUAMP00000019899.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000019899.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000019899.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A452RLB6; -.
DR STRING; 9643.ENSUAMP00000019899; -.
DR Ensembl; ENSUAMT00000022261.1; ENSUAMP00000019899.1; ENSUAMG00000015451.1.
DR GeneTree; ENSGT00940000159863; -.
DR OMA; AIKQWQV; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; 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:0002039; F:p53 binding; 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:0071391; P:cellular response to estrogen stimulus; 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 CDD; cd19845; Bbox1_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 PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 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; 1.
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:UP000291022};
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 797..844
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 903..958
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 400..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 299..326
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 402..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..511
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 113039 MW; 3B2A7A9ED09F7662 CRC64;
MEVAVEKAAT AAAAASAAAA GGPSAAPSGE NEAESRQGPD SERGGEAARL NLLDTCAVCH
QNIQSRAPKL LPCLHSFCQR CLPAPQRYLM LPAPMLGSAE TPPPVPAPGS PVSGSSPFAT
QVGVIRCPVC SQECAERHII DNFFVKDTTE VPSSTVEKSN QVCTSCEDNA EANGFCVECV
EWLCKTCIRA HQRVKFTKDH TVRQKEEVSP GNKLLEIIGL FTCLSRYQFI EEAFQNQKVI
IDTLITKLME KTKYIKFTGN QIQNRIIEVN QNQKQVEQDI KVAIFTLMVE INKKGKALLH
QLESLAKDHR MKLMQQQQEV AGLSKQLEHV MHFSKWAVSS GSSTALLYSK RLITYRLRHL
LRARCDASPV TNNTIQFHCD PSFWAQNIIN LGSLVIEDKE SQPQMPKQNP VVEQNSQPPG
GLSSNQLSKF PTQISLAQLR LQHMQQQVMA QRQQVQRRPA PVGLPNPRMQ GPIQQPSISH
QQPPPRLINF QNHSPKPNGP VLPPHPQQLR YPPNQNMPRQ AIKPNPLQMA FLAQQAIKQW
QISSGQAAAS TANSTSSTPS SPTITSAAGY DAKAFGSPMI DLSSPVGGSY NLPSLPDIDC
SSTIMLDNIV RKDTSIDHGQ PRPPSNRTVQ SPNSSVPSPG LAGPVTMTSV HPPIRSPSAS
SVGSRGSSGS SSKPAGADST HKVPVVMLEP IRIKQENSGP PENYDFPVVI VKQESDEESR
PQNTNYPRSI LTSLLLNSSQ SSASEESVLR SDAPDSTGDQ PGLHQESSSN GKSDWLAASQ
KSPLHVGETR KEDDPNEDWC AVCQNGGELL CCEKCPKVFH LSCHVPTLAN FPSGEWICTF
CRDLSKPEVE YDCDAPSHNS EKKKTEGLVK LTPIDKRKCE RLLLFLYCHE MSLAFQDPVP
LTVPDYYRII KNPMDLSTIK KRLQEDYSMY TKPEDFVADF RLIFQNCAEF NEPDSEVANA
GIKLESYFEE LLKNLYPEKR FPKLEFRNES EDNKFSDDSD DDFVQPRKKR LKSIEERQLL
K
//
