ID G3U4F7_LOXAF Unreviewed; 785 AA.
AC G3U4F7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Tripartite motif containing 28 {ECO:0000313|Ensembl:ENSLAFP00000022715.1};
GN Name=TRIM28 {ECO:0000313|Ensembl:ENSLAFP00000022715.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000022715.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000022715.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022715.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000022715.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000022715.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; G3U4F7; -.
DR STRING; 9785.ENSLAFP00000022715; -.
DR Ensembl; ENSLAFT00000029538.1; ENSLAFP00000022715.1; ENSLAFG00000026316.1.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160527; -.
DR HOGENOM; CLU_005817_2_0_1; -.
DR InParanoid; G3U4F7; -.
DR OMA; DCKDEVP; -.
DR TreeFam; TF106455; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IEA:Ensembl.
DR GO; GO:0070087; F:chromo shadow domain binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0035851; F:Krueppel-associated box domain binding; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin 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:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0060028; P:convergent extension involved in axis elongation; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0060669; P:embryonic placenta morphogenesis; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0071514; P:genomic imprinting; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:Ensembl.
DR GO; GO:1901536; P:negative regulation of DNA demethylation; IEA:Ensembl.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin formation; IEA:Ensembl.
DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0043045; P:post-fertilization epigenetic regulation of gene expression; IEA:Ensembl.
DR GO; GO:0016925; P:protein sumoylation; IEA:Ensembl.
DR GO; GO:0044790; P:suppression of viral release by host; IEA:Ensembl.
DR CDD; cd19846; Bbox1_TIF1b_C-VI; 1.
DR CDD; cd19829; Bbox2_TIF1b_C-VI; 1.
DR CDD; cd05502; Bromo_tif1_like; 1.
DR CDD; cd15623; PHD_TIF1beta; 1.
DR CDD; cd16765; RING-HC_TIF1beta; 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; IPR037373; KAP1.
DR InterPro; IPR047059; TIF1b_Bbox1_Znf.
DR InterPro; IPR047058; TIF1b_Bbox2_Znf.
DR InterPro; IPR042713; TIF1beta_RING-HC.
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 PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR PANTHER; PTHR45915:SF9; TRIPARTITE MOTIF CONTAINING 28; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00643; zf-B_box; 2.
DR Pfam; PF14634; zf-RING_5; 1.
DR SMART; SM00502; BBC; 1.
DR SMART; SM00336; BBOX; 2.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 2.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50119; ZF_BBOX; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 15..71
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 99..146
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 155..196
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 575..622
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 363..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 785 AA; 84755 MW; A655CA9A27CDD1E8 CRC64;
PVRGGGEVLE LLEHCGLCRE RLRPEREPRL LPCLHSACNA CLGPAAPAAS NSSGDGGAAG
DSAVVDCPVC KQQCFYKDIV ENYFMRDSGS KAATDSQDAN QQCCTSCEDN APATSYCVEC
SEPLCETCVE AHQRVKYTKD HTVRSTGPAK TRDGERTVYC SVHKHEPLVL FCESCDTLTC
RDCQLNAHKD HQYQFLEDAV RNQRKLLASL VKRLGDKHAT LQKSTKEVRS SIRQVSDVQK
RVQVDVKMAI LQIMKELNKR GRVLVNDAQK VTEGQQERLE RQHWTMTKIQ KHQEHILRFA
SWALESDNNT ALLLSKKLIY FQLHRALKMI VDPVEPHGEM KFQWDLNAWT KSAEAFGKIV
AERSGTNSTG PAPMAPPRAP GPLSKQGSGS SQPMEVQEGY GFGSDDPYSS AEPHVSGVKR
SRSGDGEVSG LMRKVPRVSL ERLDLDLTAD SQPPVFKVFP GNTTEDYNLI VIERGGAAAA
AGQPGTAPPG APGAPPLPGM AIVKEEETEA AIGAPPAAAE GPETKPVLMA LAEGPGSEGP
RLASPSGSTS SGLEVVAPEG ASASSGGPGA LDDSATICRV CQKPGDLVMC NQCEFCFHLD
CHLPALQDVP GEEWSCSLCH VLPDLKEEDG SLNLDEADTT GVVAKLSPAN QRKCERVLLA
LFCHEPCRPL HQLATDSTFS LDQPGGTLDL TLIRARLQEK LSPPYSSPQE FAQDVGRMFK
QFNKLTEDKA DVQSIIGLQR FFETRMNEAF GDTKFSAVLV EPPPLSLPGA GLGAPELSGG
PSDGL
//
