EKS-HOS-00503
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-HOS-00503
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
Atypical/TIF1N/AN/AN/AN/AN/A
StatusReviewed
Ensembl ProteinENSP00000253024
UniProt AccessionQ13263; O00677; Q7Z632; Q93040; Q96IM1;
Protein NameTranscription intermediary factor 1-beta
Protein Synonyms/Alias TIF1-beta; E3 SUMO-protein ligase TRIM28; KRAB-associated protein 1; KAP-1; KRAB-interacting protein 1; KRIP-1; Nuclear corepressor KAP-1; RING finger protein 96; Tripartite motif-containing protein 28;
Gene NameTRIM28
Gene Synonyms/Alias TRIM28; KAP1, RNF96, TIF1B;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSG00000130726ENSP00000342232ENST00000341753
ENSG00000130726ENSP00000253024ENST00000253024
ENSG00000130726ENSP00000471303ENST00000597136
ENSG00000130726ENSP00000470503ENST00000597968
ENSG00000130726ENSP00000473126ENST00000594806
ENSG00000130726ENSP00000472586ENST00000593582
OrganismHomo sapiens
Functional DescriptionNuclear corepressor for KRAB domain-containing zincfinger proteins (KRAB-ZFPs). Mediates gene silencing by recruiting CHD3, a subunit of the nucleosome remodeling and deacetylation (NuRD) complex, and SETDB1 (which specifically methylates histone H3 at 'Lys-9' (H3K9me)) to the promoter regions of KRAB target genes. Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. Recruitment of SETDB1 induces heterochromatinization. May play a role as a coactivator for CEBPB and NR3C1 in the transcriptional activation of ORM1. Also corepressor for ERBB4. Inhibits E2F1 activity by stimulating E2F1-HDAC1 complex formation and inhibiting E2F1 acetylation. May serve as a partial backup to prevent E2F1-mediated apoptosis in the absence of RB1. Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. Also specifically sumoylates IRF7, thereby inhibiting its transactivation activity. Ubiquitinates p53/TP53 leading to its proteosomal degradation; the function is enhanced by MAGEC2 and MAGEA2, and possibly MAGEA3 and MAGEA6.
Protein Length835
Protein Sequence
(FASTA)
MAASAAAASA AAASAASGSP GPGEGSAGGE KRSTAPSAAA SASASAAASS PAGGGAEALE 60
LLEHCGVCRE RLRPEREPRL LPCLHSACSA CLGPAAPAAA NSSGDGGAAG DGTVVDCPVC 120
KQQCFSKDIV ENYFMRDSGS KAATDAQDAN QCCTSCEDNA PATSYCVECS EPLCETCVEA 180
HQRVKYTKDH TVRSTGPAKS RDGERTVYCN VHKHEPLVLF CESCDTLTCR DCQLNAHKDH 240
QYQFLEDAVR NQRKLLASLV KRLGDKHATL QKSTKEVRSS IRQVSDVQKR VQVDVKMAIL 300
QIMKELNKRG RVLVNDAQKV TEGQQERLER QHWTMTKIQK HQEHILRFAS WALESDNNTA 360
LLLSKKLIYF QLHRALKMIV DPVEPHGEMK FQWDLNAWTK SAEAFGKIVA ERPGTNSTGP 420
APMAPPRAPG PLSKQGSGSS QPMEVQEGYG FGSGDDPYSS AEPHVSGVKR SRSGEGEVSG 480
LMRKVPRVSL ERLDLDLTAD SQPPVFKVFP GSTTEDYNLI VIERGAAAAA TGQPGTAPAG 540
TPGAPPLAGM AIVKEEETEA AIGAPPTATE GPETKPVLMA LAEGPGAEGP RLASPSGSTS 600
SGLEVVAPEG TSAPGGGPGT LDDSATICRV CQKPGDLVMC NQCEFCFHLD CHLPALQDVP 660
GEEWSCSLCH VLPDLKEEDG SLSLDGADST GVVAKLSPAN QRKCERVLLA LFCHEPCRPL 720
HQLATDSTFS LDQPGGTLDL TLIRARLQEK LSPPYSSPQE FAQDVGRMFK QFNKLTEDKA 780
DVQSIIGLQR FFETRMNEAF GDTKFSAVLV EPPPMSLPGA GLSSQELSGG PGDGP 835
Nucleotide Sequence
(FASTA)
ATGGCGGCCT CCGCGGCGGC AGCCTCGGCA GCAGCGGCCT CGGCCGCCTC TGGCAGCCCG 60
GGCCCGGGCG AGGGCTCCGC TGGCGGCGAA AAGCGCTCCA CCGCCCCTTC GGCCGCAGCC 120
TCGGCCTCTG CCTCAGCCGC GGCGTCGTCG CCCGCGGGGG GCGGCGCCGA GGCGCTGGAG 180
CTGCTGGAGC ACTGCGGCGT GTGCAGAGAG CGCCTGCGAC CCGAGAGGGA GCCCCGCCTG 240
CTGCCCTGTT TGCACTCGGC CTGTAGTGCC TGCTTAGGGC CCGCGGCCCC CGCCGCCGCC 300
AACAGCTCGG GGGACGGCGG GGCGGCGGGC GACGGCACCG TGGTGGACTG TCCCGTGTGC 360
AAGCAACAGT GCTTCTCCAA AGACATCGTG GAGAATTATT TCATGCGTGA TAGTGGCAGC 420
AAGGCTGCCA CCGACGCCCA GGATGCGAAC CAGTGCTGCA CTAGCTGTGA GGATAATGCC 480
CCAGCCACCA GCTACTGTGT GGAGTGCTCG GAGCCTCTGT GTGAGACCTG TGTAGAGGCG 540
CACCAGCGGG TGAAGTACAC CAAGGACCAT ACTGTGCGCT CTACTGGGCC AGCCAAGTCT 600
CGGGATGGTG AACGTACTGT CTATTGCAAC GTACACAAGC ATGAACCCCT TGTGCTGTTT 660
TGTGAGAGCT GTGATACTCT CACCTGCCGA GACTGCCAGC TCAATGCCCA CAAGGACCAC 720
CAGTACCAGT TCTTAGAGGA TGCAGTGAGG AACCAGCGCA AGCTCCTGGC CTCACTGGTG 780
AAGCGCCTTG GGGACAAACA TGCAACATTG CAGAAGAGCA CCAAGGAGGT TCGCAGCTCA 840
ATCCGCCAGG TGTCTGACGT ACAGAAGCGT GTGCAAGTGG ATGTCAAGAT GGCCATCCTG 900
CAGATCATGA AGGAGCTGAA TAAGCGGGGC CGTGTGCTGG TCAATGATGC CCAGAAGGTG 960
ACTGAGGGGC AGCAGGAGCG CCTGGAGCGG CAGCACTGGA CCATGACCAA GATCCAGAAG 1020
CACCAGGAGC ACATTCTGCG CTTTGCCTCT TGGGCTCTGG AGAGTGACAA CAACACAGCC 1080
CTTTTGCTTT CTAAGAAGTT GATCTACTTC CAGCTGCACC GGGCCCTCAA GATGATTGTG 1140
GATCCCGTGG AGCCACATGG CGAGATGAAG TTTCAGTGGG ACCTCAATGC CTGGACCAAG 1200
AGTGCCGAGG CCTTTGGCAA GATTGTGGCA GAGCGTCCTG GCACTAACTC AACAGGCCCT 1260
GCACCCATGG CCCCTCCAAG AGCCCCAGGG CCCCTGAGCA AGCAGGGCTC TGGCAGCAGC 1320
CAGCCCATGG AGGTGCAGGA AGGCTATGGC TTTGGGTCAG GAGATGATCC CTACTCAAGT 1380
GCAGAGCCCC ATGTGTCAGG TGTGAAACGG TCCCGCTCAG GTGAGGGCGA GGTGAGCGGC 1440
CTTATGCGCA AGGTGCCACG AGTGAGCCTT GAACGCCTGG ACCTGGACCT CACAGCTGAC 1500
AGCCAGCCAC CCGTCTTCAA GGTCTTCCCA GGCAGTACCA CTGAGGACTA CAACCTTATT 1560
GTTATTGAAC GTGGCGCTGC CGCTGCAGCT ACCGGCCAGC CAGGGACTGC GCCTGCAGGA 1620
ACCCCTGGTG CCCCACCCCT GGCTGGCATG GCCATTGTCA AGGAGGAGGA GACGGAGGCT 1680
GCCATTGGAG CCCCTCCTAC TGCCACTGAG GGCCCTGAGA CCAAACCTGT GCTTATGGCT 1740
CTTGCGGAGG GTCCTGGTGC TGAGGGTCCC CGCCTGGCCT CACCTAGTGG CAGCACCAGC 1800
TCAGGGCTGG AGGTGGTGGC TCCTGAGGGT ACCTCAGCCC CAGGTGGTGG CCCGGGAACC 1860
CTGGATGACA GTGCCACCAT TTGCCGTGTC TGCCAGAAGC CAGGCGATCT GGTTATGTGC 1920
AACCAGTGTG AGTTTTGTTT CCACCTGGAC TGTCACCTGC CGGCCCTGCA GGATGTACCA 1980
GGGGAGGAGT GGAGCTGCTC ACTCTGCCAT GTGCTCCCTG ACCTGAAGGA GGAGGATGGC 2040
AGCCTCAGCC TGGATGGTGC AGACAGCACT GGCGTGGTGG CCAAGCTCTC ACCAGCCAAC 2100
CAGCGGAAAT GTGAGCGTGT ACTGCTGGCC CTATTCTGTC ACGAACCCTG CCGCCCCCTG 2160
CATCAGCTGG CTACCGACTC CACCTTCTCC CTGGACCAGC CCGGTGGCAC CCTGGATCTG 2220
ACCCTGATCC GTGCCCGCCT CCAGGAGAAG TTGTCACCTC CCTACAGCTC CCCACAGGAG 2280
TTTGCCCAGG ATGTGGGCCG CATGTTCAAG CAATTCAACA AGTTAACTGA GGACAAGGCA 2340
GACGTGCAGT CCATCATCGG CCTGCAGCGC TTCTTCGAGA CGCGCATGAA CGAGGCCTTC 2400
GGTGACACCA AGTTCTCTGC TGTGCTGGTG GAGCCCCCGC CGATGAGCCT GCCTGGTGCT 2460
GGCCTGAGTT CCCAGGAGCT GTCTGGTGGC CCTGGTGATG GCCCCTGA 2508
Domain Profile
N/A
Domain Sequence
(FASTA)
N/A
Keyword3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Isopeptide bond; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
Sequence SourceEnsembl
Orthology
Ortholog group
Anolis carolinensis"; ?>Callithrix jacchus"; ?>Canis familiaris"; ?>Cavia porcellus"; ?>Echinops telfairi"; ?>Equus caballus"; ?>Erinaceus europaeus"; ?>Felis catus"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Macropus eugenii"; ?>Mus musculus"; ?>Mustela putorius furo"; ?>Myotis lucifugus"; ?>Nomascus leucogenys"; ?>Ornithorhynchus anatinus"; ?>Oryctolagus cuniculus"; ?>Otolemur garnettii"; ?>Pan troglodytes"; ?>Pelodiscus sinensis"; ?>Pongo abelii"; ?>Procavia capensis"; ?>Pteropus vampyrus"; ?>Rattus norvegicus"; ?>Sarcophilus harrisii"; ?>Tursiops truncatus"; ?>Xenopus tropicalis"; ?>
EKS-ANC-00490
EKS-CAJ-00512
EKS-CAF-00499
EKS-CAP-00535
EKS-ECT-00085
EKS-EQC-00483
EKS-ERE-00064
EKS-FEC-00478
EKS-ICT-00478
EKS-LAC-00511
EKS-LOA-00508
EKS-MAM-00500
EKS-MAE-00085
EKS-MUM-00527
EKS-MUP-00486
EKS-MYL-00489
EKS-NOL-00456
EKS-ORA-00433
EKS-ORC-00467
EKS-OTG-00507
EKS-PAT-00466
EKS-PES-00436
EKS-POA-00487
EKS-PRC-00084
EKS-PTV-00196
EKS-RAN-00514
EKS-SAH-00467
EKS-TUT-00203
EKS-XET-00656
Gene Ontology
GO:0005719; C:nuclear euchromatin
GO:0005720; C:nuclear heterochromatin
GO:0005654; C:nucleoplasm
GO:0003677; F:DNA binding
GO:0004672; F:protein kinase activity
GO:0043565; F:sequence-specific DNA binding
GO:0003700; F:sequence-specific DNA binding transcription factor activity
GO:0003713; F:transcription coactivator activity
GO:0003714; F:transcription corepressor activity
GO:0031625; F:ubiquitin protein ligase binding
GO:0004842; F:ubiquitin-protein ligase activity
GO:0008270; F:zinc ion binding
GO:0060028; P:convergent extension involved in axis elongation
GO:0006281; P:DNA repair
GO:0060669; P:embryonic placenta morphogenesis
GO:0001837; P:epithelial to mesenchymal transition
GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter
GO:0045892; P:negative regulation of transcription, DNA-dependent
GO:0045739; P:positive regulation of DNA repair
GO:0045893; P:positive regulation of transcription, DNA-dependent
GO:0046777; P:protein autophosphorylation
GO:0051259; P:protein oligomerization
GO:0016925; P:protein sumoylation
GO:0006367; P:transcription initiation from RNA polymerase II promoter
KEGG
hsa:10155;
InterPros
IPR003649; Bbox_C.
IPR001487; Bromodomain.
IPR019786; Zinc_finger_PHD-type_CS.
IPR000315; Znf_B-box.
IPR011011; Znf_FYVE_PHD.
IPR001965; Znf_PHD.
IPR019787; Znf_PHD-finger.
IPR001841; Znf_RING.
IPR013083; Znf_RING/FYVE/PHD.
Pfam
PF00628; PHD; 1.
PF00643; zf-B_box; 2.
SMARTs
SM00502; BBC; 1.
SM00336; BBOX; 2.
SM00297; BROMO; 1.
SM00249; PHD; 1.
SM00184; RING; 2.
Prosites
PS00633; BROMODOMAIN_1; FALSE_NEG.
PS50014; BROMODOMAIN_2; FALSE_NEG.
PS50119; ZF_BBOX; 2.
PS01359; ZF_PHD_1; 1.
PS50016; ZF_PHD_2; 1.
PS00518; ZF_RING_1; FALSE_NEG.
PS50089; ZF_RING_2; 1.
Prints
Created Date20-Feb-2013