EKS-MUM-00527
Eukaryotic Protein Kinase & Protein Phosphatase Database
TagContent
EKPD IDEKS-MUM-00527
Classification
Group/FamilyScoreE-ValueStartEndDomain Length
Atypical/TIF1N/AN/AN/AN/AN/A
StatusReviewed
Ensembl ProteinENSMUSP00000005705
UniProt AccessionQ62318; P70391; Q8C283; Q99PN4;
Protein NameTranscription intermediary factor 1-beta
Protein Synonyms/Alias TIF1-beta; E3 SUMO-protein ligase TRIM28; KRAB-A-interacting protein; KRIP-1; Tripartite motif-containing protein 28;
Gene NameTrim28
Gene Synonyms/Alias Trim28; Krip1, Tif1b;
Ensembl Information
Ensembl Gene IDEnsembl Protein IDEnsembl Transcript ID
ENSMUSG00000005566ENSMUSP00000005705ENSMUST00000005705
OrganismMus musculus
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. 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 (By similarity).
Protein Length834
Protein Sequence
(FASTA)
MAASAAATAA ASAATAASAA SGSPGSGEGS AGGEKRPAAS SAAAASAAAS SPAGGGGEAQ 60
ELLEHCGVCR ERLRPERDPR LLPCLHSACS ACLGPATPAA ANNSGDGGSA GDGAMVDCPV 120
CKQQCYSKDI VENYFMRDSG SKASSDSQDA NQCCTSCEDN APATSYCVEC SEPLCETCVE 180
AHQRVKYTKD HTVRSTGPAK TRDGERTVYC NVHKHEPLVL FCESCDTLTC RDCQLNAHKD 240
HQYQFLEDAV RNQRKLLASL VKRLGDKHAT LQKNTKEVRS SIRQVSDVQK RVQVDVKMAI 300
LQIMKELNKR GRVLVNDAQK VTEGQQERLE RQHWTMTKIQ KHQEHILRFA SWALESDNNT 360
ALLLSKKLIY FQLHRALKMI VDPVEPHGEM KFQWDLNAWT KSAEAFGKIV AERPGTNSTG 420
PGPMAPPRAP GPLSKQGSGS SQPMEVQEGY GFGSDDPYSS AEPHVSGMKR SRSGEGEVSG 480
LLRKVPRVSL ERLDLDLTSD SQPPVFKVFP GSTTEDYNLI VIERGAAAAA AGQAGTVPPG 540
APGAPPLPGM AIVKEEETEA AIGAPPAAPE GPETKPVLMP LTEGPGAEGP RLASPSGSTS 600
SGLEVVAPEV TSAPVSGPGI LDDSATICRV CQKPGDLVMC NQCEFCFHLD CHLPALQDVP 660
GEEWSCSLCH VLPDLKEEDG SLSLDGADST GVVAKLSPAN QRKCERVLLA LFCHEPCRPL 720
HQLATDSTFS MEQPGGTLDL TLIRARLQEK LSPPYSSPQE FAQDVGRMFK QFNKLTEDKA 780
DVQSIIGLQR FFETRMNDAF GDTKFSAVLV EPPPLNLPSA GLSSQELSGP GDGP 834
Nucleotide Sequence
(FASTA)
ATGGCGGCCT CGGCGGCAGC GACTGCAGCG GCCTCGGCCG CGACGGCCGC CTCGGCGGCC 60
TCTGGTAGCC CAGGGTCGGG CGAGGGCTCG GCGGGCGGTG AGAAGCGTCC GGCTGCTTCC 120
TCAGCCGCGG CGGCCTCTGC AGCCGCGTCG TCCCCTGCGG GGGGCGGTGG CGAGGCGCAG 180
GAGCTTCTGG AGCACTGCGG CGTGTGTCGC GAGCGCCTGC GGCCCGAGCG GGATCCTCGG 240
CTGCTGCCCT GTCTACATTC GGCCTGCAGT GCCTGCCTGG GCCCCGCTAC ACCCGCCGCA 300
GCGAATAATT CGGGGGATGG CGGCTCGGCG GGCGACGGCG CTATGGTGGA TTGTCCAGTG 360
TGCAAACAGC AGTGCTACTC CAAAGACATC GTGGAGAATT ATTTTATGCG TGATAGTGGC 420
AGTAAGGCCT CTTCTGATTC CCAGGATGCT AACCAGTGCT GCACTAGCTG TGAAGATAAT 480
GCCCCAGCCA CTAGCTATTG TGTGGAGTGC TCTGAACCAC TTTGTGAGAC CTGTGTGGAG 540
GCTCACCAGC GGGTGAAATA CACCAAGGAC CACACTGTGC GCTCCACAGG ACCTGCTAAG 600
ACTCGAGATG GAGAGCGAAC AGTCTACTGT AATGTGCACA AGCATGAGCC CCTCGTGCTG 660
TTCTGTGAGA GCTGTGACAC ACTCACCTGC CGCGACTGCC AGCTCAACGC TCACAAGGAC 720
CATCAGTACC AGTTTTTGGA AGATGCAGTG AGGAACCAAC GTAAACTCTT GGCTTCACTG 780
GTGAAACGTC TTGGGGACAA ACATGCCACA CTTCAGAAAA ACACCAAGGA GGTTCGAAGC 840
TCGATCCGCC AGGTGTCTGA TGTGCAGAAG CGAGTGCAGG TTGATGTCAA GATGGCCATT 900
CTGCAGATCA TGAAGGAGCT GAATAAGCGG GGTCGAGTTC TGGTCAATGA TGCCCAGAAG 960
GTGACCGAGG GTCAGCAGGA ACGTCTGGAG CGCCAGCACT GGACCATGAC CAAAATTCAG 1020
AAGCACCAGG AACACATTTT GCGTTTTGCC TCTTGGGCTC TGGAGAGTGA TAACAATACA 1080
GCTCTCTTGC TCTCTAAGAA GCTGATCTAT TTCCAGCTGC ATCGGGCCCT CAAAATGATT 1140
GTGGATCCTG TGGAGCCTCA TGGTGAGATG AAGTTTCAGT GGGATCTCAA TGCCTGGACC 1200
AAGAGTGCTG AAGCCTTTGG CAAGATTGTG GCTGAGCGTC CTGGTACGAA CTCCACAGGT 1260
CCTGGGCCCA TGGCTCCTCC AAGAGCCCCA GGCCCTCTAA GCAAGCAAGG TTCTGGCAGT 1320
AGCCAGCCCA TGGAAGTACA AGAGGGATAT GGCTTTGGGT CAGATGATCC CTATTCAAGT 1380
GCAGAGCCGC ATGTATCAGG CATGAAGCGG TCCCGCTCTG GTGAGGGAGA GGTAAGTGGC 1440
CTCTTAAGGA AGGTGCCACG TGTGAGCCTT GAACGCCTGG ATCTGGACCT CACCTCTGAC 1500
AGCCAGCCAC CAGTCTTCAA GGTCTTTCCT GGAAGCACTA CTGAGGACTA CAATCTGATT 1560
GTTATTGAGC GTGGTGCTGC TGCAGCAGCT GCTGGTCAGG CTGGGACTGT GCCACCAGGA 1620
GCCCCTGGTG CCCCACCCCT TCCTGGCATG GCCATTGTCA AGGAAGAAGA GACAGAAGCT 1680
GCTATTGGAG CTCCCCCGGC TGCCCCCGAG GGTCCTGAAA CCAAGCCTGT GTTGATGCCT 1740
CTGACTGAAG GTCCTGGTGC CGAGGGACCT CGTCTAGCTT CACCTAGTGG CAGTACCAGC 1800
TCAGGCTTGG AGGTGGTGGC TCCTGAGGTT ACCTCAGCCC CAGTAAGTGG GCCAGGTATC 1860
CTGGATGACA GTGCCACTAT CTGCCGTGTC TGCCAGAAAC CAGGTGACCT GGTCATGTGT 1920
AACCAGTGCG AATTTTGCTT CCACCTGGAT TGCCACCTCC CTGCCCTGCA GGATGTTCCA 1980
GGGGAGGAAT GGAGTTGCTC ACTCTGCCAC GTGCTCCCTG ACCTAAAGGA GGAAGATGGA 2040
AGCCTCAGCC TGGATGGAGC AGATAGCACT GGTGTGGTAG CTAAACTCTC ACCAGCCAAC 2100
CAGCGGAAAT GTGAGCGTGT TCTCCTGGCC CTGTTCTGCC ATGAACCATG CCGTCCCTTG 2160
CATCAGCTGG CTACCGACTC TACATTCTCC ATGGAGCAGC CTGGTGGTAC CCTAGACCTG 2220
ACCTTGATTC GTGCTCGCCT CCAAGAGAAG CTGTCACCTC CTTATAGCTC CCCCCAGGAG 2280
TTTGCTCAAG ATGTGGGCCG CATGTTCAAA CAGTTCAACA AGCTGACTGA GGACAAGGCA 2340
GATGTTCAGT CCATCATCGG CTTGCAGCGC TTCTTTGAGA CACGCATGAA TGATGCCTTT 2400
GGTGACACCA AGTTTTCTGC TGTGCTGGTA GAACCACCAC CATTGAACCT TCCCAGTGCT 2460
GGCCTAAGTT CTCAGGAGCT CTCTGGCCCT GGTGATGGCC CCTGA 2505
Domain Profile
N/A
Domain Sequence
(FASTA)
N/A
KeywordAcetylation; Alternative splicing; Bromodomain; Complete proteome; Isopeptide bond; Ligase; Metal-binding; Nucleus; Phosphoprotein; 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"; ?>Homo sapiens"; ?>Ictidomys tridecemlineatus"; ?>Latimeria chalumnae"; ?>Loxodonta africana"; ?>Macaca mulatta"; ?>Macropus eugenii"; ?>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-HOS-00503
EKS-ICT-00478
EKS-LAC-00511
EKS-LOA-00508
EKS-MAM-00500
EKS-MAE-00085
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:0003713; F:transcription coactivator activity
GO:0003714; F:transcription corepressor activity
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: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:0006351; P:transcription, DNA-dependent
KEGG
mmu:21849;
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