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Open data
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Basic information
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![]() | KRAB-associated protein 1 (KAP1); TRIM28, amino acids 23-812
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Function / homology | ![]() convergent extension involved in axis elongation / : / Krueppel-associated box domain binding / embryonic placenta morphogenesis / positive regulation of DNA methylation-dependent heterochromatin formation / suppression of viral release by host / genomic imprinting / negative regulation of single stranded viral RNA replication via double stranded DNA intermediate / chromo shadow domain binding / Generic Transcription Pathway ...convergent extension involved in axis elongation / : / Krueppel-associated box domain binding / embryonic placenta morphogenesis / positive regulation of DNA methylation-dependent heterochromatin formation / suppression of viral release by host / genomic imprinting / negative regulation of single stranded viral RNA replication via double stranded DNA intermediate / chromo shadow domain binding / Generic Transcription Pathway / SUMO transferase activity / protein sumoylation / epithelial to mesenchymal transition / heterochromatin / embryo implantation / positive regulation of DNA repair / SUMOylation of transcription cofactors / promoter-specific chromatin binding / RING-type E3 ubiquitin transferase / euchromatin / HCMV Early Events / positive regulation of protein import into nucleus / RNA polymerase II transcription regulator complex / ubiquitin-protein transferase activity / transcription corepressor activity / ubiquitin protein ligase activity / chromatin organization / transcription coactivator activity / protein kinase activity / innate immune response / DNA repair / negative regulation of DNA-templated transcription / ubiquitin protein ligase binding / chromatin binding / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / RNA binding / zinc ion binding / nucleoplasm / nucleus Similarity search - Function |
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![]() | ![]() Title: KAP1 is an antiparallel dimer with a functional asymmetry. Authors: Giulia Fonti / Maria J Marcaida / Louise C Bryan / Sylvain Träger / Alexandra S Kalantzi / Pierre-Yves Jl Helleboid / Davide Demurtas / Mark D Tully / Sergei Grudinin / Didier Trono / Beat ...Authors: Giulia Fonti / Maria J Marcaida / Louise C Bryan / Sylvain Träger / Alexandra S Kalantzi / Pierre-Yves Jl Helleboid / Davide Demurtas / Mark D Tully / Sergei Grudinin / Didier Trono / Beat Fierz / Matteo Dal Peraro / ![]() ![]() Abstract: KAP1 (KRAB domain-associated protein 1) plays a fundamental role in regulating gene expression in mammalian cells by recruiting different transcription factors and altering the chromatin state. In ...KAP1 (KRAB domain-associated protein 1) plays a fundamental role in regulating gene expression in mammalian cells by recruiting different transcription factors and altering the chromatin state. In doing so, KAP1 acts both as a platform for macromolecular interactions and as an E3 small ubiquitin modifier ligase. This work sheds light on the overall organization of the full-length protein combining solution scattering data, integrative modeling, and single-molecule experiments. We show that KAP1 is an elongated antiparallel dimer with an asymmetry at the C-terminal domains. This conformation is consistent with the finding that the Really Interesting New Gene (RING) domain contributes to KAP1 auto-SUMOylation. Importantly, this intrinsic asymmetry has key functional implications for the KAP1 network of interactions, as the heterochromatin protein 1 (HP1) occupies only one of the two putative HP1 binding sites on the KAP1 dimer, resulting in an unexpected stoichiometry, even in the context of chromatin fibers. |
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Structure visualization
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Related structure data | C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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External links
Related items in Molecule of the Month |
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-Models
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Sample
![]() | Name: KRAB-associated protein 1 (KAP1); TRIM28, amino acids 23-812 Specimen concentration: 12 mg/ml |
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Buffer | Name: 20 mM HEPES, 500 mM NaCl, 10 % Glycerol, 2 mM TCEP / pH: 7.5 |
Entity #1378 | Name: KAP1, residues23-812 / Type: protein Description: Transcription intermediary factor 1-beta, TIF1b, KAP1, TRIM28; amino acids 23-812 Formula weight: 87.513 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: Q13263 Sequence: MGSSHHHHHH SQDPNSSSEN LYFQGEGSAG GEKRSTAPSA AASASASAAA SSPAGGGAEA LELLEHCGVC RERLRPEREP RLLPCLHSAC SACLGPAAPA AANSSGDGGA AGDGTVVDCP VCKQQCFSKD IVENYFMRDS GSKAATDAQD ANQCCTSCED NAPATSYCVE ...Sequence: MGSSHHHHHH SQDPNSSSEN LYFQGEGSAG GEKRSTAPSA AASASASAAA SSPAGGGAEA LELLEHCGVC RERLRPEREP RLLPCLHSAC SACLGPAAPA AANSSGDGGA AGDGTVVDCP VCKQQCFSKD IVENYFMRDS GSKAATDAQD ANQCCTSCED NAPATSYCVE CSEPLCETCV EAHQRVKYTK DHTVRSTGPA KSRDGERTVY CNVHKHEPLV LFCESCDTLT CRDCQLNAHK DHQYQFLEDA VRNQRKLLAS LVKRLGDKHA TLQKSTKEVR SSIRQVSDVQ KRVQVDVKMA ILQIMKELNK RGRVLVNDAQ KVTEGQQERL ERQHWTMTKI QKHQEHILRF ASWALESDNN TALLLSKKLI YFQLHRALKM IVDPVEPHGE MKFQWDLNAW TKSAEAFGKI VAERPGTNST GPAPMAPPRA PGPLSKQGSG SSQPMEVQEG YGFGSGDDPY SSAEPHVSGV KRSRSGEGEV SGLMRKVPRV SLERLDLDLT ADSQPPVFKV FPGSTTEDYN LIVIERGAAA AATGQPGTAP AGTPGAPPLA GMAIVKEEET EAAIGAPPTA TEGPETKPVL MALAEGPGAE GPRLASPSGS TSSGLEVVAP EGTSAPGGGP GTLDDSATIC RVCQKPGDLV MCNQCEFCFH LDCHLPALQD VPGEEWSCSL CHVLPDLKEE DGSLSLDGAD STGVVAKLSP ANQRKCERVL LALFCHEPCR PLHQLATDST FSLDQPGGTL DLTLIRARLQ EKLSPPYSSP QEFAQDVGRM FKQFNKLTED KADVQSIIGL QRFFETRMNE AFGDTKFSAV LVEP |
-Experimental information
Beam | Instrument name: ESRF BM29 / City: Grenoble / 国: France ![]() | ||||||||||||||||||||||||||||||
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Detector | Name: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm | ||||||||||||||||||||||||||||||
Scan | Measurement date: Jul 6, 2017 / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 3000 / Unit: 1/nm /
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Distance distribution function P(R) |
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