Search Results

Overview

Uniprot ID	Q9UK61
Protein Name	Protein TASOR
Gene Name	TASOR
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
266	SLESMLNKSALDPTP
335	KDDIQTPKFVPSSRS
713	SKTVLKRKLEDLPEN
832	YEQPTCAKVENAQFK
904	GFRRQQSKSNNVEET

Function

Core component of the HUSH complex, a multiprotein complex that specifically mediates epigenetic repression of mobile genetic elements, such as retroviruses and transposable elements (PubMed:26022416, PubMed:28581500, PubMed:29211708, PubMed:32976585, PubMed:33009411, PubMed:37433650). The HUSH complex represses LINE-1 (L1) retrotransposons that are still capable of transposition (PubMed:29211708, PubMed:32976585). Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression (PubMed:29211708). The HUSH complex also represses exogenous retroviruses and synthetic transgenes (PubMed:26022416). The HUSH complex also represses expression of latent herpes simplex virus (PubMed:39589886). Mediates silencing of unintegrated retroviral DNA following recruitment by ZNF638: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed (PubMed:30487602). The HUSH complex is recruited to genomic loci rich in H3K9me3 and is required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3, as well as MORC2, a chromatin remodeler that compacts chromatin (PubMed:26022416, PubMed:28581500). Within the HUSH complex, TASOR acts as the central scaffold which recruits MPHOSPH8 and PPHLN1 to mobile genetic elements and mediates association with SETDB1 and MORC2 (PubMed:32976585, PubMed:33009411, PubMed:39589886). The ability to silence mobile genetic elements plays a crucial role in early embryonic development: it is required to maintain epiblast cell fitness and cell division (By similarity)

Protein Sequence

10 MATAVETEAC 20 QPTDASWESG 30 GGGDDEMKQA 40 LPELESSQQN 50 GGGGGLNIAE 60 PSGGAGREEN 70 AGAEAAQSLS 80 HEQPQDSSEA 90 GAAALPRGPE 100 EPERPVRRSF 110 QIPRKSREKK 120 ALFQPLTPGS 130 REFEDVVNIL 140 HSSYLEPTSV 150 TNFNYRRACL 160 VHNELLEKEF 170 TEKRRELKFD 180 GRLDKELSES 190 YAFLMVDRYQ 200 VQTICEKGLH 210 VGQSKITILG 220 SPSMGVYLSR 230 YADLLQANPL 240 DTGAMGDVVI 250 FKIMKGKIKS 260 IYDPMGVKSL 270 ESMLNKSALD 280 PTPKHECHVS 290 KNANRITSLL 300 AYRAYELTQY 310 YFYEYGFDEL 320 RRRPRHVCPY 330 AVVSFTYKDD 340 IQTPKFVPSS 350 RSNSFNTDRN 360 IDKYNYTLWK 370 GQLLNKGKLL 380 CYISLRSATR 390 AFLPIKLPEK 400 LDVETVMSID 410 HLKQKIPPAL 420 FYKETYLGPN 430 EVLKNGMYCS 440 LYEVVEKTRI 450 GSNMESLLQK 460 LDREKLVLVK 470 PLGDRGYLFL 480 LSPYQMVPPY 490 EYQTAKSRVL 500 HALFLFQEPR 510 SIVTSQKGST 520 NAAPQERHES 530 MPDVLKIAQF 540 LQFSLIQCRK 550 EFKNISAINF 560 HSVVEKYVSE 570 FFKRGFGSGK 580 REFIMFPYDS 590 RLDDKKFLYS 600 APRNKSHIDT 610 CLHAYIFRPE 620 VYQLPICKLK 630 ELFEENRKLQ 640 QFSPLSDYEG 650 QEEEMNGTKM 660 KFGKRNNSRG 670 EAIISGKQRS 680 SHSLDYDKDR 690 VKELINLIQC 700 RKKSVGGDSD 710 TEDMRSKTVL 720 KRKLEDLPEN 730 MRKLAKTSNL 740 SENCHLYEES 750 PQPIGSLGHD 760 ADLRRQQQDT 770 CNSGIADIHR 780 LFNWLSETLA 790 NARHSDASLT 800 DTVNKALGLS 810 TDDAYEELRQ 820 KHEYELNSTP 830 DKKDYEQPTC 840 AKVENAQFKG 850 TQSLLLEVDA 860 TSKYSVAIST 870 SEVGTDHKLH 880 LKEDPNLISV 890 NNFEDCSLCP 900 SVPIEHGFRR 910 QQSKSNNVEE 920 TEIHWKLIPI 930 TGGNARSPED 940 QLGKHGEKQT 950 PGMKSPEEQL 960 VCVPPQEAFP 970 NDPRVINRQR 980 SSDYQFPSSP 990 FTDTLKGTTE 1000 DDVLTGQVEE 1010 QCVPAAEAEP 1020 PAVSETTERT 1030 VLGEYNLFSR 1040 KIEEILKQKN 1050 VSYVSTVSTP 1060 IFSTQEKMKR 1070 LSEFIYSKTS 1080 KAGVQEFVDG 1090 LHEKLNTIII 1100 KASAKGGNLP 1110 PVSPNDSGAK 1120 IASNPLERHV 1130 IPVSSSDFNN 1140 KHLLEPLCSD 1150 PLKDTNSDEQ 1160 HSTSALTEVE 1170 MNQPQHATEL 1180 MVTSDHIVPG 1190 DMAREPVEET 1200 TKSPSDVNIS 1210 AQPALSNFIS 1220 QLEPEVFNSL 1230 VKIMKDVQKN 1240 TVKFYIHEEE 1250 ESVLCKEIKE 1260 YLIKLGNTEC 1270 HPEQFLERRS 1280 KLDKLLIIIQ 1290 NEDIAGFIHK 1300 IPGLVTLKKL 1310 PCVSFAGVDS 1320 LDDVKNHTYN 1330 ELFVSGGFIV 1340 SDESILNPEV 1350 VTVENLKNFL 1360 TFLEELSTPE 1370 GKWQWKVHCK 1380 FQKKLKELGR 1390 LNAKALSLLT 1400 LLNVYQKKHL 1410 VEILSYHNCD 1420 SQTRNAPELD 1430 CLIRLQAQNI 1440 QQRHIVFLTE 1450 KNIKMLSSYT 1460 DNGIVVATAE 1470 DFMQNFKNLV 1480 GYHNSITEEN 1490 LPQLGANENL 1500 ESQSALLEND 1510 EKDEEDMSLD 1520 SGDEISHIEV 1530 CSNFHSEIWE 1540 KETKGSRGTD 1550 QKKNTQIELQ 1560 SSPDVQNSLL 1570 EDKTYLDSEE 1580 RTSIDIVCSE 1590 GENSNSTEQD 1600 SYSNFQVYHS 1610 QLNMSHQFSH 1620 FNVLTHQTFL 1630 GTPYALSSSQ 1640 SQENENYFLS 1650 AYTESLDRDK 1660 SPPPLSWGKS 1670 DSSRPYSQEK

Gene Ontology

Classification	GO ID	Description
Cellular Component	GO:0000792	heterochromatin
Cellular Component	GO:0140283	HUSH complex
Cellular Component	GO:0005654	nucleoplasm
Molecular Function	GO:0003682	chromatin binding
Molecular Function	GO:0030674	protein-macromolecule adaptor activity
Molecular Function	GO:0003723	RNA binding
Biological Process	GO:0008595	anterior/posterior axis specification, embryo
Biological Process	GO:0140719	constitutive heterochromatin formation
Biological Process	GO:0006351	DNA-templated transcription
Biological Process	GO:0060809	mesodermal to mesenchymal transition involved in gastrulation
Biological Process	GO:0045814	negative regulation of gene expression, epigenetic
Biological Process	GO:0097355	protein localization to heterochromatin
Biological Process	GO:0141005	transposable element silencing by heterochromatin formation

Reference

PMID: N/A