TASOR_HUMAN
ID TASOR_HUMAN Reviewed; 1670 AA.
AC Q9UK61; A1L3A4; B5ME28; Q9H2F7; Q9UPP7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein TASOR {ECO:0000305};
DE AltName: Full=CTCL tumor antigen se89-1 {ECO:0000303|PubMed:11149944};
DE AltName: Full=Retinoblastoma-associated protein RAP140 {ECO:0000303|PubMed:18726359};
DE AltName: Full=Transgene activation suppressor protein {ECO:0000303|PubMed:26022416};
GN Name=TASOR {ECO:0000303|PubMed:26022416, ECO:0000312|HGNC:HGNC:30314};
GN Synonyms=C3orf63 {ECO:0000312|HGNC:HGNC:30314},
GN FAM208A {ECO:0000312|HGNC:HGNC:30314},
GN KIAA1105 {ECO:0000303|PubMed:10470851};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ARG-1046.
RC TISSUE=Fetal brain;
RX PubMed=18726359; DOI=10.1007/bf02882285;
RA Li Q., Wen H., Ao S.;
RT "Identification and cloning of the cDNA of a Rb-associated protein
RT RAP140a.";
RL Sci. China, Ser. C, Life Sci. 43:637-647(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-598 (ISOFORM 1).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 376-1670 (ISOFORM 3).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 523-1274 (ISOFORM 4), AND VARIANTS ARG-1046
RP AND VAL-1435.
RC TISSUE=Testis;
RX PubMed=11149944; DOI=10.1073/pnas.98.2.629;
RA Eichmueller S., Usener D., Dummer R., Stein A., Thiel D., Schadendorf D.;
RT "Serological detection of cutaneous T-cell lymphoma-associated antigens.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:629-634(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 941-1274 (ISOFORM 1), AND VARIANT
RP ARG-1046.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633; SER-636; SER-927 AND
RP SER-979, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633; SER-636; SER-927;
RP THR-982 AND SER-1103, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927 AND SER-1103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344; SER-673; SER-800;
RP SER-927; SER-971; SER-979; THR-1049; SER-1103 AND SER-1552, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927 AND SER-1103, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE HUSH COMPLEX.
RX PubMed=26022416; DOI=10.1126/science.aaa7227;
RA Tchasovnikarova I.A., Timms R.T., Matheson N.J., Wals K., Antrobus R.,
RA Goettgens B., Dougan G., Dawson M.A., Lehner P.J.;
RT "Epigenetic silencing by the HUSH complex mediates position-effect
RT variegation in human cells.";
RL Science 348:1481-1485(2015).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MORC2.
RX PubMed=28581500; DOI=10.1038/ng.3878;
RA Tchasovnikarova I.A., Timms R.T., Douse C.H., Roberts R.C., Dougan G.,
RA Kingston R.E., Modis Y., Lehner P.J.;
RT "Hyperactivation of HUSH complex function by Charcot-Marie-Tooth disease
RT mutation in MORC2.";
RL Nat. Genet. 49:1035-1044(2017).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-586; LYS-823; LYS-832 AND
RP LYS-872, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [20]
RP FUNCTION.
RX PubMed=29211708; DOI=10.1038/nature25179;
RA Liu N., Lee C.H., Swigut T., Grow E., Gu B., Bassik M.C., Wysocka J.;
RT "Selective silencing of euchromatic L1s revealed by genome-wide screens for
RT L1 regulators.";
RL Nature 553:228-232(2018).
RN [21]
RP FUNCTION, AND INTERACTION WITH ZNF638.
RX PubMed=30487602; DOI=10.1038/s41586-018-0750-6;
RA Zhu Y., Wang G.Z., Cingoez O., Goff S.P.;
RT "NP220 mediates silencing of unintegrated retroviral DNA.";
RL Nature 564:278-282(2018).
CC -!- FUNCTION: Component of the HUSH complex, a multiprotein complex that
CC mediates epigenetic repression (PubMed:26022416, PubMed:28581500). The
CC HUSH complex is recruited to genomic loci rich in H3K9me3 and is
CC required to maintain transcriptional silencing by promoting recruitment
CC of SETDB1, a histone methyltransferase that mediates further deposition
CC of H3K9me3, as well as MORC2 (PubMed:26022416, PubMed:28581500). Also
CC represses L1 retrotransposons in collaboration with MORC2 and,
CC probably, SETDB1, the silencing is dependent of repressive epigenetic
CC modifications, such as H3K9me3 mark. Silencing events often occur
CC within introns of transcriptionally active genes, and lead to the down-
CC regulation of host gene expression (PubMed:29211708). The HUSH complex
CC is also involved in the silencing of unintegrated retroviral DNA by
CC being recruited by ZNF638: some part of the retroviral DNA formed
CC immediately after infection remains unintegrated in the host genome and
CC is transcriptionally repressed (PubMed:30487602). Plays a crucial role
CC in early embryonic development (By similarity). Involved in the
CC organization of spindle poles and spindle apparatus assembly during
CC zygotic division (By similarity). Plays an important role in
CC maintaining epiblast fitness or potency (By similarity).
CC {ECO:0000250|UniProtKB:Q69ZR9, ECO:0000269|PubMed:26022416,
CC ECO:0000269|PubMed:28581500, ECO:0000269|PubMed:29211708,
CC ECO:0000269|PubMed:30487602}.
CC -!- SUBUNIT: Component of the HUSH complex; at least composed of TASOR,
CC PPHLN1 and MPHOSPH8 (PubMed:26022416). Interacts with MORC2; the
CC interaction associateS MORC2 with the HUSH complex which recruits MORC2
CC to heterochromatic loci (PubMed:28581500). Interacts with ZNF638;
CC leading to recruitment of the HUSH complex to unintegrated retroviral
CC DNA (PubMed:30487602). Interacts with INPP5A, EML1, SV1L, GPSM2,
CC ITGB3BP, CNTN1, ETFA, PSMD8, S100A10, MPHOSPH8, TMEM100, ALB, PARPBP,
CC HCFC2, NCBP1 and SETDB1 (By similarity). {ECO:0000250|UniProtKB:Q69ZR9,
CC ECO:0000269|PubMed:26022416, ECO:0000269|PubMed:28581500,
CC ECO:0000269|PubMed:30487602}.
CC -!- INTERACTION:
CC Q9UK61; Q99549: MPHOSPH8; NbExp=3; IntAct=EBI-308354, EBI-2653928;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26022416,
CC ECO:0000269|PubMed:28581500}. Chromosome {ECO:0000269|PubMed:26022416,
CC ECO:0000269|PubMed:28581500}. Note=Localizes to chromatin.
CC {ECO:0000269|PubMed:26022416, ECO:0000269|PubMed:28581500}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UK61-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UK61-2; Sequence=VSP_027030, VSP_027032;
CC Name=3;
CC IsoId=Q9UK61-3; Sequence=VSP_027033, VSP_027034;
CC Name=4;
CC IsoId=Q9UK61-4; Sequence=VSP_027031;
CC -!- MISCELLANEOUS: [Isoform 1]: Gene prediction based on partial mRNA data.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the TASOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG34913.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI29988.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF180425; AAD55098.1; -; mRNA.
DR EMBL; AC099781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK094486; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC129987; AAI29988.1; ALT_INIT; mRNA.
DR EMBL; AF273053; AAG34913.1; ALT_INIT; mRNA.
DR EMBL; AB029028; BAA83057.1; -; mRNA.
DR CCDS; CCDS2877.1; -. [Q9UK61-2]
DR CCDS; CCDS46853.1; -. [Q9UK61-3]
DR CCDS; CCDS87094.1; -. [Q9UK61-4]
DR RefSeq; NP_001106207.1; NM_001112736.1. [Q9UK61-3]
DR RefSeq; NP_056039.2; NM_015224.3. [Q9UK61-2]
DR RefSeq; XP_005265056.1; XM_005264999.1.
DR RefSeq; XP_011531854.1; XM_011533552.2.
DR PDB; 6SWG; X-ray; 2.51 A; C=1013-1095.
DR PDB; 6TL1; X-ray; 2.03 A; A/B=110-332.
DR PDBsum; 6SWG; -.
DR PDBsum; 6TL1; -.
DR AlphaFoldDB; Q9UK61; -.
DR SMR; Q9UK61; -.
DR BioGRID; 116873; 88.
DR CORUM; Q9UK61; -.
DR DIP; DIP-56150N; -.
DR IntAct; Q9UK61; 32.
DR MINT; Q9UK61; -.
DR STRING; 9606.ENSP00000417509; -.
DR GlyGen; Q9UK61; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q9UK61; -.
DR PhosphoSitePlus; Q9UK61; -.
DR BioMuta; FAM208A; -.
DR DMDM; 229462994; -.
DR EPD; Q9UK61; -.
DR jPOST; Q9UK61; -.
DR MassIVE; Q9UK61; -.
DR MaxQB; Q9UK61; -.
DR PaxDb; Q9UK61; -.
DR PeptideAtlas; Q9UK61; -.
DR PRIDE; Q9UK61; -.
DR ProteomicsDB; 84729; -. [Q9UK61-1]
DR ProteomicsDB; 84730; -. [Q9UK61-2]
DR ProteomicsDB; 84731; -. [Q9UK61-3]
DR ProteomicsDB; 84732; -. [Q9UK61-4]
DR Antibodypedia; 1875; 29 antibodies from 13 providers.
DR DNASU; 23272; -.
DR Ensembl; ENST00000355628.9; ENSP00000347845.5; ENSG00000163946.14. [Q9UK61-4]
DR Ensembl; ENST00000431842.6; ENSP00000399410.2; ENSG00000163946.14. [Q9UK61-2]
DR Ensembl; ENST00000493960.6; ENSP00000417509.2; ENSG00000163946.14. [Q9UK61-3]
DR Ensembl; ENST00000683822.1; ENSP00000508241.1; ENSG00000163946.14. [Q9UK61-1]
DR GeneID; 23272; -.
DR KEGG; hsa:23272; -.
DR MANE-Select; ENST00000683822.1; ENSP00000508241.1; NM_001365635.2; NP_001352564.1.
DR UCSC; uc003dic.5; human. [Q9UK61-1]
DR CTD; 23272; -.
DR DisGeNET; 23272; -.
DR GeneCards; TASOR; -.
DR HGNC; HGNC:30314; TASOR.
DR HPA; ENSG00000163946; Low tissue specificity.
DR MIM; 616493; gene.
DR neXtProt; NX_Q9UK61; -.
DR OpenTargets; ENSG00000163946; -.
DR PharmGKB; PA128395774; -.
DR VEuPathDB; HostDB:ENSG00000163946; -.
DR eggNOG; ENOG502QUY9; Eukaryota.
DR GeneTree; ENSGT00530000063735; -.
DR HOGENOM; CLU_004573_0_0_1; -.
DR InParanoid; Q9UK61; -.
DR OMA; CTKIENV; -.
DR OrthoDB; 57214at2759; -.
DR PhylomeDB; Q9UK61; -.
DR TreeFam; TF336055; -.
DR PathwayCommons; Q9UK61; -.
DR SignaLink; Q9UK61; -.
DR BioGRID-ORCS; 23272; 24 hits in 1089 CRISPR screens.
DR ChiTaRS; FAM208A; human.
DR GenomeRNAi; 23272; -.
DR Pharos; Q9UK61; Tbio.
DR PRO; PR:Q9UK61; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UK61; protein.
DR Bgee; ENSG00000163946; Expressed in secondary oocyte and 206 other tissues.
DR ExpressionAtlas; Q9UK61; baseline and differential.
DR Genevisible; Q9UK61; HS.
DR GO; GO:0000792; C:heterochromatin; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0060809; P:mesodermal to mesenchymal transition involved in gastrulation; ISS:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IDA:UniProtKB.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; IMP:UniProtKB.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; IDA:UniProtKB.
DR GO; GO:0097355; P:protein localization to heterochromatin; IDA:UniProtKB.
DR InterPro; IPR022188; DUF3715.
DR Pfam; PF12509; DUF3715; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosome;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1670
FT /note="Protein TASOR"
FT /id="PRO_0000295728"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1638..1670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1542..1558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1656..1670
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 843
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZR9"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 979
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 982
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1049
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1552
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 586
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 823
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 832
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 872
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..396
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18726359"
FT /id="VSP_027030"
FT VAR_SEQ 921..981
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11149944"
FT /id="VSP_027031"
FT VAR_SEQ 942..982
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:18726359"
FT /id="VSP_027032"
FT VAR_SEQ 1495..1512
FT /note="ALLENDEKDEEDMSLDSG -> DAVLTLTPLELGVGISQH (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027033"
FT VAR_SEQ 1513..1670
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027034"
FT VARIANT 38
FT /note="Q -> P (in dbSNP:rs958755)"
FT /id="VAR_059595"
FT VARIANT 831
FT /note="A -> G (in dbSNP:rs17056999)"
FT /id="VAR_033350"
FT VARIANT 998
FT /note="V -> I (in dbSNP:rs2291498)"
FT /id="VAR_055092"
FT VARIANT 1046
FT /note="T -> R (in dbSNP:rs9835332)"
FT /evidence="ECO:0000269|PubMed:10470851,
FT ECO:0000269|PubMed:11149944, ECO:0000269|PubMed:18726359"
FT /id="VAR_033351"
FT VARIANT 1435
FT /note="I -> V (in dbSNP:rs2291498)"
FT /evidence="ECO:0000269|PubMed:11149944"
FT /id="VAR_033352"
FT CONFLICT 941
FT /note="P -> I (in Ref. 6; BAA83057)"
FT /evidence="ECO:0000305"
FT CONFLICT 1129
FT /note="N -> S (in Ref. 1; AAD55098)"
FT /evidence="ECO:0000305"
FT CONFLICT 1135
FT /note="E -> G (in Ref. 1; AAD55098)"
FT /evidence="ECO:0000305"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6TL1"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:6TL1"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:6TL1"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:6TL1"
FT HELIX 154..169
FT /evidence="ECO:0007829|PDB:6TL1"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:6TL1"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:6TL1"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:6TL1"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:6TL1"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:6TL1"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:6TL1"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6TL1"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:6TL1"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:6TL1"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:6TL1"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:6TL1"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:6TL1"
FT HELIX 294..297
FT /evidence="ECO:0007829|PDB:6TL1"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:6TL1"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:6TL1"
FT STRAND 317..327
FT /evidence="ECO:0007829|PDB:6TL1"
FT HELIX 1016..1038
FT /evidence="ECO:0007829|PDB:6SWG"
FT HELIX 1075..1091
FT /evidence="ECO:0007829|PDB:6SWG"
SQ SEQUENCE 1670 AA; 189032 MW; A8BE5ED05A96C897 CRC64;
MATAVETEAC QPTDASWESG GGGDDEMKQA LPELESSQQN GGGGGLNIAE PSGGAGREEN
AGAEAAQSLS HEQPQDSSEA GAAALPRGPE EPERPVRRSF QIPRKSREKK ALFQPLTPGS
REFEDVVNIL HSSYLEPTSV TNFNYRRACL VHNELLEKEF TEKRRELKFD GRLDKELSES
YAFLMVDRYQ VQTICEKGLH VGQSKITILG SPSMGVYLSR YADLLQANPL DTGAMGDVVI
FKIMKGKIKS IYDPMGVKSL ESMLNKSALD PTPKHECHVS KNANRITSLL AYRAYELTQY
YFYEYGFDEL RRRPRHVCPY AVVSFTYKDD IQTPKFVPSS RSNSFNTDRN IDKYNYTLWK
GQLLNKGKLL CYISLRSATR AFLPIKLPEK LDVETVMSID HLKQKIPPAL FYKETYLGPN
EVLKNGMYCS LYEVVEKTRI GSNMESLLQK LDREKLVLVK PLGDRGYLFL LSPYQMVPPY
EYQTAKSRVL HALFLFQEPR SIVTSQKGST NAAPQERHES MPDVLKIAQF LQFSLIQCRK
EFKNISAINF HSVVEKYVSE FFKRGFGSGK REFIMFPYDS RLDDKKFLYS APRNKSHIDT
CLHAYIFRPE VYQLPICKLK ELFEENRKLQ QFSPLSDYEG QEEEMNGTKM KFGKRNNSRG
EAIISGKQRS SHSLDYDKDR VKELINLIQC RKKSVGGDSD TEDMRSKTVL KRKLEDLPEN
MRKLAKTSNL SENCHLYEES PQPIGSLGHD ADLRRQQQDT CNSGIADIHR LFNWLSETLA
NARHSDASLT DTVNKALGLS TDDAYEELRQ KHEYELNSTP DKKDYEQPTC AKVENAQFKG
TQSLLLEVDA TSKYSVAIST SEVGTDHKLH LKEDPNLISV NNFEDCSLCP SVPIEHGFRR
QQSKSNNVEE TEIHWKLIPI TGGNARSPED QLGKHGEKQT PGMKSPEEQL VCVPPQEAFP
NDPRVINRQR SSDYQFPSSP FTDTLKGTTE DDVLTGQVEE QCVPAAEAEP PAVSETTERT
VLGEYNLFSR KIEEILKQKN VSYVSTVSTP IFSTQEKMKR LSEFIYSKTS KAGVQEFVDG
LHEKLNTIII KASAKGGNLP PVSPNDSGAK IASNPLERHV IPVSSSDFNN KHLLEPLCSD
PLKDTNSDEQ HSTSALTEVE MNQPQHATEL MVTSDHIVPG DMAREPVEET TKSPSDVNIS
AQPALSNFIS QLEPEVFNSL VKIMKDVQKN TVKFYIHEEE ESVLCKEIKE YLIKLGNTEC
HPEQFLERRS KLDKLLIIIQ NEDIAGFIHK IPGLVTLKKL PCVSFAGVDS LDDVKNHTYN
ELFVSGGFIV SDESILNPEV VTVENLKNFL TFLEELSTPE GKWQWKVHCK FQKKLKELGR
LNAKALSLLT LLNVYQKKHL VEILSYHNCD SQTRNAPELD CLIRLQAQNI QQRHIVFLTE
KNIKMLSSYT DNGIVVATAE DFMQNFKNLV GYHNSITEEN LPQLGANENL ESQSALLEND
EKDEEDMSLD SGDEISHIEV CSNFHSEIWE KETKGSRGTD QKKNTQIELQ SSPDVQNSLL
EDKTYLDSEE RTSIDIVCSE GENSNSTEQD SYSNFQVYHS QLNMSHQFSH FNVLTHQTFL
GTPYALSSSQ SQENENYFLS AYTESLDRDK SPPPLSWGKS DSSRPYSQEK
