ID TLS1_HUMAN Reviewed; 289 AA. AC Q9NZ63; B3KPX8; Q8WVU6; Q9NT39; DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 160. DE RecName: Full=Splicing factor C9orf78 {ECO:0000305}; DE AltName: Full=Hepatocellular carcinoma-associated antigen 59; GN Name=C9orf78; Synonyms=HCA59 {ECO:0000303|PubMed:12097419}; 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]. RC TISSUE=Hepatoma; RX PubMed=12097419; DOI=10.4049/jimmunol.169.2.1102; RA Wang Y., Han K.-J., Pang X.-W., Vaughan H.A., Qu W., Dong X.-Y., RA Peng J.-R., Zhao H.-T., Rui J.-A., Leng X.-S., Cebon J., Burgess A.W., RA Chen W.-F.; RT "Large scale identification of human hepatocellular carcinoma-associated RT antigens by autoantibodies."; RL J. Immunol. 169:1102-1109(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow, and Placenta; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-289. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-17 AND SER-261, AND 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-17, AND RP 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-17; THR-253 AND RP SER-261, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION BY RP 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-17 AND SER-261, 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-253, AND IDENTIFICATION BY RP 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 [18] RP FUNCTION, INTERACTION WITH PRPF8, AND SUBCELLULAR LOCATION. RX PubMed=35167828; DOI=10.1016/j.yexcr.2022.113063; RA Koranne R., Brown K., Vandenbroek H., Taylor W.R.; RT "C9ORF78 partially localizes to centromeres and plays a role in chromosome RT segregation."; RL Exp. Cell Res. 413:113063-113063(2022). RN [19] {ECO:0007744|PDB:7OS2} RP STRUCTURE BY ELECTRON MICROSCOPY (2.76 ANGSTROMS) IN COMPLEX WITH SNRNP200 RP AND PRPF8, FUNCTION, IDENTIFICATION IN THE SPLICEOSOME COMPLEX, INTERACTION RP WITH PRPF8 AND SNRNP200, AND MUTAGENESIS OF PHE-8 AND ARG-41. RX PubMed=35241646; DOI=10.1038/s41467-022-28754-2; RA Bergfort A., Preussner M., Kuropka B., Ilik I.A., Hilal T., Weber G., RA Freund C., Aktas T., Heyd F., Wahl M.C.; RT "A multi-factor trafficking site on the spliceosome remodeling enzyme BRR2 RT recruits C9ORF78 to regulate alternative splicing."; RL Nat. Commun. 13:1132-1132(2022). CC -!- FUNCTION: Plays a role in pre-mRNA splicing by promoting usage of the CC upstream 3'-splice site at alternative NAGNAG splice sites; these are CC sites featuring alternative acceptor motifs separated by only a few CC nucleotides (PubMed:35241646). May also modulate exon inclusion events CC (PubMed:35241646). Plays a role in spliceosomal remodeling by CC displacing WBP4 from SNRNP200 and may act to inhibit SNRNP200 helicase CC activity (PubMed:35241646). Binds U5 snRNA (PubMed:35241646). Required CC for proper chromosome segregation (PubMed:35167828). Not required for CC splicing of shelterin components (PubMed:35167828). CC {ECO:0000269|PubMed:35167828, ECO:0000269|PubMed:35241646}. CC -!- SUBUNIT: Component of the spliceosome (PubMed:35241646). Interacts with CC SNRNP200; the interaction is direct (PubMed:35241646). Interacts with CC PRPF8 (PubMed:35167828, PubMed:35241646). {ECO:0000269|PubMed:35167828, CC ECO:0000269|PubMed:35241646}. CC -!- INTERACTION: CC Q9NZ63; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-2557577, EBI-750109; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:35167828}. CC Chromosome, centromere {ECO:0000269|PubMed:35167828}. Note=Dispersed CC throughout the nucleus during interphase (PubMed:35167828). Colocalizes CC with microtubule attachment sites at centromeres following mitotic CC checkpoint activation (PubMed:35167828). {ECO:0000269|PubMed:35167828}. CC -!- SIMILARITY: Belongs to the TLS1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF218421; AAF37561.1; -; mRNA. DR EMBL; AK057004; BAG51840.1; -; mRNA. DR EMBL; AL158207; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW87910.1; -; Genomic_DNA. DR EMBL; BC007664; AAH07664.1; -; mRNA. DR EMBL; BC017570; AAH17570.1; -; mRNA. DR EMBL; AL137549; CAB70805.1; -; mRNA. DR CCDS; CCDS6931.1; -. DR PIR; T46390; T46390. DR RefSeq; NP_057604.1; NM_016520.2. DR PDB; 7OS2; EM; 2.76 A; C=1-289. DR PDB; 8C6J; EM; 2.80 A; CT=1-289. DR PDBsum; 7OS2; -. DR PDBsum; 8C6J; -. DR AlphaFoldDB; Q9NZ63; -. DR EMDB; EMD-16452; -. DR SMR; Q9NZ63; -. DR BioGRID; 119716; 625. DR IntAct; Q9NZ63; 17. DR MINT; Q9NZ63; -. DR STRING; 9606.ENSP00000361524; -. DR GlyGen; Q9NZ63; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NZ63; -. DR MetOSite; Q9NZ63; -. DR PhosphoSitePlus; Q9NZ63; -. DR BioMuta; C9orf78; -. DR DMDM; 74753081; -. DR EPD; Q9NZ63; -. DR jPOST; Q9NZ63; -. DR MassIVE; Q9NZ63; -. DR MaxQB; Q9NZ63; -. DR PaxDb; 9606-ENSP00000361524; -. DR PeptideAtlas; Q9NZ63; -. DR ProteomicsDB; 83329; -. DR Pumba; Q9NZ63; -. DR TopDownProteomics; Q9NZ63; -. DR Antibodypedia; 17917; 125 antibodies from 23 providers. DR DNASU; 51759; -. DR Ensembl; ENST00000372447.7; ENSP00000361524.3; ENSG00000136819.15. DR GeneID; 51759; -. DR KEGG; hsa:51759; -. DR MANE-Select; ENST00000372447.7; ENSP00000361524.3; NM_016520.3; NP_057604.1. DR UCSC; uc004byp.4; human. DR AGR; HGNC:24932; -. DR GeneCards; C9orf78; -. DR HGNC; HGNC:24932; C9orf78. DR HPA; ENSG00000136819; Low tissue specificity. DR MIM; 619569; gene. DR neXtProt; NX_Q9NZ63; -. DR OpenTargets; ENSG00000136819; -. DR PharmGKB; PA134929438; -. DR VEuPathDB; HostDB:ENSG00000136819; -. DR eggNOG; KOG3345; Eukaryota. DR GeneTree; ENSGT00390000009787; -. DR HOGENOM; CLU_053736_1_0_1; -. DR InParanoid; Q9NZ63; -. DR OMA; IHNIEAT; -. DR OrthoDB; 2881172at2759; -. DR PhylomeDB; Q9NZ63; -. DR TreeFam; TF105871; -. DR PathwayCommons; Q9NZ63; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q9NZ63; -. DR SIGNOR; Q9NZ63; -. DR BioGRID-ORCS; 51759; 386 hits in 1144 CRISPR screens. DR ChiTaRS; C9orf78; human. DR GeneWiki; C9orf78; -. DR GenomeRNAi; 51759; -. DR Pharos; Q9NZ63; Tdark. DR PRO; PR:Q9NZ63; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9NZ63; Protein. DR Bgee; ENSG00000136819; Expressed in monocyte and 200 other cell types or tissues. DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central. DR GO; GO:0030623; F:U5 snRNA binding; IDA:UniProtKB. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW. DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IMP:UniProtKB. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:0060629; P:regulation of homologous chromosome segregation; IMP:UniProtKB. DR InterPro; IPR010756; Tls1-like. DR PANTHER; PTHR13486:SF2; TELOMERE LENGTH AND SILENCING PROTEIN 1 HOMOLOG; 1. DR PANTHER; PTHR13486; TELOMERE LENGTH AND SILENCING PROTEIN 1 TLS1 FAMILY MEMBER; 1. DR Pfam; PF07052; Hep_59; 1. DR Genevisible; Q9NZ63; HS. PE 1: Evidence at protein level; KW 3D-structure; Centromere; Chromosome; Chromosome partition; KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; KW Reference proteome; RNA-binding; Spliceosome. FT CHAIN 1..289 FT /note="Splicing factor C9orf78" FT /id="PRO_0000227523" FT REGION 1..27 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 5..58 FT /note="Interaction with SNRNP200" FT /evidence="ECO:0000269|PubMed:35241646, FT ECO:0007744|PDB:7OS2" FT REGION 232..289 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 232..283 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 147 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 253 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 261 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT VARIANT 70 FT /note="Q -> H (in dbSNP:rs1237745)" FT /id="VAR_050828" FT MUTAGEN 8 FT /note="F->A: Decreases binding to SNRNP200." FT /evidence="ECO:0000269|PubMed:35241646" FT MUTAGEN 41 FT /note="R->A: Abolishes binding to SNRNP200." FT /evidence="ECO:0000269|PubMed:35241646" FT CONFLICT 139 FT /note="P -> S (in Ref. 5; AAH17570)" FT /evidence="ECO:0000305" FT CONFLICT 203 FT /note="N -> S (in Ref. 5; AAH17570)" FT /evidence="ECO:0000305" FT HELIX 14..18 FT /evidence="ECO:0007829|PDB:7OS2" FT HELIX 21..40 FT /evidence="ECO:0007829|PDB:7OS2" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:7OS2" FT HELIX 49..54 FT /evidence="ECO:0007829|PDB:7OS2" SQ SEQUENCE 289 AA; 33688 MW; 3F691E6D17D1360E CRC64; MPVVRKIFRR RRGDSESEED EQDSEEVRLK LEETREVQNL RKRPNGVSAV ALLVGEKVQE ETTLVDDPFQ MKTGGMVDMK KLKERGKDKI SEEEDLHLGT SFSAETNRRD EDADMMKYIE TELKKRKGIV EHEEQKVKPK NAEDCLYELP ENIRVSSAKK TEEMLSNQML SGIPEVDLGI DAKIKNIIST EDAKARLLAE QQNKKKDSET SFVPTNMAVN YVQHNRFYHE ELNAPIRRNK EEPKARPLRV GDTEKPEPER SPPNRKRPAN EKATDDYHYE KFKKMNRRY //