ID SP110_HUMAN Reviewed; 689 AA. AC Q9HB58; B4DVI4; F5H1M1; Q14976; Q14977; Q53TG2; Q8WUZ6; Q9HCT8; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 5. DT 24-JAN-2024, entry version 199. DE RecName: Full=Sp110 nuclear body protein; DE AltName: Full=Interferon-induced protein 41/75; DE AltName: Full=Speckled 110 kDa; DE AltName: Full=Transcriptional coactivator Sp110; GN Name=SP110; 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] (ISOFORMS 2 AND 4), PHOSPHORYLATION (ISOFORM 2), RP AND VARIANT ARG-299. RC TISSUE=Lymphoma; RX PubMed=7693701; DOI=10.1016/s0021-9258(20)80544-4; RA Kadereit S., Gewert D.R., Galabru J., Hovanessian A.G., Meurs E.F.; RT "Molecular cloning of two new interferon-induced, highly related nuclear RT phosphoproteins."; RL J. Biol. Chem. 268:24432-24441(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), SUBCELLULAR LOCATION, AND RP VARIANTS ARG-299 AND THR-523. RC TISSUE=Spleen; RX PubMed=10913195; DOI=10.1128/mcb.20.16.6138-6146.2000; RA Bloch D.B., Nakajima A., Gulick T., Chiche J.-D., Orth D., RA de La Monte S.M., Bloch K.D.; RT "Sp110 localizes to the PML-Sp100 nuclear body and may function as a RT nuclear hormone receptor transcriptional coactivator."; RL Mol. Cell. Biol. 20:6138-6146(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7), AND VARIANTS RP ARG-112; LYS-207; ARG-299 AND SER-425. RC TISSUE=Ileal mucosa, and Spleen; 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 GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT ARG-299. RC TISSUE=Lymph; 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 [7] RP INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION). RX PubMed=14559998; DOI=10.1128/mcb.23.21.7498-7509.2003; RA Watashi K., Hijikata M., Tagawa A., Doi T., Marusawa H., Shimotohno K.; RT "Modulation of retinoid signaling by a cytoplasmic viral protein via RT sequestration of Sp110b, a potent transcriptional corepressor of retinoic RT acid receptor, from the nucleus."; RL Mol. Cell. Biol. 23:7498-7509(2003). RN [8] RP INVOLVEMENT IN VODI. RX PubMed=16648851; DOI=10.1038/ng1780; RA Roscioli T., Cliffe S.T., Bloch D.B., Bell C.G., Mullan G., Taylor P.J., RA Sarris M., Wang J., Donald J.A., Kirk E.P., Ziegler J.B., Salzer U., RA McDonald G.B., Wong M., Lindeman R., Buckley M.F.; RT "Mutations in the gene encoding the PML nuclear body protein Sp110 are RT associated with immunodeficiency and hepatic veno-occlusive disease."; RL Nat. Genet. 38:620-622(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-256, AND IDENTIFICATION BY RP 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-380, 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244 AND SER-380, 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 [14] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [15] RP VARIANTS VAL-128; VAL-206; LYS-207; ARG-299; MET-367 AND SER-425. RX PubMed=16816019; DOI=10.1136/jmg.2005.037960; RA Thye T., Browne E.N., Chinbuah M.A., Gyapong J., Osei I., Owusu-Dabo E., RA Niemann S., Ruesch-Gerdes S., Horstmann R.D., Meyer C.G.; RT "No associations of human pulmonary tuberculosis with Sp110 variants."; RL J. Med. Genet. 43:E32-E32(2006). RN [16] RP VARIANTS ARG-112; LYS-207; GLY-212; VAL-249; GLY-267; ARG-299; SER-425; RP THR-523 AND ILE-579. RX PubMed=16803959; DOI=10.1073/pnas.0603340103; RA Tosh K., Campbell S.J., Fielding K., Sillah J., Bah B., Gustafson P., RA Manneh K., Lisse I., Sirugo G., Bennett S., Aaby P., McAdam K.P.W.J., RA Bah-Sow O., Lienhardt C., Kramnik I., Hill A.V.S.; RT "Variants in the SP110 gene are associated with genetic susceptibility to RT tuberculosis in West Africa."; RL Proc. Natl. Acad. Sci. U.S.A. 103:10364-10368(2006). RN [17] RP VARIANTS [LARGE SCALE ANALYSIS] THR-8 AND SER-683. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Transcription factor. May be a nuclear hormone receptor CC coactivator. Enhances transcription of genes with retinoic acid CC response elements (RARE). CC -!- SUBUNIT: (Microbial infection) Isoform 3 interacts with HCV core CC protein. {ECO:0000269|PubMed:14559998}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00185, CC ECO:0000255|PROSITE-ProRule:PRU00747, ECO:0000269|PubMed:10913195, CC ECO:0000269|PubMed:25593309}. Note=Found in the nuclear body. CC {ECO:0000269|PubMed:10913195}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; CC IsoId=Q9HB58-1; Sequence=Displayed; CC Name=2; Synonyms=IFI75, 75; CC IsoId=Q9HB58-2; Sequence=VSP_005992, VSP_006001, VSP_006002; CC Name=3; Synonyms=Sp110b; CC IsoId=Q9HB58-3; Sequence=VSP_005997, VSP_006000; CC Name=4; Synonyms=IFI41, 41; CC IsoId=Q9HB58-4; Sequence=VSP_005991, VSP_005994, VSP_005995, CC VSP_005997, VSP_006000; CC Name=5; CC IsoId=Q9HB58-5; Sequence=VSP_005996, VSP_005997, VSP_006000; CC Name=6; CC IsoId=Q9HB58-6; Sequence=VSP_035593; CC Name=7; CC IsoId=Q9HB58-7; Sequence=VSP_046079, VSP_005997, VSP_006000; CC -!- TISSUE SPECIFICITY: Highly expressed in peripheral blood leukocytes and CC spleen. Detected at intermediate levels in thymus, prostate, testis, CC ovary, small intestine and colon, and at low levels in heart, brain, CC placenta, lung, liver, skeletal muscle, kidney and pancreas. CC -!- INDUCTION: By IFNG/IFN-gamma and all-trans retinoic acid (ATRA). CC -!- PTM: Phosphorylated (isoform 2). CC -!- DISEASE: Hepatic venoocclusive disease with immunodeficiency (VODI) CC [MIM:235550]: Autosomal recessive primary immunodeficiency associated CC with hepatic vascular occlusion and fibrosis. The immunodeficiency is CC characterized by severe hypogammaglobulinemia, combined T and B-cell CC immunodeficiency, absent lymph node germinal centers, and absent tissue CC plasma cells. {ECO:0000269|PubMed:16648851}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAF99318.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAG09826.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AK026488; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAF99318.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=SP110base; Note=SP110 mutation db; CC URL="http://structure.bmc.lu.se/idbase/SP110base/"; 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; L22342; AAA18806.1; -; mRNA. DR EMBL; L22343; AAD13402.1; -; mRNA. DR EMBL; AF280094; AAF99318.1; ALT_FRAME; mRNA. DR EMBL; AF280095; AAG09826.1; ALT_FRAME; mRNA. DR EMBL; AK026488; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK301097; BAG62696.1; -; mRNA. DR EMBL; AC009950; AAX93281.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70915.1; -; Genomic_DNA. DR EMBL; BC019059; AAH19059.1; -; mRNA. DR CCDS; CCDS2474.1; -. [Q9HB58-1] DR CCDS; CCDS2475.1; -. [Q9HB58-6] DR CCDS; CCDS2476.1; -. [Q9HB58-3] DR CCDS; CCDS54435.1; -. [Q9HB58-7] DR PIR; A49515; A49515. DR RefSeq; NP_001171944.1; NM_001185015.1. [Q9HB58-7] DR RefSeq; NP_004500.3; NM_004509.3. [Q9HB58-1] DR RefSeq; NP_536349.2; NM_080424.2. [Q9HB58-6] DR AlphaFoldDB; Q9HB58; -. DR SMR; Q9HB58; -. DR BioGRID; 109657; 126. DR IntAct; Q9HB58; 34. DR MINT; Q9HB58; -. DR STRING; 9606.ENSP00000258381; -. DR iPTMnet; Q9HB58; -. DR PhosphoSitePlus; Q9HB58; -. DR SwissPalm; Q9HB58; -. DR BioMuta; SP110; -. DR DMDM; 313104323; -. DR EPD; Q9HB58; -. DR jPOST; Q9HB58; -. DR MassIVE; Q9HB58; -. DR MaxQB; Q9HB58; -. DR PaxDb; 9606-ENSP00000258381; -. DR PeptideAtlas; Q9HB58; -. DR ProteomicsDB; 25699; -. DR ProteomicsDB; 81489; -. [Q9HB58-1] DR ProteomicsDB; 81490; -. [Q9HB58-2] DR ProteomicsDB; 81491; -. [Q9HB58-3] DR ProteomicsDB; 81492; -. [Q9HB58-4] DR ProteomicsDB; 81493; -. [Q9HB58-5] DR ProteomicsDB; 81494; -. [Q9HB58-6] DR Pumba; Q9HB58; -. DR Antibodypedia; 34401; 408 antibodies from 31 providers. DR DNASU; 3431; -. DR Ensembl; ENST00000258381.11; ENSP00000258381.6; ENSG00000135899.20. [Q9HB58-6] DR Ensembl; ENST00000258382.10; ENSP00000258382.5; ENSG00000135899.20. [Q9HB58-3] DR Ensembl; ENST00000358662.9; ENSP00000351488.4; ENSG00000135899.20. [Q9HB58-1] DR Ensembl; ENST00000540870.5; ENSP00000439558.1; ENSG00000135899.20. [Q9HB58-7] DR Ensembl; ENST00000698099.1; ENSP00000513563.1; ENSG00000135899.20. [Q9HB58-1] DR GeneID; 3431; -. DR KEGG; hsa:3431; -. DR MANE-Select; ENST00000258381.11; ENSP00000258381.6; NM_080424.4; NP_536349.3. [Q9HB58-6] DR UCSC; uc002vqg.5; human. [Q9HB58-1] DR AGR; HGNC:5401; -. DR CTD; 3431; -. DR DisGeNET; 3431; -. DR GeneCards; SP110; -. DR GeneReviews; SP110; -. DR HGNC; HGNC:5401; SP110. DR HPA; ENSG00000135899; Tissue enhanced (lymphoid). DR MalaCards; SP110; -. DR MIM; 235550; phenotype. DR MIM; 604457; gene. DR neXtProt; NX_Q9HB58; -. DR OpenTargets; ENSG00000135899; -. DR Orphanet; 79124; Hepatic veno-occlusive disease-immunodeficiency syndrome. DR PharmGKB; PA35104; -. DR VEuPathDB; HostDB:ENSG00000135899; -. DR eggNOG; KOG2177; Eukaryota. DR GeneTree; ENSGT00940000155124; -. DR HOGENOM; CLU_015844_2_0_1; -. DR InParanoid; Q9HB58; -. DR OMA; QKARNEC; -. DR OrthoDB; 38708at2759; -. DR PhylomeDB; Q9HB58; -. DR TreeFam; TF335091; -. DR PathwayCommons; Q9HB58; -. DR SignaLink; Q9HB58; -. DR BioGRID-ORCS; 3431; 23 hits in 1184 CRISPR screens. DR ChiTaRS; SP110; human. DR GeneWiki; SP110; -. DR GenomeRNAi; 3431; -. DR Pharos; Q9HB58; Tbio. DR PRO; PR:Q9HB58; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9HB58; Protein. DR Bgee; ENSG00000135899; Expressed in monocyte and 204 other cell types or tissues. DR ExpressionAtlas; Q9HB58; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd15626; PHD_SP110_140; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 3.10.390.10; SAND domain-like; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR004865; HSR_dom. DR InterPro; IPR010919; SAND-like_dom_sf. DR InterPro; IPR000770; SAND_dom. DR InterPro; IPR043563; Sp110/Sp140/Sp140L-like. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR46386; NUCLEAR BODY PROTEIN SP140; 1. DR PANTHER; PTHR46386:SF7; SP110 NUCLEAR BODY PROTEIN; 1. DR Pfam; PF03172; HSR; 1. DR Pfam; PF01342; SAND; 1. DR SMART; SM00297; BROMO; 1. DR SMART; SM00249; PHD; 1. DR SMART; SM00258; SAND; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF63763; SAND domain-like; 1. DR PROSITE; PS51414; HSR; 1. DR PROSITE; PS50864; SAND; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. DR Genevisible; Q9HB58; HS. PE 1: Evidence at protein level; KW Alternative splicing; Bromodomain; DNA-binding; Host-virus interaction; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..689 FT /note="Sp110 nuclear body protein" FT /id="PRO_0000074101" FT DOMAIN 1..108 FT /note="HSR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00747" FT DOMAIN 454..535 FT /note="SAND" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00185" FT DOMAIN 581..676 FT /note="Bromo" FT ZN_FING 534..580 FT /note="PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT REGION 131..216 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 231..385 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 525..529 FT /note="Nuclear hormone receptor interaction" FT /evidence="ECO:0000255" FT MOTIF 281..294 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT MOTIF 428..444 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 137..152 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 155..173 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 275..299 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 322..336 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 337..360 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 361..376 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 175 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BVK9" FT MOD_RES 177 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8BVK9" FT MOD_RES 244 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 256 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 380 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..251 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:7693701" FT /id="VSP_005991" FT VAR_SEQ 1..203 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7693701" FT /id="VSP_005992" FT VAR_SEQ 1 FT /note="M -> MGRGFRM (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046079" FT VAR_SEQ 252..275 FT /note="IRDNSPEPNDPEEPQEVSSTPSDK -> MASSGVKNTPRWRRKAPHGRERKE FT (in isoform 4)" FT /evidence="ECO:0000303|PubMed:7693701" FT /id="VSP_005994" FT VAR_SEQ 300..349 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:7693701" FT /id="VSP_005995" FT VAR_SEQ 300..303 FT /note="GTAS -> AL (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_005996" FT VAR_SEQ 531..549 FT /note="RKNSDECEVCCQGGQLLCC -> SGLLLCPPRINLKRELNSK (in FT isoform 3, isoform 4, isoform 5 and isoform 7)" FT /evidence="ECO:0000303|PubMed:10913195, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7693701" FT /id="VSP_005997" FT VAR_SEQ 550..689 FT /note="Missing (in isoform 3, isoform 4, isoform 5 and FT isoform 7)" FT /evidence="ECO:0000303|PubMed:10913195, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7693701" FT /id="VSP_006000" FT VAR_SEQ 605 FT /note="L -> LKCEFLLLKAYCHPQSSFFTGIPFN (in isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_035593" FT VAR_SEQ 606..611 FT /note="IRDYGE -> NVSSSS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7693701" FT /id="VSP_006001" FT VAR_SEQ 612..689 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7693701" FT /id="VSP_006002" FT VARIANT 8 FT /note="M -> T (in a breast cancer sample; somatic mutation; FT dbSNP:rs200067258)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036029" FT VARIANT 112 FT /note="W -> R (in dbSNP:rs1129411)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:16803959" FT /id="VAR_027170" FT VARIANT 128 FT /note="A -> V (in dbSNP:rs11556887)" FT /evidence="ECO:0000269|PubMed:16816019" FT /id="VAR_027171" FT VARIANT 173 FT /note="S -> L (in dbSNP:rs41552315)" FT /id="VAR_047051" FT VARIANT 206 FT /note="A -> V (in dbSNP:rs28930679)" FT /evidence="ECO:0000269|PubMed:16816019" FT /id="VAR_027172" FT VARIANT 207 FT /note="E -> K (in dbSNP:rs9061)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:16803959, ECO:0000269|PubMed:16816019" FT /id="VAR_027173" FT VARIANT 210 FT /note="S -> A (in dbSNP:rs1063154)" FT /id="VAR_047052" FT VARIANT 212 FT /note="E -> G (in dbSNP:rs1047254)" FT /evidence="ECO:0000269|PubMed:16803959" FT /id="VAR_027174" FT VARIANT 249 FT /note="M -> V (in dbSNP:rs3769838)" FT /evidence="ECO:0000269|PubMed:16803959" FT /id="VAR_027175" FT VARIANT 267 FT /note="E -> G (in dbSNP:rs1129425)" FT /evidence="ECO:0000269|PubMed:16803959" FT /id="VAR_027176" FT VARIANT 299 FT /note="G -> R (in dbSNP:rs1365776)" FT /evidence="ECO:0000269|PubMed:10913195, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16803959, ECO:0000269|PubMed:16816019, FT ECO:0000269|PubMed:7693701" FT /id="VAR_027177" FT VARIANT 367 FT /note="T -> M (in dbSNP:rs59573011)" FT /evidence="ECO:0000269|PubMed:16816019" FT /id="VAR_027178" FT VARIANT 425 FT /note="L -> S (may be associated with increased FT susceptibility to tuberculosis; dbSNP:rs3948464)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:16803959, ECO:0000269|PubMed:16816019" FT /id="VAR_027179" FT VARIANT 523 FT /note="M -> T (in dbSNP:rs1135791)" FT /evidence="ECO:0000269|PubMed:10913195, FT ECO:0000269|PubMed:16803959" FT /id="VAR_027180" FT VARIANT 579 FT /note="M -> I (in dbSNP:rs3948463)" FT /evidence="ECO:0000269|PubMed:16803959" FT /id="VAR_027181" FT VARIANT 683 FT /note="G -> S (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036030" FT CONFLICT 167 FT /note="D -> T (in Ref. 2; AAF99318/AAG09826)" FT /evidence="ECO:0000305" FT CONFLICT 464 FT /note="L -> S (in Ref. 1; AAA18806)" FT /evidence="ECO:0000305" FT CONFLICT 570 FT /note="M -> I (in Ref. 3; AK026488)" FT /evidence="ECO:0000305" SQ SEQUENCE 689 AA; 78396 MW; 31552E1A4C498EF7 CRC64; MFTMTRAMEE ALFQHFMHQK LGIAYAIHKP FPFFEGLLDN SIITKRMYME SLEACRNLIP VSRVVHNILT QLERTFNLSL LVTLFSQINL REYPNLVTIY RSFKRVGASY EWQSRDTPIL LEAPTGLAEG SSLHTPLALP PPQPPQPSCS PCAPRVSEPG TSSQQSDEIL SESPSPSDPV LPLPALIQEG RSTSVTNDKL TSKMNAEEDS EEMPSLLTST VQVASDNLIP QIRDKEDPQE MPHSPLGSMP EIRDNSPEPN DPEEPQEVSS TPSDKKGKKR KRCIWSTPKR RHKKKSLPGG TASSRHGIQK KLKRVDQVPQ KKDDSTCNST VETRAQKART ECARKSRSEE IIDGTSEMNE GKRSQKTPST PRRVTQGAAS PGHGIQEKLQ VVDKVTQRKD DSTWNSEVMM RVQKARTKCA RKSRLKEKKK EKDICSSSKR RFQKNIHRRG KPKSDTVDFH CSKLPVTCGE AKGILYKKKM KHGSSVKCIR NEDGTWLTPN EFEVEGKGRN AKNWKRNIRC EGMTLGELLK RKNSDECEVC CQGGQLLCCG TCPRVFHEDC HIPPVEAKRM LWSCTFCRMK RSSGSQQCHH VSKTLERQMQ PQDQLIRDYG EPFQEAMWLD LVKERLITEM YTVAWFVRDM RLMFRNHKTF YKASDFGQVG LDLEAEFEKD LKDVLGFHEA NDGGFWTLP //