SP110_HUMAN
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 03-AUG-2022, entry version 192.
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 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 [15]
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 [16]
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 Note=Found in the nuclear body.
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 CAUTION: [Isoform 3]:
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/";
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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; 124.
DR IntAct; Q9HB58; 34.
DR MINT; Q9HB58; -.
DR STRING; 9606.ENSP00000258381; -.
DR iPTMnet; Q9HB58; -.
DR PhosphoSitePlus; Q9HB58; -.
DR BioMuta; SP110; -.
DR DMDM; 313104323; -.
DR EPD; Q9HB58; -.
DR jPOST; Q9HB58; -.
DR MassIVE; Q9HB58; -.
DR MaxQB; Q9HB58; -.
DR PaxDb; Q9HB58; -.
DR PeptideAtlas; Q9HB58; -.
DR PRIDE; 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 Antibodypedia; 34401; 371 antibodies from 31 providers.
DR DNASU; 3431; -.
DR Ensembl; ENST00000258381.11; ENSP00000258381.6; ENSG00000135899.19. [Q9HB58-6]
DR Ensembl; ENST00000258382.10; ENSP00000258382.5; ENSG00000135899.19. [Q9HB58-3]
DR Ensembl; ENST00000358662.9; ENSP00000351488.4; ENSG00000135899.19. [Q9HB58-1]
DR Ensembl; ENST00000540870.5; ENSP00000439558.1; ENSG00000135899.19. [Q9HB58-7]
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 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; 377499at2759; -.
DR PhylomeDB; Q9HB58; -.
DR TreeFam; TF335091; -.
DR PathwayCommons; Q9HB58; -.
DR SignaLink; Q9HB58; -.
DR BioGRID-ORCS; 3431; 23 hits in 1104 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 202 other tissues.
DR ExpressionAtlas; Q9HB58; baseline and differential.
DR Genevisible; Q9HB58; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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 Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.10.390.10; -; 1.
DR Gene3D; 3.30.40.10; -; 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.
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; PTHR46386; 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; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF63763; SSF63763; 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.
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
