ID SNW1_HUMAN Reviewed; 536 AA. AC Q13573; A8K8A9; Q13483; Q32N03; Q5D0D6; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 215. DE RecName: Full=SNW domain-containing protein 1; DE AltName: Full=Nuclear protein SkiP; DE AltName: Full=Nuclear receptor coactivator NCoA-62 {ECO:0000303|PubMed:9632709}; DE AltName: Full=Ski-interacting protein {ECO:0000303|PubMed:11278756, ECO:0000303|PubMed:9569025}; GN Name=SNW1; GN Synonyms=SKIIP, SKIP {ECO:0000303|PubMed:10713164, GN ECO:0000303|PubMed:11371506}; 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], FUNCTION, AND INTERACTION WITH VDR. RX PubMed=9632709; DOI=10.1074/jbc.273.26.16434; RA Baudino T.A., Kraichely D.M., Jefcoat S.C. Jr., Winchester S.K., RA Partridge N.C., Macdonald P.N.; RT "Isolation and characterization of a novel coactivator protein, NCoA-62, RT involved in vitamin D-mediated transcription."; RL J. Biol. Chem. 273:16434-16441(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT. RX PubMed=9569025; DOI=10.1038/sj.onc.1201687; RA Dahl R., Wani B., Hayman M.J.; RT "The Ski oncoprotein interacts with Skip, the human homolog of Drosophila RT Bx42."; RL Oncogene 16:1579-1586(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cervix; 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 [8] RP PROTEIN SEQUENCE OF 2-23; 82-95; 179-193 AND 401-410, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V., Dozynkiewicz M., Norman J.C.; RL Submitted (JUN-2009) to UniProtKB. RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 282-536. RX PubMed=8973337; DOI=10.1016/s0378-1119(96)00483-0; RA Folk P., Puta F., Krpejsova L., Blahuskova A., Markos A., Rabino M., RA Dottin R.P.; RT "The homolog of chromatin binding protein Bx42 identified in RT Dictyostelium."; RL Gene 181:229-231(1996). RN [10] RP FUNCTION, AND INTERACTION WITH RBPJ; CIR1; HDAC2 AND EPSTEIN-BARR VIRUS RP EBNA2 PROTEIN. RX PubMed=10644367; DOI=10.1128/jvi.74.4.1939-1947.2000; RA Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.; RT "A role for SKIP in EBNA2 activation of CBF1-repressed promoters."; RL J. Virol. 74:1939-1947(2000). RN [11] RP INTERACTION WITH NOTCH1. RX PubMed=10713164; DOI=10.1128/mcb.20.7.2400-2410.2000; RA Zhou S., Fujimuro M., Hsieh J.J., Chen L., Miyamoto A., Weinmaster G., RA Hayward S.D.; RT "SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain RT of NotchIC To facilitate NotchIC function."; RL Mol. Cell. Biol. 20:2400-2410(2000). RN [12] RP FUNCTION, AND INTERACTION WITH PABPN1. RX PubMed=11371506; DOI=10.1093/hmg/10.11.1129; RA Kim Y.-J., Noguchi S., Hayashi Y.K., Tsukahara T., Shimizu T., Arahata K.; RT "The product of an oculopharyngeal muscular dystrophy gene, poly(A)-binding RT protein 2, interacts with SKIP and stimulates muscle-specific gene RT expression."; RL Hum. Mol. Genet. 10:1129-1139(2001). RN [13] RP FUNCTION, AND INTERACTION WITH SMAD2 AND SMAD3. RX PubMed=11278756; DOI=10.1074/jbc.m010815200; RA Leong G.M., Subramaniam N., Figueroa J., Flanagan J.L., Hayman M.J., RA Eisman J.A., Kouzmenko A.P.; RT "Ski-interacting protein interacts with Smad proteins to augment RT transforming growth factor-beta-dependent transcription."; RL J. Biol. Chem. 276:18243-18248(2001). RN [14] RP FUNCTION, AND SUBUNIT. RX PubMed=11514567; DOI=10.1074/jbc.m106263200; RA Zhang C., Baudino T.A., Dowd D.R., Tokumaru H., Wang W., MacDonald P.N.; RT "Ternary complexes and cooperative interplay between NCoA-62/Ski- RT interacting protein and steroid receptor coactivators in vitamin D RT receptor-mediated transcription."; RL J. Biol. Chem. 276:40614-40620(2001). RN [15] RP INTERACTION WITH HPV16 PROTEIN E7. RX PubMed=11753645; DOI=10.1038/sj.onc.1204960; RA Prathapam T., Kuhne C., Banks L.; RT "The HPV-16 E7 oncoprotein binds Skip and suppresses its transcriptional RT activity."; RL Oncogene 20:7677-7685(2001). RN [16] RP INTERACTION WITH RB1. RX PubMed=12466551; DOI=10.1093/nar/gkf658; RA Prathapam T., Kuhne C., Banks L.; RT "Skip interacts with the retinoblastoma tumor suppressor and inhibits its RT transcriptional repression activity."; RL Nucleic Acids Res. 30:5261-5268(2002). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C RP COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=11991638; DOI=10.1017/s1355838202021088; RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.; RT "Purification and characterization of native spliceosomes suitable for RT three-dimensional structural analysis."; RL RNA 8:426-439(2002). RN [18] RP INTERACTION WITH VDR. RX PubMed=12529369; DOI=10.1074/jbc.c200712200; RA Barry J.B., Leong G.M., Church W.B., Issa L.L., Eisman J.A., Gardiner E.M.; RT "Interactions of SKIP/NCoA-62, TFIIB, and retinoid X receptor with vitamin RT D receptor helix H10 residues."; RL J. Biol. Chem. 278:8224-8228(2003). RN [19] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=12840015; DOI=10.1074/jbc.m305191200; RA Zhang C., Dowd D.R., Staal A., Gu C., Lian J.B., van Wijnen A.J., RA Stein G.S., MacDonald P.N.; RT "Nuclear coactivator-62 kDa/Ski-interacting protein is a nuclear matrix- RT associated coactivator that may couple vitamin D receptor-mediated RT transcription and RNA splicing."; RL J. Biol. Chem. 278:35325-35336(2003). RN [20] RP FUNCTION. RX PubMed=14985122; DOI=10.1016/j.bbrc.2004.02.004; RA Leong G.M., Subramaniam N., Issa L.L., Barry J.B., Kino T., Driggers P.H., RA Hayman M.J., Eisman J.A., Gardiner E.M.; RT "Ski-interacting protein, a bifunctional nuclear receptor coregulator that RT interacts with N-CoR/SMRT and p300."; RL Biochem. Biophys. Res. Commun. 315:1070-1076(2004). RN [21] RP INTERACTION WITH MAGEA1. RX PubMed=15316101; DOI=10.1093/nar/gkh735; RA Laduron S., Deplus R., Zhou S., Kholmanskikh O., Godelaine D., De Smet C., RA Hayward S.D., Fuks F., Boon T., De Plaen E.; RT "MAGE-A1 interacts with adaptor SKIP and the deacetylase HDAC1 to repress RT transcription."; RL Nucleic Acids Res. 32:4340-4350(2004). RN [22] RP FUNCTION, AND SUBUNIT. RX PubMed=15194481; DOI=10.1016/j.bbrc.2004.05.096; RA Figueroa J.D., Hayman M.J.; RT "The human Ski-interacting protein functionally substitutes for the yeast RT PRP45 gene."; RL Biochem. Biophys. Res. Commun. 319:1105-1109(2004). RN [23] RP IDENTIFICATION BY 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 [24] RP INTERACTION WITH PPIL1. RX PubMed=16595688; DOI=10.1074/jbc.m511155200; RA Xu C., Zhang J., Huang X., Sun J., Xu Y., Tang Y., Wu J., Shi Y., Huang Q., RA Zhang Q.; RT "Solution structure of human peptidyl prolyl isomerase-like protein 1 and RT insights into its interaction with SKIP."; RL J. Biol. Chem. 281:15900-15908(2006). RN [25] RP INTERACTION WITH FOXN3. RX PubMed=16102918; DOI=10.1016/j.gene.2005.06.014; RA Scott K.L., Plon S.E.; RT "CHES1/FOXN3 interacts with Ski-interacting protein and acts as a RT transcriptional repressor."; RL Gene 359:119-126(2005). RN [26] RP FUNCTION, AND SUBUNIT. RX PubMed=15905409; DOI=10.1101/gad.1291705; RA Bres V., Gomes N., Pickle L., Jones K.A.; RT "A human splicing factor, SKIP, associates with P-TEFb and enhances RT transcription elongation by HIV-1 Tat."; RL Genes Dev. 19:1211-1226(2005). RN [27] RP FUNCTION, AND IDENTIFICATION IN THE SNARP COMPLEX. RX PubMed=18794151; DOI=10.1158/0008-5472.can-08-1217; RA Bracken C.P., Wall S.J., Barre B., Panov K.I., Ajuh P.M., Perkins N.D.; RT "Regulation of cyclin D1 RNA stability by SNIP1."; RL Cancer Res. 68:7621-7628(2008). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-232, 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 [29] 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 [30] RP FUNCTION, AND SUBUNIT. RX PubMed=19818711; DOI=10.1016/j.molcel.2009.08.015; RA Bres V., Yoshida T., Pickle L., Jones K.A.; RT "SKIP interacts with c-Myc and Menin to promote HIV-1 Tat RT transactivation."; RL Mol. Cell 36:75-87(2009). RN [31] RP INTERACTION WITH PPIL1, AND MUTAGENESIS OF GLU-66 AND MET-76. RX PubMed=20007319; DOI=10.1074/jbc.m109.087528; RA Wang X., Zhang S., Zhang J., Huang X., Xu C., Wang W., Liu Z., Wu J., RA Shi Y.; RT "A large intrinsically disordered region in SKIP and its disorder-order RT transition induced by PPIL1 binding revealed by NMR."; RL J. Biol. Chem. 285:4951-4963(2010). RN [32] RP INTERACTION WITH PPIL1. RX PubMed=20368803; DOI=10.1371/journal.pone.0010013; RA Stegmann C.M., Luhrmann R., Wahl M.C.; RT "The crystal structure of PPIL1 bound to cyclosporine A suggests a binding RT mode for a linear epitope of the SKIP protein."; RL PLoS ONE 5:E10013-E10013(2010). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-232 AND SER-234, AND RP 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 [34] 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 [35] RP FUNCTION, AND INTERACTION WITH U2AF2. RX PubMed=21460037; DOI=10.1101/gad.2002611; RA Chen Y., Zhang L., Jones K.A.; RT "SKIP counteracts p53-mediated apoptosis via selective regulation of RT p21Cip1 mRNA splicing."; RL Genes Dev. 25:701-716(2011). RN [36] RP FUNCTION, AND INTERACTION WITH NOTCH1 AND MAML1. RX PubMed=21245387; DOI=10.1128/mcb.00360-10; RA Vasquez-Del Carpio R., Kaplan F.M., Weaver K.L., VanWye J.D., RA Alves-Guerra M.C., Robbins D.J., Capobianco A.J.; RT "Assembly of a Notch transcriptional activation complex requires RT multimerization."; RL Mol. Cell. Biol. 31:1396-1408(2011). RN [37] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-234, 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 [38] 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=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [39] 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=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 [40] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-182; SER-190; RP SER-224; SER-232; SER-446; SER-479 AND SER-481, AND IDENTIFICATION BY MASS RP 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 [41] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-232, 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 [42] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-170; LYS-193 AND LYS-240, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [43] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-97; LYS-170; LYS-193; LYS-240 AND RP LYS-509, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [44] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-23; LYS-81; LYS-115; LYS-122; RP LYS-141; LYS-158; LYS-170; LYS-193; LYS-240; LYS-258; LYS-286; LYS-339; RP LYS-344; LYS-416; LYS-441; LYS-452 AND LYS-509, AND IDENTIFICATION BY MASS RP 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 [45] RP INTERACTION WITH PPIL1. RX PubMed=33220177; DOI=10.1016/j.neuron.2020.10.035; RA Chai G., Webb A., Li C., Antaki D., Lee S., Breuss M.W., Lang N., RA Stanley V., Anzenberg P., Yang X., Marshall T., Gaffney P., Wierenga K.J., RA Chung B.H., Tsang M.H., Pais L.S., Lovgren A.K., VanNoy G.E., Rehm H.L., RA Mirzaa G., Leon E., Diaz J., Neumann A., Kalverda A.P., Manfield I.W., RA Parry D.A., Logan C.V., Johnson C.A., Bonthron D.T., Valleley E.M.A., RA Issa M.Y., Abdel-Ghafar S.F., Abdel-Hamid M.S., Jennings P., Zaki M.S., RA Sheridan E., Gleeson J.G.; RT "Mutations in Spliceosomal Genes PPIL1 and PRP17 Cause Neurodegenerative RT Pontocerebellar Hypoplasia with Microcephaly."; RL Neuron 109:241-256(2021). RN [46] {ECO:0007744|PDB:5XJC} RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033; RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.; RT "An Atomic Structure of the Human Spliceosome."; RL Cell 169:918-929(2017). RN [47] {ECO:0007744|PDB:5MQF} RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT, RP SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=28076346; DOI=10.1038/nature21079; RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K., RA Urlaub H., Kastner B., Stark H., Luhrmann R.; RT "Cryo-EM structure of a human spliceosome activated for step 2 of RT splicing."; RL Nature 542:318-323(2017). RN [48] {ECO:0007744|PDB:7DVQ} RP STRUCTURE BY ELECTRON MICROSCOPY (2.89 ANGSTROMS), AND SUBUNIT. RX PubMed=33509932; DOI=10.1126/science.abg0879; RA Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.; RT "Structure of the activated human minor spliceosome."; RL Science 371:0-0(2021). CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome CC (PubMed:11991638, PubMed:28502770, PubMed:28076346). As a component of CC the minor spliceosome, involved in the splicing of U12-type introns in CC pre-mRNAs (Probable). Required for the specific splicing of CDKN1A pre- CC mRNA; the function probably involves the recruitment of U2AF2 to the CC mRNA. May recruit PPIL1 to the spliceosome. May be involved in cyclin- CC D1/CCND1 mRNA stability through the SNARP complex which associates with CC both the 3'end of the CCND1 gene and its mRNA. Involved in CC transcriptional regulation. Modulates TGF-beta-mediated transcription CC via association with SMAD proteins, MYOD1-mediated transcription via CC association with PABPN1, RB1-mediated transcriptional repression, and CC retinoid-X receptor (RXR)- and vitamin D receptor (VDR)-dependent gene CC transcription in a cell line-specific manner probably involving CC coactivators NCOA1 and GRIP1. Is involved in NOTCH1-mediated CC transcriptional activation. Binds to multimerized forms of Notch CC intracellular domain (NICD) and is proposed to recruit transcriptional CC coactivators such as MAML1 to form an intermediate preactivation CC complex which associates with DNA-bound CBF-1/RBPJ to form a CC transcriptional activation complex by releasing SNW1 and redundant CC NOTCH1 NICD. {ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:11278756, CC ECO:0000269|PubMed:11371506, ECO:0000269|PubMed:11514567, CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12840015, CC ECO:0000269|PubMed:14985122, ECO:0000269|PubMed:15194481, CC ECO:0000269|PubMed:15905409, ECO:0000269|PubMed:18794151, CC ECO:0000269|PubMed:19818711, ECO:0000269|PubMed:21245387, CC ECO:0000269|PubMed:21460037, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:9632709, CC ECO:0000305|PubMed:33509932}. CC -!- FUNCTION: (Microbial infection) Is recruited by HIV-1 Tat to Tat:P- CC TEFb:TAR RNA complexes and is involved in Tat transcription by CC recruitment of MYC, MEN1 and TRRAP to the HIV promoter. CC {ECO:0000269|PubMed:15905409, ECO:0000269|PubMed:19818711}. CC -!- FUNCTION: (Microbial infection) Proposed to be involved in CC transcriptional activation by EBV EBNA2 of CBF-1/RBPJ-repressed CC promoters. {ECO:0000269|PubMed:10644367}. CC -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638, CC PubMed:28502770, PubMed:28076346). Associates with U4/U6-U5 tri-small CC nuclear ribonucleoproteins (U4/U6-U5 tri-snRNPs). Component of the CC minor spliceosome, which splices U12-type introns (PubMed:33509932). CC Interacts with SKI, SMAD2,SMAD3, RBPJ, RB1, PABPN1, MAGEA1, SIRT1, CC FOXN3, U2AF2, DAXX and ATP1B4. Interacts with PPIL1 (PubMed:16595688, CC PubMed:20007319, PubMed:20368803, PubMed:33220177). Interacts with VDR CC and RXRA; preferentially associates with VDR:RXRA heterodimers CC (PubMed:9632709, PubMed:12529369). Interacts with NCOR2 CC (PubMed:10644367). Interacts with MAML1 (PubMed:21245387). Interacts CC with NOTCH1 NICD; the interaction involves multimerized NOTCH1 NICD CC (PubMed:21245387). Forms a complex with NOTCH1 NICD and MAML1; the CC association is dissociated by RBPJ (PubMed:21245387). Associates with CC positive transcription elongation factor b (P-TEFb) (PubMed:15905409). CC Component of the SNARP complex which consists at least of SNIP1, SNW1, CC THRAP3, BCLAF1 and PNN (PubMed:18794151). CC {ECO:0000250|UniProtKB:Q9CSN1, ECO:0000269|PubMed:10644367, CC ECO:0000269|PubMed:10713164, ECO:0000269|PubMed:11278756, CC ECO:0000269|PubMed:11371506, ECO:0000269|PubMed:11514567, CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12466551, CC ECO:0000269|PubMed:12529369, ECO:0000269|PubMed:12840015, CC ECO:0000269|PubMed:15194481, ECO:0000269|PubMed:15316101, CC ECO:0000269|PubMed:15905409, ECO:0000269|PubMed:16102918, CC ECO:0000269|PubMed:16595688, ECO:0000269|PubMed:18794151, CC ECO:0000269|PubMed:19818711, ECO:0000269|PubMed:20007319, CC ECO:0000269|PubMed:20368803, ECO:0000269|PubMed:21245387, CC ECO:0000269|PubMed:21460037, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:33220177, CC ECO:0000269|PubMed:33509932, ECO:0000269|PubMed:9569025, CC ECO:0000269|PubMed:9632709}. CC -!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus CC type-16 (HPV16) E7 protein. {ECO:0000269|PubMed:11753645}. CC -!- SUBUNIT: (Microbial infection) Interacts with EBV EBNA2; EBNA2 competes CC with NCOR2 for interaction with SNW1. {ECO:0000269|PubMed:10644367}. CC -!- INTERACTION: CC Q13573; O94929-2: ABLIM3; NbExp=3; IntAct=EBI-632715, EBI-11961672; CC Q13573; P07550: ADRB2; NbExp=3; IntAct=EBI-632715, EBI-491169; CC Q13573; Q96BM9: ARL8A; NbExp=2; IntAct=EBI-632715, EBI-4401082; CC Q13573; Q9NVJ2: ARL8B; NbExp=5; IntAct=EBI-632715, EBI-718376; CC Q13573; Q8TD16-2: BICD2; NbExp=3; IntAct=EBI-632715, EBI-11975051; CC Q13573; Q13895: BYSL; NbExp=3; IntAct=EBI-632715, EBI-358049; CC Q13573; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-632715, EBI-747505; CC Q13573; P55212: CASP6; NbExp=3; IntAct=EBI-632715, EBI-718729; CC Q13573; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-632715, EBI-11977221; CC Q13573; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-632715, EBI-747776; CC Q13573; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-632715, EBI-739624; CC Q13573; P36544: CHRNA7; NbExp=3; IntAct=EBI-632715, EBI-79333; CC Q13573; O94985-2: CLSTN1; NbExp=3; IntAct=EBI-632715, EBI-16041593; CC Q13573; Q8WYA6: CTNNBL1; NbExp=2; IntAct=EBI-632715, EBI-748128; CC Q13573; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-632715, EBI-5453285; CC Q13573; P99999: CYCS; NbExp=3; IntAct=EBI-632715, EBI-446479; CC Q13573; G5E9A7: DMWD; NbExp=3; IntAct=EBI-632715, EBI-10976677; CC Q13573; P19447: ERCC3; NbExp=3; IntAct=EBI-632715, EBI-1183307; CC Q13573; Q9NQT4: EXOSC5; NbExp=3; IntAct=EBI-632715, EBI-371876; CC Q13573; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-632715, EBI-6658203; CC Q13573; P22607: FGFR3; NbExp=3; IntAct=EBI-632715, EBI-348399; CC Q13573; P21333-2: FLNA; NbExp=3; IntAct=EBI-632715, EBI-9641086; CC Q13573; O00409: FOXN3; NbExp=3; IntAct=EBI-632715, EBI-372721; CC Q13573; Q06547: GABPB1; NbExp=3; IntAct=EBI-632715, EBI-618165; CC Q13573; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-632715, EBI-7960826; CC Q13573; P14136: GFAP; NbExp=3; IntAct=EBI-632715, EBI-744302; CC Q13573; Q08379: GOLGA2; NbExp=6; IntAct=EBI-632715, EBI-618309; CC Q13573; Q14957: GRIN2C; NbExp=3; IntAct=EBI-632715, EBI-8285963; CC Q13573; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-632715, EBI-717919; CC Q13573; O00291: HIP1; NbExp=3; IntAct=EBI-632715, EBI-473886; CC Q13573; Q5SUL5: HLA-A; NbExp=3; IntAct=EBI-632715, EBI-8561769; CC Q13573; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-632715, EBI-2549423; CC Q13573; P30519: HMOX2; NbExp=3; IntAct=EBI-632715, EBI-712096; CC Q13573; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-632715, EBI-10961706; CC Q13573; P01112: HRAS; NbExp=3; IntAct=EBI-632715, EBI-350145; CC Q13573; O75031: HSF2BP; NbExp=3; IntAct=EBI-632715, EBI-7116203; CC Q13573; P11021: HSPA5; NbExp=5; IntAct=EBI-632715, EBI-354921; CC Q13573; P04792: HSPB1; NbExp=3; IntAct=EBI-632715, EBI-352682; CC Q13573; P42858: HTT; NbExp=12; IntAct=EBI-632715, EBI-466029; CC Q13573; Q9Y6K9: IKBKG; NbExp=4; IntAct=EBI-632715, EBI-81279; CC Q13573; Q13422: IKZF1; NbExp=3; IntAct=EBI-632715, EBI-745305; CC Q13573; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-632715, EBI-1055254; CC Q13573; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-632715, EBI-2556193; CC Q13573; Q92993: KAT5; NbExp=3; IntAct=EBI-632715, EBI-399080; CC Q13573; O60333-2: KIF1B; NbExp=3; IntAct=EBI-632715, EBI-10975473; CC Q13573; Q6A162: KRT40; NbExp=3; IntAct=EBI-632715, EBI-10171697; CC Q13573; P02545: LMNA; NbExp=4; IntAct=EBI-632715, EBI-351935; CC Q13573; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-632715, EBI-11742507; CC Q13573; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-632715, EBI-741037; CC Q13573; P43355: MAGEA1; NbExp=3; IntAct=EBI-632715, EBI-740978; CC Q13573; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-632715, EBI-746778; CC Q13573; P31153: MAT2A; NbExp=3; IntAct=EBI-632715, EBI-1050743; CC Q13573; Q9BTE3-2: MCMBP; NbExp=3; IntAct=EBI-632715, EBI-9384556; CC Q13573; Q8IVT2: MISP; NbExp=3; IntAct=EBI-632715, EBI-2555085; CC Q13573; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-632715, EBI-742948; CC Q13573; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-632715, EBI-11522433; CC Q13573; O43639: NCK2; NbExp=3; IntAct=EBI-632715, EBI-713635; CC Q13573; Q9Y618: NCOR2; NbExp=4; IntAct=EBI-632715, EBI-80830; CC Q13573; P07196: NEFL; NbExp=3; IntAct=EBI-632715, EBI-475646; CC Q13573; P35240: NF2; NbExp=3; IntAct=EBI-632715, EBI-1014472; CC Q13573; P46531: NOTCH1; NbExp=3; IntAct=EBI-632715, EBI-636374; CC Q13573; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-632715, EBI-398874; CC Q13573; Q5BJF6-2: ODF2; NbExp=3; IntAct=EBI-632715, EBI-9090919; CC Q13573; Q96CV9: OPTN; NbExp=3; IntAct=EBI-632715, EBI-748974; CC Q13573; Q86U42: PABPN1; NbExp=5; IntAct=EBI-632715, EBI-1226435; CC Q13573; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-632715, EBI-79165; CC Q13573; Q9H307: PNN; NbExp=3; IntAct=EBI-632715, EBI-681904; CC Q13573; P62937-2: PPIA; NbExp=3; IntAct=EBI-632715, EBI-25884072; CC Q13573; Q9Y3C6: PPIL1; NbExp=15; IntAct=EBI-632715, EBI-2557649; CC Q13573; P31321: PRKAR1B; NbExp=3; IntAct=EBI-632715, EBI-2805516; CC Q13573; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-632715, EBI-5280197; CC Q13573; P41219: PRPH; NbExp=3; IntAct=EBI-632715, EBI-752074; CC Q13573; Q15276: RABEP1; NbExp=3; IntAct=EBI-632715, EBI-447043; CC Q13573; P62826: RAN; NbExp=3; IntAct=EBI-632715, EBI-286642; CC Q13573; Q06330: RBPJ; NbExp=2; IntAct=EBI-632715, EBI-632552; CC Q13573; Q6NUQ1: RINT1; NbExp=7; IntAct=EBI-632715, EBI-726876; CC Q13573; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-632715, EBI-396669; CC Q13573; O43290: SART1; NbExp=3; IntAct=EBI-632715, EBI-607761; CC Q13573; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-632715, EBI-9090795; CC Q13573; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-632715, EBI-2623095; CC Q13573; Q96EB6: SIRT1; NbExp=7; IntAct=EBI-632715, EBI-1802965; CC Q13573; Q15796: SMAD2; NbExp=3; IntAct=EBI-632715, EBI-1040141; CC Q13573; P84022: SMAD3; NbExp=5; IntAct=EBI-632715, EBI-347161; CC Q13573; Q8TAD8: SNIP1; NbExp=8; IntAct=EBI-632715, EBI-749336; CC Q13573; Q69YQ0: SPECC1L; NbExp=3; IntAct=EBI-632715, EBI-351113; CC Q13573; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-632715, EBI-5235340; CC Q13573; Q9NUJ3: TCP11L1; NbExp=3; IntAct=EBI-632715, EBI-2555179; CC Q13573; Q8IYF3: TEX11; NbExp=3; IntAct=EBI-632715, EBI-742397; CC Q13573; Q9UBB9: TFIP11; NbExp=7; IntAct=EBI-632715, EBI-1105213; CC Q13573; Q9Y2W1: THRAP3; NbExp=4; IntAct=EBI-632715, EBI-352039; CC Q13573; Q5JTV8: TOR1AIP1; NbExp=3; IntAct=EBI-632715, EBI-2559665; CC Q13573; Q13077: TRAF1; NbExp=3; IntAct=EBI-632715, EBI-359224; CC Q13573; P36406: TRIM23; NbExp=3; IntAct=EBI-632715, EBI-740098; CC Q13573; P26368: U2AF2; NbExp=5; IntAct=EBI-632715, EBI-742339; CC Q13573; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-632715, EBI-741480; CC Q13573; P22695: UQCRC2; NbExp=3; IntAct=EBI-632715, EBI-1051424; CC Q13573; P22415: USF1; NbExp=3; IntAct=EBI-632715, EBI-1054489; CC Q13573; P11473: VDR; NbExp=5; IntAct=EBI-632715, EBI-286357; CC Q13573; Q9HCS7: XAB2; NbExp=2; IntAct=EBI-632715, EBI-295232; CC Q13573; P61981: YWHAG; NbExp=3; IntAct=EBI-632715, EBI-359832; CC Q13573; Q96NB3: ZNF830; NbExp=2; IntAct=EBI-632715, EBI-3920997; CC Q13573; Q9Y649; NbExp=3; IntAct=EBI-632715, EBI-25900580; CC Q13573; Q60974: Ncor1; Xeno; NbExp=3; IntAct=EBI-632715, EBI-349004; CC Q13573; A0A0D6GID3: sifA; Xeno; NbExp=2; IntAct=EBI-632715, EBI-30861778; CC Q13573; P49140: SKI; Xeno; NbExp=4; IntAct=EBI-632715, EBI-6392357; CC Q13573; P17863: V-SKI; Xeno; NbExp=4; IntAct=EBI-632715, EBI-6392320; CC Q13573; P48281: Vdr; Xeno; NbExp=2; IntAct=EBI-632715, EBI-346797; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11991638, CC ECO:0000269|PubMed:12840015, ECO:0000269|PubMed:28076346, CC ECO:0000269|PubMed:28502770}. CC -!- SIMILARITY: Belongs to the SNW 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; AF045184; AAC31697.1; -; mRNA. DR EMBL; U51432; AAC15912.1; -; mRNA. DR EMBL; BT020060; AAV38863.1; -; mRNA. DR EMBL; BT020061; AAV38864.1; -; mRNA. DR EMBL; AK292274; BAF84963.1; -; mRNA. DR EMBL; AC008372; AAF23325.1; -; Genomic_DNA. DR EMBL; CH471061; EAW81308.1; -; Genomic_DNA. DR EMBL; BC040112; AAH40112.1; -; mRNA. DR EMBL; BC046105; AAH46105.2; -; mRNA. DR EMBL; BC108903; AAI08904.1; -; mRNA. DR EMBL; U43960; AAB48857.1; -; Genomic_DNA. DR CCDS; CCDS9867.1; -. DR RefSeq; NP_036377.1; NM_012245.2. DR PDB; 5MQF; EM; 5.90 A; C=1-536. DR PDB; 5XJC; EM; 3.60 A; R=1-536. DR PDB; 5YZG; EM; 4.10 A; R=1-536. DR PDB; 5Z58; EM; 4.90 A; R=1-536. DR PDB; 6FF4; EM; 16.00 A; C=1-536. DR PDB; 6FF7; EM; 4.50 A; C=1-536. DR PDB; 6ICZ; EM; 3.00 A; R=1-536. DR PDB; 6ID0; EM; 2.90 A; R=1-536. DR PDB; 6ID1; EM; 2.86 A; R=1-536. DR PDB; 6QDV; EM; 3.30 A; K=41-329. DR PDB; 6ZYM; EM; 3.40 A; C=1-536. DR PDB; 7A5P; EM; 5.00 A; C=1-536. DR PDB; 7AAV; EM; 4.20 A; v=1-536. DR PDB; 7ABF; EM; 3.90 A; v=1-536. DR PDB; 7ABG; EM; 7.80 A; v=1-536. DR PDB; 7ABI; EM; 8.00 A; v=1-536. DR PDB; 7DVQ; EM; 2.89 A; R=1-536. DR PDB; 7QTT; EM; 3.10 A; Y=1-536. DR PDB; 7W59; EM; 3.60 A; R=1-536. DR PDB; 7W5A; EM; 3.60 A; R=1-536. DR PDB; 7W5B; EM; 4.30 A; R=1-536. DR PDB; 8C6J; EM; 2.80 A; K=1-536. DR PDB; 8CH6; EM; 5.90 A; Y=1-536. DR PDBsum; 5MQF; -. DR PDBsum; 5XJC; -. DR PDBsum; 5YZG; -. DR PDBsum; 5Z58; -. DR PDBsum; 6FF4; -. DR PDBsum; 6FF7; -. DR PDBsum; 6ICZ; -. DR PDBsum; 6ID0; -. DR PDBsum; 6ID1; -. DR PDBsum; 6QDV; -. DR PDBsum; 6ZYM; -. DR PDBsum; 7A5P; -. DR PDBsum; 7AAV; -. DR PDBsum; 7ABF; -. DR PDBsum; 7ABG; -. DR PDBsum; 7ABI; -. DR PDBsum; 7DVQ; -. DR PDBsum; 7QTT; -. DR PDBsum; 7W59; -. DR PDBsum; 7W5A; -. DR PDBsum; 7W5B; -. DR PDBsum; 8C6J; -. DR PDBsum; 8CH6; -. DR AlphaFoldDB; Q13573; -. DR EMDB; EMD-11569; -. DR EMDB; EMD-11693; -. DR EMDB; EMD-11694; -. DR EMDB; EMD-11695; -. DR EMDB; EMD-11697; -. DR EMDB; EMD-14146; -. DR EMDB; EMD-16452; -. DR EMDB; EMD-16658; -. DR EMDB; EMD-30875; -. DR EMDB; EMD-32317; -. DR EMDB; EMD-32319; -. DR EMDB; EMD-32321; -. DR EMDB; EMD-3545; -. DR EMDB; EMD-4255; -. DR EMDB; EMD-4525; -. DR EMDB; EMD-6721; -. DR EMDB; EMD-6864; -. DR EMDB; EMD-6891; -. DR EMDB; EMD-9645; -. DR EMDB; EMD-9646; -. DR EMDB; EMD-9647; -. DR SMR; Q13573; -. DR BioGRID; 116597; 762. DR ComplexPortal; CPX-2653; SNIP1/SkIP associated RNA-processing complex. DR CORUM; Q13573; -. DR DIP; DIP-34800N; -. DR IntAct; Q13573; 715. DR MINT; Q13573; -. DR STRING; 9606.ENSP00000451129; -. DR GlyCosmos; Q13573; 1 site, 1 glycan. DR GlyGen; Q13573; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q13573; -. DR MetOSite; Q13573; -. DR PhosphoSitePlus; Q13573; -. DR SwissPalm; Q13573; -. DR BioMuta; SNW1; -. DR DMDM; 2500813; -. DR EPD; Q13573; -. DR jPOST; Q13573; -. DR MassIVE; Q13573; -. DR MaxQB; Q13573; -. DR PaxDb; 9606-ENSP00000261531; -. DR PeptideAtlas; Q13573; -. DR ProteomicsDB; 59577; -. DR Pumba; Q13573; -. DR TopDownProteomics; Q13573; -. DR Antibodypedia; 71; 157 antibodies from 30 providers. DR DNASU; 22938; -. DR Ensembl; ENST00000261531.12; ENSP00000261531.8; ENSG00000100603.14. DR GeneID; 22938; -. DR KEGG; hsa:22938; -. DR MANE-Select; ENST00000261531.12; ENSP00000261531.8; NM_012245.3; NP_036377.1. DR UCSC; uc001xuf.4; human. DR AGR; HGNC:16696; -. DR CTD; 22938; -. DR DisGeNET; 22938; -. DR GeneCards; SNW1; -. DR HGNC; HGNC:16696; SNW1. DR HPA; ENSG00000100603; Low tissue specificity. DR MIM; 603055; gene. DR neXtProt; NX_Q13573; -. DR OpenTargets; ENSG00000100603; -. DR PharmGKB; PA134883977; -. DR VEuPathDB; HostDB:ENSG00000100603; -. DR eggNOG; KOG2441; Eukaryota. DR GeneTree; ENSGT00390000010423; -. DR HOGENOM; CLU_006601_2_2_1; -. DR InParanoid; Q13573; -. DR OMA; YGQRRGW; -. DR OrthoDB; 5490078at2759; -. DR PhylomeDB; Q13573; -. DR TreeFam; TF300782; -. DR PathwayCommons; Q13573; -. DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation. DR Reactome; R-HSA-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells. DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription. DR Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity. DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants. DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants. DR Reactome; R-HSA-350054; Notch-HLH transcription pathway. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling. DR Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription. DR Reactome; R-HSA-9013695; NOTCH4 Intracellular Domain Regulates Transcription. DR Reactome; R-HSA-9793380; Formation of paraxial mesoderm. DR SABIO-RK; Q13573; -. DR SignaLink; Q13573; -. DR SIGNOR; Q13573; -. DR BioGRID-ORCS; 22938; 806 hits in 1166 CRISPR screens. DR ChiTaRS; SNW1; human. DR GeneWiki; SNW1; -. DR GenomeRNAi; 22938; -. DR Pharos; Q13573; Tbio. DR PRO; PR:Q13573; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q13573; Protein. DR Bgee; ENSG00000100603; Expressed in cervix squamous epithelium and 219 other cell types or tissues. DR ExpressionAtlas; Q13573; baseline and differential. DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:CAFA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005681; C:spliceosomal complex; IDA:UniProtKB. DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:CAFA. DR GO; GO:0005112; F:Notch binding; IPI:UniProtKB. DR GO; GO:0050681; F:nuclear androgen receptor binding; IPI:CAFA. DR GO; GO:0016922; F:nuclear receptor binding; IDA:UniProtKB. DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IDA:UniProtKB. DR GO; GO:0042809; F:nuclear vitamin D receptor binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0046332; F:SMAD binding; IDA:UniProtKB. DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB. DR GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB. DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB. DR GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:UniProtKB. DR GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0048385; P:regulation of retinoic acid receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc. DR GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IDA:UniProtKB. DR DisProt; DP00608; -. DR InterPro; IPR017862; SKI-int_prot_SKIP. DR InterPro; IPR004015; SKI-int_prot_SKIP_SNW-dom. DR PANTHER; PTHR12096; NUCLEAR PROTEIN SKIP-RELATED; 1. DR PANTHER; PTHR12096:SF0; SNW DOMAIN-CONTAINING PROTEIN 1; 1. DR Pfam; PF02731; SKIP_SNW; 1. DR Genevisible; Q13573; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; KW Host-virus interaction; Isopeptide bond; mRNA processing; mRNA splicing; KW Nucleus; Phosphoprotein; Reference proteome; Spliceosome; Transcription; KW Transcription regulation; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..536 FT /note="SNW domain-containing protein 1" FT /id="PRO_0000084827" FT REGION 1..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 59..79 FT /note="Interaction with PPIL1" FT /evidence="ECO:0000269|PubMed:16595688" FT REGION 174..339 FT /note="SNW" FT REGION 209..233 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 311..386 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 470..536 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..17 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 470..530 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 224 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 232 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 234 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 446 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 479 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 481 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 23 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 81 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 97 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364" FT CROSSLNK 115 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 122 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 141 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 158 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 170 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 193 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 240 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 258 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 286 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 339 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 344 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 416 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 441 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 452 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 509 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT MUTAGEN 66 FT /note="E->A,R: Abolishes interaction with PPIL1." FT /evidence="ECO:0000269|PubMed:20007319" FT MUTAGEN 76 FT /note="M->A: Abolishes interaction with PPIL1." FT /evidence="ECO:0000269|PubMed:20007319" FT TURN 53..56 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:6ICZ" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 98..102 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 107..109 FT /evidence="ECO:0007829|PDB:6ZYM" FT HELIX 111..114 FT /evidence="ECO:0007829|PDB:6FF4" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 130..133 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 137..159 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 160..162 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 163..167 FT /evidence="ECO:0007829|PDB:6ID0" FT STRAND 175..180 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 182..184 FT /evidence="ECO:0007829|PDB:6FF4" FT STRAND 186..191 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 195..201 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 239..244 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 264..267 FT /evidence="ECO:0007829|PDB:6ID1" FT TURN 272..274 FT /evidence="ECO:0007829|PDB:6ID1" FT HELIX 283..316 FT /evidence="ECO:0007829|PDB:6ID1" FT STRAND 328..332 FT /evidence="ECO:0007829|PDB:6FF4" FT HELIX 353..372 FT /evidence="ECO:0007829|PDB:7QTT" FT HELIX 378..381 FT /evidence="ECO:0007829|PDB:7QTT" FT STRAND 384..386 FT /evidence="ECO:0007829|PDB:7QTT" FT HELIX 389..393 FT /evidence="ECO:0007829|PDB:7QTT" FT TURN 409..413 FT /evidence="ECO:0007829|PDB:6FF4" FT TURN 421..425 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 455..458 FT /evidence="ECO:0007829|PDB:7DVQ" FT HELIX 463..469 FT /evidence="ECO:0007829|PDB:7DVQ" SQ SEQUENCE 536 AA; 61494 MW; 0CC75E0D0B2CF842 CRC64; MALTSFLPAP TQLSQDQLEA EEKARSQRSR QTSLVSSRRE PPPYGYRKGW IPRLLEDFGD GGAFPEIHVA QYPLDMGRKK KMSNALAIQV DSEGKIKYDA IARQGQSKDK VIYSKYTDLV PKEVMNADDP DLQRPDEEAI KEITEKTRVA LEKSVSQKVA AAMPVRAADK LAPAQYIRYT PSQQGVAFNS GAKQRVIRMV EMQKDPMEPP RFKINKKIPR GPPSPPAPVM HSPSRKMTVK EQQEWKIPPC ISNWKNAKGY TIPLDKRLAA DGRGLQTVHI NENFAKLAEA LYIADRKARE AVEMRAQVER KMAQKEKEKH EEKLREMAQK ARERRAGIKT HVEKEDGEAR ERDEIRHDRR KERQHDRNLS RAAPDKRSKL QRNENRDISE VIALGVPNPR TSNEVQYDQR LFNQSKGMDS GFAGGEDEIY NVYDQAWRGG KDMAQSIYRP SKNLDKDMYG DDLEARIKTN RFVPDKEFSG SDRRQRGREG PVQFEEDPFG LDKFLEEAKQ HGGSKRPSDS SRPKEHEHEG KKRRKE //