SNW1_HUMAN
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 03-AUG-2022, entry version 206.
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).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome
CC (PubMed:11991638, PubMed:28502770, PubMed:28076346). Is required in the
CC specific splicing of CDKN1A pre-mRNA; the function probably involves
CC the recruitment of U2AF2 to the mRNA. Is proposed to recruit PPIL1 to
CC the spliceosome. May be involved in cyclin-D1/CCND1 mRNA stability
CC through the SNARP complex which associates with both the 3'end of the
CC CCND1 gene and its mRNA. Involved in transcriptional regulation.
CC Modulates TGF-beta-mediated transcription via association with SMAD
CC proteins, MYOD1-mediated transcription via association with PABPN1,
CC RB1-mediated transcriptional repression, and retinoid-X receptor
CC (RXR)- and vitamin D receptor (VDR)-dependent gene transcription in a
CC cell line-specific manner probably involving coactivators NCOA1 and
CC GRIP1. Is involved in NOTCH1-mediated transcriptional activation. Binds
CC to multimerized forms of Notch intracellular domain (NICD) and is
CC proposed to recruit transcriptional coactivators such as MAML1 to form
CC an intermediate preactivation complex which associates with DNA-bound
CC CBF-1/RBPJ to form a transcriptional activation complex by releasing
CC SNW1 and redundant NOTCH1 NICD. {ECO:0000269|PubMed:10644367,
CC ECO:0000269|PubMed:11278756, ECO:0000269|PubMed:11371506,
CC ECO:0000269|PubMed:11514567, ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:12840015, ECO:0000269|PubMed:14985122,
CC ECO:0000269|PubMed:15194481, ECO:0000269|PubMed:15905409,
CC ECO:0000269|PubMed:18794151, ECO:0000269|PubMed:19818711,
CC ECO:0000269|PubMed:21245387, ECO:0000269|PubMed:21460037,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:9632709}.
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). Interacts with SKI,
CC SMAD2,SMAD3, RBPJ, RB1, PABPN1, MAGEA1, SIRT1, FOXN3, U2AF2, DAXX and
CC ATP1B4. Interacts with PPIL1 (PubMed:16595688, PubMed:20007319,
CC PubMed:20368803, PubMed:33220177). Interacts with VDR and RXRA;
CC preferentially associates with VDR:RXRA heterodimers (PubMed:9632709,
CC PubMed:12529369). Interacts with NCOR2 (PubMed:10644367). Interacts
CC with MAML1 (PubMed:21245387). Interacts with NOTCH1 NICD; the
CC interaction involves multimerized NOTCH1 NICD (PubMed:21245387). Forms
CC a complex with NOTCH1 NICD and MAML1; the association is dissociated by
CC RBPJ (PubMed:21245387). Associates with positive transcription
CC elongation factor b (P-TEFb) (PubMed:15905409). Component of the SNARP
CC complex which consists at least of SNIP1, SNW1, THRAP3, BCLAF1 and PNN
CC (PubMed:18794151). {ECO:0000250|UniProtKB:Q9CSN1,
CC ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:10713164,
CC ECO:0000269|PubMed:11278756, ECO:0000269|PubMed:11371506,
CC ECO:0000269|PubMed:11514567, ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:12466551, ECO:0000269|PubMed:12529369,
CC ECO:0000269|PubMed:12840015, ECO:0000269|PubMed:15194481,
CC ECO:0000269|PubMed:15316101, ECO:0000269|PubMed:15905409,
CC ECO:0000269|PubMed:16102918, ECO:0000269|PubMed:16595688,
CC ECO:0000269|PubMed:18794151, ECO:0000269|PubMed:19818711,
CC ECO:0000269|PubMed:20007319, ECO:0000269|PubMed:20368803,
CC ECO:0000269|PubMed:21245387, ECO:0000269|PubMed:21460037,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:33220177, 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; 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; 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}.
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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 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 AlphaFoldDB; Q13573; -.
DR SMR; Q13573; -.
DR BioGRID; 116597; 703.
DR CORUM; Q13573; -.
DR DIP; DIP-34800N; -.
DR IntAct; Q13573; 709.
DR MINT; Q13573; -.
DR STRING; 9606.ENSP00000261531; -.
DR GlyGen; Q13573; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13573; -.
DR MetOSite; Q13573; -.
DR PhosphoSitePlus; Q13573; -.
DR BioMuta; SNW1; -.
DR DMDM; 2500813; -.
DR EPD; Q13573; -.
DR jPOST; Q13573; -.
DR MassIVE; Q13573; -.
DR MaxQB; Q13573; -.
DR PaxDb; Q13573; -.
DR PeptideAtlas; Q13573; -.
DR PRIDE; Q13573; -.
DR ProteomicsDB; 59577; -.
DR TopDownProteomics; Q13573; -.
DR Antibodypedia; 71; 137 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 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; WRDSNTL; -.
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 SABIO-RK; Q13573; -.
DR SignaLink; Q13573; -.
DR SIGNOR; Q13573; -.
DR BioGRID-ORCS; 22938; 772 hits in 1088 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 217 other tissues.
DR ExpressionAtlas; Q13573; baseline and differential.
DR Genevisible; Q13573; HS.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP: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; PTHR12096; 1.
DR Pfam; PF02731; SKIP_SNW; 1.
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 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
