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Database: UniProt
Entry: Q13573
LinkDB: Q13573
Original site: Q13573 
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   29-SEP-2021, entry version 203.
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 PPIL, 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 PPIL.
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] {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   [46] {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 SKI,
CC       SMAD2,SMAD3, RBPJ, RB1, PABPN1, MAGEA1, SIRT1, FOXN3, U2AF2, PPIL1,
CC       DAXX and ATP1B4. Interacts with VDR and RXRA; preferentially associates
CC       with VDR:RXRA heterodimers (PubMed:9632709, PubMed:12529369). Interacts
CC       with NCOR2 (PubMed:10644367). Interacts with MAML1 (PubMed:21245387).
CC       Interacts with NOTCH1 NICD; the interaction involves multimerized
CC       NOTCH1 NICD (PubMed:21245387). Forms a complex with NOTCH1 NICD and
CC       MAML1; the association is dissociated by RBPJ (PubMed:21245387).
CC       Associates with positive transcription elongation factor b (P-TEFb)
CC       (PubMed:15905409). Component of the SNARP complex which consists at
CC       least of SNIP1, SNW1, 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: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   SMR; Q13573; -.
DR   BioGRID; 116597; 636.
DR   CORUM; Q13573; -.
DR   DIP; DIP-34800N; -.
DR   IntAct; Q13573; 702.
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; 126 antibodies.
DR   DNASU; 22938; -.
DR   Ensembl; ENST00000261531; ENSP00000261531; ENSG00000100603.
DR   GeneID; 22938; -.
DR   KEGG; hsa:22938; -.
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-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
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; 767 hits in 1026 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 female gonad and 256 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:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
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:0071141; C:SMAD protein complex; IEA:Ensembl.
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:0050681; F:androgen receptor binding; IPI:CAFA.
DR   GO; GO:0019899; F:enzyme binding; IPI:CAFA.
DR   GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
DR   GO; GO:0016922; F:nuclear receptor binding; IDA:UniProtKB.
DR   GO; GO:0042974; F:retinoic acid 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:0042809; F:vitamin D receptor binding; 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   GO; GO:0014010; P:Schwann cell proliferation; IEA:Ensembl.
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"
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
//
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