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SNW domain-containing protein 1 (Nuclear protein SkiP) (Nuclear receptor coactivator NCoA-62) (Ski-interacting protein)

 SNW1_HUMAN              Reviewed;         536 AA.
Q13573; A8K8A9; Q13483; Q32N03; Q5D0D6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-MAR-2018, entry version 176.
RecName: Full=SNW domain-containing protein 1;
AltName: Full=Nuclear protein SkiP;
AltName: Full=Nuclear receptor coactivator NCoA-62 {ECO:0000303|PubMed:9632709};
AltName: Full=Ski-interacting protein {ECO:0000303|PubMed:11278756, ECO:0000303|PubMed:9569025};
Name=SNW1;
Synonyms=SKIIP, SKIP {ECO:0000303|PubMed:10713164,
ECO:0000303|PubMed:11371506};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH VDR.
PubMed=9632709; DOI=10.1074/jbc.273.26.16434;
Baudino T.A., Kraichely D.M., Jefcoat S.C. Jr., Winchester S.K.,
Partridge N.C., Macdonald P.N.;
"Isolation and characterization of a novel coactivator protein, NCoA-
62, involved in vitamin D-mediated transcription.";
J. Biol. Chem. 273:16434-16441(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
PubMed=9569025; DOI=10.1038/sj.onc.1201687;
Dahl R., Wani B., Hayman M.J.;
"The Ski oncoprotein interacts with Skip, the human homolog of
Drosophila Bx42.";
Oncogene 16:1579-1586(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-23; 82-95; 179-193 AND 401-410, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Dozynkiewicz M., Norman J.C.;
Submitted (JUN-2009) to UniProtKB.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 282-536.
PubMed=8973337; DOI=10.1016/S0378-1119(96)00483-0;
Folk P., Puta F., Krpejsova L., Blahuskova A., Markos A., Rabino M.,
Dottin R.P.;
"The homolog of chromatin binding protein Bx42 identified in
Dictyostelium.";
Gene 181:229-231(1996).
[10]
FUNCTION, AND INTERACTION WITH RBPJ; CIR1; HDAC2 AND EPSTEIN-BARR
VIRUS EBNA2 PROTEIN.
PubMed=10644367; DOI=10.1128/JVI.74.4.1939-1947.2000;
Zhou S., Fujimuro M., Hsieh J.J., Chen L., Hayward S.D.;
"A role for SKIP in EBNA2 activation of CBF1-repressed promoters.";
J. Virol. 74:1939-1947(2000).
[11]
INTERACTION WITH NOTCH1.
PubMed=10713164; DOI=10.1128/MCB.20.7.2400-2410.2000;
Zhou S., Fujimuro M., Hsieh J.J., Chen L., Miyamoto A., Weinmaster G.,
Hayward S.D.;
"SKIP, a CBF1-associated protein, interacts with the ankyrin repeat
domain of NotchIC To facilitate NotchIC function.";
Mol. Cell. Biol. 20:2400-2410(2000).
[12]
FUNCTION, AND INTERACTION WITH PABPN1.
PubMed=11371506; DOI=10.1093/hmg/10.11.1129;
Kim Y.-J., Noguchi S., Hayashi Y.K., Tsukahara T., Shimizu T.,
Arahata K.;
"The product of an oculopharyngeal muscular dystrophy gene, poly(A)-
binding protein 2, interacts with SKIP and stimulates muscle-specific
gene expression.";
Hum. Mol. Genet. 10:1129-1139(2001).
[13]
FUNCTION, AND INTERACTION WITH SMAD2 AND SMAD3.
PubMed=11278756; DOI=10.1074/jbc.M010815200;
Leong G.M., Subramaniam N., Figueroa J., Flanagan J.L., Hayman M.J.,
Eisman J.A., Kouzmenko A.P.;
"Ski-interacting protein interacts with Smad proteins to augment
transforming growth factor-beta-dependent transcription.";
J. Biol. Chem. 276:18243-18248(2001).
[14]
FUNCTION, AND SUBUNIT.
PubMed=11514567; DOI=10.1074/jbc.M106263200;
Zhang C., Baudino T.A., Dowd D.R., Tokumaru H., Wang W.,
MacDonald P.N.;
"Ternary complexes and cooperative interplay between NCoA-62/Ski-
interacting protein and steroid receptor coactivators in vitamin D
receptor-mediated transcription.";
J. Biol. Chem. 276:40614-40620(2001).
[15]
INTERACTION WITH HPV16 PROTEIN E7.
PubMed=11753645; DOI=10.1038/sj.onc.1204960;
Prathapam T., Kuhne C., Banks L.;
"The HPV-16 E7 oncoprotein binds Skip and suppresses its
transcriptional activity.";
Oncogene 20:7677-7685(2001).
[16]
INTERACTION WITH RB1.
PubMed=12466551; DOI=10.1093/nar/gkf658;
Prathapam T., Kuhne C., Banks L.;
"Skip interacts with the retinoblastoma tumor suppressor and inhibits
its transcriptional repression activity.";
Nucleic Acids Res. 30:5261-5268(2002).
[17]
IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
SPLICEOSOMAL C COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=11991638; DOI=10.1017/S1355838202021088;
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
"Purification and characterization of native spliceosomes suitable for
three-dimensional structural analysis.";
RNA 8:426-439(2002).
[18]
INTERACTION WITH VDR.
PubMed=12529369; DOI=10.1074/jbc.C200712200;
Barry J.B., Leong G.M., Church W.B., Issa L.L., Eisman J.A.,
Gardiner E.M.;
"Interactions of SKIP/NCoA-62, TFIIB, and retinoid X receptor with
vitamin D receptor helix H10 residues.";
J. Biol. Chem. 278:8224-8228(2003).
[19]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=12840015; DOI=10.1074/jbc.M305191200;
Zhang C., Dowd D.R., Staal A., Gu C., Lian J.B., van Wijnen A.J.,
Stein G.S., MacDonald P.N.;
"Nuclear coactivator-62 kDa/Ski-interacting protein is a nuclear
matrix-associated coactivator that may couple vitamin D receptor-
mediated transcription and RNA splicing.";
J. Biol. Chem. 278:35325-35336(2003).
[20]
FUNCTION.
PubMed=14985122; DOI=10.1016/j.bbrc.2004.02.004;
Leong G.M., Subramaniam N., Issa L.L., Barry J.B., Kino T.,
Driggers P.H., Hayman M.J., Eisman J.A., Gardiner E.M.;
"Ski-interacting protein, a bifunctional nuclear receptor coregulator
that interacts with N-CoR/SMRT and p300.";
Biochem. Biophys. Res. Commun. 315:1070-1076(2004).
[21]
INTERACTION WITH MAGEA1.
PubMed=15316101; DOI=10.1093/nar/gkh735;
Laduron S., Deplus R., Zhou S., Kholmanskikh O., Godelaine D.,
De Smet C., Hayward S.D., Fuks F., Boon T., De Plaen E.;
"MAGE-A1 interacts with adaptor SKIP and the deacetylase HDAC1 to
repress transcription.";
Nucleic Acids Res. 32:4340-4350(2004).
[22]
FUNCTION, AND SUBUNIT.
PubMed=15194481; DOI=10.1016/j.bbrc.2004.05.096;
Figueroa J.D., Hayman M.J.;
"The human Ski-interacting protein functionally substitutes for the
yeast PRP45 gene.";
Biochem. Biophys. Res. Commun. 319:1105-1109(2004).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[24]
INTERACTION WITH PPIL1.
PubMed=16595688; DOI=10.1074/jbc.M511155200;
Xu C., Zhang J., Huang X., Sun J., Xu Y., Tang Y., Wu J., Shi Y.,
Huang Q., Zhang Q.;
"Solution structure of human peptidyl prolyl isomerase-like protein 1
and insights into its interaction with SKIP.";
J. Biol. Chem. 281:15900-15908(2006).
[25]
INTERACTION WITH FOXN3.
PubMed=16102918; DOI=10.1016/j.gene.2005.06.014;
Scott K.L., Plon S.E.;
"CHES1/FOXN3 interacts with Ski-interacting protein and acts as a
transcriptional repressor.";
Gene 359:119-126(2005).
[26]
FUNCTION, AND SUBUNIT.
PubMed=15905409; DOI=10.1101/gad.1291705;
Bres V., Gomes N., Pickle L., Jones K.A.;
"A human splicing factor, SKIP, associates with P-TEFb and enhances
transcription elongation by HIV-1 Tat.";
Genes Dev. 19:1211-1226(2005).
[27]
FUNCTION, AND IDENTIFICATION IN THE SNARP COMPLEX.
PubMed=18794151; DOI=10.1158/0008-5472.CAN-08-1217;
Bracken C.P., Wall S.J., Barre B., Panov K.I., Ajuh P.M.,
Perkins N.D.;
"Regulation of cyclin D1 RNA stability by SNIP1.";
Cancer Res. 68:7621-7628(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-232, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[29]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[30]
FUNCTION, AND SUBUNIT.
PubMed=19818711; DOI=10.1016/j.molcel.2009.08.015;
Bres V., Yoshida T., Pickle L., Jones K.A.;
"SKIP interacts with c-Myc and Menin to promote HIV-1 Tat
transactivation.";
Mol. Cell 36:75-87(2009).
[31]
INTERACTION WITH PPIL, AND MUTAGENESIS OF GLU-66 AND MET-76.
PubMed=20007319; DOI=10.1074/jbc.M109.087528;
Wang X., Zhang S., Zhang J., Huang X., Xu C., Wang W., Liu Z., Wu J.,
Shi Y.;
"A large intrinsically disordered region in SKIP and its disorder-
order transition induced by PPIL1 binding revealed by NMR.";
J. Biol. Chem. 285:4951-4963(2010).
[32]
INTERACTION WITH PPIL.
PubMed=20368803; DOI=10.1371/journal.pone.0010013;
Stegmann C.M., Luhrmann R., Wahl M.C.;
"The crystal structure of PPIL1 bound to cyclosporine A suggests a
binding mode for a linear epitope of the SKIP protein.";
PLoS ONE 5:E10013-E10013(2010).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-232 AND
SER-234, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[35]
FUNCTION, AND INTERACTION WITH U2AF2.
PubMed=21460037; DOI=10.1101/gad.2002611;
Chen Y., Zhang L., Jones K.A.;
"SKIP counteracts p53-mediated apoptosis via selective regulation of
p21Cip1 mRNA splicing.";
Genes Dev. 25:701-716(2011).
[36]
FUNCTION, AND INTERACTION WITH NOTCH1 AND MAML1.
PubMed=21245387; DOI=10.1128/MCB.00360-10;
Vasquez-Del Carpio R., Kaplan F.M., Weaver K.L., VanWye J.D.,
Alves-Guerra M.C., Robbins D.J., Capobianco A.J.;
"Assembly of a Notch transcriptional activation complex requires
multimerization.";
Mol. Cell. Biol. 31:1396-1408(2011).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-234, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[38]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[39]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[40]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-182; SER-190;
SER-224; SER-232; SER-446; SER-479 AND SER-481, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-232, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-170; LYS-193 AND
LYS-240, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[43]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-97; LYS-170; LYS-193;
LYS-240 AND LYS-509, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[44]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-23; LYS-81; LYS-115;
LYS-122; LYS-141; LYS-158; LYS-170; LYS-193; LYS-240; LYS-258;
LYS-286; LYS-339; LYS-344; LYS-416; LYS-441; LYS-452 AND LYS-509, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[45] {ECO:0000244|PDB:5XJC}
STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT,
AND SUBCELLULAR LOCATION.
PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
"An Atomic Structure of the Human Spliceosome.";
Cell 169:918-929(2017).
[46] {ECO:0000244|PDB:5MQF}
STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=28076346; DOI=10.1038/nature21079;
Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L.,
Hartmuth K., Urlaub H., Kastner B., Stark H., Luhrmann R.;
"Cryo-EM structure of a human spliceosome activated for step 2 of
splicing.";
Nature 542:318-323(2017).
-!- FUNCTION: Involved in pre-mRNA splicing as component of the
spliceosome (PubMed:11991638, PubMed:28502770, PubMed:28076346).
Is required in the specific splicing of CDKN1A pre-mRNA; the
function probably involves the recruitment of U2AF2 to the mRNA.
Is proposed to recruit PPIL1 to the spliceosome. May be involved
in cyclin-D1/CCND1 mRNA stability through the SNARP complex which
associates with both the 3'end of the CCND1 gene and its mRNA.
Involved in transcriptional regulation. Modulates TGF-beta-
mediated transcription via association with SMAD proteins, MYOD1-
mediated transcription via association with PABPN1, RB1-mediated
transcriptional repression, and retinoid-X receptor (RXR)- and
vitamin D receptor (VDR)-dependent gene transcription in a cell
line-specific manner probably involving coactivators NCOA1 and
GRIP1. Is involved in NOTCH1-mediated transcriptional activation.
Binds to multimerized forms of Notch intracellular domain (NICD)
and is proposed to recruit transcriptional coactivators such as
MAML1 to form an intermediate preactivation complex which
associates with DNA-bound CBF-1/RBPJ to form a transcriptional
activation complex by releasing SNW1 and redundant NOTCH1 NICD.
{ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:11278756,
ECO:0000269|PubMed:11371506, ECO:0000269|PubMed:11514567,
ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12840015,
ECO:0000269|PubMed:14985122, ECO:0000269|PubMed:15194481,
ECO:0000269|PubMed:15905409, ECO:0000269|PubMed:18794151,
ECO:0000269|PubMed:19818711, ECO:0000269|PubMed:21245387,
ECO:0000269|PubMed:21460037, ECO:0000269|PubMed:28076346,
ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:9632709}.
-!- FUNCTION: (Microbial infection) Is recruited by HIV-1 Tat to
Tat:P-TEFb:TAR RNA complexes and is involved in Tat transcription
by recruitment of MYC, MEN1 and TRRAP to the HIV promoter.
{ECO:0000269|PubMed:15905409, ECO:0000269|PubMed:19818711}.
-!- FUNCTION: (Microbial infection) Proposed to be involved in
transcriptional activation by EBV EBNA2 of CBF-1/RBPJ-repressed
promoters. {ECO:0000269|PubMed:10644367}.
-!- SUBUNIT: Identified in the spliceosome C complex (PubMed:11991638,
PubMed:28502770, PubMed:28076346). Associates with U4/U6-U5 tri-
small nuclear ribonucleoproteins (U4/U6-U5 tri-snRNPs). Interacts
SKI, SMAD2,SMAD3, RBPJ, RB1, PABPN1, MAGEA1, SIRT1, FOXN3, U2AF2,
PPIL1, DAXX and ATP1B4. Interacts with VDR and RXRA;
preferentially associates with VDR:RXRA heterodimers
(PubMed:9632709, PubMed:12529369). Interacts with NCOR2
(PubMed:10644367). Interacts with MAML1 (PubMed:21245387).
Interacts with NOTCH1 NICD; the interaction involves multimerized
NOTCH1 NICD (PubMed:21245387). Forms a complex with NOTCH1 NICD
and MAML1; the association is dissociated by RBPJ
(PubMed:21245387). Associates with positive transcription
elongation factor b (P-TEFb) (PubMed:15905409). Component of the
SNARP complex which consists at least of SNIP1, SNW1, THRAP3,
BCLAF1 and PNN (PubMed:18794151). {ECO:0000250|UniProtKB:Q9CSN1,
ECO:0000269|PubMed:10644367, ECO:0000269|PubMed:10713164,
ECO:0000269|PubMed:11278756, ECO:0000269|PubMed:11371506,
ECO:0000269|PubMed:11514567, ECO:0000269|PubMed:11991638,
ECO:0000269|PubMed:12466551, ECO:0000269|PubMed:12529369,
ECO:0000269|PubMed:12840015, ECO:0000269|PubMed:15194481,
ECO:0000269|PubMed:15316101, ECO:0000269|PubMed:15905409,
ECO:0000269|PubMed:16102918, ECO:0000269|PubMed:16595688,
ECO:0000269|PubMed:18794151, ECO:0000269|PubMed:19818711,
ECO:0000269|PubMed:20007319, ECO:0000269|PubMed:20368803,
ECO:0000269|PubMed:21245387, ECO:0000269|PubMed:21460037,
ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
ECO:0000269|PubMed:9569025, ECO:0000269|PubMed:9632709}.
-!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus
type-16 (HPV16) E7 protein. {ECO:0000269|PubMed:11753645}.
-!- SUBUNIT: (Microbial infection) Interacts with EBV EBNA2; EBNA2
competes with NCOR2 for interaction with SNW1.
{ECO:0000269|PubMed:10644367}.
-!- INTERACTION:
Q53EZ4:CEP55; NbExp=3; IntAct=EBI-632715, EBI-747776;
Q8WYA6:CTNNBL1; NbExp=2; IntAct=EBI-632715, EBI-748128;
O00409:FOXN3; NbExp=3; IntAct=EBI-632715, EBI-372721;
Q08379:GOLGA2; NbExp=5; IntAct=EBI-632715, EBI-618309;
P04792:HSPB1; NbExp=3; IntAct=EBI-632715, EBI-352682;
Q13422:IKZF1; NbExp=3; IntAct=EBI-632715, EBI-745305;
Q6A162:KRT40; NbExp=3; IntAct=EBI-632715, EBI-10171697;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-632715, EBI-741037;
P43355:MAGEA1; NbExp=3; IntAct=EBI-632715, EBI-740978;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-632715, EBI-742948;
Q60974:Ncor1 (xeno); NbExp=3; IntAct=EBI-632715, EBI-349004;
Q9Y618:NCOR2; NbExp=4; IntAct=EBI-632715, EBI-80830;
P46531:NOTCH1; NbExp=3; IntAct=EBI-632715, EBI-636374;
Q86U42:PABPN1; NbExp=5; IntAct=EBI-632715, EBI-1226435;
Q9Y3C6:PPIL1; NbExp=11; IntAct=EBI-632715, EBI-2557649;
Q06330:RBPJ; NbExp=2; IntAct=EBI-632715, EBI-632552;
Q6NUQ1:RINT1; NbExp=7; IntAct=EBI-632715, EBI-726876;
O43290:SART1; NbExp=3; IntAct=EBI-632715, EBI-607761;
Q96EB6:SIRT1; NbExp=7; IntAct=EBI-632715, EBI-1802965;
P49140:SKI (xeno); NbExp=4; IntAct=EBI-632715, EBI-6392357;
Q15796:SMAD2; NbExp=3; IntAct=EBI-632715, EBI-1040141;
P84022:SMAD3; NbExp=5; IntAct=EBI-632715, EBI-347161;
Q8TAD8:SNIP1; NbExp=7; IntAct=EBI-632715, EBI-749336;
Q8IYF3:TEX11; NbExp=3; IntAct=EBI-632715, EBI-742397;
Q9UBB9:TFIP11; NbExp=5; IntAct=EBI-632715, EBI-1105213;
Q9Y2W1:THRAP3; NbExp=4; IntAct=EBI-632715, EBI-352039;
Q13077:TRAF1; NbExp=3; IntAct=EBI-632715, EBI-359224;
P26368:U2AF2; NbExp=5; IntAct=EBI-632715, EBI-742339;
P17863:V-SKI (xeno); NbExp=4; IntAct=EBI-632715, EBI-6392320;
P11473:VDR; NbExp=5; IntAct=EBI-632715, EBI-286357;
P48281:Vdr (xeno); NbExp=2; IntAct=EBI-632715, EBI-346797;
Q9HCS7:XAB2; NbExp=2; IntAct=EBI-632715, EBI-295232;
Q96NB3:ZNF830; NbExp=2; IntAct=EBI-632715, EBI-3920997;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11991638,
ECO:0000269|PubMed:12840015, ECO:0000269|PubMed:28076346,
ECO:0000269|PubMed:28502770}.
-!- SIMILARITY: Belongs to the SNW family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF045184; AAC31697.1; -; mRNA.
EMBL; U51432; AAC15912.1; -; mRNA.
EMBL; BT020060; AAV38863.1; -; mRNA.
EMBL; BT020061; AAV38864.1; -; mRNA.
EMBL; AK292274; BAF84963.1; -; mRNA.
EMBL; AC008372; AAF23325.1; -; Genomic_DNA.
EMBL; CH471061; EAW81308.1; -; Genomic_DNA.
EMBL; BC040112; AAH40112.1; -; mRNA.
EMBL; BC046105; AAH46105.2; -; mRNA.
EMBL; BC108903; AAI08904.1; -; mRNA.
EMBL; U43960; AAB48857.1; -; Genomic_DNA.
CCDS; CCDS9867.1; -.
RefSeq; NP_036377.1; NM_012245.2.
UniGene; Hs.445498; -.
PDB; 5MQF; EM; 5.90 A; C=1-536.
PDB; 5XJC; EM; 3.60 A; R=1-536.
PDBsum; 5MQF; -.
PDBsum; 5XJC; -.
DisProt; DP00608; -.
ProteinModelPortal; Q13573; -.
SMR; Q13573; -.
BioGrid; 116597; 566.
CORUM; Q13573; -.
DIP; DIP-34800N; -.
IntAct; Q13573; 616.
MINT; Q13573; -.
STRING; 9606.ENSP00000261531; -.
iPTMnet; Q13573; -.
PhosphoSitePlus; Q13573; -.
BioMuta; SNW1; -.
DMDM; 2500813; -.
EPD; Q13573; -.
MaxQB; Q13573; -.
PaxDb; Q13573; -.
PeptideAtlas; Q13573; -.
PRIDE; Q13573; -.
TopDownProteomics; Q13573; -.
DNASU; 22938; -.
Ensembl; ENST00000261531; ENSP00000261531; ENSG00000100603.
GeneID; 22938; -.
KEGG; hsa:22938; -.
UCSC; uc001xuf.4; human.
CTD; 22938; -.
DisGeNET; 22938; -.
EuPathDB; HostDB:ENSG00000100603.13; -.
GeneCards; SNW1; -.
HGNC; HGNC:16696; SNW1.
HPA; CAB009931; -.
HPA; HPA002457; -.
HPA; HPA017370; -.
MIM; 603055; gene.
neXtProt; NX_Q13573; -.
OpenTargets; ENSG00000100603; -.
PharmGKB; PA134883977; -.
eggNOG; KOG2441; Eukaryota.
eggNOG; ENOG410XQGT; LUCA.
GeneTree; ENSGT00390000010423; -.
HOGENOM; HOG000160386; -.
HOVERGEN; HBG047516; -.
InParanoid; Q13573; -.
KO; K06063; -.
PhylomeDB; Q13573; -.
TreeFam; TF300782; -.
Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-350054; Notch-HLH transcription pathway.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
SignaLink; Q13573; -.
SIGNOR; Q13573; -.
ChiTaRS; SNW1; human.
GeneWiki; SNW1; -.
GenomeRNAi; 22938; -.
PRO; PR:Q13573; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100603; -.
CleanEx; HS_SNW1; -.
ExpressionAtlas; Q13573; baseline and differential.
Genevisible; Q13573; HS.
GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:CAFA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0071014; C:post-mRNA release spliceosomal complex; IBA:GO_Central.
GO; GO:0005681; C:spliceosomal complex; IDA:UniProtKB.
GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
GO; GO:0050681; F:androgen receptor binding; IPI:CAFA.
GO; GO:0019899; F:enzyme binding; IPI:CAFA.
GO; GO:0005112; F:Notch binding; IPI:UniProtKB.
GO; GO:0035257; F:nuclear hormone receptor binding; IDA:UniProtKB.
GO; GO:0042974; F:retinoic acid receptor binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0046332; F:SMAD binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0042809; F:vitamin D receptor binding; IDA:UniProtKB.
GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
GO; GO:0000350; P:generation of catalytic spliceosome for second transesterification step; IBA:GO_Central.
GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:UniProtKB.
GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
GO; GO:0048026; P:positive regulation of mRNA splicing, via spliceosome; IMP:UniProtKB.
GO; GO:0050769; P:positive regulation of neurogenesis; ISS:UniProtKB.
GO; GO:0045747; P:positive regulation of Notch signaling pathway; TAS:Reactome.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; TAS:Reactome.
GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
GO; GO:0070564; P:positive regulation of vitamin D receptor signaling pathway; IDA:UniProtKB.
GO; GO:0048385; P:regulation of retinoic acid receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IDA:UniProtKB.
GO; GO:0048384; P:retinoic acid receptor signaling pathway; IDA:UniProtKB.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR017862; SKI-int_prot_SKIP.
InterPro; IPR004015; SKI-int_prot_SKIP_SNW-dom.
PANTHER; PTHR12096; PTHR12096; 1.
Pfam; PF02731; SKIP_SNW; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome;
Direct protein sequencing; Host-virus interaction; Isopeptide bond;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Reference proteome; Spliceosome; Transcription;
Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
CHAIN 2 536 SNW domain-containing protein 1.
/FTId=PRO_0000084827.
REGION 59 79 Interaction with PPIL1.
{ECO:0000269|PubMed:16595688}.
REGION 174 339 SNW.
COMPBIAS 219 233 Pro-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.8}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 234 234 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 446 446 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 479 479 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 481 481 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 23 23 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 81 81 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 97 97 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364}.
CROSSLNK 115 115 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 141 141 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 158 158 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 170 170 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 193 193 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 240 240 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 258 258 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 286 286 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 339 339 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 344 344 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 416 416 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 441 441 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 452 452 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 509 509 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
MUTAGEN 66 66 E->A,R: Abolishes interaction with PPIL1.
{ECO:0000269|PubMed:20007319}.
MUTAGEN 76 76 M->A: Abolishes interaction with PPIL1.
{ECO:0000269|PubMed:20007319}.
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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EIAAB39055 Mouse,Mus musculus,Nuclear protein SkiP,Ski-interacting protein,Skiip,SNW domain-containing protein 1,Snw1
EIAAB39056 Bos taurus,Bovine,Nuclear protein SkiP,Ski-interacting protein,SKIIP,SNW domain-containing protein 1,SNW1
EIAAB26564 Aib1,AIB-1,Amplified in breast cancer-1 protein homolog,Ncoa3,NCoA-3,Nuclear receptor coactivator 3,Rat,Rattus norvegicus
EIAAB05063 Antigen nuclear dot 52 kDa protein,Calcium-binding and coiled-coil domain-containing protein 2,CALCOCO2,Homo sapiens,Human,NDP52,Nuclear domain 10 protein 52,Nuclear domain 10 protein NDP52,Nuclear do
EIAAB42191 Ncoa6ip,Nuclear receptor coactivator 6-interacting protein,PIMT,Pimt,PIPMT,PRIP-interacting protein with methyltransferase motif,Rat,Rattus norvegicus,Tgs1,Trimethylguanosine synthase
EIAAB42192 Mouse,Mus musculus,Ncoa6ip,Nuclear receptor coactivator 6-interacting protein,PIMT,Pimt,PIPMT,PRIP-interacting protein with methyltransferase motif,Tgs1,Trimethylguanosine synthase
EIAAB26567 CIA,Coactivator independent of AF-2,Mouse,Mus musculus,Ncoa5,NCoA-5,Nuclear receptor coactivator 5
EIAAB26558 bHLHe74,BHLHE74,Class E basic helix-loop-helix protein 74,Homo sapiens,Human,NCOA1,NCoA-1,Nuclear receptor coactivator 1,Protein Hin-2,Renal carcinoma antigen NY-REN-52,RIP160,SRC1,SRC-1,Steroid recep
EIAAB26574 140 kDa estrogen receptor-associated protein,ERAP140,ESNA1,Estrogen nuclear receptor coactivator 1,Homo sapiens,Human,Nbla00052,Nbla10993,NCOA7,Nuclear receptor coactivator 7
EIAAB27868 Homo sapiens,Human,NRIP1,Nuclear factor RIP140,Nuclear receptor-interacting protein 1,Receptor-interacting protein 140
EIAAB26568 CIA,Coactivator independent of AF-2,Homo sapiens,Human,KIAA1637,NCOA5,NCoA-5,Nuclear receptor coactivator 5
EIAAB26559 NCOA1,NCoA-1,Nuclear receptor coactivator 1,Pig,SRC1,SRC-1,Steroid receptor coactivator 1,Sus scrofa
EIAAB27869 Mouse,Mus musculus,Nrip1,Nuclear factor RIP140,Nuclear receptor-interacting protein 1,Receptor-interacting protein 140
ABP-PAB-10254 Nuclear receptor coactivator 6 interacting protein (NCOA6IP, PIMT) polyclonal antibody 100 ug
LF-PA41075 anti-Nuclear Protein Skip (SNW1) , Rabbit polyclonal to Nuclear Protein Skip (SNW1) , Isotype IgG, Host Rabbit 50 ug
EIAAB26570 Activating signal cointegrator 2,Aib3,Amplified in breast cancer protein 3,ASC-2,Cancer-amplified transcriptional coactivator ASC-2,Ncoa6,NRC,Nuclear receptor coactivator 6,Nuclear receptor coactivato
EIAAB26571 Activating signal cointegrator 2,Aib3,Amplified in breast cancer protein 3,ASC-2,Cancer-amplified transcriptional coactivator ASC-2,Mouse,Mus musculus,Ncoa6,NRC,Nuclear receptor coactivator 6,Nuclear


 

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