U520_HUMAN
ID U520_HUMAN Reviewed; 2136 AA.
AC O75643; O94884; Q6NZY0; Q6PX59; Q8NBE6; Q96IF2; Q9H7S0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=U5 small nuclear ribonucleoprotein 200 kDa helicase;
DE EC=3.6.4.13 {ECO:0000269|PubMed:23045696};
DE AltName: Full=Activating signal cointegrator 1 complex subunit 3-like 1;
DE AltName: Full=BRR2 homolog;
DE AltName: Full=U5 snRNP-specific 200 kDa protein;
DE Short=U5-200KD;
GN Name=SNRNP200; Synonyms=ASCC3L1, HELIC2, KIAA0788;
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] (ISOFORM 1), FUNCTION, SUBUNIT, AND VARIANT RP33
RP LEU-1087.
RX PubMed=16723661; DOI=10.1261/rna.55406;
RA Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.;
RT "The network of protein-protein interactions within the human U4/U6.U5 tri-
RT snRNP.";
RL RNA 12:1418-1430(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 264-2136 (ISOFORM 1).
RC TISSUE=Cerebellum, and Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-2136 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 436-2136, PROTEIN SEQUENCE OF 672-690;
RP 1200-1213; 1295-1317; 1326-1338 AND 1717-1728, FUNCTION, AND SUBUNIT.
RC TISSUE=Fetal brain;
RX PubMed=8670905; DOI=10.1002/j.1460-2075.1996.tb00774.x;
RA Lauber J., Fabrizio P., Teigelkamp S., Lane W.S., Hartmann E.,
RA Luehrmann R.;
RT "The HeLa 200 kDa U5 snRNP-specific protein and its homologue in
RT Saccharomyces cerevisiae are members of the DEXH-box protein family of
RT putative RNA helicases.";
RL EMBO J. 15:4001-4015(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 316-2136.
RC TISSUE=Placenta, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9539711; DOI=10.1073/pnas.95.8.4188;
RA Laggerbauer B., Achsel T., Luehrmann R.;
RT "The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4188-4192(1998).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; THR-2131; SER-2133 AND
RP SER-2135, AND 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2131; SER-2133 AND SER-2135,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-971, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-225, 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 [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-26; SER-225; THR-389;
RP THR-1428 AND SER-2002, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-225, 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 [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-46, 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 [23]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1808-2136.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of Q9P172/SEC63 from Homo sapiens.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF 402-2125 IN COMPLEX WITH ATP,
RP CATALYTIC ACTIVITY, FUNCTION, DOMAIN, CHARACTERIZATION OF VARIANT RP33
RP LEU-1087, AND MUTAGENESIS OF ARG-603; ARG-637; LYS-1544; HIS-1548 AND
RP THR-1578.
RX PubMed=23045696; DOI=10.1073/pnas.1208098109;
RA Santos K.F., Jovin S.M., Weber G., Pena V., Luhrmann R., Wahl M.C.;
RT "Structural basis for functional cooperation between tandem helicase
RT cassettes in Brr2-mediated remodeling of the spliceosome.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:17418-17423(2012).
RN [25] {ECO:0007744|PDB:3JCR}
RP STRUCTURE BY ELECTRON MICROSCOPY (7.00 ANGSTROMS), SUBUNIT, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=26912367; DOI=10.1126/science.aad2085;
RA Agafonov D.E., Kastner B., Dybkov O., Hofele R.V., Liu W.T., Urlaub H.,
RA Luhrmann R., Stark H.;
RT "Molecular architecture of the human U4/U6.U5 tri-snRNP.";
RL Science 351:1416-1420(2016).
RN [26] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
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 [27] {ECO:0007744|PDB:5O9Z}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=28781166; DOI=10.1016/j.cell.2017.07.011;
RA Bertram K., Agafonov D.E., Dybkov O., Haselbach D., Leelaram M.N.,
RA Will C.L., Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for
RT Activation.";
RL Cell 170:701-713(2017).
RN [28] {ECO:0007744|PDB:6FF7}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=29361316; DOI=10.1016/j.cell.2018.01.010;
RA Haselbach D., Komarov I., Agafonov D.E., Hartmuth K., Graf B., Dybkov O.,
RA Urlaub H., Kastner B., Luhrmann R., Stark H.;
RT "Structure and Conformational Dynamics of the Human Spliceosomal Bact
RT Complex.";
RL Cell 172:454-464(2018).
RN [29] {ECO:0007744|PDB:6AH0}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.70 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=30315277; DOI=10.1038/s41422-018-0094-7;
RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.;
RT "Structures of the human pre-catalytic spliceosome and its precursor
RT spliceosome.";
RL Cell Res. 28:1129-1140(2018).
RN [30] {ECO:0007744|PDB:5Z56, ECO:0007744|PDB:5Z57, ECO:0007744|PDB:5Z58}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=29360106; DOI=10.1038/cr.2018.14;
RA Zhang X., Yan C., Zhan X., Li L., Lei J., Shi Y.;
RT "Structure of the human activated spliceosome in three conformational
RT states.";
RL Cell Res. 28:307-322(2018).
RN [31] {ECO:0007744|PDB:5YZG}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=29301961; DOI=10.1126/science.aar6401;
RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.;
RT "Structure of a human catalytic step I spliceosome.";
RL Science 359:537-545(2018).
RN [32] {ECO:0007744|PDB:6ICZ}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.00 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=30728453; DOI=10.1038/s41422-019-0143-x;
RA Zhang X., Zhan X., Yan C., Zhang W., Liu D., Lei J., Shi Y.;
RT "Structures of the human spliceosomes before and after release of the
RT ligated exon.";
RL Cell Res. 29:274-285(2019).
RN [33] {ECO:0007744|PDB:6QDV}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.30 ANGSTROMS) OF 404-2125, FUNCTION,
RP SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=30705154; DOI=10.1126/science.aaw5569;
RA Fica S.M., Oubridge C., Wilkinson M.E., Newman A.J., Nagai K.;
RT "A human postcatalytic spliceosome structure reveals essential roles of
RT metazoan factors for exon ligation.";
RL Science 363:710-714(2019).
RN [34]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-1736.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [35]
RP VARIANT RP33 LEU-1087, AND TISSUE SPECIFICITY.
RX PubMed=19878916; DOI=10.1016/j.ajhg.2009.09.020;
RA Zhao C., Bellur D.L., Lu S., Zhao F., Grassi M.A., Bowne S.J.,
RA Sullivan L.S., Daiger S.P., Chen L.J., Pang C.P., Zhao K., Staley J.P.,
RA Larsson C.;
RT "Autosomal-dominant retinitis pigmentosa caused by a mutation in SNRNP200,
RT a gene required for unwinding of U4/U6 snRNAs.";
RL Am. J. Hum. Genet. 85:617-627(2009).
RN [36]
RP VARIANT RP33 LEU-1090.
RX PubMed=19710410; DOI=10.1167/iovs.09-3725;
RA Li N., Mei H., MacDonald I.M., Jiao X., Hejtmancik J.F.;
RT "Mutations in ASCC3L1 on 2q11.2 are associated with autosomal dominant
RT retinitis pigmentosa in a Chinese family.";
RL Invest. Ophthalmol. Vis. Sci. 51:1036-1043(2010).
RN [37]
RP VARIANTS RP33 CYS-681; HIS-681; LEU-683; CYS-689 AND LEU-1087.
RX PubMed=21618346; DOI=10.1002/humu.21485;
RA Benaglio P., McGee T.L., Capelli L.P., Harper S., Berson E.L., Rivolta C.;
RT "Next generation sequencing of pooled samples reveals new SNRNP200
RT mutations associated with retinitis pigmentosa.";
RL Hum. Mutat. 32:E2246-E2258(2011).
RN [38]
RP VARIANT RP33 GLU-885.
RX PubMed=23029027; DOI=10.1371/journal.pone.0045464;
RA Liu T., Jin X., Zhang X., Yuan H., Cheng J., Lee J., Zhang B., Zhang M.,
RA Wu J., Wang L., Tian G., Wang W.;
RT "A novel missense SNRNP200 mutation associated with autosomal dominant
RT retinitis pigmentosa in a Chinese family.";
RL PLoS ONE 7:E45464-E45464(2012).
RN [39]
RP VARIANTS RP33 ARG-502; VAL-698 AND HIS-1779, AND VARIANT THR-1995.
RX PubMed=23887765; DOI=10.1038/eye.2013.137;
RA Zhang X., Lai T.Y., Chiang S.W., Tam P.O., Liu D.T., Chan C.K., Pang C.P.,
RA Zhao C., Chen L.J.;
RT "Contribution of SNRNP200 sequence variations to retinitis pigmentosa.";
RL Eye 27:1204-1213(2013).
RN [40]
RP VARIANTS RP33 VAL-542; CYS-681; HIS-681; SER-682 AND LEU-1087.
RX PubMed=24319334;
RA Bowne S.J., Sullivan L.S., Avery C.E., Sasser E.M., Roorda A., Duncan J.L.,
RA Wheaton D.H., Birch D.G., Branham K.E., Heckenlively J.R., Sieving P.A.,
RA Daiger S.P.;
RT "Mutations in the small nuclear riboprotein 200 kDa gene (SNRNP200) cause
RT 1.6% of autosomal dominant retinitis pigmentosa.";
RL Mol. Vis. 19:2407-2417(2013).
CC -!- FUNCTION: Plays role in pre-mRNA splicing as core component of
CC precatalytic, catalytic and postcatalytic spliceosomal complexes
CC (PubMed:28502770, PubMed:28781166, PubMed:29361316, PubMed:30315277,
CC PubMed:29360106, PubMed:29301961, PubMed:30728453, PubMed:30705154).
CC Involved in spliceosome assembly, activation and disassembly. Mediates
CC changes in the dynamic network of RNA-RNA interactions in the
CC spliceosome. Catalyzes the ATP-dependent unwinding of U4/U6 RNA
CC duplices, an essential step in the assembly of a catalytically active
CC spliceosome. {ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:23045696,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166,
CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106,
CC ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30315277,
CC ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453,
CC ECO:0000269|PubMed:8670905, ECO:0000269|PubMed:9539711}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:23045696};
CC -!- SUBUNIT: Component of a core complex containing at least PRPF8,
CC SNRNP200, EFTUD2 and SNRNP40. Component of the U5 snRNP and U4/U6-U5
CC tri-snRNP complexes, building blocks of the spliceosome. Component of
CC the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and
CC at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40,
CC DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39 (PubMed:16723661,
CC PubMed:8670905, PubMed:26912367). Component of precatalytic, catalytic
CC and postcatalytic spliceosomal complexes (PubMed:11991638,
CC PubMed:28502770, PubMed:28781166, PubMed:29361316, PubMed:30315277,
CC PubMed:29360106, PubMed:29301961, PubMed:30728453, PubMed:30705154).
CC {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:16723661,
CC ECO:0000269|PubMed:23045696, ECO:0000269|PubMed:26912367,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166,
CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106,
CC ECO:0000269|PubMed:29361316, ECO:0000269|PubMed:30315277,
CC ECO:0000269|PubMed:30705154, ECO:0000269|PubMed:30728453,
CC ECO:0000269|PubMed:8670905}.
CC -!- INTERACTION:
CC O75643; Q7LBR1: CHMP1B; NbExp=3; IntAct=EBI-1045395, EBI-2118090;
CC O75643; Q14749: GNMT; NbExp=3; IntAct=EBI-1045395, EBI-744239;
CC O75643; O94906: PRPF6; NbExp=5; IntAct=EBI-1045395, EBI-536755;
CC O75643; Q6P2Q9: PRPF8; NbExp=3; IntAct=EBI-1045395, EBI-538479;
CC O75643; O15541: RNF113A; NbExp=2; IntAct=EBI-1045395, EBI-2130294;
CC O75643; O43290: SART1; NbExp=5; IntAct=EBI-1045395, EBI-607761;
CC O75643; O75643: SNRNP200; NbExp=2; IntAct=EBI-1045395, EBI-1045395;
CC O75643; Q96DI7: SNRNP40; NbExp=2; IntAct=EBI-1045395, EBI-538492;
CC O75643; O75554: WBP4; NbExp=11; IntAct=EBI-1045395, EBI-7251981;
CC O75643-1; Q6P2Q9: PRPF8; NbExp=2; IntAct=EBI-5456052, EBI-538479;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:28781166, ECO:0000269|PubMed:29301961,
CC ECO:0000269|PubMed:29360106, ECO:0000269|PubMed:29361316,
CC ECO:0000269|PubMed:30315277, ECO:0000269|PubMed:30705154,
CC ECO:0000269|PubMed:30728453, ECO:0000269|PubMed:9539711}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75643-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75643-2; Sequence=VSP_026622;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:19878916}.
CC -!- DOMAIN: Contains two helicase domains. The N-terminal helicase domain
CC has catalytic activity by itself, contrary to the C-terminal helicase
CC domain that may have a regulatory role and enhance the activity of the
CC first helicase domain. {ECO:0000269|PubMed:23045696}.
CC -!- DISEASE: Retinitis pigmentosa 33 (RP33) [MIM:610359]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:16723661,
CC ECO:0000269|PubMed:19710410, ECO:0000269|PubMed:19878916,
CC ECO:0000269|PubMed:21618346, ECO:0000269|PubMed:23029027,
CC ECO:0000269|PubMed:23045696, ECO:0000269|PubMed:23887765,
CC ECO:0000269|PubMed:24319334}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14906.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; AY572488; AAS78571.1; -; mRNA.
DR EMBL; AK024391; BAB14906.1; ALT_INIT; mRNA.
DR EMBL; AK090671; BAC03499.1; -; mRNA.
DR EMBL; AB018331; BAA34508.2; -; mRNA.
DR EMBL; Z70200; CAA94089.1; -; Genomic_DNA.
DR EMBL; BC065924; AAH65924.1; -; mRNA.
DR EMBL; BC007577; AAH07577.1; -; mRNA.
DR CCDS; CCDS2020.1; -. [O75643-1]
DR RefSeq; NP_054733.2; NM_014014.4. [O75643-1]
DR RefSeq; XP_016859092.1; XM_017003603.1.
DR PDB; 2Q0Z; X-ray; 2.00 A; X=1808-2136.
DR PDB; 3JCR; EM; 7.00 A; C=1-2136.
DR PDB; 4F91; X-ray; 2.70 A; B=402-2125.
DR PDB; 4F92; X-ray; 2.66 A; B=402-2125.
DR PDB; 4F93; X-ray; 2.92 A; B=402-2125.
DR PDB; 4KIT; X-ray; 3.60 A; B=395-2129.
DR PDB; 5O9Z; EM; 4.50 A; C=1-2136.
DR PDB; 5URJ; X-ray; 2.75 A; A=395-2129.
DR PDB; 5URK; X-ray; 2.95 A; A=395-2129.
DR PDB; 5URM; X-ray; 2.80 A; A/B=395-2129.
DR PDB; 5XJC; EM; 3.60 A; D=1-2136.
DR PDB; 5YZG; EM; 4.10 A; D=1-2136.
DR PDB; 5Z56; EM; 5.10 A; D=1-2136.
DR PDB; 5Z57; EM; 6.50 A; D=1-2136.
DR PDB; 5Z58; EM; 4.90 A; D=1-2136.
DR PDB; 6AH0; EM; 5.70 A; D=1-2136.
DR PDB; 6AHD; EM; 3.80 A; D=1-2136.
DR PDB; 6FF7; EM; 4.50 A; r=1-2136.
DR PDB; 6ICZ; EM; 3.00 A; D=1-2136.
DR PDB; 6QDV; EM; 3.30 A; B=404-2125.
DR PDB; 6QW6; EM; 2.92 A; 5B=1-2136.
DR PDB; 6QX9; EM; 3.28 A; 5B=1-2136.
DR PDB; 6S8O; X-ray; 3.17 A; B=394-2136.
DR PDB; 6S8Q; X-ray; 2.39 A; B=394-2136.
DR PDB; 6S9I; X-ray; 2.60 A; B=394-2136.
DR PDB; 7A5P; EM; 5.00 A; q=1-2136.
DR PDB; 7ABG; EM; 7.80 A; s=1-2136.
DR PDB; 7ABI; EM; 8.00 A; s=1-2136.
DR PDB; 7BDI; X-ray; 2.80 A; B=394-2136.
DR PDB; 7BDJ; X-ray; 2.59 A; B=394-2136.
DR PDB; 7BDK; X-ray; 2.52 A; B=394-2136.
DR PDB; 7BDL; X-ray; 2.69 A; B=394-2136.
DR PDB; 7DVQ; EM; 2.89 A; D=1-2136.
DR PDB; 7OS1; EM; 3.30 A; B=395-2129.
DR PDB; 7OS2; EM; 2.76 A; B=395-2129.
DR PDB; 7PX3; EM; 3.05 A; B=394-2136.
DR PDBsum; 2Q0Z; -.
DR PDBsum; 3JCR; -.
DR PDBsum; 4F91; -.
DR PDBsum; 4F92; -.
DR PDBsum; 4F93; -.
DR PDBsum; 4KIT; -.
DR PDBsum; 5O9Z; -.
DR PDBsum; 5URJ; -.
DR PDBsum; 5URK; -.
DR PDBsum; 5URM; -.
DR PDBsum; 5XJC; -.
DR PDBsum; 5YZG; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 5Z58; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6AHD; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6QDV; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR PDBsum; 6S8O; -.
DR PDBsum; 6S8Q; -.
DR PDBsum; 6S9I; -.
DR PDBsum; 7A5P; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABI; -.
DR PDBsum; 7BDI; -.
DR PDBsum; 7BDJ; -.
DR PDBsum; 7BDK; -.
DR PDBsum; 7BDL; -.
DR PDBsum; 7DVQ; -.
DR PDBsum; 7OS1; -.
DR PDBsum; 7OS2; -.
DR PDBsum; 7PX3; -.
DR AlphaFoldDB; O75643; -.
DR SMR; O75643; -.
DR BioGRID; 116661; 326.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; O75643; -.
DR DIP; DIP-31659N; -.
DR IntAct; O75643; 128.
DR MINT; O75643; -.
DR STRING; 9606.ENSP00000317123; -.
DR BindingDB; O75643; -.
DR ChEMBL; CHEMBL4105972; -.
DR CarbonylDB; O75643; -.
DR GlyGen; O75643; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75643; -.
DR MetOSite; O75643; -.
DR PhosphoSitePlus; O75643; -.
DR SwissPalm; O75643; -.
DR BioMuta; SNRNP200; -.
DR EPD; O75643; -.
DR jPOST; O75643; -.
DR MassIVE; O75643; -.
DR MaxQB; O75643; -.
DR PaxDb; O75643; -.
DR PeptideAtlas; O75643; -.
DR PRIDE; O75643; -.
DR ProteomicsDB; 50136; -. [O75643-1]
DR ProteomicsDB; 50137; -. [O75643-2]
DR Antibodypedia; 32425; 83 antibodies from 20 providers.
DR DNASU; 23020; -.
DR Ensembl; ENST00000323853.10; ENSP00000317123.5; ENSG00000144028.15. [O75643-1]
DR GeneID; 23020; -.
DR KEGG; hsa:23020; -.
DR MANE-Select; ENST00000323853.10; ENSP00000317123.5; NM_014014.5; NP_054733.2.
DR UCSC; uc002svu.4; human. [O75643-1]
DR CTD; 23020; -.
DR DisGeNET; 23020; -.
DR GeneCards; SNRNP200; -.
DR GeneReviews; SNRNP200; -.
DR HGNC; HGNC:30859; SNRNP200.
DR HPA; ENSG00000144028; Low tissue specificity.
DR MalaCards; SNRNP200; -.
DR MIM; 601664; gene.
DR MIM; 610359; phenotype.
DR neXtProt; NX_O75643; -.
DR OpenTargets; ENSG00000144028; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA164726004; -.
DR VEuPathDB; HostDB:ENSG00000144028; -.
DR eggNOG; KOG0951; Eukaryota.
DR GeneTree; ENSGT00940000154966; -.
DR HOGENOM; CLU_000335_2_1_1; -.
DR InParanoid; O75643; -.
DR OMA; ESFWIIV; -.
DR OrthoDB; 154891at2759; -.
DR PhylomeDB; O75643; -.
DR TreeFam; TF300056; -.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; O75643; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; O75643; -.
DR BioGRID-ORCS; 23020; 792 hits in 1087 CRISPR screens.
DR ChiTaRS; SNRNP200; human.
DR EvolutionaryTrace; O75643; -.
DR GeneWiki; ASCC3L1; -.
DR GenomeRNAi; 23020; -.
DR Pharos; O75643; Tchem.
DR PRO; PR:O75643; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O75643; protein.
DR Bgee; ENSG00000144028; Expressed in ventricular zone and 211 other tissues.
DR ExpressionAtlas; O75643; baseline and differential.
DR Genevisible; O75643; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
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:0071006; C:U2-type catalytic step 1 spliceosome; IDA:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:CAFA.
DR GO; GO:0005682; C:U5 snRNP; IDA:HGNC-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IDA:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0000354; P:cis assembly of pre-catalytic spliceosome; IC:HGNC-UCL.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0000388; P:spliceosome conformational change to release U4 (or U4atac) and U1 (or U11); IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF52540; SSF52540; 4.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Coiled coil;
KW Direct protein sequencing; Disease variant; Helicase; Hydrolase;
KW Isopeptide bond; mRNA processing; mRNA splicing; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Retinitis pigmentosa;
KW Spliceosome; Ubl conjugation.
FT CHAIN 1..2136
FT /note="U5 small nuclear ribonucleoprotein 200 kDa helicase"
FT /id="PRO_0000102087"
FT DOMAIN 490..673
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 684..921
FT /note="Helicase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 981..1286
FT /note="SEC63 1"
FT DOMAIN 1337..1512
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1545..1753
FT /note="Helicase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1812..2124
FT /note="SEC63 2"
FT REGION 50..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 54..84
FT /evidence="ECO:0000255"
FT MOTIF 615..618
FT /note="DEIH box"
FT MOTIF 1454..1457
FT /note="DEVH box"
FT COMPBIAS 51..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 503..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541,
FT ECO:0000269|PubMed:23045696, ECO:0007744|PDB:4F93"
FT BINDING 1350..1357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541,
FT ECO:0000269|PubMed:23045696, ECO:0007744|PDB:4F93"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 389
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 709
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:F1LNJ2"
FT MOD_RES 971
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1428
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1765
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4T2"
FT MOD_RES 2002
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2131
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 2133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 2135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 561..2071
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026622"
FT VARIANT 502
FT /note="C -> R (in RP33)"
FT /evidence="ECO:0000269|PubMed:23887765"
FT /id="VAR_071689"
FT VARIANT 542
FT /note="A -> V (in RP33)"
FT /evidence="ECO:0000269|PubMed:24319334"
FT /id="VAR_071690"
FT VARIANT 681
FT /note="R -> C (in RP33; dbSNP:rs959069360)"
FT /evidence="ECO:0000269|PubMed:21618346,
FT ECO:0000269|PubMed:24319334"
FT /id="VAR_065587"
FT VARIANT 681
FT /note="R -> H (in RP33; dbSNP:rs527236113)"
FT /evidence="ECO:0000269|PubMed:21618346,
FT ECO:0000269|PubMed:24319334"
FT /id="VAR_065588"
FT VARIANT 682
FT /note="P -> S (in RP33)"
FT /evidence="ECO:0000269|PubMed:24319334"
FT /id="VAR_071691"
FT VARIANT 683
FT /note="V -> L (in RP33; unknown pathological significance;
FT dbSNP:rs527236114)"
FT /evidence="ECO:0000269|PubMed:21618346"
FT /id="VAR_065589"
FT VARIANT 689
FT /note="Y -> C (in RP33)"
FT /evidence="ECO:0000269|PubMed:21618346"
FT /id="VAR_065590"
FT VARIANT 698
FT /note="I -> V (in RP33; dbSNP:rs1457428682)"
FT /evidence="ECO:0000269|PubMed:23887765"
FT /id="VAR_071692"
FT VARIANT 885
FT /note="Q -> E (in RP33; dbSNP:rs397514575)"
FT /evidence="ECO:0000269|PubMed:23029027"
FT /id="VAR_071693"
FT VARIANT 1087
FT /note="S -> L (in RP33; strongly reduced RNA helicase
FT activity; dbSNP:rs267607077)"
FT /evidence="ECO:0000269|PubMed:16723661,
FT ECO:0000269|PubMed:19878916, ECO:0000269|PubMed:21618346,
FT ECO:0000269|PubMed:23045696, ECO:0000269|PubMed:24319334"
FT /id="VAR_063539"
FT VARIANT 1090
FT /note="R -> L (in RP33; dbSNP:rs397514574)"
FT /evidence="ECO:0000269|PubMed:19710410"
FT /id="VAR_063540"
FT VARIANT 1736
FT /note="F -> L (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035943"
FT VARIANT 1779
FT /note="R -> H (in RP33; dbSNP:rs749546665)"
FT /evidence="ECO:0000269|PubMed:23887765"
FT /id="VAR_071694"
FT VARIANT 1995
FT /note="A -> T (in dbSNP:rs201691299)"
FT /evidence="ECO:0000269|PubMed:23887765"
FT /id="VAR_071695"
FT MUTAGEN 603
FT /note="R->A: Strongly decreased ATP-dependent RNA helicase
FT activity."
FT /evidence="ECO:0000269|PubMed:23045696"
FT MUTAGEN 637
FT /note="R->A: Strongly decreased ATP-dependent RNA helicase
FT activity."
FT /evidence="ECO:0000269|PubMed:23045696"
FT MUTAGEN 1544
FT /note="K->A: Decreased ATP-dependent RNA helicase
FT activity."
FT /evidence="ECO:0000269|PubMed:23045696"
FT MUTAGEN 1548
FT /note="H->A: Strongly decreased ATP-dependent RNA helicase
FT activity."
FT /evidence="ECO:0000269|PubMed:23045696"
FT MUTAGEN 1578
FT /note="T->A: Decreased ATP-dependent RNA helicase
FT activity."
FT /evidence="ECO:0000269|PubMed:23045696"
FT CONFLICT 588
FT /note="C -> F (in Ref. 6; AAH65924)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="I -> V (in Ref. 5; CAA94089)"
FT /evidence="ECO:0000305"
FT CONFLICT 802
FT /note="A -> G (in Ref. 5; CAA94089)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="R -> H (in Ref. 2; BAB14906)"
FT /evidence="ECO:0000305"
FT CONFLICT 1322
FT /note="Q -> R (in Ref. 2; BAB14906)"
FT /evidence="ECO:0000305"
FT CONFLICT 1371
FT /note="S -> N (in Ref. 5; CAA94089)"
FT /evidence="ECO:0000305"
FT CONFLICT 1383..1386
FT /note="EALA -> RLWQ (in Ref. 5; CAA94089)"
FT /evidence="ECO:0000305"
FT CONFLICT 1476
FT /note="Y -> N (in Ref. 2; BAB14906)"
FT /evidence="ECO:0000305"
FT CONFLICT 1547
FT /note="Y -> F (in Ref. 5; CAA94089)"
FT /evidence="ECO:0000305"
FT CONFLICT 1667
FT /note="Q -> L (in Ref. 5; CAA94089)"
FT /evidence="ECO:0000305"
FT CONFLICT 1956
FT /note="K -> E (in Ref. 5; CAA94089)"
FT /evidence="ECO:0000305"
FT CONFLICT 1961..1962
FT /note="KQ -> RR (in Ref. 5; CAA94089)"
FT /evidence="ECO:0000305"
FT CONFLICT 1965..1971
FT /note="HFTSEHI -> PFPSGLF (in Ref. 5; CAA94089)"
FT /evidence="ECO:0000305"
FT CONFLICT 2031
FT /note="S -> R (in Ref. 2; BAB14906)"
FT /evidence="ECO:0000305"
FT CONFLICT 2065
FT /note="W -> L (in Ref. 6; AAH65924)"
FT /evidence="ECO:0000305"
FT CONFLICT 2101..2104
FT /note="AHNY -> GRHN (in Ref. 5; CAA94089)"
FT /evidence="ECO:0000305"
FT HELIX 107..124
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 129..144
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 442..447
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 464..466
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 469..472
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 483..493
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:6S8O"
FT HELIX 509..522
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 527..531
FT /evidence="ECO:0007829|PDB:7BDK"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:7BDK"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 545..559
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 569..571
FT /evidence="ECO:0007829|PDB:7BDJ"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:6S9I"
FT HELIX 578..582
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 584..588
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 590..599
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 601..603
FT /evidence="ECO:0007829|PDB:6S9I"
FT HELIX 606..608
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 609..615
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 617..621
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 625..642
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 647..652
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 658..664
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 669..671
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 672..675
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 678..680
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 685..692
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 697..713
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 714..718
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 721..724
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 728..744
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 748..750
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 751..753
FT /evidence="ECO:0007829|PDB:4F93"
FT STRAND 754..756
FT /evidence="ECO:0007829|PDB:7BDK"
FT HELIX 757..767
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 772..777
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 778..780
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 782..785
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 787..789
FT /evidence="ECO:0007829|PDB:4F92"
FT HELIX 792..802
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 807..811
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 813..818
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 823..829
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 831..835
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 836..839
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 840..843
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 846..854
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 859..861
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 865..872
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 873..875
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 876..883
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 893..906
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 913..920
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 924..931
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 933..936
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 940..944
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 950..966
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 969..972
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 974..976
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 978..981
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 983..990
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 995..1004
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1011..1019
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1022..1024
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1031..1033
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1034..1043
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1044..1046
FT /evidence="ECO:0007829|PDB:4F92"
FT STRAND 1052..1054
FT /evidence="ECO:0007829|PDB:7BDL"
FT HELIX 1055..1067
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1075..1101
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1105..1120
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1124..1126
FT /evidence="ECO:0007829|PDB:4F93"
FT HELIX 1128..1131
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1132..1135
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1137..1145
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1150..1153
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1154..1156
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1158..1165
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1168..1170
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1171..1180
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1184..1206
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1212..1215
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1218..1226
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1228..1230
FT /evidence="ECO:0007829|PDB:7BDI"
FT STRAND 1232..1242
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1243..1245
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1246..1248
FT /evidence="ECO:0007829|PDB:6S8O"
FT STRAND 1250..1257
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1264..1274
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1279..1285
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1309..1312
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1315..1318
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 1319..1324
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1326..1328
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1330..1340
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1346..1349
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1352..1355
FT /evidence="ECO:0007829|PDB:6S8O"
FT HELIX 1356..1370
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1376..1379
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1383..1397
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 1398..1401
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1405..1407
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1412..1421
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1423..1427
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1429..1436
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1437..1441
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1443..1446
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1449..1453
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1456..1460
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1464..1481
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1486..1492
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1497..1503
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1508..1510
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1511..1513
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1516..1518
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1523..1530
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1535..1553
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1555..1557
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1559..1565
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1566..1582
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 1586..1589
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 1594..1597
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1598..1601
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1607..1613
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 1614..1616
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1617..1620
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1626..1637
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1640..1647
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1648..1650
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1651..1653
FT /evidence="ECO:0007829|PDB:7BDJ"
FT STRAND 1658..1664
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1666..1670
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 1671..1674
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1675..1678
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1681..1688
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 1694..1696
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1700..1707
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1708..1710
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1711..1718
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1728..1730
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1733..1741
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1748..1756
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1759..1766
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1768..1771
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1778..1798
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1801..1805
FT /evidence="ECO:0007829|PDB:6S8Q"
FT TURN 1806..1808
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 1809..1812
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1814..1822
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1826..1835
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1842..1850
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT HELIX 1853..1855
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT HELIX 1862..1864
FT /evidence="ECO:0007829|PDB:6S8Q"
FT HELIX 1865..1874
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT STRAND 1875..1877
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT STRAND 1884..1886
FT /evidence="ECO:0007829|PDB:6S9I"
FT HELIX 1887..1899
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT HELIX 1906..1932
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT HELIX 1936..1951
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT STRAND 1955..1957
FT /evidence="ECO:0007829|PDB:7BDK"
FT HELIX 1959..1962
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT STRAND 1963..1965
FT /evidence="ECO:0007829|PDB:5URK"
FT HELIX 1968..1976
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT HELIX 1982..1987
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT HELIX 1990..1997
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT HELIX 2001..2011
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT STRAND 2017..2023
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT HELIX 2026..2028
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT STRAND 2033..2043
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT STRAND 2048..2050
FT /evidence="ECO:0007829|PDB:7BDK"
FT STRAND 2056..2058
FT /evidence="ECO:0007829|PDB:6S8Q"
FT STRAND 2064..2070
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT TURN 2071..2074
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT STRAND 2075..2082
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT STRAND 2085..2095
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT STRAND 2098..2112
FT /evidence="ECO:0007829|PDB:2Q0Z"
FT STRAND 2114..2116
FT /evidence="ECO:0007829|PDB:6S8O"
FT STRAND 2118..2127
FT /evidence="ECO:0007829|PDB:2Q0Z"
SQ SEQUENCE 2136 AA; 244508 MW; 3F3811BDCCC9DDB7 CRC64;
MADVTARSLQ YEYKANSNLV LQADRSLIDR TRRDEPTGEV LSLVGKLEGT RMGDKAQRTK
PQMQEERRAK RRKRDEDRHD INKMKGYTLL SEGIDEMVGI IYKPKTKETR ETYEVLLSFI
QAALGDQPRD ILCGAADEVL AVLKNEKLRD KERRKEIDLL LGQTDDTRYH VLVNLGKKIT
DYGGDKEIQN MDDNIDETYG VNVQFESDEE EGDEDVYGEV REEASDDDME GDEAVVRCTL
SANLVASGEL MSSKKKDLHP RDIDAFWLQR QLSRFYDDAI VSQKKADEVL EILKTASDDR
ECENQLVLLL GFNTFDFIKV LRQHRMMILY CTLLASAQSE AEKERIMGKM EADPELSKFL
YQLHETEKED LIREERSRRE RVRQSRMDTD LETMDLDQGG EALAPRQVLD LEDLVFTQGS
HFMANKRCQL PDGSFRRQRK GYEEVHVPAL KPKPFGSEEQ LLPVEKLPKY AQAGFEGFKT
LNRIQSKLYR AALETDENLL LCAPTGAGKT NVALMCMLRE IGKHINMDGT INVDDFKIIY
IAPMRSLVQE MVGSFGKRLA TYGITVAELT GDHQLCKEEI SATQIIVCTP EKWDIITRKG
GERTYTQLVR LIILDEIHLL HDDRGPVLEA LVARAIRNIE MTQEDVRLIG LSATLPNYED
VATFLRVDPA KGLFYFDNSF RPVPLEQTYV GITEKKAIKR FQIMNEIVYE KIMEHAGKNQ
VLVFVHSRKE TGKTARAIRD MCLEKDTLGL FLREGSASTE VLRTEAEQCK NLELKDLLPY
GFAIHHAGMT RVDRTLVEDL FADKHIQVLV STATLAWGVN LPAHTVIIKG TQVYSPEKGR
WTELGALDIL QMLGRAGRPQ YDTKGEGILI TSHGELQYYL SLLNQQLPIE SQMVSKLPDM
LNAEIVLGNV QNAKDAVNWL GYAYLYIRML RSPTLYGISH DDLKGDPLLD QRRLDLVHTA
ALMLDKNNLV KYDKKTGNFQ VTELGRIASH YYITNDTVQT YNQLLKPTLS EIELFRVFSL
SSEFKNITVR EEEKLELQKL LERVPIPVKE SIEEPSAKIN VLLQAFISQL KLEGFALMAD
MVYVTQSAGR LMRAIFEIVL NRGWAQLTDK TLNLCKMIDK RMWQSMCPLR QFRKLPEEVV
KKIEKKNFPF ERLYDLNHNE IGELIRMPKM GKTIHKYVHL FPKLELSVHL QPITRSTLKV
ELTITPDFQW DEKVHGSSEA FWILVEDVDS EVILHHEYFL LKAKYAQDEH LITFFVPVFE
PLPPQYFIRV VSDRWLSCET QLPVSFRHLI LPEKYPPPTE LLDLQPLPVS ALRNSAFESL
YQDKFPFFNP IQTQVFNTVY NSDDNVFVGA PTGSGKTICA EFAILRMLLQ SSEGRCVYIT
PMEALAEQVY MDWYEKFQDR LNKKVVLLTG ETSTDLKLLG KGNIIISTPE KWDILSRRWK
QRKNVQNINL FVVDEVHLIG GENGPVLEVI CSRMRYISSQ IERPIRIVAL SSSLSNAKDV
AHWLGCSATS TFNFHPNVRP VPLELHIQGF NISHTQTRLL SMAKPVYHAI TKHSPKKPVI
VFVPSRKQTR LTAIDILTTC AADIQRQRFL HCTEKDLIPY LEKLSDSTLK ETLLNGVGYL
HEGLSPMERR LVEQLFSSGA IQVVVASRSL CWGMNVAAHL VIIMDTQYYN GKIHAYVDYP
IYDVLQMVGH ANRPLQDDEG RCVIMCQGSK KDFFKKFLYE PLPVESHLDH CMHDHFNAEI
VTKTIENKQD AVDYLTWTFL YRRMTQNPNY YNLQGISHRH LSDHLSELVE QTLSDLEQSK
CISIEDEMDV APLNLGMIAA YYYINYTTIE LFSMSLNAKT KVRGLIEIIS NAAEYENIPI
RHHEDNLLRQ LAQKVPHKLN NPKFNDPHVK TNLLLQAHLS RMQLSAELQS DTEEILSKAI
RLIQACVDVL SSNGWLSPAL AAMELAQMVT QAMWSKDSYL KQLPHFTSEH IKRCTDKGVE
SVFDIMEMED EERNALLQLT DSQIADVARF CNRYPNIELS YEVVDKDSIR SGGPVVVLVQ
LEREEEVTGP VIAPLFPQKR EEGWWVVIGD AKSNSLISIK RLTLQQKAKV KLDFVAPATG
AHNYTLYFMS DAYMGCDQEY KFSVDVKEAE TDSDSD
