SAFB1_HUMAN
ID SAFB1_HUMAN Reviewed; 915 AA.
AC Q15424; A0AV56; B7Z5B6; B7ZLP6; F5H0H3; O60406; Q59HH8;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 4.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Scaffold attachment factor B1;
DE Short=SAF-B;
DE Short=SAF-B1;
DE AltName: Full=HSP27 estrogen response element-TATA box-binding protein;
DE Short=HSP27 ERE-TATA-binding protein;
GN Name=SAFB; Synonyms=HAP, HET, SAFB1;
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), AND CHARACTERIZATION.
RC TISSUE=Mammary carcinoma;
RX PubMed=9328833;
RX DOI=10.1002/(sici)1097-4644(19971101)67:2<275::aid-jcb13>3.0.co;2-e;
RA Oesterreich S., Lee A.V., Sullivan T.M., Samuel S.K., Davie J.R.,
RA Fuqua S.A.W.;
RT "Novel nuclear matrix protein HET binds to and influences activity of the
RT HSP27 promoter in human breast cancer cells.";
RL J. Cell. Biochem. 67:275-286(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-753 (ISOFORM 4).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 2-30; 419-428; 571-578 AND 601-612, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Mammary carcinoma;
RA Bienvenut W.V., Matallanas D., Kolch W.;
RL Submitted (JUL-2009) to UniProtKB.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-915 (ISOFORM 1), CHARACTERIZATION, AND
RP PHOSPHORYLATION.
RC TISSUE=Cervix carcinoma;
RX PubMed=8600450; DOI=10.1093/nar/24.5.843;
RA Renz A., Fackelmayer F.O.;
RT "Purification and molecular cloning of the scaffold attachment factor B
RT (SAF-B), a novel human nuclear protein that specifically binds to S/MAR-
RT DNA.";
RL Nucleic Acids Res. 24:843-849(1996).
RN [8]
RP FUNCTION, AND INTERACTION WITH POLR2A; SRSF1; SRFS9 AND SRFS10.
RX PubMed=9671816; DOI=10.1093/nar/26.15.3542;
RA Nayler O., Straetling W., Bourquin J.-P., Stagljar I., Lindemann L.,
RA Jasper H., Hartmann A.M., Fackelmeyer F.O., Ullrich A., Stamm S.;
RT "SAF-B couples transcription and pre-mRNA splicing to SAR/MAR elements.";
RL Nucleic Acids Res. 26:3542-3549(1998).
RN [9]
RP INTERACTION WITH SRPK1.
RX PubMed=11509566; DOI=10.1074/jbc.m104755200;
RA Nikolakaki E., Kohen R., Hartmann A.M., Stamm S., Georgatsou E.,
RA Giannakouros T.;
RT "Cloning and characterization of an alternatively spliced form of SR
RT protein kinase 1 that interacts specifically with scaffold attachment
RT factor-B.";
RL J. Biol. Chem. 276:40175-40182(2001).
RN [10]
RP CHARACTERIZATION, AND SUBUNIT.
RX PubMed=12660241; DOI=10.1074/jbc.m212988200;
RA Townson S.M., Dobrzycka K.M., Lee A.V., Air M., Deng W., Kang K., Jiang S.,
RA Kioka N., Michaelis K., Oesterreich S.;
RT "SAFB2, a new scaffold attachment factor homolog and estrogen receptor
RT corepressor.";
RL J. Biol. Chem. 278:20059-20068(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601 AND SER-604, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-383 AND SER-384, 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 [15]
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 [16]
RP INTERACTION WITH SRPK1, AND SUBCELLULAR LOCATION.
RX PubMed=19674106; DOI=10.1111/j.1742-4658.2009.07217.x;
RA Tsianou D., Nikolakaki E., Tzitzira A., Bonanou S., Giannakouros T.,
RA Georgatsou E.;
RT "The enzymatic activity of SR protein kinases 1 and 1a is negatively
RT affected by interaction with scaffold attachment factors B1 and 2.";
RL FEBS J. 276:5212-5227(2009).
RN [17]
RP 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-607, 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-383; SER-384; SER-415; SER-580; SER-582; SER-601 AND
RP SER-604, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], 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 [20]
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 [21]
RP SUMOYLATION AT LYS-231 AND LYS-294.
RX PubMed=21527249; DOI=10.1016/j.bbrc.2011.04.040;
RA Garee J.P., Meyer R., Oesterreich S.;
RT "Co-repressor activity of scaffold attachment factor B1 requires
RT sumoylation.";
RL Biochem. Biophys. Res. Commun. 408:516-522(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-383; SER-601 AND SER-604, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 [23]
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 [24]
RP INTERACTION WITH ZBED4, AND SUBCELLULAR LOCATION.
RX PubMed=22693546; DOI=10.1371/journal.pone.0035317;
RA Mokhonov V.V., Theendakara V.P., Gribanova Y.E., Ahmedli N.B., Farber D.B.;
RT "Sequence-specific binding of recombinant Zbed4 to DNA: insights into Zbed4
RT participation in gene transcription and its association with other
RT proteins.";
RL PLoS ONE 7:e35317-e35317(2012).
RN [25]
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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-79; SER-580; SER-601
RP AND SER-604, 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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-188; SER-195; SER-197 AND
RP SER-604, AND 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 [28]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-811; ARG-868; ARG-874 AND
RP ARG-884, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-172 AND LYS-543, AND
RP 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 [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-578, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [31]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-483; LYS-543 AND LYS-578, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [33]
RP INTERACTION WITH FUS.
RX PubMed=27731383; DOI=10.1038/srep35195;
RA Yamaguchi A., Takanashi K.;
RT "FUS interacts with nuclear matrix-associated protein SAFB1 as well as
RT Matrin3 to regulate splicing and ligand-mediated transcription.";
RL Sci. Rep. 6:35195-35195(2016).
RN [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-172; LYS-186; LYS-381; LYS-392;
RP LYS-483; LYS-514; LYS-543; LYS-570; LYS-578 AND LYS-847, AND IDENTIFICATION
RP BY MASS 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).
CC -!- FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA and
CC forms a molecular assembly point to allow the formation of a
CC 'transcriptosomal' complex (consisting of SR proteins and RNA
CC polymerase II) coupling transcription and RNA processing
CC (PubMed:9671816). Functions as an estrogen receptor corepressor and can
CC also bind to the HSP27 promoter and decrease its transcription
CC (PubMed:12660241). Thereby acts as a negative regulator of cell
CC proliferation (PubMed:12660241). When associated with RBMX, binds to
CC and stimulates transcription from the SREBF1 promoter (By similarity).
CC {ECO:0000250|UniProtKB:D3YXK2, ECO:0000269|PubMed:12660241,
CC ECO:0000269|PubMed:9671816}.
CC -!- SUBUNIT: Monomer and homodimer (PubMed:12660241). Forms heterodimers
CC with SAFB2 (PubMed:12660241). Interacts with KHDRBS3 (By similarity).
CC Interacts with CLK2 (By similarity). Interacts with POLR2A, SRSF1/ASF,
CC SRSF9/SRp30c and SFSF10/TRA2B (PubMed:9671816). Interacts with isoform
CC 1 and isoform 2 of SRPK1 and inhibits its activity (PubMed:19674106).
CC Interacts with RBMX (By similarity). Interacts with FUS
CC (PubMed:27731383). Interacts with ZBED4 (PubMed:22693546).
CC {ECO:0000250|UniProtKB:D3YXK2, ECO:0000250|UniProtKB:O88453,
CC ECO:0000269|PubMed:12660241, ECO:0000269|PubMed:19674106,
CC ECO:0000269|PubMed:22693546, ECO:0000269|PubMed:27731383,
CC ECO:0000269|PubMed:9671816}.
CC -!- INTERACTION:
CC Q15424; P35637: FUS; NbExp=7; IntAct=EBI-348298, EBI-400434;
CC Q15424; Q9GZQ8: MAP1LC3B; NbExp=3; IntAct=EBI-348298, EBI-373144;
CC Q15424; Q14151: SAFB2; NbExp=3; IntAct=EBI-348298, EBI-352869;
CC Q15424; Q96SB4-2: SRPK1; NbExp=2; IntAct=EBI-348298, EBI-5773439;
CC Q15424; Q96SB4-3: SRPK1; NbExp=2; IntAct=EBI-348298, EBI-7160164;
CC Q15424; P04637: TP53; NbExp=5; IntAct=EBI-348298, EBI-366083;
CC Q15424; Q9JKL7: Srek1; Xeno; NbExp=3; IntAct=EBI-348298, EBI-6452221;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19674106,
CC ECO:0000269|PubMed:22693546}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q15424-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15424-2; Sequence=VSP_045838, VSP_045839;
CC Name=3;
CC IsoId=Q15424-3; Sequence=VSP_045839;
CC Name=4;
CC IsoId=Q15424-4; Sequence=VSP_046902, VSP_045839;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the CNS and
CC at low levels in the liver. Expressed in a wide number of breast cancer
CC cell lines.
CC -!- PTM: Sumoylated by PIAS1 with SUMO1 and SUMO2/3, desumoylated by SENP1.
CC Sumoylation is required for transcriptional repressor activity.
CC {ECO:0000269|PubMed:21527249}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92017.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U72355; AAC00056.1; -; mRNA.
DR EMBL; AK298707; BAH12852.1; -; mRNA.
DR EMBL; AC004611; AAC14667.1; -; Genomic_DNA.
DR EMBL; AC011499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC134303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC126219; AAI26220.1; -; mRNA.
DR EMBL; BC143937; AAI43938.1; -; mRNA.
DR EMBL; BC143939; AAI43940.1; -; mRNA.
DR EMBL; AB208780; BAD92017.1; ALT_INIT; mRNA.
DR EMBL; L43631; AAC18697.1; -; mRNA.
DR CCDS; CCDS12142.1; -. [Q15424-1]
DR CCDS; CCDS56077.1; -. [Q15424-2]
DR CCDS; CCDS59339.1; -. [Q15424-3]
DR CCDS; CCDS59340.1; -. [Q15424-4]
DR PIR; S64732; S64732.
DR RefSeq; NP_001188267.1; NM_001201338.1. [Q15424-3]
DR RefSeq; NP_001188268.1; NM_001201339.1. [Q15424-4]
DR RefSeq; NP_001188269.1; NM_001201340.1. [Q15424-2]
DR RefSeq; NP_001307500.1; NM_001320571.1.
DR RefSeq; NP_001307501.1; NM_001320572.1.
DR RefSeq; NP_002958.2; NM_002967.3. [Q15424-1]
DR AlphaFoldDB; Q15424; -.
DR SMR; Q15424; -.
DR BioGRID; 112201; 182.
DR IntAct; Q15424; 59.
DR MINT; Q15424; -.
DR STRING; 9606.ENSP00000467423; -.
DR GlyGen; Q15424; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15424; -.
DR PhosphoSitePlus; Q15424; -.
DR SwissPalm; Q15424; -.
DR BioMuta; SAFB; -.
DR DMDM; 116242782; -.
DR EPD; Q15424; -.
DR jPOST; Q15424; -.
DR MassIVE; Q15424; -.
DR MaxQB; Q15424; -.
DR PaxDb; Q15424; -.
DR PeptideAtlas; Q15424; -.
DR PRIDE; Q15424; -.
DR ProteomicsDB; 25341; -.
DR ProteomicsDB; 60586; -. [Q15424-1]
DR Antibodypedia; 4536; 308 antibodies from 32 providers.
DR DNASU; 6294; -.
DR Ensembl; ENST00000292123.9; ENSP00000292123.4; ENSG00000160633.13. [Q15424-1]
DR Ensembl; ENST00000454510.5; ENSP00000415895.1; ENSG00000160633.13. [Q15424-2]
DR Ensembl; ENST00000588852.2; ENSP00000467423.1; ENSG00000160633.13. [Q15424-3]
DR Ensembl; ENST00000592224.5; ENSP00000464840.1; ENSG00000160633.13. [Q15424-4]
DR GeneID; 6294; -.
DR KEGG; hsa:6294; -.
DR MANE-Select; ENST00000588852.2; ENSP00000467423.1; NM_001201338.2; NP_001188267.1. [Q15424-3]
DR UCSC; uc002mce.5; human. [Q15424-1]
DR CTD; 6294; -.
DR DisGeNET; 6294; -.
DR GeneCards; SAFB; -.
DR HGNC; HGNC:10520; SAFB.
DR HPA; ENSG00000160633; Low tissue specificity.
DR MIM; 602895; gene.
DR neXtProt; NX_Q15424; -.
DR OpenTargets; ENSG00000160633; -.
DR PharmGKB; PA34928; -.
DR VEuPathDB; HostDB:ENSG00000160633; -.
DR eggNOG; KOG4661; Eukaryota.
DR GeneTree; ENSGT00940000155916; -.
DR HOGENOM; CLU_015021_0_0_1; -.
DR InParanoid; Q15424; -.
DR OMA; AAPFCAR; -.
DR OrthoDB; 803886at2759; -.
DR PhylomeDB; Q15424; -.
DR TreeFam; TF325240; -.
DR PathwayCommons; Q15424; -.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR SignaLink; Q15424; -.
DR SIGNOR; Q15424; -.
DR BioGRID-ORCS; 6294; 94 hits in 1084 CRISPR screens.
DR ChiTaRS; SAFB; human.
DR GeneWiki; SAFB; -.
DR GenomeRNAi; 6294; -.
DR Pharos; Q15424; Tbio.
DR PRO; PR:Q15424; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q15424; protein.
DR Bgee; ENSG00000160633; Expressed in sural nerve and 207 other tissues.
DR ExpressionAtlas; Q15424; baseline and differential.
DR Genevisible; Q15424; HS.
DR GO; GO:0030496; C:midbody; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; TAS:ProtInc.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034781; SAFB1.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR PANTHER; PTHR15683:SF6; PTHR15683:SF6; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; RNA-binding; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..915
FT /note="Scaffold attachment factor B1"
FT /id="PRO_0000081905"
FT DOMAIN 31..65
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 406..484
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..792
FT /note="Interaction with POLR2A. Interaction with SFRS1;
FT SFRS9 and SFRS10"
FT /evidence="ECO:0000250|UniProtKB:O88453,
FT ECO:0000269|PubMed:9671816"
FT REGION 599..915
FT /note="Interaction with SAFB2"
FT /evidence="ECO:0000269|PubMed:12660241"
FT REGION 671..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 599..616
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 77..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..118
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 811..853
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.6, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88453"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88453"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 607
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 811
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 868
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 874
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 884
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 172
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 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:21527249"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:21527249"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 392
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 483
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 514
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 543
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 570
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 578
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 578
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 847
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 114..182
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045838"
FT VAR_SEQ 621
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_046902"
FT VAR_SEQ 817
FT /note="P -> PRG (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.5"
FT /id="VSP_045839"
FT CONFLICT 16
FT /note="A -> P (in Ref. 1; AAC00056)"
FT /evidence="ECO:0000305"
FT CONFLICT 42..43
FT /note="EL -> DV (in Ref. 1; AAC00056)"
FT /evidence="ECO:0000305"
FT CONFLICT 197
FT /note="S -> P (in Ref. 2; BAH12852)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="C -> Y (in Ref. 2; BAH12852)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="E -> V (in Ref. 2; BAH12852)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="A -> G (in Ref. 1; AAC00056 and 7; AAC18697)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="D -> E (in Ref. 1; AAC00056 and 7; AAC18697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 915 AA; 102642 MW; E865940BC7783C4A CRC64;
MAETLSGLGD SGAAGAAALS SASSETGTRR LSDLRVIDLR AELRKRNVDS SGNKSVLMER
LKKAIEDEGG NPDEIEITSE GNKKTSKRSS KGRKPEEEGV EDNGLEENSG DGQEDVETSL
ENLQDIDIMD ISVLDEAEID NGSVADCVED DDADNLQESL SDSRELVEGE MKELPEQLQE
HAIEDKETIN NLDTSSSDFT ILQEIEEPSL EPENEKILDI LGETCKSEPV KEESSELEQP
FAQDTSSVGP DRKLAEEEDL FDSAHPEEGD LDLASESTAH AQSSKADSLL AVVKREPAEQ
PGDGERTDCE PVGLEPAVEQ SSAASELAEA SSEELAEAPT EAPSPEARDS KEDGRKFDFD
ACNEVPPAPK ESSTSEGADQ KMSSPEDDSD TKRLSKEEKG RSSCGRNFWV SGLSSTTRAT
DLKNLFSKYG KVVGAKVVTN ARSPGARCYG FVTMSTAEEA TKCINHLHKT ELHGKMISVE
KAKNEPVGKK TSDKRDSDGK KEKSSNSDRS TNLKRDDKCD RKDDAKKGDD GSGEKSKDQD
DQKPGPSERS RATKSGSRGT ERTVVMDKSK GVPVISVKTS GSKERASKSQ DRKSASREKR
SVVSFDKVKE PRKSRDSESH SRVRERSERE QRMQAQWERE ERERLEIARE RLAFQRQRLE
RERMERERLE RERMHVEHER RREQERIHRE REELRRQQEL RYEQERRPAV RRPYDLDRRD
DAYWPEAKRA ALDERYHSDF NRQDRFHDFD HRDRGRYPDH SVDRREGSRS MMGEREGQHY
PERHGGPERH GRDSRDGWGG YGSDKRMSEG RGLPPPPRRD WGDHGRREDD RSWQGTADGG
MMDRDHKRWQ GGERSMSGHS GPGHMMNRGG MSGRGSFAPG GASRGHPIPH GGMQGGFGGQ
SRGSRPSDAR FTRRY
