SRSF1_HUMAN
ID SRSF1_HUMAN Reviewed; 248 AA.
AC Q07955; B2R6Z7; D3DTZ3; Q13809;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 247.
DE RecName: Full=Serine/arginine-rich splicing factor 1 {ECO:0000305};
DE AltName: Full=Alternative-splicing factor 1;
DE Short=ASF-1;
DE AltName: Full=Splicing factor, arginine/serine-rich 1;
DE AltName: Full=pre-mRNA-splicing factor SF2, P33 subunit;
GN Name=SRSF1 {ECO:0000312|HGNC:HGNC:10780}; Synonyms=ASF, SF2, SF2P33, SFRS1;
GN ORFNames=OK/SW-cl.3;
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] (ISOFORMS ASF-1 AND ASF-2), PARTIAL PROTEIN
RP SEQUENCE, AND ALTERNATIVE SPLICING.
RX PubMed=1855257; DOI=10.1016/0092-8674(91)90626-a;
RA Ge H., Zuo P., Manley J.L.;
RT "Primary structure of the human splicing factor ASF reveals similarities
RT with Drosophila regulators.";
RL Cell 66:373-382(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ASF-1), AND PROTEIN SEQUENCE OF 144-161
RP AND 167-175.
RX PubMed=1830244; DOI=10.1016/0092-8674(91)90627-b;
RA Krainer A.R., Mayeda A., Kozak D., Binns G.;
RT "Functional expression of cloned human splicing factor SF2: homology to
RT RNA-binding proteins, U1 70K, and Drosophila splicing regulators.";
RL Cell 66:383-394(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ASF-1).
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ASF-1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ASF-1 AND ASF-3).
RC TISSUE=Brain, and Placenta;
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 PROTEIN SEQUENCE OF 18-28; 31-38; 52-65; 75-83; 123-138 AND 143-164, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 123-140.
RX PubMed=1577277; DOI=10.1101/gad.6.5.837;
RA Zahler A.M., Lane W.S., Stolk J.A., Roth M.B.;
RT "SR proteins: a conserved family of pre-mRNA splicing factors.";
RL Genes Dev. 6:837-847(1992).
RN [9]
RP CHARACTERIZATION.
RX PubMed=1741384; DOI=10.1073/pnas.89.4.1301;
RA Mayeda A., Zahler A.M., Krainer A.R., Roth M.B.;
RT "Two members of a conserved family of nuclear phosphoproteins are involved
RT in pre-mRNA splicing.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1301-1304(1992).
RN [10]
RP INTERACTION IN SPLICEOSOME ASSEMBLY.
RX PubMed=8261509; DOI=10.1016/0092-8674(93)90316-i;
RA Wu J.Y., Maniatis T.;
RT "Specific interactions between proteins implicated in splice site selection
RT and regulated alternative splicing.";
RL Cell 75:1061-1070(1993).
RN [11]
RP MUTAGENESIS, AND CHARACTERIZATION OF FUNCTIONAL DOMAINS.
RX PubMed=8223481; DOI=10.1002/j.1460-2075.1993.tb06161.x;
RA Zuo P., Manley J.L.;
RT "Functional domains of the human splicing factor ASF/SF2.";
RL EMBO J. 12:4727-4737(1993).
RN [12]
RP FUNCTION IN RECRUITMENT OF U1-70K TO PRE-MRNA.
RX PubMed=8139654; DOI=10.1038/368119a0;
RA Kohtz J.D., Jamison S.F., Will C.L., Zuo P., Luehrmann R.,
RA Garcia-Blanco M.A., Manley J.L.;
RT "Protein-protein interactions and 5'-splice-site recognition in mammalian
RT mRNA precursors.";
RL Nature 368:119-124(1994).
RN [13]
RP RECOGNITION OF PRE-MRNA 5'SPLICE SITES.
RX PubMed=7512732; DOI=10.1073/pnas.91.8.3363;
RA Zuo P., Manley J.L.;
RT "The human splicing factor ASF/SF2 can specifically recognize pre-mRNA 5'
RT splice sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3363-3367(1994).
RN [14]
RP RNA-BINDING SPECIFICITY.
RX PubMed=7543047; DOI=10.1002/j.1460-2075.1995.tb07360.x;
RA Tacke R., Manley J.L.;
RT "The human splicing factors ASF/SF2 and SC35 possess distinct, functionally
RT significant RNA binding specificities.";
RL EMBO J. 14:3540-3551(1995).
RN [15]
RP INTERACTION WITH ZRSR2.
RX PubMed=9237760; DOI=10.1038/41137;
RA Tronchere H., Wang J., Fu X.D.;
RT "A protein related to splicing factor U2AF35 that interacts with U2AF65 and
RT SR proteins in splicing of pre-mRNA.";
RL Nature 388:397-400(1997).
RN [16]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-162 AND PHE-180.
RX PubMed=9420331; DOI=10.1101/gad.12.1.55;
RA Caceres J.F., Screaton G.R., Krainer A.R.;
RT "A specific subset of SR proteins shuttles continuously between the nucleus
RT and the cytoplasm.";
RL Genes Dev. 12:55-66(1998).
RN [17]
RP INTERACTION WITH PSIP1.
RX PubMed=9885563; DOI=10.1016/s1097-2765(00)80290-7;
RA Ge H., Si Y., Wolffe A.P.;
RT "A novel transcriptional coactivator, p52, functionally interacts with the
RT essential splicing factor ASF/SF2.";
RL Mol. Cell 2:751-759(1998).
RN [18]
RP INTERACTION WITH SAFB/SAFB1.
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 [19]
RP INTERACTION WITH SREK1.
RX PubMed=10757789; DOI=10.1128/mcb.20.9.3049-3057.2000;
RA Barnard D.C., Patton J.G.;
RT "Identification and characterization of a novel serine-arginine-rich
RT splicing regulatory protein.";
RL Mol. Cell. Biol. 20:3049-3057(2000).
RN [20]
RP SUBCELLULAR LOCATION.
RX PubMed=12215544; DOI=10.1128/mcb.22.19.6871-6882.2002;
RA Cazalla D., Zhu J., Manche L., Huber E., Krainer A.R., Caceres J.F.;
RT "Nuclear export and retention signals in the RS domain of SR proteins.";
RL Mol. Cell. Biol. 22:6871-6882(2002).
RN [21]
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 [22]
RP INTERACTION WITH NXF1.
RX PubMed=12667464; DOI=10.1016/s1097-2765(03)00089-3;
RA Huang Y., Gattoni R., Stevenin J., Steitz J.A.;
RT "SR splicing factors serve as adapter proteins for TAP-dependent mRNA
RT export.";
RL Mol. Cell 11:837-843(2003).
RN [23]
RP PHOSPHORYLATION AT SERINE RESIDUES, AND INTERACTION WITH SRPK1.
RX PubMed=14555757; DOI=10.1073/pnas.1635129100;
RA Aubol B.E., Chakrabarti S., Ngo J., Shaffer J., Nolen B., Fu X.-D.,
RA Ghosh G., Adams J.A.;
RT "Processive phosphorylation of alternative splicing factor/splicing factor
RT 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12601-12606(2003).
RN [24]
RP INTERACTION WITH RSRC1.
RX PubMed=15798186; DOI=10.1128/mcb.25.8.2969-2980.2005;
RA Cazalla D., Newton K., Caceres J.F.;
RT "A novel SR-related protein is required for the second step of pre-mRNA
RT splicing.";
RL Mol. Cell. Biol. 25:2969-2980(2005).
RN [25]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [26]
RP INTERACTION WITH CCNL1; CCNL2 AND CDK11B.
RX PubMed=18216018; DOI=10.1074/jbc.m708188200;
RA Loyer P., Trembley J.H., Grenet J.A., Busson A., Corlu A., Zhao W.,
RA Kocak M., Kidd V.J., Lahti J.M.;
RT "Characterization of cyclin L1 and L2 interactions with CDK11 and splicing
RT factors: influence of cyclin L isoforms on splice site selection.";
RL J. Biol. Chem. 283:7721-7732(2008).
RN [27]
RP PHOSPHORYLATION BY SRPK1, AND THE MECHANISM OF PHOSPHORYLATION.
RX PubMed=18155240; DOI=10.1016/j.jmb.2007.08.029;
RA Ma C.T., Velazquez-Dones A., Hagopian J.C., Ghosh G., Fu X.D., Adams J.A.;
RT "Ordered multi-site phosphorylation of the splicing factor ASF/SF2 by
RT SRPK1.";
RL J. Mol. Biol. 376:55-68(2008).
RN [28]
RP PHOSPHORYLATION BY SRPK1, AND THE MECHANISM OF PHOSPHORYLATION.
RX PubMed=18687337; DOI=10.1016/j.jmb.2008.07.055;
RA Hagopian J.C., Ma C.T., Meade B.R., Albuquerque C.P., Ngo J.C., Ghosh G.,
RA Jennings P.A., Fu X.D., Adams J.A.;
RT "Adaptable molecular interactions guide phosphorylation of the SR protein
RT ASF/SF2 by SRPK1.";
RL J. Mol. Biol. 382:894-909(2008).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-205; SER-231;
RP SER-234 AND SER-238, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [30]
RP PHOSPHORYLATION BY SRPK1, AND THE MECHANISM OF PHOSPHORYLATION.
RX PubMed=19886675; DOI=10.1021/bi901107q;
RA Huynh N., Ma C.T., Giang N., Hagopian J., Ngo J., Adams J., Ghosh G.;
RT "Allosteric interactions direct binding and phosphorylation of ASF/SF2 by
RT SRPK1.";
RL Biochemistry 48:11432-11440(2009).
RN [31]
RP PHOSPHORYLATION BY SRPK1, AND THE MECHANISM OF PHOSPHORYLATION.
RX PubMed=19477182; DOI=10.1016/j.jmb.2009.05.060;
RA Ma C.T., Hagopian J.C., Ghosh G., Fu X.D., Adams J.A.;
RT "Regiospecific phosphorylation control of the SR protein ASF/SF2 by
RT SRPK1.";
RL J. Mol. Biol. 390:618-634(2009).
RN [32]
RP RNA-BINDING.
RX PubMed=19561594; DOI=10.1038/nbt.1550;
RA Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S.,
RA Blencowe B.J., Morris Q., Hughes T.R.;
RT "Rapid and systematic analysis of the RNA recognition specificities of RNA-
RT binding proteins.";
RL Nat. Biotechnol. 27:667-670(2009).
RN [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-38 AND LYS-179, AND
RP IDENTIFICATION BY MASS 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 [34]
RP METHYLATION AT ARG-93; ARG-97 AND ARG-109, MUTAGENESIS OF ARG-93; ARG-97
RP AND ARG-109, AND SUBCELLULAR LOCATION.
RX PubMed=20308322; DOI=10.1128/mcb.01270-09;
RA Sinha R., Allemand E., Zhang Z., Karni R., Myers M.P., Krainer A.R.;
RT "Arginine methylation controls the subcellular localization and functions
RT of the oncoprotein splicing factor SF2/ASF.";
RL Mol. Cell. Biol. 30:2762-2774(2010).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP 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 [36]
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 [37]
RP INTERACTION WITH CCDC55.
RX PubMed=21296756; DOI=10.1093/nar/gkq1267;
RA Kim Y.D., Lee J.Y., Oh K.M., Araki M., Araki K., Yamamura K.I., Jun C.D.;
RT "NSrp70 is a novel nuclear speckle-related protein that modulates
RT alternative pre-mRNA splicing in vivo.";
RL Nucleic Acids Res. 39:4300-4314(2011).
RN [38]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2 AND SER-199, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [39]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-133; SER-199; SER-201
RP AND SER-205, 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 [40]
RP IDENTIFICATION IN RIBONUCLEOPROTEIN COMPLEX, INTERACTION WITH ARVCF, AND
RP SUBCELLULAR LOCATION.
RX PubMed=24644279; DOI=10.1074/jbc.m113.530717;
RA Rappe U., Schlechter T., Aschoff M., Hotz-Wagenblatt A., Hofmann I.;
RT "Nuclear ARVCF protein binds splicing factors and contributes to the
RT regulation of alternative splicing.";
RL J. Biol. Chem. 289:12421-12434(2014).
RN [41]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-201 AND TYR-202, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [42]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-93; ARG-97; ARG-109 AND ARG-111,
RP 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 [43]
RP INTERACTION WITH RRP1B.
RX PubMed=23604122; DOI=10.1038/onc.2013.133;
RG NISC Comparative Sequencing Program;
RA Lee M., Dworkin A.M., Gildea D., Trivedi N.S., Moorhead G.B.,
RA Crawford N.P.;
RT "RRP1B is a metastasis modifier that regulates the expression of
RT alternative mRNA isoforms through interactions with SRSF1.";
RL Oncogene 33:1818-1827(2014).
RN [44]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-38, AND IDENTIFICATION BY MASS
RP 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 [45]
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 [46]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-30 AND LYS-38, 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).
RN [47]
RP STRUCTURE BY NMR OF 1-98.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in splicing factor SF2.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [48]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 105-219 IN COMPLEX WITH SRPK1,
RP MECHANISM OF ITS PHOSPHORYLATION BY SRPK1, AND DOMAIN RRM.
RX PubMed=18342604; DOI=10.1016/j.molcel.2007.12.017;
RA Ngo J.C., Giang K., Chakrabarti S., Ma C.T., Huynh N., Hagopian J.C.,
RA Dorrestein P.C., Fu X.D., Adams J.A., Ghosh G.;
RT "A sliding docking interaction is essential for sequential and processive
RT phosphorylation of an SR protein by SRPK1.";
RL Mol. Cell 29:563-576(2008).
RN [49] {ECO:0007744|PDB:4C0O}
RP X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 106-230 IN COMPLEX WITH TNPO3,
RP PHOSPHORYLATION AT SER-201; SER-207 AND SER-209, AND SUBCELLULAR LOCATION.
RX PubMed=24449914; DOI=10.1073/pnas.1320755111;
RA Maertens G.N., Cook N.J., Wang W., Hare S., Gupta S.S., Oztop I., Lee K.,
RA Pye V.E., Cosnefroy O., Snijders A.P., KewalRamani V.N., Fassati A.,
RA Engelman A., Cherepanov P.;
RT "Structural basis for nuclear import of splicing factors by human
RT Transportin 3.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:2728-2733(2014).
RN [50]
RP VARIANT [LARGE SCALE ANALYSIS] SER-89.
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).
CC -!- FUNCTION: Plays a role in preventing exon skipping, ensuring the
CC accuracy of splicing and regulating alternative splicing. Interacts
CC with other spliceosomal components, via the RS domains, to form a
CC bridge between the 5'- and 3'-splice site binding components, U1 snRNP
CC and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-
CC containing pre-mRNA. Binds to purine-rich RNA sequences, either the
CC octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers,
CC AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif
CC in vitro. Three copies of the octamer constitute a powerful splicing
CC enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can
CC specifically activate ASE-dependent splicing. Isoform ASF-2 and isoform
CC ASF-3 act as splicing repressors. May function as export adapter
CC involved in mRNA nuclear export through the TAP/NXF1 pathway.
CC {ECO:0000269|PubMed:8139654}.
CC -!- SUBUNIT: Consists of two polypeptides of p32 and p33. Identified in the
CC spliceosome C complex (PubMed:11991638). Component of a
CC ribonucleoprotein complex containing mRNAs and RNA-binding proteins
CC including DDX5, HNRNPH2 and SRSF1 as well as splicing regulator ARVCF
CC (PubMed:24644279). In vitro, self-associates and binds SRSF2, SNRNP70
CC and U2AF1 but not U2AF2. Binds SREK1/SFRS12. Interacts with SAFB/SAFB1.
CC Interacts with PSIP1/LEDGF. Interacts with RSRC1 (via Arg/Ser-rich
CC domain). Interacts with ZRSR2/U2AF1-RS2. Interacts with CCDC55 (via C-
CC terminus). Interacts with SRPK1 and a sliding docking interaction is
CC essential for its sequential and processive phosphorylation by SRPK1.
CC Interacts with NXF1. Interacts with CCNL1, CCNL2 and CDK11B
CC (PubMed:18216018). Interacts with RRP1B (PubMed:23604122). Interacts
CC (when phosphorylated in its RS domain) with TNPO3; promoting nuclear
CC import (PubMed:24449914). Interacts with ILDR1 (via C-terminus) and
CC ILDR2 (By similarity). {ECO:0000250|UniProtKB:Q6PDM2,
CC ECO:0000269|PubMed:10757789, ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:12667464, ECO:0000269|PubMed:14555757,
CC ECO:0000269|PubMed:15798186, ECO:0000269|PubMed:18216018,
CC ECO:0000269|PubMed:18342604, ECO:0000269|PubMed:21296756,
CC ECO:0000269|PubMed:23604122, ECO:0000269|PubMed:24449914,
CC ECO:0000269|PubMed:24644279, ECO:0000269|PubMed:8261509,
CC ECO:0000269|PubMed:9237760, ECO:0000269|PubMed:9671816,
CC ECO:0000269|PubMed:9885563}.
CC -!- INTERACTION:
CC Q07955; Q86X95: CIR1; NbExp=3; IntAct=EBI-398920, EBI-627102;
CC Q07955; P49759-3: CLK1; NbExp=3; IntAct=EBI-398920, EBI-11981867;
CC Q07955; P23511: NFYA; NbExp=5; IntAct=EBI-398920, EBI-389739;
CC Q07955; Q9UBU9: NXF1; NbExp=5; IntAct=EBI-398920, EBI-398874;
CC Q07955; Q14684: RRP1B; NbExp=6; IntAct=EBI-398920, EBI-372051;
CC Q07955; P08621: SNRNP70; NbExp=3; IntAct=EBI-398920, EBI-1049228;
CC Q07955; Q96SB4: SRPK1; NbExp=3; IntAct=EBI-398920, EBI-539478;
CC Q07955; P62995: TRA2B; NbExp=3; IntAct=EBI-398920, EBI-725485;
CC Q07955; O00463: TRAF5; NbExp=2; IntAct=EBI-398920, EBI-523498;
CC Q07955; Q01081: U2AF1; NbExp=4; IntAct=EBI-398920, EBI-632461;
CC Q07955; O70551: Srpk1; Xeno; NbExp=5; IntAct=EBI-398920, EBI-593343;
CC Q07955; O54781: Srpk2; Xeno; NbExp=3; IntAct=EBI-398920, EBI-593325;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12215544,
CC ECO:0000269|PubMed:20308322, ECO:0000269|PubMed:24449914,
CC ECO:0000269|PubMed:9420331}. Nucleus speckle
CC {ECO:0000269|PubMed:12215544, ECO:0000269|PubMed:20308322,
CC ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24644279,
CC ECO:0000269|PubMed:9420331}. Note=In nuclear speckles. Shuttles between
CC the nucleus and the cytoplasm (PubMed:12215544, PubMed:20308322,
CC PubMed:9420331, PubMed:24449914). Nuclear import is mediated via
CC interaction with TNPO3 (PubMed:24449914). {ECO:0000269|PubMed:12215544,
CC ECO:0000269|PubMed:20308322, ECO:0000269|PubMed:24449914,
CC ECO:0000269|PubMed:9420331}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=ASF-1;
CC IsoId=Q07955-1; Sequence=Displayed;
CC Name=ASF-2;
CC IsoId=Q07955-2; Sequence=VSP_005856;
CC Name=ASF-3;
CC IsoId=Q07955-3; Sequence=VSP_005857, VSP_005858;
CC -!- DOMAIN: The RRM 2 domain plays an important role in governing both the
CC binding mode and the phosphorylation mechanism of the RS domain by
CC SRPK1. RS domain and RRM 2 are uniquely positioned to initiate a highly
CC directional (C-terminus to N-terminus) phosphorylation reaction in
CC which the RS domain slides through an extended electronegative channel
CC separating the docking groove of SRPK1 and the active site. RRM 2 binds
CC toward the periphery of the active site and guides the directional
CC phosphorylation mechanism. Both the RS domain and an RRM domain are
CC required for nucleocytoplasmic shuttling.
CC {ECO:0000269|PubMed:18342604}.
CC -!- PTM: Phosphorylated by CLK1, CLK2, CLK3 and CLK4. Phosphorylated by
CC SRPK1 at multiple serines in its RS domain via a directional (C-
CC terminal to N-terminal) and a dual-track mechanism incorporating both
CC processive phosphorylation (in which the kinase stays attached to the
CC substrate after each round of phosphorylation) and distributive
CC phosphorylation steps (in which the kinase and substrate dissociate
CC after each phosphorylation event). The RS domain of SRSF1 binds to a
CC docking groove in the large lobe of the kinase domain of SRPK1 and this
CC induces certain structural changes in SRPK1 and/or RRM 2 domain of
CC SRSF1, allowing RRM 2 to bind the kinase and initiate phosphorylation.
CC The cycles continue for several phosphorylation steps in a processive
CC manner (steps 1-8) until the last few phosphorylation steps
CC (approximately steps 9-12). During that time, a mechanical stress
CC induces the unfolding of the beta-4 motif in RRM 2, which then docks at
CC the docking groove of SRPK1. This also signals RRM 2 to begin to
CC dissociate, which facilitates SRSF1 dissociation after phosphorylation
CC is completed. {ECO:0000269|PubMed:14555757,
CC ECO:0000269|PubMed:18155240, ECO:0000269|PubMed:18687337,
CC ECO:0000269|PubMed:19477182, ECO:0000269|PubMed:19886675}.
CC -!- PTM: Asymmetrically dimethylated at arginines, probably by PRMT1,
CC methylation promotes localization to nuclear speckles.
CC {ECO:0000269|PubMed:20308322}.
CC -!- MISCELLANEOUS: [Isoform ASF-3]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SRSF1ID47631ch17q22.html";
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DR EMBL; M72709; AAA35565.1; -; mRNA.
DR EMBL; M72709; AAA35564.1; -; mRNA.
DR EMBL; M69040; AAA03476.1; -; mRNA.
DR EMBL; AB062124; BAB93456.1; -; mRNA.
DR EMBL; AK312781; BAG35644.1; -; mRNA.
DR EMBL; CH471109; EAW94485.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94486.1; -; Genomic_DNA.
DR EMBL; BC010264; AAH10264.1; -; mRNA.
DR EMBL; BC033785; AAH33785.1; -; mRNA.
DR CCDS; CCDS11600.1; -. [Q07955-1]
DR CCDS; CCDS58580.1; -. [Q07955-3]
DR PIR; A40040; A40040.
DR PIR; B40040; B40040.
DR PIR; C40040; C40040.
DR RefSeq; NP_001071634.1; NM_001078166.1. [Q07955-3]
DR RefSeq; NP_008855.1; NM_006924.4. [Q07955-1]
DR PDB; 1X4A; NMR; -; A=1-96.
DR PDB; 2M7S; NMR; -; A=106-195.
DR PDB; 2M8D; NMR; -; B=107-196.
DR PDB; 2O3D; NMR; -; A=107-215.
DR PDB; 3BEG; X-ray; 2.90 A; B=105-219.
DR PDB; 4C0O; X-ray; 2.56 A; C/D=106-230.
DR PDB; 6HPJ; NMR; -; B=1-97.
DR PDB; 7ABG; EM; 7.80 A; A6=1-248.
DR PDBsum; 1X4A; -.
DR PDBsum; 2M7S; -.
DR PDBsum; 2M8D; -.
DR PDBsum; 2O3D; -.
DR PDBsum; 3BEG; -.
DR PDBsum; 4C0O; -.
DR PDBsum; 6HPJ; -.
DR PDBsum; 7ABG; -.
DR AlphaFoldDB; Q07955; -.
DR BMRB; Q07955; -.
DR SMR; Q07955; -.
DR BioGRID; 112324; 473.
DR CORUM; Q07955; -.
DR DIP; DIP-2155N; -.
DR IntAct; Q07955; 119.
DR MINT; Q07955; -.
DR STRING; 9606.ENSP00000258962; -.
DR ChEMBL; CHEMBL4295805; -.
DR DrugBank; DB09130; Copper.
DR GlyGen; Q07955; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q07955; -.
DR PhosphoSitePlus; Q07955; -.
DR SwissPalm; Q07955; -.
DR BioMuta; SRSF1; -.
DR DMDM; 730773; -.
DR EPD; Q07955; -.
DR jPOST; Q07955; -.
DR MassIVE; Q07955; -.
DR MaxQB; Q07955; -.
DR PaxDb; Q07955; -.
DR PeptideAtlas; Q07955; -.
DR PRIDE; Q07955; -.
DR ProteomicsDB; 58560; -. [Q07955-1]
DR ProteomicsDB; 58561; -. [Q07955-2]
DR ProteomicsDB; 58562; -. [Q07955-3]
DR TopDownProteomics; Q07955-1; -. [Q07955-1]
DR TopDownProteomics; Q07955-2; -. [Q07955-2]
DR TopDownProteomics; Q07955-3; -. [Q07955-3]
DR Antibodypedia; 4585; 315 antibodies from 35 providers.
DR DNASU; 6426; -.
DR Ensembl; ENST00000258962.5; ENSP00000258962.4; ENSG00000136450.13. [Q07955-1]
DR Ensembl; ENST00000581979.5; ENSP00000463223.1; ENSG00000136450.13. [Q07955-3]
DR Ensembl; ENST00000582730.6; ENSP00000462215.1; ENSG00000136450.13. [Q07955-3]
DR GeneID; 6426; -.
DR KEGG; hsa:6426; -.
DR MANE-Select; ENST00000258962.5; ENSP00000258962.4; NM_006924.5; NP_008855.1.
DR UCSC; uc002ivi.4; human. [Q07955-1]
DR CTD; 6426; -.
DR DisGeNET; 6426; -.
DR GeneCards; SRSF1; -.
DR HGNC; HGNC:10780; SRSF1.
DR HPA; ENSG00000136450; Low tissue specificity.
DR MIM; 600812; gene.
DR neXtProt; NX_Q07955; -.
DR OpenTargets; ENSG00000136450; -.
DR PharmGKB; PA35696; -.
DR VEuPathDB; HostDB:ENSG00000136450; -.
DR eggNOG; KOG0105; Eukaryota.
DR GeneTree; ENSGT00940000155585; -.
DR HOGENOM; CLU_012062_34_5_1; -.
DR InParanoid; Q07955; -.
DR OMA; TIAEYDC; -.
DR OrthoDB; 1321443at2759; -.
DR PhylomeDB; Q07955; -.
DR TreeFam; TF106261; -.
DR PathwayCommons; Q07955; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR SignaLink; Q07955; -.
DR SIGNOR; Q07955; -.
DR BioGRID-ORCS; 6426; 803 hits in 1087 CRISPR screens.
DR ChiTaRS; SRSF1; human.
DR EvolutionaryTrace; Q07955; -.
DR GeneWiki; ASF/SF2; -.
DR GenomeRNAi; 6426; -.
DR Pharos; Q07955; Tbio.
DR PRO; PR:Q07955; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q07955; protein.
DR Bgee; ENSG00000136450; Expressed in ganglionic eminence and 175 other tissues.
DR ExpressionAtlas; Q07955; baseline and differential.
DR Genevisible; Q07955; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0044547; F:DNA topoisomerase binding; IPI:CAFA.
DR GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IDA:GO_Central.
DR GO; GO:0000395; P:mRNA 5'-splice site recognition; IDA:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0006376; P:mRNA splice site selection; TAS:ProtInc.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR CDD; cd12597; RRM1_SRSF1; 1.
DR DisProt; DP01641; -.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034520; SRSF1_RRM1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Methylation; mRNA processing;
KW mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding; Spliceosome; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CHAIN 2..248
FT /note="Serine/arginine-rich splicing factor 1"
FT /id="PRO_0000081911"
FT DOMAIN 16..91
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 121..195
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 88..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..247
FT /note="Interaction with SAFB1"
FT COMPBIAS 205..225
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 38
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 93
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:20308322"
FT MOD_RES 93
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 97
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:20308322"
FT MOD_RES 97
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 109
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000269|PubMed:20308322"
FT MOD_RES 109
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 111
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24449914,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 202
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24449914"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24449914"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 30
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 38
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 VAR_SEQ 185..248
FT /note="GETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPR
FT YSPRHSRSRSRT -> FCLSNREKLPTSGLKLMGPEVQVMEDLDLEAVVVAEAVAEATA
FT GVAVTPQGEAEDHHAILPVIADLALVHKMIGDTFCRTHVVYSFPLFSTIFSFFNSNCFV
FT QNGLKC (in isoform ASF-2)"
FT /evidence="ECO:0000303|PubMed:1855257"
FT /id="VSP_005856"
FT VAR_SEQ 185..201
FT /note="GETAYIRVKVDGPRSPS -> VGYTRILFFDQNWIQWS (in isoform
FT ASF-3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005857"
FT VAR_SEQ 202..248
FT /note="Missing (in isoform ASF-3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005858"
FT VARIANT 89
FT /note="P -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035488"
FT MUTAGEN 58..59
FT /note="FV->SR: In FV1; loss of ability to activate
FT splicing. Slight reduction in splice site switching
FT activity and no effect on RNA-binding."
FT /evidence="ECO:0000269|PubMed:8223481"
FT MUTAGEN 93
FT /note="R->A: Predominantly localizes to cytoplasm and fails
FT to modulate splicing of endogenous pre-mRNAs; when
FT associated with Ala-97 and Ala-109."
FT /evidence="ECO:0000269|PubMed:20308322"
FT MUTAGEN 97
FT /note="R->A: Predominantly localizes to cytoplasm and fails
FT to modulate splicing of endogenous pre-mRNAs; when
FT associated with Ala-93 and Ala-109."
FT /evidence="ECO:0000269|PubMed:20308322"
FT MUTAGEN 109
FT /note="R->A: Predominantly localizes to cytoplasm and fails
FT to modulate splicing of endogenous pre-mRNAs; when
FT associated with Ala-93 and Ala-97."
FT /evidence="ECO:0000269|PubMed:20308322"
FT MUTAGEN 162..163
FT /note="FV->SR: In FV2; loss of ability to activate
FT splicing. Great reduction in splice site switching activity
FT and RNA-binding."
FT /evidence="ECO:0000269|PubMed:8223481"
FT MUTAGEN 162
FT /note="F->A: In AV; loss of ability to activate splicing.
FT Great reduction in splice site switching activity and no
FT effect on RNA-binding."
FT /evidence="ECO:0000269|PubMed:9420331"
FT MUTAGEN 162
FT /note="F->D: Reduced nucleocytoplasmic shuttling; when
FT associated with D-190."
FT /evidence="ECO:0000269|PubMed:9420331"
FT MUTAGEN 180
FT /note="F->D: Reduced nucleocytoplasmic shuttling; when
FT associated with D-162."
FT /evidence="ECO:0000269|PubMed:9420331"
FT MUTAGEN 182..248
FT /note="Missing: In MR-B; strongly inhibits splicing."
FT /evidence="ECO:0000269|PubMed:8223481"
FT MUTAGEN 182..199
FT /note="Missing: In MR-E; loss of ability to activate
FT splicing."
FT /evidence="ECO:0000269|PubMed:8223481"
FT MUTAGEN 192..248
FT /note="Missing: In MR-A; loss of ability to activate
FT splicing."
FT /evidence="ECO:0000269|PubMed:8223481"
FT MUTAGEN 192..199
FT /note="Missing: In MR-D; loss of ability to activate
FT splicing."
FT /evidence="ECO:0000269|PubMed:8223481"
FT MUTAGEN 199..224
FT /note="Missing: In RS-A; loss of ability to activate
FT splicing but retains splice site switching."
FT /evidence="ECO:0000269|PubMed:8223481"
FT MUTAGEN 215..248
FT /note="Missing: In RS-C; loss of ability to activate
FT splicing but retains splice site switching."
FT /evidence="ECO:0000269|PubMed:8223481"
FT MUTAGEN 226..248
FT /note="Missing: In RS-B; retains both splice activation and
FT splice site switching activity."
FT /evidence="ECO:0000269|PubMed:8223481"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6HPJ"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:1X4A"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:1X4A"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1X4A"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:1X4A"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1X4A"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:1X4A"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:1X4A"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:1X4A"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:2M8D"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:4C0O"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:4C0O"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3BEG"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:4C0O"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:4C0O"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:4C0O"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:4C0O"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:4C0O"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:2M7S"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:4C0O"
FT STRAND 191..197
FT /evidence="ECO:0007829|PDB:4C0O"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:4C0O"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:2O3D"
SQ SEQUENCE 248 AA; 27745 MW; C28A0B2F112EA713 CRC64;
MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE
FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE
NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF
RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR
HSRSRSRT
