ID SF01_HUMAN Reviewed; 639 AA. AC Q15637; B7Z1Q1; C9JJE2; Q14818; Q14819; Q15913; Q8IY00; Q92744; Q92745; AC Q969H7; Q9BW01; Q9UEI0; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 227. DE RecName: Full=Splicing factor 1; DE AltName: Full=Mammalian branch point-binding protein; DE Short=BBP; DE Short=mBBP; DE AltName: Full=Transcription factor ZFM1; DE AltName: Full=Zinc finger gene in MEN1 locus; DE AltName: Full=Zinc finger protein 162; GN Name=SF1; Synonyms=ZFM1, ZNF162; 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 1 AND 2), PROTEIN SEQUENCE OF 20-30 RP AND 136-150, VARIANT THR-357, FUNCTION, INTERACTION WITH U1 SNRNA, AND RP RNA-BINDING. RC TISSUE=Bone, and Cervix carcinoma; RX PubMed=8752089; RA Arning S., Grueter P., Bilbe G., Kraemer A.; RT "Mammalian splicing factor SF1 is encoded by variant cDNAs and binds to RT RNA."; RL RNA 2:794-810(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6). RC TISSUE=Myeloid leukemia cell; RX PubMed=9192847; DOI=10.1006/geno.1997.4705; RA Caslini C., Spinelli O., Cazzaniga G., Golay J., De Gioia L., Pedretti A., RA Breviario F., Amaru R., Barbui T., Biondi A., Introna M., Rambaldi A.; RT "Identification of two novel isoforms of the ZNF162 gene: a growing family RT of signal transduction and activator of RNA proteins."; RL Genomics 42:268-277(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND TISSUE SPECIFICITY. RC TISSUE=Brain cortex, Cerebellum, and Fetal liver; RX PubMed=7912130; DOI=10.1093/hmg/3.3.465; RA Toda T., Iida A., Miwa T., Nakamura Y., Imai T.; RT "Isolation and characterization of a novel gene encoding nuclear protein at RT a locus (D11S636) tightly linked to multiple endocrine neoplasia type 1 RT (MEN1)."; RL Hum. Mol. Genet. 3:465-470(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5). RC TISSUE=Brain, Eye, Kidney, Muscle, 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-295. RX PubMed=9573336; DOI=10.1016/s0378-1119(98)00058-4; RA Kraemer A., Quentin M., Mulhauser F.; RT "Diverse modes of alternative splicing of human splicing factor SF1 deduced RT from the exon-intron structure of the gene."; RL Gene 211:29-37(1998). RN [8] RP PROTEIN SEQUENCE OF 2-15, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=T-cell; RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.; RL Submitted (MAY-2006) to UniProtKB. RN [9] RP PROTEIN SEQUENCE OF 19-28; 94-103; 228-239 AND 298-308, FUNCTION, RP INTERACTION WITH U2AF2, MUTAGENESIS OF SER-20, AND PHOSPHORYLATION AT RP SER-20. RX PubMed=10449420; DOI=10.1093/emboj/18.16.4549; RA Wang X., Bruderer S., Rafi Z., Xue J., Milburn P.J., Kraemer A., RA Robinson P.J.; RT "Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein RT kinase regulates spliceosome assembly."; RL EMBO J. 18:4549-4559(1999). RN [10] RP PROTEIN SEQUENCE OF 110-135, IDENTIFICATION BY MASS SPECTROMETRY, AND RP INTERACTION WITH THE SPLICEOSOME. RX PubMed=12176931; DOI=10.1101/gr.473902; RA Rappsilber J., Ryder U., Lamond A.I., Mann M.; RT "Large-scale proteomic analysis of the human spliceosome."; RL Genome Res. 12:1231-1245(2002). RN [11] RP FUNCTION, AND INTERACTION WITH EWSR1; FUS AND TAF15. RX PubMed=9660765; DOI=10.1074/jbc.273.29.18086; RA Zhang D., Paley A.J., Childs G.; RT "The transcriptional repressor ZFM1 interacts with and modulates the RT ability of EWS to activate transcription."; RL J. Biol. Chem. 273:18086-18091(1998). RN [12] 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 (ISOFORM 6), 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 [14] RP INTERACTION WITH RBM17. RX PubMed=17589525; DOI=10.1038/nsmb1260; RA Corsini L., Bonnal S., Basquin J., Hothorn M., Scheffzek K., Valcarcel J., RA Sattler M.; RT "U2AF-homology motif interactions are required for alternative splicing RT regulation by SPF45."; RL Nat. Struct. Mol. Biol. 14:620-629(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 (ISOFORM 6), AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 (ISOFORM 6), 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 [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] 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 [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=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 [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-80 AND SER-82, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-87 AND SER-89, 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 [26] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-467 (ISOFORM 6), AND RP 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 [27] RP STRUCTURE BY NMR OF 133-255 IN COMPLEX WITH THE BRANCH SITE SEQUENCE RP 5'-UAUACUAACAA-3', AND MUTAGENESIS OF ASN-151; ARG-160; LYS-184; LEU-244; RP LEU-247; LEU-254 AND ARG-255. RX PubMed=11691992; DOI=10.1126/science.1064719; RA Liu Z., Luyten I., Bottomley M.J., Messias A.C., Houngninou-Molango S., RA Sprangers R., Zanier K., Kraemer A., Sattler M.; RT "Structural basis for recognition of the intron branch site RNA by splicing RT factor 1."; RL Science 294:1098-1102(2001). RN [28] RP STRUCTURE BY NMR OF 13-25 IN COMPLEX WITH U2AF2, AND MUTAGENESIS OF RP 16-LYS--ARG-18; 17-LYS-LYS-18; ARG-21 AND TRP-22. RX PubMed=12718882; DOI=10.1016/s1097-2765(03)00115-1; RA Selenko P., Gregorovic G., Sprangers R., Stier G., Rhani Z., Kraemer A., RA Sattler M.; RT "Structural basis for the molecular recognition between human splicing RT factors U2AF65 and SF1/mBBP."; RL Mol. Cell 11:965-976(2003). CC -!- FUNCTION: Necessary for the ATP-dependent first step of spliceosome CC assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' CC of the pre-mRNA. May act as transcription repressor. CC {ECO:0000269|PubMed:10449420, ECO:0000269|PubMed:8752089, CC ECO:0000269|PubMed:9660765}. CC -!- SUBUNIT: Binds U2AF2. Interacts with U1 snRNA. Binds EWSR1, FUS and CC TAF15. Interacts with RBM17. {ECO:0000269|PubMed:10449420, CC ECO:0000269|PubMed:11691992, ECO:0000269|PubMed:12176931, CC ECO:0000269|PubMed:12718882, ECO:0000269|PubMed:17589525, CC ECO:0000269|PubMed:8752089, ECO:0000269|PubMed:9660765}. CC -!- INTERACTION: CC Q15637; P42684: ABL2; NbExp=3; IntAct=EBI-744603, EBI-1102694; CC Q15637; O60308: CEP104; NbExp=4; IntAct=EBI-744603, EBI-2685240; CC Q15637; Q8IWX8: CHERP; NbExp=6; IntAct=EBI-744603, EBI-2555370; CC Q15637; O76071: CIAO1; NbExp=3; IntAct=EBI-744603, EBI-725145; CC Q15637; Q92841: DDX17; NbExp=4; IntAct=EBI-744603, EBI-746012; CC Q15637; P17844: DDX5; NbExp=3; IntAct=EBI-744603, EBI-351962; CC Q15637; Q92567: FAM168A; NbExp=4; IntAct=EBI-744603, EBI-7957930; CC Q15637; Q99729: HNRNPAB; NbExp=4; IntAct=EBI-744603, EBI-1044873; CC Q15637; O14979: HNRNPDL; NbExp=4; IntAct=EBI-744603, EBI-299727; CC Q15637; Q7Z7F0: KHDC4; NbExp=5; IntAct=EBI-744603, EBI-751942; CC Q15637; P52294: KPNA1; NbExp=3; IntAct=EBI-744603, EBI-358383; CC Q15637; P52292: KPNA2; NbExp=5; IntAct=EBI-744603, EBI-349938; CC Q15637; O60684: KPNA6; NbExp=4; IntAct=EBI-744603, EBI-359923; CC Q15637; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-744603, EBI-3957672; CC Q15637; Q13064: MKRN3; NbExp=3; IntAct=EBI-744603, EBI-2340269; CC Q15637; P55345: PRMT2; NbExp=5; IntAct=EBI-744603, EBI-78458; CC Q15637; O75400: PRPF40A; NbExp=3; IntAct=EBI-744603, EBI-473291; CC Q15637; P25788: PSMA3; NbExp=3; IntAct=EBI-744603, EBI-348380; CC Q15637; Q96I25: RBM17; NbExp=8; IntAct=EBI-744603, EBI-740272; CC Q15637; Q15637: SF1; NbExp=3; IntAct=EBI-744603, EBI-744603; CC Q15637; Q15459: SF3A1; NbExp=8; IntAct=EBI-744603, EBI-1054743; CC Q15637; Q15428: SF3A2; NbExp=2; IntAct=EBI-744603, EBI-2462271; CC Q15637; Q12872: SFSWAP; NbExp=2; IntAct=EBI-744603, EBI-1055938; CC Q15637; Q86WT6: TRIM69; NbExp=3; IntAct=EBI-744603, EBI-749955; CC Q15637; P26368: U2AF2; NbExp=22; IntAct=EBI-744603, EBI-742339; CC Q15637; Q8TAS1: UHMK1; NbExp=4; IntAct=EBI-744603, EBI-1753608; CC Q15637; Q80V31: Cep104; Xeno; NbExp=3; IntAct=EBI-744603, EBI-11073001; CC Q15637; Q8CGZ0: Cherp; Xeno; NbExp=3; IntAct=EBI-744603, EBI-2366446; CC Q15637; Q68FD5: Cltc; Xeno; NbExp=3; IntAct=EBI-744603, EBI-769168; CC Q15637; Q3TCX3: Khdc4; Xeno; NbExp=3; IntAct=EBI-744603, EBI-11298408; CC Q15637; Q60960: Kpna1; Xeno; NbExp=3; IntAct=EBI-744603, EBI-8573008; CC Q15637; P52293: Kpna2; Xeno; NbExp=3; IntAct=EBI-744603, EBI-3043908; CC Q15637; O35343: Kpna4; Xeno; NbExp=3; IntAct=EBI-744603, EBI-8372758; CC Q15637; Q3USH5: Sfswap; Xeno; NbExp=3; IntAct=EBI-744603, EBI-8387273; CC Q15637; P26369: U2af2; Xeno; NbExp=3; IntAct=EBI-744603, EBI-8321355; CC Q15637-4; P54253: ATXN1; NbExp=3; IntAct=EBI-12223157, EBI-930964; CC Q15637-4; O43639: NCK2; NbExp=3; IntAct=EBI-12223157, EBI-713635; CC Q15637-4; Q9UHX1-2: PUF60; NbExp=3; IntAct=EBI-12223157, EBI-11529177; CC Q15637-4; Q96I25: RBM17; NbExp=3; IntAct=EBI-12223157, EBI-740272; CC Q15637-4; Q15436: SEC23A; NbExp=3; IntAct=EBI-12223157, EBI-81088; CC Q15637-4; O14787-2: TNPO2; NbExp=3; IntAct=EBI-12223157, EBI-12076664; CC Q15637-4; Q9NX01: TXNL4B; NbExp=3; IntAct=EBI-12223157, EBI-10309345; CC Q15637-4; P26368-2: U2AF2; NbExp=5; IntAct=EBI-12223157, EBI-11097439; CC Q15637-4; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-12223157, EBI-607755; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=SF1-HL1; CC IsoId=Q15637-1; Sequence=Displayed; CC Name=2; Synonyms=SF1-Bo, Bone; CC IsoId=Q15637-2; Sequence=VSP_008839; CC Name=3; Synonyms=ZFM1-A, ZFM1-ABCDEF; CC IsoId=Q15637-3; Sequence=VSP_008838; CC Name=4; Synonyms=ZFM1-B, ZFM1-ABCDF; CC IsoId=Q15637-4; Sequence=VSP_008835, VSP_008836; CC Name=5; CC IsoId=Q15637-5; Sequence=VSP_008833, VSP_008835, VSP_008836; CC Name=6; Synonyms=ZFM1-D, B6; CC IsoId=Q15637-6; Sequence=VSP_008834, VSP_008837; CC Name=7; CC IsoId=Q15637-7; Sequence=VSP_045274; CC -!- TISSUE SPECIFICITY: Detected in lung, ovary, adrenal gland, colon, CC kidney, muscle, pancreas, thyroid, placenta, brain, liver and heart. CC {ECO:0000269|PubMed:7912130}. CC -!- PTM: Phosphorylation on Ser-20 interferes with U2AF2 binding and CC spliceosome assembly. Isoform 6 is phosphorylated on Ser-463. CC {ECO:0000269|PubMed:10449420}. CC -!- SIMILARITY: Belongs to the BBP/SF1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH00773.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y08765; CAA70018.1; -; mRNA. DR EMBL; Y08766; CAA70019.1; -; mRNA. DR EMBL; L49345; AAB03514.1; -; mRNA. DR EMBL; L49380; AAB04033.1; -; mRNA. DR EMBL; D26120; BAA05116.1; -; mRNA. DR EMBL; D26120; BAA05117.1; -; mRNA. DR EMBL; AK293753; BAH11587.1; -; mRNA. DR EMBL; AP001462; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000773; AAH00773.1; ALT_INIT; mRNA. DR EMBL; BC008080; AAH08080.1; -; mRNA. DR EMBL; BC008724; AAH08724.1; -; mRNA. DR EMBL; BC011657; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC020217; AAH20217.1; -; mRNA. DR EMBL; BC038446; AAH38446.1; -; mRNA. DR EMBL; AJ000051; CAA03883.1; -; Genomic_DNA. DR EMBL; AJ000052; CAA03883.1; JOINED; Genomic_DNA. DR CCDS; CCDS31599.1; -. [Q15637-1] DR CCDS; CCDS44642.2; -. [Q15637-6] DR CCDS; CCDS53660.1; -. [Q15637-7] DR CCDS; CCDS53661.1; -. [Q15637-5] DR CCDS; CCDS8080.1; -. [Q15637-2] DR CCDS; CCDS8081.1; -. [Q15637-4] DR PIR; G02919; G02919. DR RefSeq; NP_001171501.1; NM_001178030.1. [Q15637-5] DR RefSeq; NP_001171502.1; NM_001178031.2. [Q15637-7] DR RefSeq; NP_001333292.1; NM_001346363.1. DR RefSeq; NP_001333293.1; NM_001346364.1. DR RefSeq; NP_004621.2; NM_004630.3. [Q15637-1] DR RefSeq; NP_973724.1; NM_201995.2. [Q15637-2] DR RefSeq; NP_973726.2; NM_201997.2. [Q15637-6] DR RefSeq; NP_973727.1; NM_201998.2. [Q15637-4] DR RefSeq; XP_016873733.1; XM_017018244.1. DR PDB; 1K1G; NMR; -; A=133-260. DR PDB; 1O0P; NMR; -; B=13-25. DR PDB; 1OPI; NMR; -; B=13-25. DR PDB; 2M09; NMR; -; A=27-145. DR PDB; 2M0G; NMR; -; A=1-145. DR PDB; 4FXW; X-ray; 2.29 A; B/D=14-132. DR PDB; 4FXX; X-ray; 2.48 A; A/B/C/D=26-132. DR PDB; 7VH9; NMR; -; A=296-327. DR PDB; 7VPX; EM; 3.00 A; D=1-639. DR PDBsum; 1K1G; -. DR PDBsum; 1O0P; -. DR PDBsum; 1OPI; -. DR PDBsum; 2M09; -. DR PDBsum; 2M0G; -. DR PDBsum; 4FXW; -. DR PDBsum; 4FXX; -. DR PDBsum; 7VH9; -. DR PDBsum; 7VPX; -. DR AlphaFoldDB; Q15637; -. DR BMRB; Q15637; -. DR EMDB; EMD-32074; -. DR SMR; Q15637; -. DR BioGRID; 113368; 321. DR ComplexPortal; CPX-1074; SF1-U2AF65 splicing factor complex. DR CORUM; Q15637; -. DR DIP; DIP-29410N; -. DR ELM; Q15637; -. DR IntAct; Q15637; 232. DR MINT; Q15637; -. DR STRING; 9606.ENSP00000366604; -. DR DrugBank; DB11638; Artenimol. DR MoonDB; Q15637; Predicted. DR GlyCosmos; Q15637; 9 sites, 2 glycans. DR GlyGen; Q15637; 10 sites, 2 O-linked glycans (10 sites). DR iPTMnet; Q15637; -. DR MetOSite; Q15637; -. DR PhosphoSitePlus; Q15637; -. DR SwissPalm; Q15637; -. DR BioMuta; SF1; -. DR DMDM; 38258418; -. DR EPD; Q15637; -. DR jPOST; Q15637; -. DR MassIVE; Q15637; -. DR MaxQB; Q15637; -. DR PaxDb; 9606-ENSP00000366604; -. DR PeptideAtlas; Q15637; -. DR ProteomicsDB; 10457; -. DR ProteomicsDB; 60669; -. [Q15637-1] DR ProteomicsDB; 60670; -. [Q15637-2] DR ProteomicsDB; 60671; -. [Q15637-3] DR ProteomicsDB; 60672; -. [Q15637-4] DR ProteomicsDB; 60673; -. [Q15637-5] DR ProteomicsDB; 60674; -. [Q15637-6] DR Pumba; Q15637; -. DR TopDownProteomics; Q15637-4; -. [Q15637-4] DR Antibodypedia; 15586; 503 antibodies from 32 providers. DR DNASU; 7536; -. DR Ensembl; ENST00000227503.13; ENSP00000227503.9; ENSG00000168066.22. [Q15637-4] DR Ensembl; ENST00000334944.9; ENSP00000334414.5; ENSG00000168066.22. [Q15637-2] DR Ensembl; ENST00000377387.5; ENSP00000366604.1; ENSG00000168066.22. [Q15637-5] DR Ensembl; ENST00000377390.8; ENSP00000366607.3; ENSG00000168066.22. [Q15637-1] DR Ensembl; ENST00000377394.7; ENSP00000366611.3; ENSG00000168066.22. [Q15637-6] DR Ensembl; ENST00000433274.6; ENSP00000396793.2; ENSG00000168066.22. [Q15637-7] DR GeneID; 7536; -. DR KEGG; hsa:7536; -. DR MANE-Select; ENST00000377390.8; ENSP00000366607.3; NM_004630.4; NP_004621.2. DR UCSC; uc001oaz.3; human. [Q15637-1] DR AGR; HGNC:12950; -. DR CTD; 7536; -. DR DisGeNET; 7536; -. DR GeneCards; SF1; -. DR HGNC; HGNC:12950; SF1. DR HPA; ENSG00000168066; Low tissue specificity. DR MIM; 601516; gene. DR neXtProt; NX_Q15637; -. DR OpenTargets; ENSG00000168066; -. DR PharmGKB; PA37533; -. DR VEuPathDB; HostDB:ENSG00000168066; -. DR eggNOG; KOG0119; Eukaryota. DR GeneTree; ENSGT00940000157258; -. DR HOGENOM; CLU_016864_5_0_1; -. DR InParanoid; Q15637; -. DR OMA; KPWQQRG; -. DR OrthoDB; 1397at2759; -. DR PhylomeDB; Q15637; -. DR TreeFam; TF319159; -. DR PathwayCommons; Q15637; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q15637; -. DR SIGNOR; Q15637; -. DR BioGRID-ORCS; 7536; 856 hits in 1181 CRISPR screens. DR ChiTaRS; SF1; human. DR EvolutionaryTrace; Q15637; -. DR GeneWiki; SF1_(gene); -. DR GenomeRNAi; 7536; -. DR Pharos; Q15637; Tbio. DR PRO; PR:Q15637; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q15637; Protein. DR Bgee; ENSG00000168066; Expressed in right uterine tube and 212 other cell types or tissues. DR ExpressionAtlas; Q15637; baseline and differential. DR GO; GO:0016604; C:nuclear body; IEA:Ensembl. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005840; C:ribosome; NAS:UniProtKB. DR GO; GO:0005681; C:spliceosomal complex; IDA:HGNC-UCL. DR GO; GO:0089701; C:U2AF complex; IPI:ComplexPortal. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0033327; P:Leydig cell differentiation; IEA:Ensembl. DR GO; GO:0030238; P:male sex determination; IEA:Ensembl. DR GO; GO:0000389; P:mRNA 3'-splice site recognition; TAS:HGNC-UCL. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; NAS:ComplexPortal. DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IEA:Ensembl. DR GO; GO:0030575; P:nuclear body organization; IEA:Ensembl. DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:0050810; P:regulation of steroid biosynthetic process; IEA:Ensembl. DR GO; GO:0000245; P:spliceosomal complex assembly; NAS:UniProtKB. DR CDD; cd22382; KH-I_SF1; 1. DR DisProt; DP01449; -. DR Gene3D; 6.10.140.1790; -; 1. DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1. DR IDEAL; IID00247; -. DR InterPro; IPR045071; BBP-like. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR036612; KH_dom_type_1_sf. DR InterPro; IPR032570; SF1-HH. DR InterPro; IPR047086; SF1-HH_sf. DR InterPro; IPR001878; Znf_CCHC. DR PANTHER; PTHR11208; RNA-BINDING PROTEIN RELATED; 1. DR PANTHER; PTHR11208:SF45; SPLICING FACTOR 1; 1. DR Pfam; PF00013; KH_1; 1. DR Pfam; PF16275; SF1-HH; 1. DR Pfam; PF00098; zf-CCHC; 1. DR SMART; SM00322; KH; 1. DR SMART; SM00343; ZnF_C2HC; 1. DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1. DR PROSITE; PS50084; KH_TYPE_1; 1. DR PROSITE; PS50158; ZF_CCHC; 1. DR Genevisible; Q15637; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW Metal-binding; Methylation; mRNA processing; mRNA splicing; Nucleus; KW Phosphoprotein; Reference proteome; Repressor; RNA-binding; Spliceosome; KW Transcription; Transcription regulation; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT CHAIN 2..639 FT /note="Splicing factor 1" FT /id="PRO_0000050129" FT DOMAIN 141..222 FT /note="KH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT ZN_FING 277..296 FT /note="CCHC-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047" FT REGION 1..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 65..94 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 325..639 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 15..19 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 346..361 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 415..445 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 472..518 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 519..561 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 564..610 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 625..639 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 20 FT /note="Phosphoserine; by PKG" FT /evidence="ECO:0000269|PubMed:10449420" FT MOD_RES 80 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 82 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 87 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 89 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..26 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045274" FT VAR_SEQ 10 FT /note="L -> LGKLGPPGLPPLPGPKGGFEPGPPPAPGPGAGLLAPGPPPPPPVGSM FT GALTAAFPFAALPPPPPPPPPPPPQQPPPPPPPPSPGASYPPPQPPPPPPLYQRVSPPQ FT PPPPQPPRKDQQPGPAGGGG (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_008833" FT VAR_SEQ 448..548 FT /note="DQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSGQPPPPPSGPLPP FT WQQQQQQPPPPPPPSSSMASSTPLPWQQNTTTTTTSAGTGSIPPWQQQQ -> GKSVPG FT KYACGLWGLSPASRKRYDAATTYGHDA (in isoform 6)" FT /evidence="ECO:0000303|PubMed:9192847" FT /id="VSP_008834" FT VAR_SEQ 528..548 FT /note="NTTTTTTSAGTGSIPPWQQQQ -> RSLPAAAMARAMRVRTFRAHW (in FT isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7912130" FT /id="VSP_008835" FT VAR_SEQ 549..639 FT /note="Missing (in isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7912130" FT /id="VSP_008836" FT VAR_SEQ 555..639 FT /note="PGAPQMQGNPTMVPLPPGVQPPLPPGAPPPPPPPPPGSAGMMYAPPPPPPPP FT MDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN -> QWAAPTPSLWSSSPMATTAAAA FT SATPSAQQQYGFQYPLAMAAKIPPRGGDGPSHESEDFPRPLVTLPGRQPQQRPWWTGWF FT GKAA (in isoform 6)" FT /evidence="ECO:0000303|PubMed:9192847" FT /id="VSP_008837" FT VAR_SEQ 587..639 FT /note="PPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQ FT N -> RSIECLLCLLSLLTQLPLPLPKPGRQDPSPRRRWPEP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:7912130" FT /id="VSP_008838" FT VAR_SEQ 597..639 FT /note="YAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPPQN -> IPPRG FT GDGPSHESEDFPRPLVTLPGRQPQQRPWWTGWFGKAA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8752089" FT /id="VSP_008839" FT VARIANT 357 FT /note="S -> T" FT /evidence="ECO:0000269|PubMed:8752089" FT /id="VAR_017196" FT MUTAGEN 15..17 FT /note="KKR->EED: Abolishes interaction with U2AF2." FT MUTAGEN 16..18 FT /note="KRK->EDE: Abolishes interaction with U2AF2." FT /evidence="ECO:0000269|PubMed:12718882" FT MUTAGEN 20 FT /note="S->A: Strongly decreases interaction with U2AF2 and FT spliceosome assembly." FT /evidence="ECO:0000269|PubMed:10449420" FT MUTAGEN 20 FT /note="S->T: Decreases interaction with U2AF2." FT /evidence="ECO:0000269|PubMed:10449420" FT MUTAGEN 21 FT /note="R->A: Decreases interaction with U2AF2 and FT spliceosome assembly." FT /evidence="ECO:0000269|PubMed:12718882" FT MUTAGEN 21 FT /note="R->K: No effect." FT /evidence="ECO:0000269|PubMed:12718882" FT MUTAGEN 22 FT /note="W->A: Abolishes interaction with U2AF2." FT /evidence="ECO:0000269|PubMed:12718882" FT MUTAGEN 22 FT /note="W->F: No effect." FT /evidence="ECO:0000269|PubMed:12718882" FT MUTAGEN 151 FT /note="N->A: Decreases RNA-binding." FT /evidence="ECO:0000269|PubMed:11691992" FT MUTAGEN 160 FT /note="R->A: Strongly reduces RNA-binding." FT /evidence="ECO:0000269|PubMed:11691992" FT MUTAGEN 184 FT /note="K->A: Abolishes RNA-binding." FT /evidence="ECO:0000269|PubMed:11691992" FT MUTAGEN 244 FT /note="L->A: Decreases RNA-binding." FT /evidence="ECO:0000269|PubMed:11691992" FT MUTAGEN 247 FT /note="L->A: Decreases RNA-binding." FT /evidence="ECO:0000269|PubMed:11691992" FT MUTAGEN 254 FT /note="L->A: Slightly decreases RNA-binding." FT /evidence="ECO:0000269|PubMed:11691992" FT MUTAGEN 255 FT /note="R->A: Slightly decreases RNA-binding." FT /evidence="ECO:0000269|PubMed:11691992" FT CONFLICT 269 FT /note="E -> G (in Ref. 3; BAA05116/BAA05117)" FT /evidence="ECO:0000305" FT CONFLICT 348 FT /note="A -> R (in Ref. 2; AAB03514/AAB04033)" FT /evidence="ECO:0000305" FT CONFLICT 377 FT /note="R -> W (in Ref. 3; BAA05116/BAA05117)" FT /evidence="ECO:0000305" FT CONFLICT 570 FT /note="P -> L (in Ref. 4; BAH11587)" FT /evidence="ECO:0000305" FT CONFLICT 591 FT /note="G -> V (in Ref. 2; AAB04033)" FT /evidence="ECO:0000305" FT CONFLICT 623 FT /note="M -> I (in Ref. 2; AAB04033)" FT /evidence="ECO:0000305" FT STRAND 15..17 FT /evidence="ECO:0007829|PDB:1O0P" FT HELIX 27..30 FT /evidence="ECO:0007829|PDB:4FXX" FT HELIX 46..67 FT /evidence="ECO:0007829|PDB:4FXW" FT HELIX 76..79 FT /evidence="ECO:0007829|PDB:2M09" FT STRAND 93..95 FT /evidence="ECO:0007829|PDB:4FXW" FT HELIX 97..115 FT /evidence="ECO:0007829|PDB:4FXW" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:4FXW" FT STRAND 136..141 FT /evidence="ECO:0007829|PDB:1K1G" FT TURN 144..146 FT /evidence="ECO:0007829|PDB:1K1G" FT HELIX 150..157 FT /evidence="ECO:0007829|PDB:1K1G" FT STRAND 159..161 FT /evidence="ECO:0007829|PDB:1K1G" FT HELIX 162..170 FT /evidence="ECO:0007829|PDB:1K1G" FT STRAND 174..190 FT /evidence="ECO:0007829|PDB:1K1G" FT STRAND 203..211 FT /evidence="ECO:0007829|PDB:1K1G" FT HELIX 212..226 FT /evidence="ECO:0007829|PDB:1K1G" FT TURN 227..230 FT /evidence="ECO:0007829|PDB:1K1G" FT HELIX 238..244 FT /evidence="ECO:0007829|PDB:1K1G" FT HELIX 245..248 FT /evidence="ECO:0007829|PDB:1K1G" FT TURN 249..252 FT /evidence="ECO:0007829|PDB:1K1G" FT HELIX 305..320 FT /evidence="ECO:0007829|PDB:7VH9" FT MOD_RES Q15637-6:463 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648" FT MOD_RES Q15637-6:467 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" SQ SEQUENCE 639 AA; 68330 MW; EEBC6A02B29DAE4D CRC64; MATGANATPL DFPSKKRKRS RWNQDTMEQK TVIPGMPTVI PPGLTREQER AYIVQLQIED LTRKLRTGDL GIPPNPEDRS PSPEPIYNSE GKRLNTREFR TRKKLEEERH NLITEMVALN PDFKPPADYK PPATRVSDKV MIPQDEYPEI NFVGLLIGPR GNTLKNIEKE CNAKIMIRGK GSVKEGKVGR KDGQMLPGED EPLHALVTAN TMENVKKAVE QIRNILKQGI ETPEDQNDLR KMQLRELARL NGTLREDDNR ILRPWQSSET RSITNTTVCT KCGGAGHIAS DCKFQRPGDP QSAQDKARMD KEYLSLMAEL GEAPVPASVG STSGPATTPL ASAPRPAAPA NNPPPPSLMS TTQSRPPWMN SGPSESRPYH GMHGGGPGGP GGGPHSFPHP LPSLTGGHGG HPMQHNPNGP PPPWMQPPPP PMNQGPHPPG HHGPPPMDQY LGSTPVGSGV YRLHQGKGMM PPPPMGMMPP PPPPPSGQPP PPPSGPLPPW QQQQQQPPPP PPPSSSMASS TPLPWQQNTT TTTTSAGTGS IPPWQQQQAA AAASPGAPQM QGNPTMVPLP PGVQPPLPPG APPPPPPPPP GSAGMMYAPP PPPPPPMDPS NFVTMMGMGV AGMPPFGMPP APPPPPPQN //