SF01_HUMAN
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 03-AUG-2022, entry version 218.
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};
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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_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 PDBsum; 1K1G; -.
DR PDBsum; 1O0P; -.
DR PDBsum; 1OPI; -.
DR PDBsum; 2M09; -.
DR PDBsum; 2M0G; -.
DR PDBsum; 4FXW; -.
DR PDBsum; 4FXX; -.
DR AlphaFoldDB; Q15637; -.
DR BMRB; Q15637; -.
DR SMR; Q15637; -.
DR BioGRID; 113368; 271.
DR ComplexPortal; CPX-1074; SF1-U2AF65 splicing factor complex.
DR CORUM; Q15637; -.
DR DIP; DIP-29410N; -.
DR ELM; Q15637; -.
DR IntAct; Q15637; 228.
DR MINT; Q15637; -.
DR STRING; 9606.ENSP00000366604; -.
DR DrugBank; DB11638; Artenimol.
DR MoonDB; Q15637; Predicted.
DR GlyGen; Q15637; 9 sites, 2 O-linked glycans (9 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; Q15637; -.
DR PeptideAtlas; Q15637; -.
DR PRIDE; 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 TopDownProteomics; Q15637-4; -. [Q15637-4]
DR Antibodypedia; 15586; 428 antibodies from 32 providers.
DR DNASU; 7536; -.
DR Ensembl; ENST00000227503.13; ENSP00000227503.9; ENSG00000168066.21. [Q15637-4]
DR Ensembl; ENST00000334944.9; ENSP00000334414.5; ENSG00000168066.21. [Q15637-2]
DR Ensembl; ENST00000377387.5; ENSP00000366604.1; ENSG00000168066.21. [Q15637-5]
DR Ensembl; ENST00000377390.8; ENSP00000366607.3; ENSG00000168066.21. [Q15637-1]
DR Ensembl; ENST00000377394.7; ENSP00000366611.3; ENSG00000168066.21. [Q15637-6]
DR Ensembl; ENST00000433274.6; ENSP00000396793.2; ENSG00000168066.21. [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 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; GAAPWHQ; -.
DR OrthoDB; 887669at2759; -.
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; 819 hits in 1094 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 210 other tissues.
DR ExpressionAtlas; Q15637; baseline and differential.
DR Genevisible; Q15637; HS.
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:0045131; F:pre-mRNA branch point binding; IEA:InterPro.
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; IC:HGNC-UCL.
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 DisProt; DP01449; -.
DR Gene3D; 3.30.1370.10; -; 1.
DR IDEAL; IID00247; -.
DR InterPro; IPR045071; BBP-like.
DR InterPro; IPR031150; BBP/SF1.
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; IPR001878; Znf_CCHC.
DR PANTHER; PTHR11208; PTHR11208; 1.
DR PANTHER; PTHR11208:SF45; PTHR11208:SF45; 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; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
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 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
