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Splicing factor 1 (Mammalian branch point-binding protein) (BBP) (mBBP) (Transcription factor ZFM1) (Zinc finger gene in MEN1 locus) (Zinc finger protein 162)

 SF01_HUMAN              Reviewed;         639 AA.
Q15637; B7Z1Q1; C9JJE2; Q14818; Q14819; Q15913; Q8IY00; Q92744;
Q92745; Q969H7; Q9BW01; Q9UEI0;
07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
25-OCT-2017, entry version 186.
RecName: Full=Splicing factor 1;
AltName: Full=Mammalian branch point-binding protein;
Short=BBP;
Short=mBBP;
AltName: Full=Transcription factor ZFM1;
AltName: Full=Zinc finger gene in MEN1 locus;
AltName: Full=Zinc finger protein 162;
Name=SF1; Synonyms=ZFM1, ZNF162;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
20-30 AND 136-150, VARIANT THR-357, FUNCTION, INTERACTION WITH U1
SNRNA, AND RNA-BINDING.
TISSUE=Bone, and Cervix carcinoma;
PubMed=8752089;
Arning S., Grueter P., Bilbe G., Kraemer A.;
"Mammalian splicing factor SF1 is encoded by variant cDNAs and binds
to RNA.";
RNA 2:794-810(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6).
TISSUE=Myeloid leukemia cell;
PubMed=9192847; DOI=10.1006/geno.1997.4705;
Caslini C., Spinelli O., Cazzaniga G., Golay J., De Gioia L.,
Pedretti A., Breviario F., Amaru R., Barbui T., Biondi A., Introna M.,
Rambaldi A.;
"Identification of two novel isoforms of the ZNF162 gene: a growing
family of signal transduction and activator of RNA proteins.";
Genomics 42:268-277(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND TISSUE SPECIFICITY.
TISSUE=Brain cortex, Cerebellum, and Fetal liver;
PubMed=7912130; DOI=10.1093/hmg/3.3.465;
Toda T., Iida A., Miwa T., Nakamura Y., Imai T.;
"Isolation and characterization of a novel gene encoding nuclear
protein at a locus (D11S636) tightly linked to multiple endocrine
neoplasia type 1 (MEN1).";
Hum. Mol. Genet. 3:465-470(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
TISSUE=Brain, Eye, Kidney, Muscle, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-295.
PubMed=9573336; DOI=10.1016/S0378-1119(98)00058-4;
Kraemer A., Quentin M., Mulhauser F.;
"Diverse modes of alternative splicing of human splicing factor SF1
deduced from the exon-intron structure of the gene.";
Gene 211:29-37(1998).
[8]
PROTEIN SEQUENCE OF 2-15, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=T-cell;
Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
Submitted (MAY-2006) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 19-28; 94-103; 228-239 AND 298-308, FUNCTION,
INTERACTION WITH U2AF2, MUTAGENESIS OF SER-20, AND PHOSPHORYLATION AT
SER-20.
PubMed=10449420; DOI=10.1093/emboj/18.16.4549;
Wang X., Bruderer S., Rafi Z., Xue J., Milburn P.J., Kraemer A.,
Robinson P.J.;
"Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent
protein kinase regulates spliceosome assembly.";
EMBO J. 18:4549-4559(1999).
[10]
PROTEIN SEQUENCE OF 110-135, IDENTIFICATION BY MASS SPECTROMETRY, AND
INTERACTION WITH THE SPLICEOSOME.
PubMed=12176931; DOI=10.1101/gr.473902;
Rappsilber J., Ryder U., Lamond A.I., Mann M.;
"Large-scale proteomic analysis of the human spliceosome.";
Genome Res. 12:1231-1245(2002).
[11]
FUNCTION, AND INTERACTION WITH EWSR1; FUS AND TAF15.
PubMed=9660765; DOI=10.1074/jbc.273.29.18086;
Zhang D., Paley A.J., Childs G.;
"The transcriptional repressor ZFM1 interacts with and modulates the
ability of EWS to activate transcription.";
J. Biol. Chem. 273:18086-18091(1998).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 (ISOFORM 6), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
INTERACTION WITH RBM17.
PubMed=17589525; DOI=10.1038/nsmb1260;
Corsini L., Bonnal S., Basquin J., Hothorn M., Scheffzek K.,
Valcarcel J., Sattler M.;
"U2AF-homology motif interactions are required for alternative
splicing regulation by SPF45.";
Nat. Struct. Mol. Biol. 14:620-629(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 (ISOFORM 6), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 (ISOFORM 6), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-80 AND SER-82,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-87 AND SER-89, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-467 (ISOFORM 6), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[27]
STRUCTURE BY NMR OF 133-255 IN COMPLEX WITH THE BRANCH SITE SEQUENCE
5'-UAUACUAACAA-3', AND MUTAGENESIS OF ASN-151; ARG-160; LYS-184;
LEU-244; LEU-247; LEU-254 AND ARG-255.
PubMed=11691992; DOI=10.1126/science.1064719;
Liu Z., Luyten I., Bottomley M.J., Messias A.C.,
Houngninou-Molango S., Sprangers R., Zanier K., Kraemer A.,
Sattler M.;
"Structural basis for recognition of the intron branch site RNA by
splicing factor 1.";
Science 294:1098-1102(2001).
[28]
STRUCTURE BY NMR OF 13-25 IN COMPLEX WITH U2AF2, AND MUTAGENESIS OF
16-LYS--ARG-18; 17-LYS-LYS-18; ARG-21 AND TRP-22.
PubMed=12718882; DOI=10.1016/S1097-2765(03)00115-1;
Selenko P., Gregorovic G., Sprangers R., Stier G., Rhani Z.,
Kraemer A., Sattler M.;
"Structural basis for the molecular recognition between human splicing
factors U2AF65 and SF1/mBBP.";
Mol. Cell 11:965-976(2003).
-!- FUNCTION: Necessary for the ATP-dependent first step of
spliceosome assembly. Binds to the intron branch point sequence
(BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription
repressor. {ECO:0000269|PubMed:10449420,
ECO:0000269|PubMed:8752089, ECO:0000269|PubMed:9660765}.
-!- SUBUNIT: Binds U2AF2. Interacts with U1 snRNA. Binds EWSR1, FUS
and TAF15. Interacts with RBM17. {ECO:0000269|PubMed:10449420,
ECO:0000269|PubMed:11691992, ECO:0000269|PubMed:12176931,
ECO:0000269|PubMed:12718882, ECO:0000269|PubMed:17589525,
ECO:0000269|PubMed:8752089, ECO:0000269|PubMed:9660765}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-744603, EBI-744603;
P42684:ABL2; NbExp=3; IntAct=EBI-744603, EBI-1102694;
O60308:CEP104; NbExp=4; IntAct=EBI-744603, EBI-2685240;
Q80V31:Cep104 (xeno); NbExp=3; IntAct=EBI-744603, EBI-11073001;
Q8IWX8:CHERP; NbExp=6; IntAct=EBI-744603, EBI-2555370;
Q8CGZ0:Cherp (xeno); NbExp=3; IntAct=EBI-744603, EBI-2366446;
O76071:CIAO1; NbExp=3; IntAct=EBI-744603, EBI-725145;
Q68FD5:Cltc (xeno); NbExp=3; IntAct=EBI-744603, EBI-769168;
Q92841:DDX17; NbExp=4; IntAct=EBI-744603, EBI-746012;
P17844:DDX5; NbExp=3; IntAct=EBI-744603, EBI-351962;
Q92567:FAM168A; NbExp=3; IntAct=EBI-744603, EBI-7957930;
Q99729:HNRNPAB; NbExp=4; IntAct=EBI-744603, EBI-1044873;
O14979:HNRNPDL; NbExp=4; IntAct=EBI-744603, EBI-299727;
Q7Z7F0:KIAA0907; NbExp=5; IntAct=EBI-744603, EBI-751942;
Q3TCX3:Kiaa0907 (xeno); NbExp=3; IntAct=EBI-744603, EBI-11298408;
P52294:KPNA1; NbExp=3; IntAct=EBI-744603, EBI-358383;
Q60960:Kpna1 (xeno); NbExp=3; IntAct=EBI-744603, EBI-8573008;
P52292:KPNA2; NbExp=5; IntAct=EBI-744603, EBI-349938;
P52293:Kpna2 (xeno); NbExp=3; IntAct=EBI-744603, EBI-3043908;
O35343:Kpna4 (xeno); NbExp=3; IntAct=EBI-744603, EBI-8372758;
O60684:KPNA6; NbExp=4; IntAct=EBI-744603, EBI-359923;
Q6PEX3:KRTAP26-1; NbExp=3; IntAct=EBI-744603, EBI-3957672;
Q13064:MKRN3; NbExp=3; IntAct=EBI-744603, EBI-2340269;
P55345:PRMT2; NbExp=5; IntAct=EBI-744603, EBI-78458;
O75400:PRPF40A; NbExp=3; IntAct=EBI-744603, EBI-473291;
P25788:PSMA3; NbExp=3; IntAct=EBI-744603, EBI-348380;
Q96I25:RBM17; NbExp=8; IntAct=EBI-744603, EBI-740272;
Q15459:SF3A1; NbExp=8; IntAct=EBI-744603, EBI-1054743;
Q15428:SF3A2; NbExp=2; IntAct=EBI-744603, EBI-2462271;
Q12872:SFSWAP; NbExp=2; IntAct=EBI-744603, EBI-1055938;
Q3USH5:Sfswap (xeno); NbExp=3; IntAct=EBI-744603, EBI-8387273;
Q86WT6:TRIM69; NbExp=3; IntAct=EBI-744603, EBI-749955;
P26368:U2AF2; NbExp=19; IntAct=EBI-744603, EBI-742339;
P26369:U2af2 (xeno); NbExp=3; IntAct=EBI-744603, EBI-8321355;
Q8TAS1:UHMK1; NbExp=4; IntAct=EBI-744603, EBI-1753608;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=SF1-HL1;
IsoId=Q15637-1; Sequence=Displayed;
Name=2; Synonyms=SF1-Bo, Bone;
IsoId=Q15637-2; Sequence=VSP_008839;
Name=3; Synonyms=ZFM1-A, ZFM1-ABCDEF;
IsoId=Q15637-3; Sequence=VSP_008838;
Name=4; Synonyms=ZFM1-B, ZFM1-ABCDF;
IsoId=Q15637-4; Sequence=VSP_008835, VSP_008836;
Name=5;
IsoId=Q15637-5; Sequence=VSP_008833, VSP_008835, VSP_008836;
Note=No experimental confirmation available.;
Name=6; Synonyms=ZFM1-D, B6;
IsoId=Q15637-6; Sequence=VSP_008834, VSP_008837;
Note=Contains a phosphoserine at position 463. Contains a
omega-N-methylarginine at position 467.
{ECO:0000307|PubMed:16964243, ECO:0000307|PubMed:18220336,
ECO:0000307|PubMed:18669648, ECO:0000307|PubMed:24129315};
Name=7;
IsoId=Q15637-7; Sequence=VSP_045274;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Detected in lung, ovary, adrenal gland, colon,
kidney, muscle, pancreas, thyroid, placenta, brain, liver and
heart. {ECO:0000269|PubMed:7912130}.
-!- PTM: Phosphorylation on Ser-20 interferes with U2AF2 binding and
spliceosome assembly. Isoform 6 is phosphorylated on Ser-463.
{ECO:0000269|PubMed:10449420}.
-!- SIMILARITY: Belongs to the BBP/SF1 family. {ECO:0000320}.
-!- SEQUENCE CAUTION:
Sequence=AAH00773.1; Type=Erroneous initiation; Evidence={ECO:0000320};
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EMBL; Y08765; CAA70018.1; -; mRNA.
EMBL; Y08766; CAA70019.1; -; mRNA.
EMBL; L49345; AAB03514.1; -; mRNA.
EMBL; L49380; AAB04033.1; -; mRNA.
EMBL; D26120; BAA05116.1; -; mRNA.
EMBL; D26120; BAA05117.1; -; mRNA.
EMBL; AK293753; BAH11587.1; -; mRNA.
EMBL; AP001462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000773; AAH00773.1; ALT_INIT; mRNA.
EMBL; BC008080; AAH08080.1; -; mRNA.
EMBL; BC008724; AAH08724.1; -; mRNA.
EMBL; BC011657; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC020217; AAH20217.1; -; mRNA.
EMBL; BC038446; AAH38446.1; -; mRNA.
EMBL; AJ000051; CAA03883.1; -; Genomic_DNA.
EMBL; AJ000052; CAA03883.1; JOINED; Genomic_DNA.
CCDS; CCDS31599.1; -. [Q15637-1]
CCDS; CCDS44642.2; -. [Q15637-6]
CCDS; CCDS53660.1; -. [Q15637-7]
CCDS; CCDS53661.1; -. [Q15637-5]
CCDS; CCDS8080.1; -. [Q15637-2]
CCDS; CCDS8081.1; -. [Q15637-4]
PIR; G02919; G02919.
RefSeq; NP_001171501.1; NM_001178030.1. [Q15637-5]
RefSeq; NP_001171502.1; NM_001178031.2. [Q15637-7]
RefSeq; NP_001333292.1; NM_001346363.1.
RefSeq; NP_001333293.1; NM_001346364.1.
RefSeq; NP_004621.2; NM_004630.3. [Q15637-1]
RefSeq; NP_973724.1; NM_201995.2. [Q15637-2]
RefSeq; NP_973727.1; NM_201998.2. [Q15637-4]
RefSeq; XP_016873733.1; XM_017018244.1. [Q15637-7]
UniGene; Hs.502829; -.
PDB; 1K1G; NMR; -; A=133-260.
PDB; 1O0P; NMR; -; B=13-25.
PDB; 1OPI; NMR; -; B=13-25.
PDB; 2M09; NMR; -; A=27-145.
PDB; 2M0G; NMR; -; A=1-145.
PDB; 4FXW; X-ray; 2.29 A; B/D=14-132.
PDB; 4FXX; X-ray; 2.48 A; A/B/C/D=26-132.
PDBsum; 1K1G; -.
PDBsum; 1O0P; -.
PDBsum; 1OPI; -.
PDBsum; 2M09; -.
PDBsum; 2M0G; -.
PDBsum; 4FXW; -.
PDBsum; 4FXX; -.
ProteinModelPortal; Q15637; -.
SMR; Q15637; -.
BioGrid; 113368; 149.
CORUM; Q15637; -.
DIP; DIP-29410N; -.
ELM; Q15637; -.
IntAct; Q15637; 207.
MINT; MINT-1582417; -.
STRING; 9606.ENSP00000366604; -.
iPTMnet; Q15637; -.
PhosphoSitePlus; Q15637; -.
SwissPalm; Q15637; -.
BioMuta; SF1; -.
DMDM; 38258418; -.
EPD; Q15637; -.
MaxQB; Q15637; -.
PaxDb; Q15637; -.
PeptideAtlas; Q15637; -.
PRIDE; Q15637; -.
TopDownProteomics; Q15637-4; -. [Q15637-4]
DNASU; 7536; -.
Ensembl; ENST00000227503; ENSP00000227503; ENSG00000168066. [Q15637-4]
Ensembl; ENST00000334944; ENSP00000334414; ENSG00000168066. [Q15637-2]
Ensembl; ENST00000377387; ENSP00000366604; ENSG00000168066. [Q15637-5]
Ensembl; ENST00000377390; ENSP00000366607; ENSG00000168066. [Q15637-1]
Ensembl; ENST00000377394; ENSP00000366611; ENSG00000168066. [Q15637-6]
Ensembl; ENST00000433274; ENSP00000396793; ENSG00000168066. [Q15637-7]
GeneID; 7536; -.
KEGG; hsa:7536; -.
UCSC; uc001oaz.3; human. [Q15637-1]
CTD; 7536; -.
DisGeNET; 7536; -.
EuPathDB; HostDB:ENSG00000168066.20; -.
GeneCards; SF1; -.
HGNC; HGNC:12950; SF1.
HPA; HPA018883; -.
MIM; 601516; gene.
neXtProt; NX_Q15637; -.
OpenTargets; ENSG00000168066; -.
PharmGKB; PA37533; -.
eggNOG; KOG0119; Eukaryota.
eggNOG; COG5176; LUCA.
GeneTree; ENSGT00550000074434; -.
HOGENOM; HOG000237321; -.
HOVERGEN; HBG063318; -.
InParanoid; Q15637; -.
KO; K13095; -.
OMA; PPLMPWM; -.
OrthoDB; EOG091G0AEL; -.
PhylomeDB; Q15637; -.
TreeFam; TF319159; -.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
SIGNOR; Q15637; -.
ChiTaRS; SF1; human.
EvolutionaryTrace; Q15637; -.
GeneWiki; SF1_(gene); -.
GenomeRNAi; 7536; -.
PRO; PR:Q15637; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000168066; -.
CleanEx; HS_SF1; -.
ExpressionAtlas; Q15637; baseline and differential.
Genevisible; Q15637; HS.
GO; GO:0016604; C:nuclear body; RCA:Ensembl.
GO; GO:0005654; C:nucleoplasm; HTP:HPA.
GO; GO:0005634; C:nucleus; IBD:UniProtKB.
GO; GO:0005840; C:ribosome; IBD:UniProtKB.
GO; GO:0005681; C:spliceosomal complex; HTP:HGNC.
GO; GO:0042802; F:identical protein binding; IDA:IntAct.
GO; GO:0045131; F:pre-mRNA branch point binding; RCA:InterPro.
GO; GO:0003723; F:RNA binding; HTP:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IBA:ProtInc.
GO; GO:0008270; F:zinc ion binding; RCA:InterPro.
GO; GO:0033327; P:Leydig cell differentiation; RCA:Ensembl.
GO; GO:0030238; P:male sex determination; RCA:Ensembl.
GO; GO:0000389; P:mRNA 3'-splice site recognition; IBA:HGNC.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:Reactome.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; RCA:Ensembl.
GO; GO:0030575; P:nuclear body organization; RCA:Ensembl.
GO; GO:0050810; P:regulation of steroid biosynthetic process; RCA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; RCA:UniProtKB-KW.
GO; GO:0000245; P:spliceosomal complex assembly; IBD:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; RCA:UniProtKB-KW.
Gene3D; 3.30.1370.10; -; 1.
Gene3D; 4.10.60.10; -; 1.
InterPro; IPR031150; BBP/SF1.
InterPro; IPR004087; KH_dom.
InterPro; IPR004088; KH_dom_type_1.
InterPro; IPR036612; KH_dom_type_1_sf.
InterPro; IPR032570; SF1-HH.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
PANTHER; PTHR11208:SF45; PTHR11208:SF45; 3.
Pfam; PF00013; KH_1; 1.
Pfam; PF16275; SF1-HH; 1.
Pfam; PF00098; zf-CCHC; 1.
SMART; SM00322; KH; 1.
SMART; SM00343; ZnF_C2HC; 1.
SUPFAM; SSF54791; SSF54791; 1.
PROSITE; PS50084; KH_TYPE_1; 1.
PROSITE; PS50158; ZF_CCHC; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Metal-binding; Methylation;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repressor; RNA-binding; Spliceosome;
Transcription; Transcription regulation; Zinc; Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.8,
ECO:0000307|PubMed:19413330,
ECO:0000307|PubMed:22223895,
ECO:0000307|PubMed:22814378}.
CHAIN 2 639 Splicing factor 1.
/FTId=PRO_0000050129.
DOMAIN 141 222 KH. {ECO:0000270|PROSITE-
ProRule:PRU00117}.
ZN_FING 277 296 CCHC-type. {ECO:0000270|PROSITE-
ProRule:PRU00047}.
MOTIF 15 19 Nuclear localization signal.
{ECO:0000270}.
COMPBIAS 324 637 Pro-rich.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.8,
ECO:0000307|PubMed:19413330,
ECO:0000307|PubMed:22223895,
ECO:0000307|PubMed:22814378}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000307|PubMed:23186163}.
MOD_RES 20 20 Phosphoserine; by PKG.
{ECO:0000269|PubMed:10449420}.
MOD_RES 80 80 Phosphoserine.
{ECO:0000307|PubMed:18669648,
ECO:0000307|PubMed:19690332,
ECO:0000307|PubMed:20068231,
ECO:0000307|PubMed:21406692,
ECO:0000307|PubMed:23186163}.
MOD_RES 82 82 Phosphoserine.
{ECO:0000307|PubMed:18669648,
ECO:0000307|PubMed:19690332,
ECO:0000307|PubMed:20068231,
ECO:0000307|PubMed:21406692,
ECO:0000307|PubMed:23186163}.
MOD_RES 87 87 Phosphotyrosine.
{ECO:0000307|PubMed:24275569}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000307|PubMed:24275569}.
VAR_SEQ 1 26 Missing (in isoform 7).
{ECO:0000319|PubMed:14702039}.
/FTId=VSP_045274.
VAR_SEQ 10 10 L -> LGKLGPPGLPPLPGPKGGFEPGPPPAPGPGAGLLAP
GPPPPPPVGSMGALTAAFPFAALPPPPPPPPPPPPQQPPPP
PPPPSPGASYPPPQPPPPPPLYQRVSPPQPPPPQPPRKDQQ
PGPAGGGG (in isoform 5).
{ECO:0000319|PubMed:15489334}.
/FTId=VSP_008833.
VAR_SEQ 448 548 DQYLGSTPVGSGVYRLHQGKGMMPPPPMGMMPPPPPPPSGQ
PPPPPSGPLPPWQQQQQQPPPPPPPSSSMASSTPLPWQQNT
TTTTTSAGTGSIPPWQQQQ -> GKSVPGKYACGLWGLSPA
SRKRYDAATTYGHDA (in isoform 6).
{ECO:0000319|PubMed:9192847}.
/FTId=VSP_008834.
VAR_SEQ 528 548 NTTTTTTSAGTGSIPPWQQQQ -> RSLPAAAMARAMRVRT
FRAHW (in isoform 4 and isoform 5).
{ECO:0000319|PubMed:15489334,
ECO:0000319|PubMed:7912130}.
/FTId=VSP_008835.
VAR_SEQ 549 639 Missing (in isoform 4 and isoform 5).
{ECO:0000319|PubMed:15489334,
ECO:0000319|PubMed:7912130}.
/FTId=VSP_008836.
VAR_SEQ 555 639 PGAPQMQGNPTMVPLPPGVQPPLPPGAPPPPPPPPPGSAGM
MYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPP
PQN -> QWAAPTPSLWSSSPMATTAAAASATPSAQQQYGF
QYPLAMAAKIPPRGGDGPSHESEDFPRPLVTLPGRQPQQRP
WWTGWFGKAA (in isoform 6).
{ECO:0000319|PubMed:9192847}.
/FTId=VSP_008837.
VAR_SEQ 587 639 PPPPGSAGMMYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFG
MPPAPPPPPPQN -> RSIECLLCLLSLLTQLPLPLPKPGR
QDPSPRRRWPEP (in isoform 3).
{ECO:0000319|PubMed:7912130}.
/FTId=VSP_008838.
VAR_SEQ 597 639 YAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPPP
QN -> IPPRGGDGPSHESEDFPRPLVTLPGRQPQQRPWWT
GWFGKAA (in isoform 2).
{ECO:0000319|PubMed:8752089}.
/FTId=VSP_008839.
VARIANT 357 357 S -> T. {ECO:0000269|PubMed:8752089}.
/FTId=VAR_017196.
MUTAGEN 15 17 KKR->EED: Abolishes interaction with
U2AF2.
MUTAGEN 16 18 KRK->EDE: Abolishes interaction with
U2AF2. {ECO:0000269|PubMed:12718882}.
MUTAGEN 20 20 S->A: Strongly decreases interaction with
U2AF2 and spliceosome assembly.
{ECO:0000269|PubMed:10449420}.
MUTAGEN 20 20 S->T: Decreases interaction with U2AF2.
{ECO:0000269|PubMed:10449420}.
MUTAGEN 21 21 R->A: Decreases interaction with U2AF2
and spliceosome assembly.
{ECO:0000269|PubMed:12718882}.
MUTAGEN 21 21 R->K: No effect.
{ECO:0000269|PubMed:12718882}.
MUTAGEN 22 22 W->A: Abolishes interaction with U2AF2.
{ECO:0000269|PubMed:12718882}.
MUTAGEN 22 22 W->F: No effect.
{ECO:0000269|PubMed:12718882}.
MUTAGEN 151 151 N->A: Decreases RNA-binding.
{ECO:0000269|PubMed:11691992}.
MUTAGEN 160 160 R->A: Strongly reduces RNA-binding.
{ECO:0000269|PubMed:11691992}.
MUTAGEN 184 184 K->A: Abolishes RNA-binding.
{ECO:0000269|PubMed:11691992}.
MUTAGEN 244 244 L->A: Decreases RNA-binding.
{ECO:0000269|PubMed:11691992}.
MUTAGEN 247 247 L->A: Decreases RNA-binding.
{ECO:0000269|PubMed:11691992}.
MUTAGEN 254 254 L->A: Slightly decreases RNA-binding.
{ECO:0000269|PubMed:11691992}.
MUTAGEN 255 255 R->A: Slightly decreases RNA-binding.
{ECO:0000269|PubMed:11691992}.
CONFLICT 269 269 E -> G (in Ref. 3; BAA05116/BAA05117).
{ECO:0000320}.
CONFLICT 348 348 A -> R (in Ref. 2; AAB03514/AAB04033).
{ECO:0000320}.
CONFLICT 377 377 R -> W (in Ref. 3; BAA05116/BAA05117).
{ECO:0000320}.
CONFLICT 570 570 P -> L (in Ref. 4; BAH11587).
{ECO:0000320}.
CONFLICT 591 591 G -> V (in Ref. 2; AAB04033).
{ECO:0000320}.
CONFLICT 623 623 M -> I (in Ref. 2; AAB04033).
{ECO:0000320}.
STRAND 15 17 {ECO:0000307|PDB:1O0P}.
HELIX 27 30 {ECO:0000307|PDB:4FXX}.
HELIX 46 67 {ECO:0000307|PDB:4FXW}.
HELIX 76 79 {ECO:0000307|PDB:2M09}.
STRAND 93 95 {ECO:0000307|PDB:4FXW}.
HELIX 97 115 {ECO:0000307|PDB:4FXW}.
HELIX 116 118 {ECO:0000307|PDB:4FXW}.
STRAND 136 141 {ECO:0000307|PDB:1K1G}.
TURN 144 146 {ECO:0000307|PDB:1K1G}.
HELIX 150 157 {ECO:0000307|PDB:1K1G}.
STRAND 159 161 {ECO:0000307|PDB:1K1G}.
HELIX 162 170 {ECO:0000307|PDB:1K1G}.
STRAND 174 190 {ECO:0000307|PDB:1K1G}.
STRAND 203 211 {ECO:0000307|PDB:1K1G}.
HELIX 212 226 {ECO:0000307|PDB:1K1G}.
TURN 227 230 {ECO:0000307|PDB:1K1G}.
HELIX 238 244 {ECO:0000307|PDB:1K1G}.
HELIX 245 248 {ECO:0000307|PDB:1K1G}.
TURN 249 252 {ECO:0000307|PDB:1K1G}.
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


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