ID   FUSIP_HUMAN    STANDARD;      PRT;   262 AA.
AC   O75494; O60572; Q96G09; Q96P17;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   16-MAY-2006, entry version 49.
DE   FUS-interacting serine-arginine-rich protein 1 (TLS-associated protein
DE   with Ser-Arg repeats) (TLS-associated protein with SR repeats) (TASR)
DE   (TLS-associated serine-arginine protein) (TLS-associated SR protein)
DE   (40 kDa SR-repressor protein) (SRrp40) (Splicing factor SRp38).
GN   Name=FUSIP1; Synonyms=TASR;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 3), AND INTERACTION WITH FUS.
RC   TISSUE=Leukemia;
RX   MEDLINE=98447613; PubMed=9774382; DOI=10.1074/jbc.273.43.27761;
RA   Yang L., Embree L.J., Tsai S., Hickstein D.D.;
RT   "Oncoprotein TLS interacts with serine-arginine proteins involved in
RT   RNA splicing.";
RL   J. Biol. Chem. 273:27761-27764(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX   MEDLINE=20242028; PubMed=10779324;
RX   DOI=10.1128/MCB.20.10.3345-3354.2000;
RA   Yang L., Embree L.J., Hickstein D.D.;
RT   "TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by
RT   serine-arginine proteins.";
RL   Mol. Cell. Biol. 20:3345-3354(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21623667; PubMed=11684676; DOI=10.1074/jbc.M103967200;
RA   Cowper A.E., Caceres J.F., Mayeda A., Screaton G.R.;
RT   "Serine-arginine (SR) protein-like factors that antagonize authentic
RT   SR proteins and regulate alternative splicing.";
RL   J. Biol. Chem. 276:48908-48914(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 3), FUNCTION, AND PHOSPHORYLATION.
RX   MEDLINE=22306915; PubMed=12419250; DOI=10.1016/S0092-8674(02)01038-3;
RA   Shin C., Manley J.L.;
RT   "The SR protein SRp38 represses splicing in M Phase cells.";
RL   Cell 111:407-417(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE, ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), AND
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21888629; PubMed=11891055; DOI=10.1016/S0378-1119(02)00382-7;
RA   Clinton J.M., Chansky H.A., Odell D.D., Zielinska-Kwiatkowska A.,
RA   Hickstein D.D., Yang L.;
RT   "Characterization and expression of the human gene encoding two
RT   translocation liposarcoma protein-associated serine-arginine (TASR)
RT   proteins.";
RL   Gene 284:141-147(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Muscle, Placenta, and Uterus;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN   [8]
RP   FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH SFRS10 AND SNRP70.
RX   PubMed=14765198; DOI=10.1038/nature02288;
RA   Shin C., Feng Y., Manley J.L.;
RT   "Dephosphorylated SRp38 acts as a splicing repressor in response to
RT   heat shock.";
RL   Nature 427:553-558(2004).
RN   [9]
RP   PHOSPHORYLATION AT SER-133.
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
CC   -!- FUNCTION: Splicing factor that in its dephosphorylated form acts
CC       as a general repressor of pre-mRNA splicing. Seems to interfere
CC       with the U1 snRNP 5'-splice recognition of SNRP70. Required for
CC       splicing repression in M-phase cells and after heat shock. May be
CC       involved in regulation of alternative splicing in neurons, with
CC       isoform 1 acting as a positive and isoform 3 as a negative
CC       regulator.
CC   -!- SUBUNIT: The phosphorylated but not the dephosphorylated form
CC       interacts with SFRS10. The dephosphorylated form interacts with
CC       SNRP70. Isoform 1 and isoform 3 interact with FUS C-terminus.
CC   -!- SUBCELLULAR LOCATION: Nucleus; nucleoplasm; nuclear speckle.
CC       Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=TASR-1;
CC         IsoId=O75494-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O75494-2; Sequence=VSP_010421;
CC       Name=3; Synonyms=TASR-2, SRp38-2;
CC         IsoId=O75494-3; Sequence=VSP_010424, VSP_010425;
CC       Name=4;
CC         IsoId=O75494-4; Sequence=VSP_010422, VSP_010423;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- PTM: Phosphorylated. Fully dephosphorylated in mitosis and
CC       partially dephosphorylated on heat shock.
CC   -!- SIMILARITY: Belongs to the splicing factor SR family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR   EMBL; AF047448; AAC70918.1; -; mRNA.
DR   EMBL; AF067730; AAC26727.1; -; mRNA.
DR   EMBL; AF449427; AAL57514.1; -; mRNA.
DR   EMBL; AY150180; AAN65380.1; -; mRNA.
DR   EMBL; AY150181; AAN65381.1; -; mRNA.
DR   EMBL; AF419331; AAL16665.1; -; mRNA.
DR   EMBL; AF419332; AAL16666.1; -; Genomic_DNA.
DR   EMBL; AY048592; AAL06098.1; -; Genomic_DNA.
DR   EMBL; AY048592; AAL06099.1; -; Genomic_DNA.
DR   EMBL; AK001286; BAA91601.1; -; mRNA.
DR   EMBL; BC001107; AAH01107.1; -; mRNA.
DR   EMBL; BC005039; AAH05039.1; -; mRNA.
DR   EMBL; BC010074; AAH10074.1; -; mRNA.
DR   UniGene; Hs.3530; -.
DR   UniGene; Hs.515717; -.
DR   HSSP; P11940; 1CVJ.
DR   IntAct; O75494; -.
DR   HGNC; HGNC:16713; FUSIP1.
DR   MIM; 605221; gene.
DR   LinkHub; O75494; -.
DR   GO; GO:0005737; C:cytoplasm; NAS.
DR   GO; GO:0005654; C:nucleoplasm; IDA.
DR   GO; GO:0005634; C:nucleus; IC.
DR   GO; GO:0031202; F:RNA splicing factor activity, transesterifi...; IDA.
DR   GO; GO:0050733; F:RS domain binding; NAS.
DR   GO; GO:0051082; F:unfolded protein binding; NAS.
DR   GO; GO:0000244; P:assembly of spliceosomal tri-snRNP; NAS.
DR   GO; GO:0016482; P:cytoplasmic transport; IDA.
DR   GO; GO:0006406; P:mRNA export from nucleus; NAS.
DR   GO; GO:0006376; P:mRNA splice site selection; IDA.
DR   GO; GO:0048025; P:negative regulation of nuclear mRNA splicin...; IDA.
DR   GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; IDA.
DR   GO; GO:0045449; P:regulation of transcription; NAS.
DR   InterPro; IPR012677; a_b_plait_nuc_bd.
DR   InterPro; IPR000504; RNP1_RNA_bd.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
KW   Alternative splicing; mRNA processing; mRNA splicing; Nuclear protein;
KW   Phosphorylation; RNA-binding.
FT   CHAIN         1    262       FUS-interacting serine-arginine-rich
FT                                protein 1.
FT                                /FTId=PRO_0000081593.
FT   DOMAIN       10     88       RRM.
FT   COMPBIAS    106    260       Arg/Ser-rich (RS domain).
FT   MOD_RES     133    133       Phosphoserine.
FT   VARSPLIC    147    147       Missing (in isoform 2).
FT                                /FTId=VSP_010421.
FT   VARSPLIC    164    173       RFKHRNRSFS -> SQVSKKKNER (in isoform 4).
FT                                /FTId=VSP_010422.
FT   VARSPLIC    165    183       FKHRNRSFSRSKSNSRSRS -> PNCSWNTQYSSAYYTSRK
FT                                I (in isoform 3).
FT                                /FTId=VSP_010424.
FT   VARSPLIC    174    262       Missing (in isoform 4).
FT                                /FTId=VSP_010423.
FT   VARSPLIC    184    262       Missing (in isoform 3).
FT                                /FTId=VSP_010425.
SQ   SEQUENCE   262 AA;  31301 MW;  205F95D36CBBFAB4 CRC64;
     MSRYLRPPNT SLFVRNVADD TRSEDLRREF GRYGPIVDVY VPLDFYTRRP RGFAYVQFED
     VRDAEDALHN LDRKWICGRQ IEIQFAQGDR KTPNQMKAKE GRNVYSSSRY DDYDRYRRSR
     SRSYERRRSR SRSFDYNYRR SYSPRNSRPT GRPRRSRSHS DNDRFKHRNR SFSRSKSNSR
     SRSKSQPKKE MKAKSRSRSA SHTKTRGTSK TDSKTHYKSG SRYEKESRKK EPPRSKSQSR
     SQSRSRSKSR SRSWTSPKSS GH
//