SRPK1_HUMAN
ID SRPK1_HUMAN Reviewed; 655 AA.
AC Q96SB4; B4DS61; Q12890; Q5R364; Q5R365; Q8IY12;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=SRSF protein kinase 1;
DE EC=2.7.11.1;
DE AltName: Full=SFRS protein kinase 1;
DE AltName: Full=Serine/arginine-rich protein-specific kinase 1;
DE Short=SR-protein-specific kinase 1;
GN Name=SRPK1 {ECO:0000312|EMBL:CAC39299.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAA20530.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RC TISSUE=Cervix carcinoma;
RX PubMed=8208298; DOI=10.1038/369678a0;
RA Gui J.F., Lane W.S., Fu X.-D.;
RT "A serine kinase regulates intracellular localization of splicing factors
RT in the cell cycle.";
RL Nature 369:678-682(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH SAFB.
RC TISSUE=Testis {ECO:0000269|PubMed:11509566};
RX PubMed=11509566; DOI=10.1074/jbc.m104755200;
RA Nikolakaki E., Kohen R., Hartmann A.M., Stamm S., Georgatsou E.,
RA Giannakouros T.;
RT "Cloning and characterization of an alternatively spliced form of SR
RT protein kinase 1 that interacts specifically with scaffold attachment
RT factor-B.";
RL J. Biol. Chem. 276:40175-40182(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis {ECO:0000312|EMBL:AAH38292.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 330-345 AND 353-375, AND FUNCTION IN PHOSPHORYLATION OF
RP HEPATITIS B VIRUS CORE PROTEIN.
RX PubMed=12134018; DOI=10.1128/jvi.76.16.8124-8137.2002;
RA Daub H., Blencke S., Habenberger P., Kurtenbach A., Dennenmoser J.,
RA Wissing J., Ullrich A., Cotten M.;
RT "Identification of SRPK1 and SRPK2 as the major cellular protein kinases
RT phosphorylating hepatitis B virus core protein.";
RL J. Virol. 76:8124-8137(2002).
RN [8]
RP PROTEIN SEQUENCE OF 376-400 AND 616-636, FUNCTION, AND IDENTIFICATION IN A
RP TOPOSOME COMPLEX.
RX PubMed=15034300;
RA Lee C.G., Hague L.K., Li H., Donnelly R.;
RT "Identification of toposome, a novel multisubunit complex containing
RT topoisomerase IIalpha.";
RL Cell Cycle 3:638-647(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH ZRSR2.
RX PubMed=9237760; DOI=10.1038/41137;
RA Tronchere H., Wang J., Fu X.D.;
RT "A protein related to splicing factor U2AF35 that interacts with U2AF65 and
RT SR proteins in splicing of pre-mRNA.";
RL Nature 388:397-400(1997).
RN [10]
RP FUNCTION IN PHOSPHORYLATION OF LBR.
RX PubMed=10049757; DOI=10.1006/bbrc.1999.0249;
RA Papoutsopoulou S., Nikolakaki E., Giannakouros T.;
RT "SRPK1 and LBR protein kinases show identical substrate specificities.";
RL Biochem. Biophys. Res. Commun. 255:602-607(1999).
RN [11]
RP FUNCTION IN PHOSPHORYLATION OF PRM1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=10390541; DOI=10.1093/nar/27.14.2972;
RA Papoutsopoulou S., Nikolakaki E., Chalepakis G., Kruft V., Chevaillier P.,
RA Giannakouros T.;
RT "SR protein-specific kinase 1 is highly expressed in testis and
RT phosphorylates protamine 1.";
RL Nucleic Acids Res. 27:2972-2980(1999).
RN [12]
RP FUNCTION, AND INTERACTION WITH SFRS1.
RX PubMed=14555757; DOI=10.1073/pnas.1635129100;
RA Aubol B.E., Chakrabarti S., Ngo J., Shaffer J., Nolen B., Fu X.-D.,
RA Ghosh G., Adams J.A.;
RT "Processive phosphorylation of alternative splicing factor/splicing factor
RT 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12601-12606(2003).
RN [13]
RP ACTIVITY REGULATION, PHOSPHORYLATION AT SER-51 AND SER-555, AND MUTAGENESIS
RP OF SER-37; SER-51; SER-222; SER-311; SER-436; SER-555 AND SER-619.
RX PubMed=12565829; DOI=10.1016/s0006-291x(02)03055-3;
RA Mylonis I., Giannakouros T.;
RT "Protein kinase CK2 phosphorylates and activates the SR protein-specific
RT kinase 1.";
RL Biochem. Biophys. Res. Commun. 301:650-656(2003).
RN [14]
RP FUNCTION IN NEGATIVE REGULATION OF HEPATITIS B VIRUS (HBV) REPLICATION.
RX PubMed=16122776; DOI=10.1016/j.virol.2005.07.030;
RA Zheng Y., Fu X.D., Ou J.H.;
RT "Suppression of hepatitis B virus replication by SRPK1 and SRPK2 via a
RT pathway independent of the phosphorylation of the viral core protein.";
RL Virology 342:150-158(2005).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP 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 [16]
RP FUNCTION IN PHOSPHORYLATION OF SRSF1, AND THE MECHANISM OF PHOSPHORYLATION.
RX PubMed=18155240; DOI=10.1016/j.jmb.2007.08.029;
RA Ma C.T., Velazquez-Dones A., Hagopian J.C., Ghosh G., Fu X.D., Adams J.A.;
RT "Ordered multi-site phosphorylation of the splicing factor ASF/SF2 by
RT SRPK1.";
RL J. Mol. Biol. 376:55-68(2008).
RN [17]
RP FUNCTION IN PHOSPHORYLATION OF SRSF1, AND THE MECHANISM OF PHOSPHORYLATION.
RX PubMed=18687337; DOI=10.1016/j.jmb.2008.07.055;
RA Hagopian J.C., Ma C.T., Meade B.R., Albuquerque C.P., Ngo J.C., Ghosh G.,
RA Jennings P.A., Fu X.D., Adams J.A.;
RT "Adaptable molecular interactions guide phosphorylation of the SR protein
RT ASF/SF2 by SRPK1.";
RL J. Mol. Biol. 382:894-909(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP 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 [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [21]
RP FUNCTION IN PHOSPHORYLATION OF SRSF1, AND THE MECHANISM OF PHOSPHORYLATION.
RX PubMed=19886675; DOI=10.1021/bi901107q;
RA Huynh N., Ma C.T., Giang N., Hagopian J., Ngo J., Adams J., Ghosh G.;
RT "Allosteric interactions direct binding and phosphorylation of ASF/SF2 by
RT SRPK1.";
RL Biochemistry 48:11432-11440(2009).
RN [22]
RP INTERACTION WITH SAFB/SAFB1 AND SAFB2.
RX PubMed=19674106; DOI=10.1111/j.1742-4658.2009.07217.x;
RA Tsianou D., Nikolakaki E., Tzitzira A., Bonanou S., Giannakouros T.,
RA Georgatsou E.;
RT "The enzymatic activity of SR protein kinases 1 and 1a is negatively
RT affected by interaction with scaffold attachment factors B1 and 2.";
RL FEBS J. 276:5212-5227(2009).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DNAJC8 AND AHSA1/AHA1.
RX PubMed=19240134; DOI=10.1101/gad.1752109;
RA Zhong X.Y., Ding J.H., Adams J.A., Ghosh G., Fu X.D.;
RT "Regulation of SR protein phosphorylation and alternative splicing by
RT modulating kinetic interactions of SRPK1 with molecular chaperones.";
RL Genes Dev. 23:482-495(2009).
RN [24]
RP FUNCTION IN PHOSPHORYLATION OF SRSF1, AND THE MECHANISM OF PHOSPHORYLATION.
RX PubMed=19477182; DOI=10.1016/j.jmb.2009.05.060;
RA Ma C.T., Hagopian J.C., Ghosh G., Fu X.D., Adams J.A.;
RT "Regiospecific phosphorylation control of the SR protein ASF/SF2 by
RT SRPK1.";
RL J. Mol. Biol. 390:618-634(2009).
RN [25]
RP INTERACTION WITH HHV-1 ICP27 PROTEIN (MICROBIAL INFECTION).
RX PubMed=19553338; DOI=10.1128/jvi.00801-09;
RA Souki S.K., Sandri-Goldin R.M.;
RT "Arginine methylation of the ICP27 RGG box regulates the functional
RT interactions of ICP27 with SRPK1 and Aly/REF during herpes simplex virus 1
RT infection.";
RL J. Virol. 83:8970-8975(2009).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP 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 [27]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION OF
RP ISOFORM 1 IN A COMPLEX WITH DHX9; MOV10; MATR3; HNRNPU; NCL; DDX21;
RP HSD17B4; PABPC1; HNRNPM; IGF2BP1; SYNCRIP; RPL3; VIM; YBX1; NPM1;
RP HNRNPA2B1; HNRNPC; RPLP0; RPL7A AND RALY.
RX PubMed=20708644; DOI=10.1016/j.bbamcr.2010.07.008;
RA Sanidas I., Kotoula V., Ritou E., Daans J., Lenz C., Mairhofer M.,
RA Daniilidou M., Kolbus A., Kruft V., Ponsaerts P., Nikolakaki E.;
RT "The ratio of SRPK1/SRPK1a regulates erythroid differentiation in K562
RT leukaemic cells.";
RL Biochim. Biophys. Acta 1803:1319-1331(2010).
RN [28]
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 [29]
RP SUBCELLULAR LOCATION.
RX PubMed=21157427; DOI=10.1038/emboj.2010.333;
RA Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C., Brambilla E.,
RA Gazzeri S., Eymin B.;
RT "Acetylation and phosphorylation of SRSF2 control cell fate decision in
RT response to cisplatin.";
RL EMBO J. 30:510-523(2011).
RN [30]
RP REVIEW ON FUNCTION.
RX PubMed=21205200; DOI=10.1111/j.1742-4658.2010.07987.x;
RA Giannakouros T., Nikolakaki E., Mylonis I., Georgatsou E.;
RT "Serine-arginine protein kinases: a small protein kinase family with a
RT large cellular presence.";
RL FEBS J. 278:570-586(2011).
RN [31]
RP REVIEW ON FUNCTION.
RX PubMed=21205204; DOI=10.1111/j.1742-4658.2010.07992.x;
RA Ghosh G., Adams J.A.;
RT "Phosphorylation mechanism and structure of serine-arginine protein
RT kinases.";
RL FEBS J. 278:587-597(2011).
RN [32]
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 [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-309; SER-311 AND
RP SER-333, AND 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 [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-311, 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 [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [36]
RP SUBCELLULAR LOCATION.
RX PubMed=28076779; DOI=10.1016/j.celrep.2016.12.050;
RA Sridhara S.C., Carvalho S., Grosso A.R., Gallego-Paez L.M.,
RA Carmo-Fonseca M., de Almeida S.F.;
RT "Transcription Dynamics Prevent RNA-Mediated Genomic Instability through
RT SRPK2-Dependent DDX23 Phosphorylation.";
RL Cell Rep. 18:334-343(2017).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 42-438 IN COMPLEX WITH ATP AND
RP SUBSTRATE PEPTIDE, FUNCTION, AND INTERACTION WITH SFRS1.
RX PubMed=16209947; DOI=10.1016/j.molcel.2005.08.025;
RA Ngo J.C.K., Chakrabarti S., Ding J.-H., Velazquez-Dones A., Nolen B.,
RA Aubol B.E., Adams J.A., Fu X.-D., Ghosh G.;
RT "Interplay between SRPK and Clk/Sty kinases in phosphorylation of the
RT splicing factor ASF/SF2 is regulated by a docking motif in ASF/SF2.";
RL Mol. Cell 20:77-89(2005).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 42-655, AND SUBUNIT.
RX PubMed=17223538; DOI=10.1016/j.str.2006.11.011;
RA Ngo J.C., Gullingsrud J., Giang K., Yeh M.J., Fu X.D., Adams J.A.,
RA McCammon J.A., Ghosh G.;
RT "SR protein kinase 1 is resilient to inactivation.";
RL Structure 15:123-133(2007).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 58-655 IN COMPLEX WITH SRSF1, AND
RP MECHANISM OF PHOSPHORYLATION OF SRSF1.
RX PubMed=18342604; DOI=10.1016/j.molcel.2007.12.017;
RA Ngo J.C., Giang K., Chakrabarti S., Ma C.T., Huynh N., Hagopian J.C.,
RA Dorrestein P.C., Fu X.D., Adams J.A., Ghosh G.;
RT "A sliding docking interaction is essential for sequential and processive
RT phosphorylation of an SR protein by SRPK1.";
RL Mol. Cell 29:563-576(2008).
CC -!- FUNCTION: Serine/arginine-rich protein-specific kinase which
CC specifically phosphorylates its substrates at serine residues located
CC in regions rich in arginine/serine dipeptides, known as RS domains and
CC is involved in the phosphorylation of SR splicing factors and the
CC regulation of splicing. Plays a central role in the regulatory network
CC for splicing, controlling the intranuclear distribution of splicing
CC factors in interphase cells and the reorganization of nuclear speckles
CC during mitosis. Can influence additional steps of mRNA maturation, as
CC well as other cellular activities, such as chromatin reorganization in
CC somatic and sperm cells and cell cycle progression. Isoform 2
CC phosphorylates SFRS2, ZRSR2, LBR and PRM1. Isoform 2 phosphorylates
CC SRSF1 using a directional (C-terminal to N-terminal) and a dual-track
CC mechanism incorporating both processive phosphorylation (in which the
CC kinase stays attached to the substrate after each round of
CC phosphorylation) and distributive phosphorylation steps (in which the
CC kinase and substrate dissociate after each phosphorylation event). The
CC RS domain of SRSF1 binds first to a docking groove in the large lobe of
CC the kinase domain of SRPK1. This induces certain structural changes in
CC SRPK1 and/or RRM2 domain of SRSF1, allowing RRM2 to bind the kinase and
CC initiate phosphorylation. The cycles continue for several
CC phosphorylation steps in a processive manner (steps 1-8) until the last
CC few phosphorylation steps (approximately steps 9-12). During that time,
CC a mechanical stress induces the unfolding of the beta-4 motif in RRM2,
CC which then docks at the docking groove of SRPK1. This also signals RRM2
CC to begin to dissociate, which facilitates SRSF1 dissociation after
CC phosphorylation is completed. Isoform 2 can mediate hepatitis B virus
CC (HBV) core protein phosphorylation. It plays a negative role in the
CC regulation of HBV replication through a mechanism not involving the
CC phosphorylation of the core protein but by reducing the packaging
CC efficiency of the pregenomic RNA (pgRNA) without affecting the
CC formation of the viral core particles. Isoform 1 and isoform 2 can
CC induce splicing of exon 10 in MAPT/TAU. The ratio of isoform 1/isoform
CC 2 plays a decisive role in determining cell fate in K-562 leukaemic
CC cell line: isoform 2 favors proliferation where as isoform 1 favors
CC differentiation. {ECO:0000269|PubMed:10049757,
CC ECO:0000269|PubMed:10390541, ECO:0000269|PubMed:11509566,
CC ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:14555757,
CC ECO:0000269|PubMed:15034300, ECO:0000269|PubMed:16122776,
CC ECO:0000269|PubMed:16209947, ECO:0000269|PubMed:18155240,
CC ECO:0000269|PubMed:18687337, ECO:0000269|PubMed:19240134,
CC ECO:0000269|PubMed:19477182, ECO:0000269|PubMed:19886675,
CC ECO:0000269|PubMed:20708644, ECO:0000269|PubMed:8208298,
CC ECO:0000269|PubMed:9237760}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000269|PubMed:11509566, ECO:0000269|PubMed:12134018,
CC ECO:0000269|PubMed:12565829, ECO:0000269|PubMed:14555757,
CC ECO:0000269|PubMed:15034300, ECO:0000269|PubMed:8208298};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000269|PubMed:11509566,
CC ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:12565829,
CC ECO:0000269|PubMed:14555757, ECO:0000269|PubMed:15034300,
CC ECO:0000269|PubMed:8208298};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11509566, ECO:0000269|PubMed:12134018,
CC ECO:0000269|PubMed:12565829, ECO:0000269|PubMed:14555757,
CC ECO:0000269|PubMed:15034300, ECO:0000269|PubMed:8208298};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Ser-51 and Ser-
CC 555. {ECO:0000269|PubMed:12565829}.
CC -!- SUBUNIT: Monomer. Isoform 2 is found in a multisubunit complex
CC containing seven proteins, named toposome, which separates entangled
CC circular chromatin DNA during chromosome segregation. Isoform 2
CC interacts with DNAJC8 and AHSA1/AHA1 and this mediates formation of a
CC complex with the Hsp70 /Hsp90 machinery. Isoform 1 is found in a
CC complex with: DHX9, MOV10, MATR3, HNRNPU, NCL, DDX21, HSD17B4, PABPC1,
CC HNRNPM, IGF2BP1, SYNCRIP, RPL3, VIM, YBX1, NPM1, HNRNPA2B1, HNRNPC,
CC RPLP0, RPL7A and RALY. Isoform 2 binds to IGF2BP1, SYNCRIP, HNRNPA2B1
CC and HNRNPC. Isoform 1 and isoform 2 interact with SAFB which inhibits
CC its activity. Isoform 2 interacts with SAFB2 which inhibits its
CC activity. {ECO:0000269|PubMed:11509566, ECO:0000269|PubMed:14555757,
CC ECO:0000269|PubMed:15034300, ECO:0000269|PubMed:16209947,
CC ECO:0000269|PubMed:17223538, ECO:0000269|PubMed:18342604,
CC ECO:0000269|PubMed:19240134, ECO:0000269|PubMed:19674106,
CC ECO:0000269|PubMed:9237760}.
CC -!- SUBUNIT: (Microbial infection) Isoform 2 interacts with HHV-1 ICP27
CC protein. {ECO:0000269|PubMed:19553338}.
CC -!- INTERACTION:
CC Q96SB4; P50613: CDK7; NbExp=2; IntAct=EBI-539478, EBI-1245958;
CC Q96SB4; Q8WYQ5: DGCR8; NbExp=3; IntAct=EBI-539478, EBI-528411;
CC Q96SB4; Q14562: DHX8; NbExp=2; IntAct=EBI-539478, EBI-2511477;
CC Q96SB4; Q13601: KRR1; NbExp=2; IntAct=EBI-539478, EBI-744525;
CC Q96SB4; Q9NQ29: LUC7L; NbExp=2; IntAct=EBI-539478, EBI-473747;
CC Q96SB4; Q9Y383: LUC7L2; NbExp=3; IntAct=EBI-539478, EBI-352851;
CC Q96SB4; Q8NAV1: PRPF38A; NbExp=3; IntAct=EBI-539478, EBI-715374;
CC Q96SB4; Q05397: PTK2; NbExp=2; IntAct=EBI-539478, EBI-702142;
CC Q96SB4; Q14498: RBM39; NbExp=3; IntAct=EBI-539478, EBI-395290;
CC Q96SB4; Q9Y5S9: RBM8A; NbExp=2; IntAct=EBI-539478, EBI-447231;
CC Q96SB4; Q15287: RNPS1; NbExp=3; IntAct=EBI-539478, EBI-395959;
CC Q96SB4; P08621: SNRNP70; NbExp=2; IntAct=EBI-539478, EBI-1049228;
CC Q96SB4; Q8WXA9: SREK1; NbExp=2; IntAct=EBI-539478, EBI-1044237;
CC Q96SB4; Q9UPE1: SRPK3; NbExp=3; IntAct=EBI-539478, EBI-6381269;
CC Q96SB4; Q07955: SRSF1; NbExp=3; IntAct=EBI-539478, EBI-398920;
CC Q96SB4; Q16629: SRSF7; NbExp=2; IntAct=EBI-539478, EBI-398885;
CC Q96SB4; Q9BRL6: SRSF8; NbExp=2; IntAct=EBI-539478, EBI-6380719;
CC Q96SB4; P04637: TP53; NbExp=3; IntAct=EBI-539478, EBI-366083;
CC Q96SB4; Q01081: U2AF1; NbExp=3; IntAct=EBI-539478, EBI-632461;
CC Q96SB4; Q53GS9: USP39; NbExp=2; IntAct=EBI-539478, EBI-1044822;
CC Q96SB4; Q96MU7: YTHDC1; NbExp=3; IntAct=EBI-539478, EBI-2849854;
CC Q96SB4; Q15696: ZRSR2; NbExp=2; IntAct=EBI-539478, EBI-6657923;
CC Q96SB4; P0DTC9: N; Xeno; NbExp=3; IntAct=EBI-539478, EBI-25475856;
CC Q96SB4; O88453: Safb; Xeno; NbExp=2; IntAct=EBI-539478, EBI-539530;
CC Q96SB4; A7Y3Z3; Xeno; NbExp=4; IntAct=EBI-539478, EBI-7321730;
CC Q96SB4-2; Q15424: SAFB; NbExp=2; IntAct=EBI-5773439, EBI-348298;
CC Q96SB4-3; Q15424: SAFB; NbExp=2; IntAct=EBI-7160164, EBI-348298;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus. Nucleus matrix.
CC Microsome. Note=Shuttles between the nucleus and the cytoplasm.
CC Inhibition of the Hsp90 ATPase activity, osmotic stress and interaction
CC with HHV-1 ICP27 protein can induce its translocation to the nucleus.
CC KAT5/TIP60 inhibits its nuclear translocation.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus matrix.
CC Microsome. Note=Mainly localized in the microsomal fraction and the
CC cytoplasm, and to a lesser extent in the nuclear matrix.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28076779}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:28076779}. Nucleus speckle
CC {ECO:0000269|PubMed:28076779}. Chromosome
CC {ECO:0000269|PubMed:28076779}. Note=Preferentially localizes to the
CC promoter of gene coding regions. {ECO:0000269|PubMed:28076779}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=2 {ECO:0000269|PubMed:11509566, ECO:0000269|PubMed:8208298};
CC IsoId=Q96SB4-2; Sequence=Displayed;
CC Name=1; Synonyms=1a;
CC IsoId=Q96SB4-3; Sequence=VSP_042130;
CC Name=3;
CC IsoId=Q96SB4-4; Sequence=VSP_057356;
CC -!- TISSUE SPECIFICITY: Isoform 2 is predominantly expressed in the testis
CC but is also present at lower levels in heart, ovary, small intestine,
CC liver, kidney, pancreas and skeletal muscle. Isoform 1 is only seen in
CC the testis, at lower levels than isoform 2. Highly expressed in
CC different erythroid and lymphoid cell lines, with isoform 2 being far
CC more abundant than isoform 1. {ECO:0000269|PubMed:10390541,
CC ECO:0000269|PubMed:11509566, ECO:0000269|PubMed:20708644}.
CC -!- MISCELLANEOUS: [Isoform 1]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; U09564; AAA20530.1; -; mRNA.
DR EMBL; AJ318054; CAC39299.1; -; mRNA.
DR EMBL; AK299591; BAG61523.1; -; mRNA.
DR EMBL; Z99128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03859.1; -; Genomic_DNA.
DR EMBL; BC038292; AAH38292.1; -; mRNA.
DR CCDS; CCDS47415.1; -. [Q96SB4-2]
DR PIR; S45337; S45337.
DR RefSeq; NP_003128.3; NM_003137.4. [Q96SB4-2]
DR PDB; 1WAK; X-ray; 1.73 A; A=42-655.
DR PDB; 1WBP; X-ray; 2.40 A; A=42-655.
DR PDB; 3BEG; X-ray; 2.90 A; A=58-255, A=474-655.
DR PDB; 4WUA; X-ray; 2.00 A; A=42-255, A=474-655.
DR PDB; 5MXX; X-ray; 1.75 A; A=40-655.
DR PDB; 5MY8; X-ray; 1.70 A; A=58-255, A=474-655.
DR PDB; 5NNG; X-ray; 1.20 A; B=582-591.
DR PDB; 5XV7; X-ray; 2.32 A; A=67-655.
DR PDB; 6FAD; X-ray; 2.80 A; A/B/C/D=42-655.
DR PDB; 7DD1; X-ray; 2.05 A; A=58-255, A=474-655.
DR PDBsum; 1WAK; -.
DR PDBsum; 1WBP; -.
DR PDBsum; 3BEG; -.
DR PDBsum; 4WUA; -.
DR PDBsum; 5MXX; -.
DR PDBsum; 5MY8; -.
DR PDBsum; 5NNG; -.
DR PDBsum; 5XV7; -.
DR PDBsum; 6FAD; -.
DR PDBsum; 7DD1; -.
DR AlphaFoldDB; Q96SB4; -.
DR SMR; Q96SB4; -.
DR BioGRID; 112610; 338.
DR CORUM; Q96SB4; -.
DR DIP; DIP-33888N; -.
DR IntAct; Q96SB4; 344.
DR MINT; Q96SB4; -.
DR STRING; 9606.ENSP00000362931; -.
DR BindingDB; Q96SB4; -.
DR ChEMBL; CHEMBL4375; -.
DR DrugCentral; Q96SB4; -.
DR GuidetoPHARMACOLOGY; 2208; -.
DR MoonDB; Q96SB4; Predicted.
DR GlyGen; Q96SB4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96SB4; -.
DR MetOSite; Q96SB4; -.
DR PhosphoSitePlus; Q96SB4; -.
DR SwissPalm; Q96SB4; -.
DR BioMuta; SRPK1; -.
DR DMDM; 209572680; -.
DR EPD; Q96SB4; -.
DR jPOST; Q96SB4; -.
DR MassIVE; Q96SB4; -.
DR MaxQB; Q96SB4; -.
DR PaxDb; Q96SB4; -.
DR PeptideAtlas; Q96SB4; -.
DR PRIDE; Q96SB4; -.
DR ProteomicsDB; 78098; -. [Q96SB4-2]
DR ProteomicsDB; 78099; -. [Q96SB4-3]
DR Antibodypedia; 6714; 482 antibodies from 32 providers.
DR DNASU; 6732; -.
DR Ensembl; ENST00000373825.7; ENSP00000362931.2; ENSG00000096063.16. [Q96SB4-2]
DR Ensembl; ENST00000423325.6; ENSP00000391069.2; ENSG00000096063.16. [Q96SB4-4]
DR GeneID; 6732; -.
DR KEGG; hsa:6732; -.
DR MANE-Select; ENST00000373825.7; ENSP00000362931.2; NM_003137.5; NP_003128.3.
DR UCSC; uc003olj.4; human. [Q96SB4-2]
DR CTD; 6732; -.
DR DisGeNET; 6732; -.
DR GeneCards; SRPK1; -.
DR HGNC; HGNC:11305; SRPK1.
DR HPA; ENSG00000096063; Low tissue specificity.
DR MIM; 601939; gene.
DR neXtProt; NX_Q96SB4; -.
DR OpenTargets; ENSG00000096063; -.
DR PharmGKB; PA36129; -.
DR VEuPathDB; HostDB:ENSG00000096063; -.
DR eggNOG; KOG1290; Eukaryota.
DR GeneTree; ENSGT00940000155264; -.
DR HOGENOM; CLU_000288_81_9_1; -.
DR InParanoid; Q96SB4; -.
DR OMA; HEGQRPP; -.
DR OrthoDB; 290680at2759; -.
DR PhylomeDB; Q96SB4; -.
DR TreeFam; TF105334; -.
DR PathwayCommons; Q96SB4; -.
DR Reactome; R-HSA-9694631; Maturation of nucleoprotein.
DR SignaLink; Q96SB4; -.
DR SIGNOR; Q96SB4; -.
DR BioGRID-ORCS; 6732; 34 hits in 1086 CRISPR screens.
DR ChiTaRS; SRPK1; human.
DR EvolutionaryTrace; Q96SB4; -.
DR GeneWiki; SRPK1; -.
DR GenomeRNAi; 6732; -.
DR Pharos; Q96SB4; Tchem.
DR PRO; PR:Q96SB4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96SB4; protein.
DR Bgee; ENSG00000096063; Expressed in sperm and 206 other tissues.
DR ExpressionAtlas; Q96SB4; baseline and differential.
DR Genevisible; Q96SB4; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IC:BHF-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:BHF-UCL.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IDA:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0050684; P:regulation of mRNA processing; IDA:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; TAS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0035092; P:sperm DNA condensation; TAS:UniProtKB.
DR GO; GO:0000245; P:spliceosomal complex assembly; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Chromosome;
KW Chromosome partition; Cytoplasm; Differentiation;
KW Direct protein sequencing; Endoplasmic reticulum; Host-virus interaction;
KW Kinase; Microsome; mRNA processing; mRNA splicing; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..655
FT /note="SRSF protein kinase 1"
FT /id="PRO_0000086674"
FT DOMAIN 80..653
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /note="Proton acceptor"
FT BINDING 86..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:16209947"
FT BINDING 109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:16209947"
FT BINDING 166..168
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:16209947"
FT MOD_RES 51
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:12565829,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 555
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:12565829"
FT VAR_SEQ 1..25
FT /note="MERKVLALQARKKRTKAKKDKAQRK -> MGIFVSFLR (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057356"
FT VAR_SEQ 4
FT /note="K -> KGERWSGLRHEGQWSPGRGPGQRRELRLTAAVRFPDVRRPSTEVAPP
FT HTPCLWAAGPRPSFRASSGAGRSRPLFPARPARALGPLQGPALGGRRRPPPARPLTRPE
FT TPPAHPARALLCAPWAASPTPAASPSPQPPPRQAPQPGLAPLLGLHPHLGRLLSSTFAL
FT HPSLSPA (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:11509566"
FT /id="VSP_042130"
FT VARIANT 72
FT /note="I -> T (in dbSNP:rs35519113)"
FT /id="VAR_051669"
FT MUTAGEN 37
FT /note="S->A: No effect on protein phosphorylation."
FT /evidence="ECO:0000269|PubMed:12565829"
FT MUTAGEN 51
FT /note="S->A: Protein phosphorylation impaired at this
FT position."
FT /evidence="ECO:0000269|PubMed:12565829"
FT MUTAGEN 222
FT /note="S->A: No effect on protein phosphorylation."
FT /evidence="ECO:0000269|PubMed:12565829"
FT MUTAGEN 311
FT /note="S->G: No effect on protein phosphorylation."
FT /evidence="ECO:0000269|PubMed:12565829"
FT MUTAGEN 436
FT /note="S->G: No effect on protein phosphorylation."
FT /evidence="ECO:0000269|PubMed:12565829"
FT MUTAGEN 555
FT /note="S->A: Protein phosphorylation impaired at this
FT position."
FT /evidence="ECO:0000269|PubMed:12565829"
FT MUTAGEN 619
FT /note="S->A: No effect on protein phosphorylation."
FT /evidence="ECO:0000269|PubMed:12565829"
FT CONFLICT 210
FT /note="I -> T (in Ref. 6; AAH38292)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="I -> L (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="I -> L (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..401
FT /note="SQ -> LP (in Ref. 1; AAA20530)"
FT /evidence="ECO:0000305"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5MXX"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5MY8"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:5MY8"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:5MY8"
FT TURN 100..103
FT /evidence="ECO:0007829|PDB:5MY8"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 115..133
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:5MY8"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:5MY8"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:5MY8"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:1WBP"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:5MY8"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 186..205
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:5MY8"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 485..490
FT /evidence="ECO:0007829|PDB:5MY8"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:1WAK"
FT TURN 504..506
FT /evidence="ECO:0007829|PDB:5MXX"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 520..524
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 531..546
FT /evidence="ECO:0007829|PDB:5MY8"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 561..573
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 578..583
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 587..589
FT /evidence="ECO:0007829|PDB:5MY8"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 608..614
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 620..630
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 631..634
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 644..648
FT /evidence="ECO:0007829|PDB:5MY8"
FT HELIX 651..654
FT /evidence="ECO:0007829|PDB:5MY8"
SQ SEQUENCE 655 AA; 74325 MW; 900E980FE1C16B9A CRC64;
MERKVLALQA RKKRTKAKKD KAQRKSETQH RGSAPHSESD LPEQEEEILG SDDDEQEDPN
DYCKGGYHLV KIGDLFNGRY HVIRKLGWGH FSTVWLSWDI QGKKFVAMKV VKSAEHYTET
ALDEIRLLKS VRNSDPNDPN REMVVQLLDD FKISGVNGTH ICMVFEVLGH HLLKWIIKSN
YQGLPLPCVK KIIQQVLQGL DYLHTKCRII HTDIKPENIL LSVNEQYIRR LAAEATEWQR
SGAPPPSGSA VSTAPQPKPA DKMSKNKKKK LKKKQKRQAE LLEKRMQEIE EMEKESGPGQ
KRPNKQEESE SPVERPLKEN PPNKMTQEKL EESSTIGQDQ TLMERDTEGG AAEINCNGVI
EVINYTQNSN NETLRHKEDL HNANDCDVQN LNQESSFLSS QNGDSSTSQE TDSCTPITSE
VSDTMVCQSS STVGQSFSEQ HISQLQESIR AEIPCEDEQE QEHNGPLDNK GKSTAGNFLV
NPLEPKNAEK LKVKIADLGN ACWVHKHFTE DIQTRQYRSL EVLIGSGYNT PADIWSTACM
AFELATGDYL FEPHSGEEYT RDEDHIALII ELLGKVPRKL IVAGKYSKEF FTKKGDLKHI
TKLKPWGLFE VLVEKYEWSQ EEAAGFTDFL LPMLELIPEK RATAAECLRH PWLNS
