Full text data of SRPK1
SRPK1
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
SRSF protein kinase 1; 2.7.11.1 (SFRS protein kinase 1; Serine/arginine-rich protein-specific kinase 1; SR-protein-specific kinase 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
SRSF protein kinase 1; 2.7.11.1 (SFRS protein kinase 1; Serine/arginine-rich protein-specific kinase 1; SR-protein-specific kinase 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00290439
IPI00290439 SRPK1a protein kinase SRPK1a protein kinase membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00290439 SRPK1a protein kinase SRPK1a protein kinase membrane n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q96SB4
ID SRPK1_HUMAN Reviewed; 655 AA.
AC Q96SB4; Q12890; Q5R364; Q5R365; Q8IY12;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 14-OCT-2008, sequence version 2.
DT 22-JAN-2014, entry version 125.
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;
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 [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
RT factors in the cell cycle.";
RL Nature 369:678-682(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH SAFB.
RC TISSUE=Testis;
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 [3]
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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 330-345 AND 353-375, AND FUNCTION IN
RP PHOSPHORYLATION OF 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
RT kinases phosphorylating hepatitis B virus core protein.";
RL J. Virol. 76:8124-8137(2002).
RN [6]
RP PROTEIN SEQUENCE OF 376-400 AND 616-636, FUNCTION, AND IDENTIFICATION
RP IN A 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 [7]
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
RT U2AF65 and SR proteins in splicing of pre-mRNA.";
RL Nature 388:397-400(1997).
RN [8]
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
RT specificities.";
RL Biochem. Biophys. Res. Commun. 255:602-607(1999).
RN [9]
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.,
RA Chevaillier P., 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 [10]
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
RT factor 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12601-12606(2003).
RN [11]
RP ENZYME REGULATION, PHOSPHORYLATION AT SER-51 AND SER-555, AND
RP MUTAGENESIS OF SER-37; SER-51; SER-222; SER-311; SER-436; SER-555 AND
RP 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-
RT specific kinase 1.";
RL Biochem. Biophys. Res. Commun. 301:650-656(2003).
RN [12]
RP FUNCTION IN NEGATIVE REGULATION OF HEPATITIS B VIRUS (HBV)
RP 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
RT protein.";
RL Virology 342:150-158(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [14]
RP FUNCTION IN PHOSPHORYLATION OF SRSF1, AND THE MECHANISM OF
RP PHOSPHORYATION.
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.,
RA 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 [15]
RP FUNCTION IN PHOSPHORYLATION OF SRSF1, AND THE MECHANISM OF
RP PHOSPHORYATION.
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.,
RA Ghosh G., Jennings P.A., Fu X.D., Adams J.A.;
RT "Adaptable molecular interactions guide phosphorylation of the SR
RT protein ASF/SF2 by SRPK1.";
RL J. Mol. Biol. 382:894-909(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
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 [18]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP FUNCTION IN PHOSPHORYLATION OF SRSF1, AND THE MECHANISM OF
RP PHOSPHORYATION.
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
RT by SRPK1.";
RL Biochemistry 48:11432-11440(2009).
RN [20]
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 [21]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DNAJB1/HSP40 AND
RP 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 [22]
RP FUNCTION IN PHOSPHORYLATION OF SRSF1, AND THE MECHANISM OF
RP PHOSPHORYATION.
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 [23]
RP INTERACTION WITH HHV-1 ICP27 PROTEIN.
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
RT virus 1 infection.";
RL J. Virol. 83:8970-8975(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
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 [25]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION
RP OF 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 [26]
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.,
RA Buerckstuemmer T., 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 [27]
RP SUBCELLULAR LOCATION.
RX PubMed=21157427; DOI=10.1038/emboj.2010.333;
RA Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C.,
RA Brambilla E., Gazzeri S., Eymin B.;
RT "Acetylation and phosphorylation of SRSF2 control cell fate decision
RT in response to cisplatin.";
RL EMBO J. 30:510-523(2011).
RN [28]
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 [29]
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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 42-438 IN COMPLEX WITH ATP
RP AND 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 [32]
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 [33]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 58-655 IN COMPLEX WITH SRSF1,
RP AND 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
RT processive 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
CC located in regions rich in arginine/serine dipeptides, known as RS
CC domains and is involved in the phosphorylation of SR splicing
CC factors and the regulation of splicing. Plays a central role in
CC the regulatory network for splicing, controlling the intranuclear
CC distribution of splicing factors in interphase cells and the
CC reorganization of nuclear speckles during mitosis. Can influence
CC additional steps of mRNA maturation, as well as other cellular
CC activities, such as chromatin reorganization in somatic and sperm
CC cells and cell cycle progression. Isoform 2 phosphorylates SFRS2,
CC ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a
CC directional (C-terminal to N-terminal) and a dual-track mechanism
CC incorporating both processive phosphorylation (in which the kinase
CC stays attached to the substrate after each round of
CC phosphorylation) and distributive phosphorylation steps (in which
CC the kinase and substrate dissociate after each phosphorylation
CC event). The RS domain of SRSF1 binds first to a docking groove in
CC the large lobe of the kinase domain of SRPK1. This induces certain
CC structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing
CC RRM2 to bind the kinase and initiate phosphorylation. The cycles
CC continue for several phosphorylation steps in a processive manner
CC (steps 1-8) until the last few phosphorylation steps
CC (approximately steps 9-12). During that time, a mechanical stress
CC induces the unfolding of the beta-4 motif in RRM2, which then
CC docks at the docking groove of SRPK1. This also signals RRM2 to
CC begin to dissociate, which facilitates SRSF1 dissociation after
CC phosphorylation is completed. Isoform 2 can mediate hepatitis B
CC virus (HBV) core protein phosphorylation. It plays a negative role
CC in the regulation of HBV replication through a mechanism not
CC involving the phosphorylation of the core protein but by reducing
CC the packaging efficiency of the pregenomic RNA (pgRNA) without
CC affecting the formation of the viral core particles. Isoform 1 and
CC isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of
CC isoform 1/isoform 2 plays a decisive role in determining cell fate
CC in K-562 leukaemic cell line: isoform 2 favors proliferation where
CC as isoform 1 favors differentiation.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Activated by phosphorylation on Ser-51 and Ser-
CC 555.
CC -!- SUBUNIT: Monomer. Isoform 2 is found in a multisubunit complex
CC containing seven proteins, named toposome, which separates
CC entangled circular chromatin DNA during chromosome segregation.
CC Isoform 2 interacts with HHV-1 ICP27 protein. Isoform 2 interacts
CC with DNAJB1/HSP40 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,
CC PABPC1, HNRNPM, IGF2BP1, SYNCRIP, RPL3, VIM, YBX1, NPM1,
CC HNRNPA2B1, HNRNPC, RPLP0, RPL7A and RALY. Isoform 2 binds to
CC IGF2BP1, SYNCRIP, HNRNPA2B1 and HNRNPC. Isoform 1 and isoform 2
CC interact with SAFB which inhibits its activity. Isoform 2
CC interacts with SAFB2 which inhibits its activity.
CC -!- INTERACTION:
CC A7Y3Z3:- (xeno); NbExp=4; IntAct=EBI-539478, EBI-7321730;
CC Q8WYQ5:DGCR8; NbExp=3; IntAct=EBI-539478, EBI-528411;
CC Q9NQ29:LUC7L; NbExp=2; IntAct=EBI-539478, EBI-473747;
CC Q9Y383:LUC7L2; NbExp=2; IntAct=EBI-539478, EBI-352851;
CC Q8NAV1:PRPF38A; NbExp=2; IntAct=EBI-539478, EBI-715374;
CC Q14498:RBM39; NbExp=2; IntAct=EBI-539478, EBI-395290;
CC Q9Y5S9:RBM8A; NbExp=2; IntAct=EBI-539478, EBI-447231;
CC Q15287:RNPS1; NbExp=2; IntAct=EBI-539478, EBI-395959;
CC Q15424:SAFB; NbExp=2; IntAct=EBI-5773439, EBI-348298;
CC O88453:Safb (xeno); NbExp=2; IntAct=EBI-539478, EBI-539530;
CC Q9UPE1:SRPK3; NbExp=2; IntAct=EBI-539478, EBI-6381269;
CC Q07955:SRSF1; NbExp=3; IntAct=EBI-539478, EBI-398920;
CC Q16629:SRSF7; NbExp=2; IntAct=EBI-539478, EBI-398885;
CC Q9BRL6:SRSF8; NbExp=2; IntAct=EBI-539478, EBI-6380719;
CC P04637:TP53; NbExp=3; IntAct=EBI-539478, EBI-366083;
CC Q96MU7:YTHDC1; NbExp=3; IntAct=EBI-539478, EBI-2849854;
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. Nucleus
CC matrix. Microsome. Note=Shuttles between the nucleus and the
CC cytoplasm. Inhibition of the Hsp90 ATPase activity, osmotic stress
CC and interaction with HHV-1 ICP27 protein can induce its
CC translocation to the nucleus. KAT5/TIP60 inhibits its nuclear
CC translocation.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus matrix.
CC Microsome. Note=Mainly localized in the microsomal fraction and
CC the cytoplasm, and to a lesser extent in the nuclear matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q96SB4-2; Sequence=Displayed;
CC Name=1; Synonyms=1a;
CC IsoId=Q96SB4-3; Sequence=VSP_042130;
CC Note=Due to intron retention;
CC -!- TISSUE SPECIFICITY: Isoform 2 is predominantly expressed in the
CC testis but is also present at lower levels in heart, ovary, small
CC intestine, liver, kidney, pancreas and skeletal muscle. Isoform 1
CC is only seen in the testis, at lower levels than isoform 2. Highly
CC expressed in different erythroid and lymphoid cell lines, with
CC isoform 2 being far more abundant than isoform 1.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC Ser/Thr protein kinase family.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI20544.1; Type=Erroneous gene model prediction;
CC Sequence=CAI20545.1; Type=Erroneous gene model prediction;
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DR EMBL; U09564; AAA20530.1; -; mRNA.
DR EMBL; AJ318054; CAC39299.1; -; mRNA.
DR EMBL; Z99128; CAI20544.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z99128; CAI20545.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC038292; AAH38292.1; -; mRNA.
DR PIR; S45337; S45337.
DR RefSeq; NP_003128.3; NM_003137.4.
DR UniGene; Hs.443861; -.
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=58-655.
DR PDBsum; 1WAK; -.
DR PDBsum; 1WBP; -.
DR PDBsum; 3BEG; -.
DR ProteinModelPortal; Q96SB4; -.
DR SMR; Q96SB4; 63-263, 477-655.
DR IntAct; Q96SB4; 218.
DR MINT; MINT-262701; -.
DR STRING; 9606.ENSP00000391069; -.
DR BindingDB; Q96SB4; -.
DR ChEMBL; CHEMBL4375; -.
DR GuidetoPHARMACOLOGY; 2208; -.
DR PhosphoSite; Q96SB4; -.
DR DMDM; 209572680; -.
DR PaxDb; Q96SB4; -.
DR PRIDE; Q96SB4; -.
DR DNASU; 6732; -.
DR Ensembl; ENST00000373825; ENSP00000362931; ENSG00000096063.
DR GeneID; 6732; -.
DR KEGG; hsa:6732; -.
DR UCSC; uc003olh.3; human.
DR CTD; 6732; -.
DR GeneCards; GC06M035801; -.
DR H-InvDB; HIX0005813; -.
DR HGNC; HGNC:11305; SRPK1.
DR HPA; HPA016431; -.
DR MIM; 601939; gene.
DR neXtProt; NX_Q96SB4; -.
DR PharmGKB; PA36129; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000171558; -.
DR HOVERGEN; HBG108512; -.
DR KO; K15409; -.
DR OrthoDB; EOG70S74X; -.
DR SignaLink; Q96SB4; -.
DR EvolutionaryTrace; Q96SB4; -.
DR GeneWiki; SRPK1; -.
DR GenomeRNAi; 6732; -.
DR NextBio; 26262; -.
DR PRO; PR:Q96SB4; -.
DR ArrayExpress; Q96SB4; -.
DR Bgee; Q96SB4; -.
DR CleanEx; HS_SRPK1; -.
DR Genevestigator; Q96SB4; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IC:BHF-UCL.
DR GO; GO:0007243; P:intracellular protein kinase cascade; IDA:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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: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 chromatin condensation; TAS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom.
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 SUPFAM; SSF56112; SSF56112; 2.
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 partition;
KW Complete proteome; Cytoplasm; Differentiation;
KW Direct protein sequencing; Endoplasmic reticulum;
KW Host-virus interaction; Kinase; Microsome; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1 655 SRSF protein kinase 1.
FT /FTId=PRO_0000086674.
FT DOMAIN 80 653 Protein kinase.
FT NP_BIND 86 94 ATP.
FT NP_BIND 166 168 ATP.
FT ACT_SITE 213 213 Proton acceptor.
FT BINDING 109 109 ATP.
FT MOD_RES 51 51 Phosphoserine; by CK2.
FT MOD_RES 309 309 Phosphoserine (By similarity).
FT MOD_RES 311 311 Phosphoserine.
FT MOD_RES 555 555 Phosphoserine; by CK2.
FT VAR_SEQ 4 4 K -> KGERWSGLRHEGQWSPGRGPGQRRELRLTAAVRFPD
FT VRRPSTEVAPPHTPCLWAAGPRPSFRASSGAGRSRPLFPAR
FT PARALGPLQGPALGGRRRPPPARPLTRPETPPAHPARALLC
FT APWAASPTPAASPSPQPPPRQAPQPGLAPLLGLHPHLGRLL
FT SSTFALHPSLSPA (in isoform 1).
FT /FTId=VSP_042130.
FT VARIANT 72 72 I -> T (in dbSNP:rs35519113).
FT /FTId=VAR_051669.
FT MUTAGEN 37 37 S->A: No effect on protein
FT phosphorylation.
FT MUTAGEN 51 51 S->A: Protein phosphorylation impaired at
FT this position.
FT MUTAGEN 222 222 S->A: No effect on protein
FT phosphorylation.
FT MUTAGEN 311 311 S->G: No effect on protein
FT phosphorylation.
FT MUTAGEN 436 436 S->G: No effect on protein
FT phosphorylation.
FT MUTAGEN 555 555 S->A: Protein phosphorylation impaired at
FT this position.
FT MUTAGEN 619 619 S->A: No effect on protein
FT phosphorylation.
FT CONFLICT 210 210 I -> T (in Ref. 4; AAH38292).
FT CONFLICT 360 360 I -> L (in Ref. 5; AA sequence).
FT CONFLICT 363 363 I -> L (in Ref. 5; AA sequence).
FT CONFLICT 400 401 SQ -> LP (in Ref. 1; AAA20530).
FT TURN 77 79
FT STRAND 80 88
FT STRAND 90 99
FT TURN 100 103
FT STRAND 104 111
FT HELIX 115 133
FT HELIX 139 143
FT STRAND 147 155
FT STRAND 158 165
FT STRAND 168 171
FT HELIX 172 178
FT TURN 179 181
FT HELIX 186 205
FT HELIX 216 218
FT STRAND 219 221
FT HELIX 225 235
FT HELIX 485 490
FT STRAND 493 495
FT HELIX 498 500
FT STRAND 502 506
FT HELIX 515 517
FT HELIX 520 524
FT HELIX 531 546
FT STRAND 557 559
FT HELIX 561 573
FT HELIX 578 583
FT HELIX 587 589
FT STRAND 595 599
FT HELIX 608 614
FT HELIX 620 630
FT HELIX 631 634
FT HELIX 638 640
FT HELIX 644 648
FT HELIX 651 654
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
//
ID SRPK1_HUMAN Reviewed; 655 AA.
AC Q96SB4; Q12890; Q5R364; Q5R365; Q8IY12;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 14-OCT-2008, sequence version 2.
DT 22-JAN-2014, entry version 125.
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;
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 [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
RT factors in the cell cycle.";
RL Nature 369:678-682(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH SAFB.
RC TISSUE=Testis;
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 [3]
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.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA 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.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 330-345 AND 353-375, AND FUNCTION IN
RP PHOSPHORYLATION OF 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
RT kinases phosphorylating hepatitis B virus core protein.";
RL J. Virol. 76:8124-8137(2002).
RN [6]
RP PROTEIN SEQUENCE OF 376-400 AND 616-636, FUNCTION, AND IDENTIFICATION
RP IN A 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 [7]
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
RT U2AF65 and SR proteins in splicing of pre-mRNA.";
RL Nature 388:397-400(1997).
RN [8]
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
RT specificities.";
RL Biochem. Biophys. Res. Commun. 255:602-607(1999).
RN [9]
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.,
RA Chevaillier P., 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 [10]
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
RT factor 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12601-12606(2003).
RN [11]
RP ENZYME REGULATION, PHOSPHORYLATION AT SER-51 AND SER-555, AND
RP MUTAGENESIS OF SER-37; SER-51; SER-222; SER-311; SER-436; SER-555 AND
RP 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-
RT specific kinase 1.";
RL Biochem. Biophys. Res. Commun. 301:650-656(2003).
RN [12]
RP FUNCTION IN NEGATIVE REGULATION OF HEPATITIS B VIRUS (HBV)
RP 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
RT protein.";
RL Virology 342:150-158(2005).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [14]
RP FUNCTION IN PHOSPHORYLATION OF SRSF1, AND THE MECHANISM OF
RP PHOSPHORYATION.
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.,
RA 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 [15]
RP FUNCTION IN PHOSPHORYLATION OF SRSF1, AND THE MECHANISM OF
RP PHOSPHORYATION.
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.,
RA Ghosh G., Jennings P.A., Fu X.D., Adams J.A.;
RT "Adaptable molecular interactions guide phosphorylation of the SR
RT protein ASF/SF2 by SRPK1.";
RL J. Mol. Biol. 382:894-909(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
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 [18]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [19]
RP FUNCTION IN PHOSPHORYLATION OF SRSF1, AND THE MECHANISM OF
RP PHOSPHORYATION.
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
RT by SRPK1.";
RL Biochemistry 48:11432-11440(2009).
RN [20]
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 [21]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DNAJB1/HSP40 AND
RP 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 [22]
RP FUNCTION IN PHOSPHORYLATION OF SRSF1, AND THE MECHANISM OF
RP PHOSPHORYATION.
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 [23]
RP INTERACTION WITH HHV-1 ICP27 PROTEIN.
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
RT virus 1 infection.";
RL J. Virol. 83:8970-8975(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP SPECTROMETRY.
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 [25]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION
RP OF 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 [26]
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.,
RA Buerckstuemmer T., 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 [27]
RP SUBCELLULAR LOCATION.
RX PubMed=21157427; DOI=10.1038/emboj.2010.333;
RA Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C.,
RA Brambilla E., Gazzeri S., Eymin B.;
RT "Acetylation and phosphorylation of SRSF2 control cell fate decision
RT in response to cisplatin.";
RL EMBO J. 30:510-523(2011).
RN [28]
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 [29]
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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [31]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 42-438 IN COMPLEX WITH ATP
RP AND 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 [32]
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 [33]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 58-655 IN COMPLEX WITH SRSF1,
RP AND 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
RT processive 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
CC located in regions rich in arginine/serine dipeptides, known as RS
CC domains and is involved in the phosphorylation of SR splicing
CC factors and the regulation of splicing. Plays a central role in
CC the regulatory network for splicing, controlling the intranuclear
CC distribution of splicing factors in interphase cells and the
CC reorganization of nuclear speckles during mitosis. Can influence
CC additional steps of mRNA maturation, as well as other cellular
CC activities, such as chromatin reorganization in somatic and sperm
CC cells and cell cycle progression. Isoform 2 phosphorylates SFRS2,
CC ZRSR2, LBR and PRM1. Isoform 2 phosphorylates SRSF1 using a
CC directional (C-terminal to N-terminal) and a dual-track mechanism
CC incorporating both processive phosphorylation (in which the kinase
CC stays attached to the substrate after each round of
CC phosphorylation) and distributive phosphorylation steps (in which
CC the kinase and substrate dissociate after each phosphorylation
CC event). The RS domain of SRSF1 binds first to a docking groove in
CC the large lobe of the kinase domain of SRPK1. This induces certain
CC structural changes in SRPK1 and/or RRM2 domain of SRSF1, allowing
CC RRM2 to bind the kinase and initiate phosphorylation. The cycles
CC continue for several phosphorylation steps in a processive manner
CC (steps 1-8) until the last few phosphorylation steps
CC (approximately steps 9-12). During that time, a mechanical stress
CC induces the unfolding of the beta-4 motif in RRM2, which then
CC docks at the docking groove of SRPK1. This also signals RRM2 to
CC begin to dissociate, which facilitates SRSF1 dissociation after
CC phosphorylation is completed. Isoform 2 can mediate hepatitis B
CC virus (HBV) core protein phosphorylation. It plays a negative role
CC in the regulation of HBV replication through a mechanism not
CC involving the phosphorylation of the core protein but by reducing
CC the packaging efficiency of the pregenomic RNA (pgRNA) without
CC affecting the formation of the viral core particles. Isoform 1 and
CC isoform 2 can induce splicing of exon 10 in MAPT/TAU. The ratio of
CC isoform 1/isoform 2 plays a decisive role in determining cell fate
CC in K-562 leukaemic cell line: isoform 2 favors proliferation where
CC as isoform 1 favors differentiation.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Activated by phosphorylation on Ser-51 and Ser-
CC 555.
CC -!- SUBUNIT: Monomer. Isoform 2 is found in a multisubunit complex
CC containing seven proteins, named toposome, which separates
CC entangled circular chromatin DNA during chromosome segregation.
CC Isoform 2 interacts with HHV-1 ICP27 protein. Isoform 2 interacts
CC with DNAJB1/HSP40 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,
CC PABPC1, HNRNPM, IGF2BP1, SYNCRIP, RPL3, VIM, YBX1, NPM1,
CC HNRNPA2B1, HNRNPC, RPLP0, RPL7A and RALY. Isoform 2 binds to
CC IGF2BP1, SYNCRIP, HNRNPA2B1 and HNRNPC. Isoform 1 and isoform 2
CC interact with SAFB which inhibits its activity. Isoform 2
CC interacts with SAFB2 which inhibits its activity.
CC -!- INTERACTION:
CC A7Y3Z3:- (xeno); NbExp=4; IntAct=EBI-539478, EBI-7321730;
CC Q8WYQ5:DGCR8; NbExp=3; IntAct=EBI-539478, EBI-528411;
CC Q9NQ29:LUC7L; NbExp=2; IntAct=EBI-539478, EBI-473747;
CC Q9Y383:LUC7L2; NbExp=2; IntAct=EBI-539478, EBI-352851;
CC Q8NAV1:PRPF38A; NbExp=2; IntAct=EBI-539478, EBI-715374;
CC Q14498:RBM39; NbExp=2; IntAct=EBI-539478, EBI-395290;
CC Q9Y5S9:RBM8A; NbExp=2; IntAct=EBI-539478, EBI-447231;
CC Q15287:RNPS1; NbExp=2; IntAct=EBI-539478, EBI-395959;
CC Q15424:SAFB; NbExp=2; IntAct=EBI-5773439, EBI-348298;
CC O88453:Safb (xeno); NbExp=2; IntAct=EBI-539478, EBI-539530;
CC Q9UPE1:SRPK3; NbExp=2; IntAct=EBI-539478, EBI-6381269;
CC Q07955:SRSF1; NbExp=3; IntAct=EBI-539478, EBI-398920;
CC Q16629:SRSF7; NbExp=2; IntAct=EBI-539478, EBI-398885;
CC Q9BRL6:SRSF8; NbExp=2; IntAct=EBI-539478, EBI-6380719;
CC P04637:TP53; NbExp=3; IntAct=EBI-539478, EBI-366083;
CC Q96MU7:YTHDC1; NbExp=3; IntAct=EBI-539478, EBI-2849854;
CC -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus. Nucleus
CC matrix. Microsome. Note=Shuttles between the nucleus and the
CC cytoplasm. Inhibition of the Hsp90 ATPase activity, osmotic stress
CC and interaction with HHV-1 ICP27 protein can induce its
CC translocation to the nucleus. KAT5/TIP60 inhibits its nuclear
CC translocation.
CC -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus matrix.
CC Microsome. Note=Mainly localized in the microsomal fraction and
CC the cytoplasm, and to a lesser extent in the nuclear matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q96SB4-2; Sequence=Displayed;
CC Name=1; Synonyms=1a;
CC IsoId=Q96SB4-3; Sequence=VSP_042130;
CC Note=Due to intron retention;
CC -!- TISSUE SPECIFICITY: Isoform 2 is predominantly expressed in the
CC testis but is also present at lower levels in heart, ovary, small
CC intestine, liver, kidney, pancreas and skeletal muscle. Isoform 1
CC is only seen in the testis, at lower levels than isoform 2. Highly
CC expressed in different erythroid and lymphoid cell lines, with
CC isoform 2 being far more abundant than isoform 1.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC Ser/Thr protein kinase family.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI20544.1; Type=Erroneous gene model prediction;
CC Sequence=CAI20545.1; Type=Erroneous gene model prediction;
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DR EMBL; U09564; AAA20530.1; -; mRNA.
DR EMBL; AJ318054; CAC39299.1; -; mRNA.
DR EMBL; Z99128; CAI20544.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z99128; CAI20545.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC038292; AAH38292.1; -; mRNA.
DR PIR; S45337; S45337.
DR RefSeq; NP_003128.3; NM_003137.4.
DR UniGene; Hs.443861; -.
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=58-655.
DR PDBsum; 1WAK; -.
DR PDBsum; 1WBP; -.
DR PDBsum; 3BEG; -.
DR ProteinModelPortal; Q96SB4; -.
DR SMR; Q96SB4; 63-263, 477-655.
DR IntAct; Q96SB4; 218.
DR MINT; MINT-262701; -.
DR STRING; 9606.ENSP00000391069; -.
DR BindingDB; Q96SB4; -.
DR ChEMBL; CHEMBL4375; -.
DR GuidetoPHARMACOLOGY; 2208; -.
DR PhosphoSite; Q96SB4; -.
DR DMDM; 209572680; -.
DR PaxDb; Q96SB4; -.
DR PRIDE; Q96SB4; -.
DR DNASU; 6732; -.
DR Ensembl; ENST00000373825; ENSP00000362931; ENSG00000096063.
DR GeneID; 6732; -.
DR KEGG; hsa:6732; -.
DR UCSC; uc003olh.3; human.
DR CTD; 6732; -.
DR GeneCards; GC06M035801; -.
DR H-InvDB; HIX0005813; -.
DR HGNC; HGNC:11305; SRPK1.
DR HPA; HPA016431; -.
DR MIM; 601939; gene.
DR neXtProt; NX_Q96SB4; -.
DR PharmGKB; PA36129; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000171558; -.
DR HOVERGEN; HBG108512; -.
DR KO; K15409; -.
DR OrthoDB; EOG70S74X; -.
DR SignaLink; Q96SB4; -.
DR EvolutionaryTrace; Q96SB4; -.
DR GeneWiki; SRPK1; -.
DR GenomeRNAi; 6732; -.
DR NextBio; 26262; -.
DR PRO; PR:Q96SB4; -.
DR ArrayExpress; Q96SB4; -.
DR Bgee; Q96SB4; -.
DR CleanEx; HS_SRPK1; -.
DR Genevestigator; Q96SB4; -.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IC:BHF-UCL.
DR GO; GO:0007243; P:intracellular protein kinase cascade; IDA:UniProtKB.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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: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 chromatin condensation; TAS:UniProtKB.
DR InterPro; IPR011009; Kinase-like_dom.
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 SUPFAM; SSF56112; SSF56112; 2.
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 partition;
KW Complete proteome; Cytoplasm; Differentiation;
KW Direct protein sequencing; Endoplasmic reticulum;
KW Host-virus interaction; Kinase; Microsome; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1 655 SRSF protein kinase 1.
FT /FTId=PRO_0000086674.
FT DOMAIN 80 653 Protein kinase.
FT NP_BIND 86 94 ATP.
FT NP_BIND 166 168 ATP.
FT ACT_SITE 213 213 Proton acceptor.
FT BINDING 109 109 ATP.
FT MOD_RES 51 51 Phosphoserine; by CK2.
FT MOD_RES 309 309 Phosphoserine (By similarity).
FT MOD_RES 311 311 Phosphoserine.
FT MOD_RES 555 555 Phosphoserine; by CK2.
FT VAR_SEQ 4 4 K -> KGERWSGLRHEGQWSPGRGPGQRRELRLTAAVRFPD
FT VRRPSTEVAPPHTPCLWAAGPRPSFRASSGAGRSRPLFPAR
FT PARALGPLQGPALGGRRRPPPARPLTRPETPPAHPARALLC
FT APWAASPTPAASPSPQPPPRQAPQPGLAPLLGLHPHLGRLL
FT SSTFALHPSLSPA (in isoform 1).
FT /FTId=VSP_042130.
FT VARIANT 72 72 I -> T (in dbSNP:rs35519113).
FT /FTId=VAR_051669.
FT MUTAGEN 37 37 S->A: No effect on protein
FT phosphorylation.
FT MUTAGEN 51 51 S->A: Protein phosphorylation impaired at
FT this position.
FT MUTAGEN 222 222 S->A: No effect on protein
FT phosphorylation.
FT MUTAGEN 311 311 S->G: No effect on protein
FT phosphorylation.
FT MUTAGEN 436 436 S->G: No effect on protein
FT phosphorylation.
FT MUTAGEN 555 555 S->A: Protein phosphorylation impaired at
FT this position.
FT MUTAGEN 619 619 S->A: No effect on protein
FT phosphorylation.
FT CONFLICT 210 210 I -> T (in Ref. 4; AAH38292).
FT CONFLICT 360 360 I -> L (in Ref. 5; AA sequence).
FT CONFLICT 363 363 I -> L (in Ref. 5; AA sequence).
FT CONFLICT 400 401 SQ -> LP (in Ref. 1; AAA20530).
FT TURN 77 79
FT STRAND 80 88
FT STRAND 90 99
FT TURN 100 103
FT STRAND 104 111
FT HELIX 115 133
FT HELIX 139 143
FT STRAND 147 155
FT STRAND 158 165
FT STRAND 168 171
FT HELIX 172 178
FT TURN 179 181
FT HELIX 186 205
FT HELIX 216 218
FT STRAND 219 221
FT HELIX 225 235
FT HELIX 485 490
FT STRAND 493 495
FT HELIX 498 500
FT STRAND 502 506
FT HELIX 515 517
FT HELIX 520 524
FT HELIX 531 546
FT STRAND 557 559
FT HELIX 561 573
FT HELIX 578 583
FT HELIX 587 589
FT STRAND 595 599
FT HELIX 608 614
FT HELIX 620 630
FT HELIX 631 634
FT HELIX 638 640
FT HELIX 644 648
FT HELIX 651 654
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
//
MIM
601939
*RECORD*
*FIELD* NO
601939
*FIELD* TI
*601939 PROTEIN KINASE, SERINE/ARGININE-SPECIFIC, 1; SRPK1
;;PROTEIN KINASE, ARGININE/SERINE-RICH SPLICING FACTOR, 1;;
read moreSFRS PROTEIN KINASE 1
*FIELD* TX
CLONING
Small nuclear ribonucleoprotein particles (snRNPs) and non-snRNP
splicing factors containing a serine/arginine-rich domain (SR proteins)
concentrate in 'speckles' in the nucleus of interphase cells. These
nuclear 'speckles' act as storage sites for splicing factors. Gui et al.
(1994) identified a kinase, designated SRPK1 (SR protein-specific
kinase-1), based on its ability to phosphorylate SC35 (SFRS2; 600813).
The SRPK1 gene was cloned; it encodes a protein of 655 amino acids.
SRPK1 is similar to a hypothetical C. elegans kinase, CEHK, and to the
fission yeast kinase Dsk1. The association of phosphorylation of SR
proteins in vivo with SRPK1 activity in the extracts, together with the
fact that SRPK1 was the only major kinase for SR proteins obtained
during purification, strongly suggests that SRPK1 is responsible for
phosphorylation of SR proteins during the cell cycle in vivo.
MAPPING
Using a somatic cell hybrid mapping panel and FISH, Wang et al. (1999)
mapped the SRPK1 gene to chromosome 6p21.3-p21.2. They mapped the mouse
Srpk1 gene to chromosome 17.
*FIELD* RF
1. Gui, J.-F.; Lane, W. S.; Fu, X.-D.: A serine kinase regulates
intracellular localization of splicing factors in the cell cycle. Nature 369:
678-682, 1994.
2. Wang, H.-Y.; Arden, K. C.; Bermingham, J. R., Jr.; Viars, C. S.;
Lin, W.; Boyer, A. D.; Fu, X.-D.: Localization of serine kinases,
SRPK1 (SFRSK1) and SRPK2 (SFRSK2), specific for the SR family of splicing
factors in mouse and human chromosomes. Genomics 57: 310-315, 1999.
*FIELD* CN
Carol A. Bocchini - updated: 7/15/2008
*FIELD* CD
Lori M. Kelman: 8/18/1997
*FIELD* ED
terry: 07/15/2008
carol: 7/15/2008
carol: 8/19/1998
psherman: 8/18/1998
dholmes: 8/25/1997
alopez: 8/19/1997
dholmes: 8/18/1997
*RECORD*
*FIELD* NO
601939
*FIELD* TI
*601939 PROTEIN KINASE, SERINE/ARGININE-SPECIFIC, 1; SRPK1
;;PROTEIN KINASE, ARGININE/SERINE-RICH SPLICING FACTOR, 1;;
read moreSFRS PROTEIN KINASE 1
*FIELD* TX
CLONING
Small nuclear ribonucleoprotein particles (snRNPs) and non-snRNP
splicing factors containing a serine/arginine-rich domain (SR proteins)
concentrate in 'speckles' in the nucleus of interphase cells. These
nuclear 'speckles' act as storage sites for splicing factors. Gui et al.
(1994) identified a kinase, designated SRPK1 (SR protein-specific
kinase-1), based on its ability to phosphorylate SC35 (SFRS2; 600813).
The SRPK1 gene was cloned; it encodes a protein of 655 amino acids.
SRPK1 is similar to a hypothetical C. elegans kinase, CEHK, and to the
fission yeast kinase Dsk1. The association of phosphorylation of SR
proteins in vivo with SRPK1 activity in the extracts, together with the
fact that SRPK1 was the only major kinase for SR proteins obtained
during purification, strongly suggests that SRPK1 is responsible for
phosphorylation of SR proteins during the cell cycle in vivo.
MAPPING
Using a somatic cell hybrid mapping panel and FISH, Wang et al. (1999)
mapped the SRPK1 gene to chromosome 6p21.3-p21.2. They mapped the mouse
Srpk1 gene to chromosome 17.
*FIELD* RF
1. Gui, J.-F.; Lane, W. S.; Fu, X.-D.: A serine kinase regulates
intracellular localization of splicing factors in the cell cycle. Nature 369:
678-682, 1994.
2. Wang, H.-Y.; Arden, K. C.; Bermingham, J. R., Jr.; Viars, C. S.;
Lin, W.; Boyer, A. D.; Fu, X.-D.: Localization of serine kinases,
SRPK1 (SFRSK1) and SRPK2 (SFRSK2), specific for the SR family of splicing
factors in mouse and human chromosomes. Genomics 57: 310-315, 1999.
*FIELD* CN
Carol A. Bocchini - updated: 7/15/2008
*FIELD* CD
Lori M. Kelman: 8/18/1997
*FIELD* ED
terry: 07/15/2008
carol: 7/15/2008
carol: 8/19/1998
psherman: 8/18/1998
dholmes: 8/25/1997
alopez: 8/19/1997
dholmes: 8/18/1997