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SRSF protein kinase 2 (EC 2.7.11.1) (SFRS protein kinase 2) (Serine/arginine-rich protein-specific kinase 2) (SR-protein-specific kinase 2) [Cleaved into: SRSF protein kinase 2 N-terminal; SRSF protein kinase 2 C-terminal]

 SRPK2_HUMAN             Reviewed;         688 AA.
P78362; A8MVX2; O75220; O75221; Q6NUL0; Q6V1X2; Q8IYQ3;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
13-JUL-2010, sequence version 3.
22-NOV-2017, entry version 169.
RecName: Full=SRSF protein kinase 2;
EC=2.7.11.1;
AltName: Full=SFRS protein kinase 2;
AltName: Full=Serine/arginine-rich protein-specific kinase 2;
Short=SR-protein-specific kinase 2;
Contains:
RecName: Full=SRSF protein kinase 2 N-terminal;
Contains:
RecName: Full=SRSF protein kinase 2 C-terminal;
Name=SRPK2 {ECO:0000312|EMBL:AAH68547.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC05299.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND SUBCELLULAR LOCATION.
TISSUE=Fetal brain {ECO:0000269|PubMed:9472028};
PubMed=9472028; DOI=10.1083/jcb.140.4.737;
Wang H.-Y., Lin W., Dyck J.A., Yeakley J.M., Songyang Z.,
Cantley L.C., Fu X.-D.;
"SRPK2: a differentially expressed SR protein-specific kinase involved
in mediating the interaction and localization of pre-mRNA splicing
factors in mammalian cells.";
J. Cell Biol. 140:737-750(1998).
[2] {ECO:0000312|EMBL:AAC29141.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[3] {ECO:0000312|EMBL:AAQ63886.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000312|EMBL:AAH35214.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [MRNA] OF 1-99 (ISOFORM 2).
TISSUE=Retinoblastoma, Skin {ECO:0000312|EMBL:AAH35214.1}, and
Testis {ECO:0000312|EMBL:AAH68547.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5] {ECO:0000312|EMBL:AAQ63886.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 1-537 (ISOFORM 1).
TISSUE=Testis {ECO:0000312|EMBL:AAQ63886.1};
Sha J.H., Zhou Z.M., Li J.M.;
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[6] {ECO:0000305}
FUNCTION IN PHOSPHORYLATION OF HEPATITIS B VIRUS CORE PROTEIN.
PubMed=12134018; DOI=10.1128/JVI.76.16.8124-8137.2002;
Daub H., Blencke S., Habenberger P., Kurtenbach A., Dennenmoser J.,
Wissing J., Ullrich A., Cotten M.;
"Identification of SRPK1 and SRPK2 as the major cellular protein
kinases phosphorylating hepatitis B virus core protein.";
J. Virol. 76:8124-8137(2002).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[8]
FUNCTION IN NEGATIVE REGULATION OF HEPATITIS B VIRUS (HBV)
REPLICATION.
PubMed=16122776; DOI=10.1016/j.virol.2005.07.030;
Zheng Y., Fu X.D., Ou J.H.;
"Suppression of hepatitis B virus replication by SRPK1 and SRPK2 via a
pathway independent of the phosphorylation of the viral core
protein.";
Virology 342:150-158(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[10]
FUNCTION IN PHOSPHORYLATION OF ACIN1, AND INTERACTION WITH ACIN1.
PubMed=18559500; DOI=10.1158/0008-5472.CAN-08-0021;
Jang S.W., Yang S.J., Ehlen A., Dong S., Khoury H., Chen J.,
Persson J.L., Ye K.;
"Serine/arginine protein-specific kinase 2 promotes leukemia cell
proliferation by phosphorylating acinus and regulating cyclin A1.";
Cancer Res. 68:4559-4570(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[12]
FUNCTION IN PHOSPHORYLATION OF DDX23/PRP28, AND ASSOCIATION WITH
U4/U6-U5 TRI-SNRNPS.
PubMed=18425142; DOI=10.1038/nsmb.1415;
Mathew R., Hartmuth K., Moehlmann S., Urlaub H., Ficner R.,
Luehrmann R.;
"Phosphorylation of human PRP28 by SRPK2 is required for integration
of the U4/U6-U5 tri-snRNP into the spliceosome.";
Nat. Struct. Mol. Biol. 15:435-443(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND SER-497, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
FUNCTION, PHOSPHORYLATION AT THR-492 BY PKB/AKT1, AND INTERACTION WITH
PKB/AKT1; YWHAB; YWHAE AND SFN.
PubMed=19592491; DOI=10.1074/jbc.M109.026237;
Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.;
"Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell
cycle and cell death in neurons.";
J. Biol. Chem. 284:24512-24525(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-494 AND
SER-497, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
FUNCTION IN PHOSPHORYLATION OF SRSF2, AND SUBCELLULAR LOCATION.
PubMed=21157427; DOI=10.1038/emboj.2010.333;
Edmond V., Moysan E., Khochbin S., Matthias P., Brambilla C.,
Brambilla E., Gazzeri S., Eymin B.;
"Acetylation and phosphorylation of SRSF2 control cell fate decision
in response to cisplatin.";
EMBO J. 30:510-523(2011).
[20]
REVIEW ON FUNCTION.
PubMed=21205200; DOI=10.1111/j.1742-4658.2010.07987.x;
Giannakouros T., Nikolakaki E., Mylonis I., Georgatsou E.;
"Serine-arginine protein kinases: a small protein kinase family with a
large cellular presence.";
FEBS J. 278:570-586(2011).
[21]
FUNCTION, CASPASE-3 CLEAVAGE AT ASP-139 AND ASP-403, AND SUBCELLULAR
LOCATION.
PubMed=21056976; DOI=10.1074/jbc.M110.193441;
Hong Y., Jang S.W., Ye K.;
"The N-terminal fragment from caspase-cleaved serine/arginine protein-
specific kinase2 (SRPK2) translocates into the nucleus and promotes
apoptosis.";
J. Biol. Chem. 286:777-786(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND SER-497, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-380 AND SER-497,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
VARIANTS [LARGE SCALE ANALYSIS] LEU-43; ASP-243; PRO-426; PHE-486 AND
THR-515.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Serine/arginine-rich protein-specific kinase which
specifically phosphorylates its substrates at serine residues
located in regions rich in arginine/serine dipeptides, known as RS
domains and is involved in the phosphorylation of SR splicing
factors and the regulation of splicing. Promotes neuronal
apoptosis by up-regulating cyclin-D1 (CCND1) expression. This is
done by the phosphorylation of SRSF2, leading to the suppression
of p53/TP53 phosphorylation thereby relieving the repressive
effect of p53/TP53 on cyclin-D1 (CCND1) expression. Phosphorylates
ACIN1, and redistributes it from the nuclear speckles to the
nucleoplasm, resulting in cyclin A1 but not cyclin A2 up-
regulation. Plays an essential role in spliceosomal B complex
formation via the phosphorylation of DDX23/PRP28. Can mediate
hepatitis B virus (HBV) core protein phosphorylation. Plays a
negative role in the regulation of HBV replication through a
mechanism not involving the phosphorylation of the core protein
but by reducing the packaging efficiency of the pregenomic RNA
(pgRNA) without affecting the formation of the viral core
particles. {ECO:0000269|PubMed:12134018,
ECO:0000269|PubMed:16122776, ECO:0000269|PubMed:18425142,
ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:19592491,
ECO:0000269|PubMed:21056976, ECO:0000269|PubMed:21157427,
ECO:0000269|PubMed:9472028}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:9472028}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12134018,
ECO:0000269|PubMed:9472028};
-!- ENZYME REGULATION: Activated by phosphorylation on Ser-52 and Ser-
588. {ECO:0000250|UniProtKB:Q96SB4}.
-!- SUBUNIT: Interacts with PKB/AKT1 in a phosphorylation-dependent
manner. The phosphorylated form (by PKB/AKT1) interacts with YWHAB
and YWHAE. Interaction with YWHAB suppresses its cleavage by
caspases and inhibits the release of its N-terminal pro-apoptotic
fragment. Interacts with SFN. Associates with U4/U6-U5 tri-small
nuclear ribonucleoproteins (U4/U6-U5 tri-snRNPs).
{ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:19592491}.
-!- INTERACTION:
Q08117:AES; NbExp=3; IntAct=EBI-593303, EBI-717810;
Q9NWB6:ARGLU1; NbExp=2; IntAct=EBI-593303, EBI-2808785;
P49760:CLK2; NbExp=3; IntAct=EBI-593303, EBI-750020;
P49761:CLK3; NbExp=4; IntAct=EBI-593303, EBI-745579;
P51116:FXR2; NbExp=3; IntAct=EBI-593303, EBI-740459;
P07910:HNRNPC; NbExp=2; IntAct=EBI-593303, EBI-357966;
Q9NQ29:LUC7L; NbExp=2; IntAct=EBI-593303, EBI-473747;
Q9Y383:LUC7L2; NbExp=2; IntAct=EBI-593303, EBI-352851;
Q9P127:LUZP4; NbExp=3; IntAct=EBI-593303, EBI-10198848;
Q9BU76:MMTAG2; NbExp=2; IntAct=EBI-593303, EBI-742459;
Q8NAV1:PRPF38A; NbExp=5; IntAct=EBI-593303, EBI-715374;
Q86U06:RBM23; NbExp=2; IntAct=EBI-593303, EBI-780319;
Q14498:RBM39; NbExp=9; IntAct=EBI-593303, EBI-395290;
Q9Y5S9:RBM8A; NbExp=2; IntAct=EBI-593303, EBI-447231;
D3DU92:RNPS1; NbExp=3; IntAct=EBI-593303, EBI-10176640;
Q15287:RNPS1; NbExp=3; IntAct=EBI-593303, EBI-395959;
Q8TAD8:SNIP1; NbExp=3; IntAct=EBI-593303, EBI-749336;
Q8WVK2:SNRNP27; NbExp=5; IntAct=EBI-593303, EBI-2512550;
P08621:SNRNP70; NbExp=3; IntAct=EBI-593303, EBI-1049228;
Q16629:SRSF7; NbExp=2; IntAct=EBI-593303, EBI-398885;
Q9BRL6:SRSF8; NbExp=2; IntAct=EBI-593303, EBI-6380719;
P62995:TRA2B; NbExp=3; IntAct=EBI-593303, EBI-725485;
Q01081:U2AF1; NbExp=7; IntAct=EBI-593303, EBI-632461;
Q01081-2:U2AF1; NbExp=3; IntAct=EBI-593303, EBI-10176676;
P26368:U2AF2; NbExp=4; IntAct=EBI-593303, EBI-742339;
Q96MU7:YTHDC1; NbExp=3; IntAct=EBI-593303, EBI-2849854;
P31946:YWHAB; NbExp=2; IntAct=EBI-593303, EBI-359815;
Q15696:ZRSR2; NbExp=6; IntAct=EBI-593303, EBI-6657923;
O15535:ZSCAN9; NbExp=5; IntAct=EBI-593303, EBI-751531;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
the nucleus and the cytoplasm. KAT5/TIP60 inhibits its nuclear
translocation. Phosphorylation at Thr-492 by PKB/AKT1 promotes
nuclear translocation.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P78362-1; Sequence=Displayed;
Name=2;
IsoId=P78362-2; Sequence=VSP_039386;
-!- TISSUE SPECIFICITY: Highly expressed in brain, moderately
expressed in heart and skeletal muscle and at low levels in lung,
liver, and kidney. {ECO:0000269|PubMed:9472028}.
-!- PTM: Phosphorylation at Thr-492 by PKB/AKT1 enhances its
stimulatory activity in triggering cyclin-D1 (CCND1) expression
and promoting apoptosis in neurons, which can be blocked by YWHAB.
It also enhances its protein kinase activity toward ACIN1 and
SRSF2, promotes its nuclear translocation and prevents its
proteolytic cleavage. {ECO:0000269|PubMed:19592491}.
-!- PTM: Proteolytically cleaved at Asp-139 and Asp-403 by caspase-3
during apoptotic cell death. Cleavage at Asp-139 which is the
major site of cleavage, produces a small N-terminal fragment that
translocates into nucleus and promotes VP16-induced apoptosis.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAQ63886.1; Type=Miscellaneous discrepancy; Note=The cDNA appears to contain a duplicated region.; Evidence={ECO:0000305};
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EMBL; U88666; AAC05299.1; -; mRNA.
EMBL; AC005070; AAC29140.1; -; Genomic_DNA.
EMBL; AC005070; AAC29141.1; -; Genomic_DNA.
EMBL; AC004884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073138; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471070; EAW83359.1; -; Genomic_DNA.
EMBL; BC035214; AAH35214.1; -; mRNA.
EMBL; BC068547; AAH68547.1; -; mRNA.
EMBL; BE781215; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AY354201; AAQ63886.1; ALT_SEQ; mRNA.
CCDS; CCDS34724.1; -. [P78362-2]
CCDS; CCDS5735.1; -. [P78362-1]
RefSeq; NP_001265202.1; NM_001278273.1. [P78362-1]
RefSeq; NP_872633.1; NM_182691.2. [P78362-1]
RefSeq; NP_872634.1; NM_182692.2. [P78362-2]
RefSeq; XP_016868055.1; XM_017012566.1.
UniGene; Hs.285197; -.
PDB; 2X7G; X-ray; 2.50 A; A=51-688.
PDB; 5MYV; X-ray; 2.90 A; A/B/C/D=51-688.
PDBsum; 2X7G; -.
PDBsum; 5MYV; -.
ProteinModelPortal; P78362; -.
SMR; P78362; -.
BioGrid; 112611; 451.
IntAct; P78362; 244.
MINT; MINT-1468300; -.
STRING; 9606.ENSP00000377262; -.
BindingDB; P78362; -.
ChEMBL; CHEMBL5668; -.
DrugBank; DB00173; Adenine.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB02733; Purvalanol.
GuidetoPHARMACOLOGY; 2209; -.
iPTMnet; P78362; -.
PhosphoSitePlus; P78362; -.
DMDM; 300669676; -.
EPD; P78362; -.
MaxQB; P78362; -.
PaxDb; P78362; -.
PeptideAtlas; P78362; -.
PRIDE; P78362; -.
DNASU; 6733; -.
Ensembl; ENST00000357311; ENSP00000349863; ENSG00000135250. [P78362-1]
Ensembl; ENST00000393651; ENSP00000377262; ENSG00000135250. [P78362-2]
Ensembl; ENST00000489828; ENSP00000419791; ENSG00000135250. [P78362-1]
GeneID; 6733; -.
KEGG; hsa:6733; -.
UCSC; uc003vct.5; human. [P78362-1]
CTD; 6733; -.
DisGeNET; 6733; -.
EuPathDB; HostDB:ENSG00000135250.16; -.
GeneCards; SRPK2; -.
H-InvDB; HIX0006976; -.
HGNC; HGNC:11306; SRPK2.
HPA; HPA015522; -.
HPA; HPA020876; -.
MIM; 602980; gene.
neXtProt; NX_P78362; -.
OpenTargets; ENSG00000135250; -.
PharmGKB; PA36130; -.
eggNOG; KOG1290; Eukaryota.
eggNOG; ENOG410XRBH; LUCA.
GeneTree; ENSGT00530000063566; -.
HOVERGEN; HBG108512; -.
InParanoid; P78362; -.
KO; K08831; -.
OMA; EKYHFKE; -.
OrthoDB; EOG091G05H9; -.
PhylomeDB; P78362; -.
TreeFam; TF105334; -.
SignaLink; P78362; -.
SIGNOR; P78362; -.
ChiTaRS; SRPK2; human.
EvolutionaryTrace; P78362; -.
GeneWiki; SRPK2; -.
GenomeRNAi; 6733; -.
PRO; PR:P78362; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000135250; -.
CleanEx; HS_SRPK2; -.
ExpressionAtlas; P78362; baseline and differential.
Genevisible; P78362; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; ISS:BHF-UCL.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0001525; P:angiogenesis; ISS:BHF-UCL.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IC:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:BHF-UCL.
GO; GO:0035063; P:nuclear speck organization; ISS:BHF-UCL.
GO; GO:0045787; P:positive regulation of cell cycle; ISS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:BHF-UCL.
GO; GO:0045070; P:positive regulation of viral genome replication; IDA:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; TAS:UniProtKB.
GO; GO:0008380; P:RNA splicing; IDA:UniProtKB.
GO; GO:0000245; P:spliceosomal complex assembly; IDA:UniProtKB.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 2.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Differentiation; Kinase; mRNA processing; mRNA splicing;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 688 SRSF protein kinase 2.
/FTId=PRO_0000086677.
CHAIN 1 139 SRSF protein kinase 2 N-terminal.
/FTId=PRO_0000414751.
CHAIN 140 688 SRSF protein kinase 2 C-terminal.
/FTId=PRO_0000414752.
DOMAIN 81 684 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 87 95 ATP. {ECO:0000250|UniProtKB:Q9UPE1,
ECO:0000255|PROSITE-ProRule:PRU00159}.
ACT_SITE 214 214 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 110 110 ATP. {ECO:0000250|UniProtKB:Q9UPE1,
ECO:0000255|PROSITE-ProRule:PRU00159}.
SITE 139 140 Cleavage; by caspase-3.
SITE 403 404 Cleavage; by caspase-3.
MOD_RES 52 52 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 380 380 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 475 475 Phosphoserine.
{ECO:0000250|UniProtKB:O54781}.
MOD_RES 478 478 Phosphothreonine.
{ECO:0000250|UniProtKB:O54781}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000250|UniProtKB:O54781}.
MOD_RES 486 486 Phosphoserine.
{ECO:0000250|UniProtKB:O54781}.
MOD_RES 490 490 Phosphoserine.
{ECO:0000250|UniProtKB:O54781}.
MOD_RES 492 492 Phosphothreonine; by PKB/AKT1.
{ECO:0000269|PubMed:19592491}.
MOD_RES 494 494 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 497 497 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 588 588 Phosphoserine; by CK2. {ECO:0000250}.
VAR_SEQ 1 13 MSVNSEKSSSSER -> MSSRKVLAIQARKRRPKREKHPKK
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_039386.
VARIANT 43 43 P -> L (in dbSNP:rs34699980).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041114.
VARIANT 243 243 G -> D (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041115.
VARIANT 426 426 T -> P (in dbSNP:rs55743527).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041116.
VARIANT 486 486 S -> F (in dbSNP:rs56112661).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041117.
VARIANT 515 515 P -> T (in dbSNP:rs56017595).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041118.
VARIANT 608 608 S -> N (in dbSNP:rs1050413).
/FTId=VAR_060390.
VARIANT 615 615 L -> I (in dbSNP:rs1050418).
/FTId=VAR_057111.
CONFLICT 137 137 P -> R (in Ref. 4; AAH68547).
{ECO:0000305}.
CONFLICT 236 237 AT -> P (in Ref. 1; AAC05299).
{ECO:0000305}.
CONFLICT 521 521 A -> R (in Ref. 1; AAC05299).
{ECO:0000305}.
CONFLICT 601 601 H -> L (in Ref. 2; AAC29141).
{ECO:0000305}.
CONFLICT 608 609 SI -> KV (in Ref. 2; AAC29141).
{ECO:0000305}.
CONFLICT 612 616 HFALS -> KYAML (in Ref. 2; AAC29141).
{ECO:0000305}.
CONFLICT 621 621 R -> K (in Ref. 2; AAC29141).
{ECO:0000305}.
CONFLICT 625 627 NRR -> TRK (in Ref. 2; AAC29141).
{ECO:0000305}.
CONFLICT 640 640 S -> G (in Ref. 4; AAH68547).
{ECO:0000305}.
CONFLICT 681 681 Missing (in Ref. 1; AAC05299).
{ECO:0000305}.
TURN 78 80 {ECO:0000244|PDB:2X7G}.
STRAND 81 89 {ECO:0000244|PDB:2X7G}.
STRAND 91 100 {ECO:0000244|PDB:2X7G}.
TURN 101 104 {ECO:0000244|PDB:2X7G}.
STRAND 105 112 {ECO:0000244|PDB:2X7G}.
HELIX 116 134 {ECO:0000244|PDB:2X7G}.
HELIX 140 144 {ECO:0000244|PDB:2X7G}.
STRAND 150 156 {ECO:0000244|PDB:2X7G}.
STRAND 159 166 {ECO:0000244|PDB:2X7G}.
HELIX 173 179 {ECO:0000244|PDB:2X7G}.
TURN 180 182 {ECO:0000244|PDB:2X7G}.
HELIX 187 206 {ECO:0000244|PDB:2X7G}.
HELIX 217 219 {ECO:0000244|PDB:2X7G}.
STRAND 220 222 {ECO:0000244|PDB:2X7G}.
HELIX 226 233 {ECO:0000244|PDB:2X7G}.
HELIX 518 520 {ECO:0000244|PDB:2X7G}.
TURN 521 523 {ECO:0000244|PDB:2X7G}.
STRAND 526 528 {ECO:0000244|PDB:2X7G}.
HELIX 531 533 {ECO:0000244|PDB:2X7G}.
HELIX 548 550 {ECO:0000244|PDB:2X7G}.
HELIX 553 557 {ECO:0000244|PDB:2X7G}.
HELIX 564 579 {ECO:0000244|PDB:2X7G}.
HELIX 594 606 {ECO:0000244|PDB:2X7G}.
HELIX 611 614 {ECO:0000244|PDB:2X7G}.
HELIX 620 623 {ECO:0000244|PDB:2X7G}.
STRAND 630 632 {ECO:0000244|PDB:2X7G}.
HELIX 641 649 {ECO:0000244|PDB:2X7G}.
HELIX 653 666 {ECO:0000244|PDB:2X7G}.
HELIX 671 673 {ECO:0000244|PDB:2X7G}.
HELIX 677 681 {ECO:0000244|PDB:2X7G}.
HELIX 684 686 {ECO:0000244|PDB:2X7G}.
SEQUENCE 688 AA; 77527 MW; ACCAF2A887444EC2 CRC64;
MSVNSEKSSS SERPEPQQKA PLVPPPPPPP PPPPPPLPDP TPPEPEEEIL GSDDEEQEDP
ADYCKGGYHP VKIGDLFNGR YHVIRKLGWG HFSTVWLCWD MQGKRFVAMK VVKSAQHYTE
TALDEIKLLK CVRESDPSDP NKDMVVQLID DFKISGMNGI HVCMVFEVLG HHLLKWIIKS
NYQGLPVRCV KSIIRQVLQG LDYLHSKCKI IHTDIKPENI LMCVDDAYVR RMAAEATEWQ
KAGAPPPSGS AVSTAPQQKP IGKISKNKKK KLKKKQKRQA ELLEKRLQEI EELEREAERK
IIEENITSAA PSNDQDGEYC PEVKLKTTGL EEAAEAETAK DNGEAEDQEE KEDAEKENIE
KDEDDVDQEL ANIDPTWIES PKTNGHIENG PFSLEQQLDD EDDDEEDCPN PEEYNLDEPN
AESDYTYSSS YEQFNGELPN GRHKIPESQF PEFSTSLFSG SLEPVACGSV LSEGSPLTEQ
EESSPSHDRS RTVSASSTGD LPKAKTRAAD LLVNPLDPRN ADKIRVKIAD LGNACWVHKH
FTEDIQTRQY RSIEVLIGAG YSTPADIWST ACMAFELATG DYLFEPHSGE DYSRDEDHIA
HIIELLGSIP RHFALSGKYS REFFNRRGEL RHITKLKPWS LFDVLVEKYG WPHEDAAQFT
DFLIPMLEMV PEKRASAGEC LRHPWLNS


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