ID SRPK2_HUMAN Reviewed; 688 AA. AC P78362; A8MVX2; O75220; O75221; Q6NUL0; Q6V1X2; Q8IYQ3; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 13-JUL-2010, sequence version 3. DT 24-JAN-2024, entry version 207. DE RecName: Full=SRSF protein kinase 2; DE EC=2.7.11.1 {ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:9472028, ECO:0000305|PubMed:21157427}; DE AltName: Full=SFRS protein kinase 2; DE AltName: Full=Serine/arginine-rich protein-specific kinase 2; DE Short=SR-protein-specific kinase 2; DE Contains: DE RecName: Full=SRSF protein kinase 2 N-terminal; DE Contains: DE RecName: Full=SRSF protein kinase 2 C-terminal; GN Name=SRPK2 {ECO:0000312|EMBL:AAH68547.1}; 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:AAC05299.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, RP COFACTOR, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION. RC TISSUE=Fetal brain {ECO:0000269|PubMed:9472028}; RX PubMed=9472028; DOI=10.1083/jcb.140.4.737; RA Wang H.-Y., Lin W., Dyck J.A., Yeakley J.M., Songyang Z., Cantley L.C., RA Fu X.-D.; RT "SRPK2: a differentially expressed SR protein-specific kinase involved in RT mediating the interaction and localization of pre-mRNA splicing factors in RT mammalian cells."; RL J. Cell Biol. 140:737-750(1998). RN [2] {ECO:0000312|EMBL:AAC29141.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [3] {ECO:0000312|EMBL:AAQ63886.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 [4] {ECO:0000312|EMBL:AAH35214.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [MRNA] OF 1-99 (ISOFORM 2). RC TISSUE=Retinoblastoma, Skin {ECO:0000312|EMBL:AAH35214.1}, and Testis RC {ECO:0000312|EMBL:AAH68547.1}; 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 [5] {ECO:0000312|EMBL:AAQ63886.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-537 (ISOFORM 1). RC TISSUE=Testis {ECO:0000312|EMBL:AAQ63886.1}; RA Sha J.H., Zhou Z.M., Li J.M.; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000305} RP FUNCTION IN PHOSPHORYLATION OF HEPATITIS B VIRUS CORE PROTEIN, CATALYTIC RP ACTIVITY, AND COFACTOR. 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [10] RP FUNCTION IN PHOSPHORYLATION OF ACIN1, CATALYTIC ACTIVITY, AND INTERACTION RP WITH ACIN1. RX PubMed=18559500; DOI=10.1158/0008-5472.can-08-0021; RA Jang S.W., Yang S.J., Ehlen A., Dong S., Khoury H., Chen J., Persson J.L., RA Ye K.; RT "Serine/arginine protein-specific kinase 2 promotes leukemia cell RT proliferation by phosphorylating acinus and regulating cyclin A1."; RL Cancer Res. 68:4559-4570(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380, 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 [12] RP FUNCTION IN PHOSPHORYLATION OF DDX23/PRP28, AND ASSOCIATION WITH U4/U6-U5 RP TRI-SNRNPS. RX PubMed=18425142; DOI=10.1038/nsmb.1415; RA Mathew R., Hartmuth K., Moehlmann S., Urlaub H., Ficner R., Luehrmann R.; RT "Phosphorylation of human PRP28 by SRPK2 is required for integration of the RT U4/U6-U5 tri-snRNP into the spliceosome."; RL Nat. Struct. Mol. Biol. 15:435-443(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND SER-497, AND RP IDENTIFICATION BY 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 [14] 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 [15] RP FUNCTION, INTERACTION WITH AKT1; YWHAB; YWHAE AND SFN, SUBCELLULAR RP LOCATION, AND PHOSPHORYLATION AT THR-492. RX PubMed=19592491; DOI=10.1074/jbc.m109.026237; RA Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.; RT "Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell cycle RT and cell death in neurons."; RL J. Biol. Chem. 284:24512-24525(2009). RN [16] RP IDENTIFICATION BY 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380; SER-494 AND SER-497, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] 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 [19] RP FUNCTION IN PHOSPHORYLATION OF SRSF2, CATALYTIC ACTIVITY, AND SUBCELLULAR RP 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 [20] 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 [21] RP FUNCTION, CATALYTIC ACTIVITY, PROTEOLYTIC CLEAVAGE AT ASP-139 AND ASP-403 RP BY CASPASE-3, AND SUBCELLULAR LOCATION. RX PubMed=21056976; DOI=10.1074/jbc.m110.193441; RA Hong Y., Jang S.W., Ye K.; RT "The N-terminal fragment from caspase-cleaved serine/arginine protein- RT specific kinase2 (SRPK2) translocates into the nucleus and promotes RT apoptosis."; RL J. Biol. Chem. 286:777-786(2011). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND SER-497, AND 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494, AND IDENTIFICATION BY RP 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 [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-380 AND SER-497, 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 [25] RP FUNCTION, INTERACTION WITH POLR2A, AND 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 [26] RP VARIANTS [LARGE SCALE ANALYSIS] LEU-43; ASP-243; PRO-426; PHE-486 AND RP THR-515. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). 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 (PubMed:9472028, PubMed:18559500, CC PubMed:21056976). Promotes neuronal apoptosis by up-regulating cyclin- CC D1 (CCND1) expression (PubMed:19592491). This is done by the CC phosphorylation of SRSF2, leading to the suppression of p53/TP53 CC phosphorylation thereby relieving the repressive effect of p53/TP53 on CC cyclin-D1 (CCND1) expression (PubMed:21205200). Phosphorylates ACIN1, CC and redistributes it from the nuclear speckles to the nucleoplasm, CC resulting in cyclin A1 but not cyclin A2 up-regulation CC (PubMed:18559500). Plays an essential role in spliceosomal B complex CC formation via the phosphorylation of DDX23/PRP28 (PubMed:18425142). CC Probably by phosphorylating DDX23, leads to the suppression of CC incorrect R-loops formed during transcription; R-loops are composed of CC a DNA:RNA hybrid and the associated non-template single-stranded DNA CC (PubMed:28076779). Can mediate hepatitis B virus (HBV) core protein CC phosphorylation (PubMed:12134018). 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 (PubMed:16122776). CC {ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:16122776, CC ECO:0000269|PubMed:18425142, ECO:0000269|PubMed:18559500, CC ECO:0000269|PubMed:19592491, ECO:0000269|PubMed:21056976, CC ECO:0000269|PubMed:21205200, ECO:0000269|PubMed:28076779, CC ECO:0000269|PubMed:9472028}. 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:12134018, ECO:0000269|PubMed:18559500, CC ECO:0000269|PubMed:9472028, ECO:0000305|PubMed:21157427}; 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:12134018, CC ECO:0000269|PubMed:9472028, ECO:0000305|PubMed:21157427}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:12134018, ECO:0000269|PubMed:9472028}; CC -!- ACTIVITY REGULATION: Activated by phosphorylation on Ser-52 and Ser- CC 588. {ECO:0000250|UniProtKB:Q96SB4}. CC -!- SUBUNIT: Associates with U4/U6-U5 tri-small nuclear ribonucleoproteins CC (U4/U6-U5 tri-snRNPs) (PubMed:18425142). Interacts with PKB/AKT1 in a CC phosphorylation-dependent manner (PubMed:19592491). The phosphorylated CC form (by PKB/AKT1) interacts with YWHAB and YWHAE (PubMed:19592491). CC Interaction with YWHAB suppresses its cleavage by caspases and inhibits CC the release of its N-terminal pro-apoptotic fragment (PubMed:19592491). CC Interacts with SFN (PubMed:19592491). Interacts with ACIN1 CC (PubMed:18559500). Interacts with POLR2A/RNA polymerase II; the CC interaction occurs during the co-transcriptional formation of CC inappropriate R-loops (PubMed:28076779). {ECO:0000269|PubMed:18425142, CC ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:19592491, CC ECO:0000269|PubMed:28076779}. CC -!- INTERACTION: CC P78362; Q9NWB6: ARGLU1; NbExp=2; IntAct=EBI-593303, EBI-2808785; CC P78362; Q66PJ3: ARL6IP4; NbExp=2; IntAct=EBI-593303, EBI-2683099; CC P78362; P50613: CDK7; NbExp=2; IntAct=EBI-593303, EBI-1245958; CC P78362; Q9Y3Y2: CHTOP; NbExp=2; IntAct=EBI-593303, EBI-347794; CC P78362; P49760: CLK2; NbExp=3; IntAct=EBI-593303, EBI-750020; CC P78362; P49761: CLK3; NbExp=5; IntAct=EBI-593303, EBI-745579; CC P78362; P38432: COIL; NbExp=3; IntAct=EBI-593303, EBI-945751; CC P78362; Q7L014: DDX46; NbExp=3; IntAct=EBI-593303, EBI-2555356; CC P78362; P51114-2: FXR1; NbExp=3; IntAct=EBI-593303, EBI-11022345; CC P78362; P51116: FXR2; NbExp=4; IntAct=EBI-593303, EBI-740459; CC P78362; P07910: HNRNPC; NbExp=2; IntAct=EBI-593303, EBI-357966; CC P78362; P17509: HOXB6; NbExp=3; IntAct=EBI-593303, EBI-741308; CC P78362; Q9NQ29: LUC7L; NbExp=3; IntAct=EBI-593303, EBI-473747; CC P78362; Q9Y383: LUC7L2; NbExp=3; IntAct=EBI-593303, EBI-352851; CC P78362; Q9P127: LUZP4; NbExp=3; IntAct=EBI-593303, EBI-10198848; CC P78362; Q9BU76: MMTAG2; NbExp=3; IntAct=EBI-593303, EBI-742459; CC P78362; Q5C9Z4: NOM1; NbExp=3; IntAct=EBI-593303, EBI-2685618; CC P78362; Q8NAV1: PRPF38A; NbExp=6; IntAct=EBI-593303, EBI-715374; CC P78362; P86480: PRR20D; NbExp=3; IntAct=EBI-593303, EBI-12754095; CC P78362; Q86U06: RBM23; NbExp=2; IntAct=EBI-593303, EBI-780319; CC P78362; Q14498: RBM39; NbExp=10; IntAct=EBI-593303, EBI-395290; CC P78362; Q9Y5S9: RBM8A; NbExp=2; IntAct=EBI-593303, EBI-447231; CC P78362; D3DU92: RNPS1; NbExp=3; IntAct=EBI-593303, EBI-10176640; CC P78362; Q15287: RNPS1; NbExp=5; IntAct=EBI-593303, EBI-395959; CC P78362; Q8TAD8: SNIP1; NbExp=4; IntAct=EBI-593303, EBI-749336; CC P78362; Q8WVK2: SNRNP27; NbExp=5; IntAct=EBI-593303, EBI-2512550; CC P78362; P08621: SNRNP70; NbExp=4; IntAct=EBI-593303, EBI-1049228; CC P78362; Q8WXA9: SREK1; NbExp=2; IntAct=EBI-593303, EBI-1044237; CC P78362; Q8IYB3: SRRM1; NbExp=3; IntAct=EBI-593303, EBI-1055880; CC P78362; O75494: SRSF10; NbExp=2; IntAct=EBI-593303, EBI-353655; CC P78362; Q05519-2: SRSF11; NbExp=3; IntAct=EBI-593303, EBI-11975029; CC P78362; Q13243: SRSF5; NbExp=2; IntAct=EBI-593303, EBI-720503; CC P78362; Q16629: SRSF7; NbExp=2; IntAct=EBI-593303, EBI-398885; CC P78362; Q9BRL6: SRSF8; NbExp=2; IntAct=EBI-593303, EBI-6380719; CC P78362; Q9BRL6-2: SRSF8; NbExp=3; IntAct=EBI-593303, EBI-10976394; CC P78362; Q13428: TCOF1; NbExp=2; IntAct=EBI-593303, EBI-396105; CC P78362; Q08117: TLE5; NbExp=3; IntAct=EBI-593303, EBI-717810; CC P78362; Q13595: TRA2A; NbExp=2; IntAct=EBI-593303, EBI-2685506; CC P78362; P62995: TRA2B; NbExp=5; IntAct=EBI-593303, EBI-725485; CC P78362; Q01081: U2AF1; NbExp=7; IntAct=EBI-593303, EBI-632461; CC P78362; Q01081-2: U2AF1; NbExp=3; IntAct=EBI-593303, EBI-10176676; CC P78362; P26368: U2AF2; NbExp=5; IntAct=EBI-593303, EBI-742339; CC P78362; P26368-2: U2AF2; NbExp=3; IntAct=EBI-593303, EBI-11097439; CC P78362; Q96MU7: YTHDC1; NbExp=4; IntAct=EBI-593303, EBI-2849854; CC P78362; P31946: YWHAB; NbExp=2; IntAct=EBI-593303, EBI-359815; CC P78362; Q15696: ZRSR2; NbExp=7; IntAct=EBI-593303, EBI-6657923; CC P78362; O43309: ZSCAN12; NbExp=3; IntAct=EBI-593303, EBI-1210440; CC P78362; O15535: ZSCAN9; NbExp=6; IntAct=EBI-593303, EBI-751531; CC P78362; P0DTC9: N; Xeno; NbExp=2; IntAct=EBI-593303, EBI-25475856; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21056976, CC ECO:0000269|PubMed:21157427, ECO:0000269|PubMed:28076779, CC ECO:0000269|PubMed:9472028}. Nucleus, nucleoplasm CC {ECO:0000269|PubMed:21157427, ECO:0000269|PubMed:28076779, CC ECO:0000269|PubMed:9472028}. Nucleus speckle CC {ECO:0000269|PubMed:28076779, ECO:0000269|PubMed:9472028}. Chromosome CC {ECO:0000269|PubMed:28076779}. Note=Shuttles between the nucleus and CC the cytoplasm (PubMed:19592491, PubMed:21157427, PubMed:21056976). CC KAT5/TIP60 inhibits its nuclear translocation (PubMed:21157427). CC Phosphorylation at Thr-492 by PKB/AKT1 promotes nuclear translocation CC (PubMed:19592491). Preferentially localizes across the entire gene CC coding region (PubMed:28076779). During transcription, accumulates at CC chromatin loci where unscheduled R-loops form and colocalizes with CC paused 'Ser-5'-phosphorlyated POLR2A/RNA polymerase II and helicase CC DDX23 (PubMed:28076779). {ECO:0000269|PubMed:19592491, CC ECO:0000269|PubMed:21056976, ECO:0000269|PubMed:21157427, CC ECO:0000269|PubMed:28076779}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P78362-1; Sequence=Displayed; CC Name=2; CC IsoId=P78362-2; Sequence=VSP_039386; CC -!- TISSUE SPECIFICITY: Highly expressed in brain, moderately expressed in CC heart and skeletal muscle and at low levels in lung, liver, and kidney. CC {ECO:0000269|PubMed:9472028}. CC -!- PTM: Phosphorylation at Thr-492 by PKB/AKT1 enhances its stimulatory CC activity in triggering cyclin-D1 (CCND1) expression and promoting CC apoptosis in neurons, which can be blocked by YWHAB. It also enhances CC its protein kinase activity toward ACIN1 and SRSF2, promotes its CC nuclear translocation and prevents its proteolytic cleavage. CC {ECO:0000269|PubMed:19592491}. CC -!- PTM: Proteolytically cleaved at Asp-139 and Asp-403 by caspase-3 during CC apoptotic cell death. Cleavage at Asp-139 which is the major site of CC cleavage, produces a small N-terminal fragment that translocates into CC nucleus and promotes VP16-induced apoptosis. CC {ECO:0000269|PubMed:21056976}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC protein kinase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAQ63886.1; Type=Miscellaneous discrepancy; Note=The cDNA appears to contain a duplicated region.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U88666; AAC05299.1; -; mRNA. DR EMBL; AC005070; AAC29140.1; -; Genomic_DNA. DR EMBL; AC005070; AAC29141.1; -; Genomic_DNA. DR EMBL; AC004884; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC073138; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471070; EAW83359.1; -; Genomic_DNA. DR EMBL; BC035214; AAH35214.1; -; mRNA. DR EMBL; BC068547; AAH68547.1; -; mRNA. DR EMBL; BE781215; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AY354201; AAQ63886.1; ALT_SEQ; mRNA. DR CCDS; CCDS34724.1; -. [P78362-2] DR CCDS; CCDS5735.1; -. [P78362-1] DR RefSeq; NP_001265202.1; NM_001278273.1. [P78362-1] DR RefSeq; NP_872633.1; NM_182691.2. [P78362-1] DR RefSeq; NP_872634.1; NM_182692.2. [P78362-2] DR RefSeq; XP_016868055.1; XM_017012566.1. DR PDB; 2X7G; X-ray; 2.50 A; A=51-688. DR PDB; 5MYV; X-ray; 2.90 A; A/B/C/D=51-688. DR PDB; 7ZKX; X-ray; 2.06 A; A=70-688. DR PDBsum; 2X7G; -. DR PDBsum; 5MYV; -. DR PDBsum; 7ZKX; -. DR AlphaFoldDB; P78362; -. DR SMR; P78362; -. DR BioGRID; 112611; 724. DR IntAct; P78362; 388. DR MINT; P78362; -. DR STRING; 9606.ENSP00000377262; -. DR BindingDB; P78362; -. DR ChEMBL; CHEMBL5668; -. DR DrugBank; DB00173; Adenine. DR DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester. DR DrugBank; DB02733; Purvalanol. DR DrugCentral; P78362; -. DR MoonDB; P78362; Predicted. DR GlyCosmos; P78362; 1 site, 1 glycan. DR GlyGen; P78362; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P78362; -. DR PhosphoSitePlus; P78362; -. DR BioMuta; SRPK2; -. DR DMDM; 300669676; -. DR CPTAC; CPTAC-2929; -. DR CPTAC; CPTAC-2930; -. DR EPD; P78362; -. DR jPOST; P78362; -. DR MassIVE; P78362; -. DR MaxQB; P78362; -. DR PaxDb; 9606-ENSP00000377262; -. DR PeptideAtlas; P78362; -. DR ProteomicsDB; 57591; -. [P78362-1] DR ProteomicsDB; 57592; -. [P78362-2] DR Pumba; P78362; -. DR Antibodypedia; 17064; 194 antibodies from 29 providers. DR DNASU; 6733; -. DR Ensembl; ENST00000357311.7; ENSP00000349863.3; ENSG00000135250.17. [P78362-1] DR Ensembl; ENST00000393651.8; ENSP00000377262.3; ENSG00000135250.17. [P78362-2] DR Ensembl; ENST00000489828.5; ENSP00000419791.1; ENSG00000135250.17. [P78362-1] DR GeneID; 6733; -. DR KEGG; hsa:6733; -. DR MANE-Select; ENST00000393651.8; ENSP00000377262.3; NM_182692.3; NP_872634.1. [P78362-2] DR UCSC; uc003vct.5; human. [P78362-1] DR AGR; HGNC:11306; -. DR CTD; 6733; -. DR DisGeNET; 6733; -. DR GeneCards; SRPK2; -. DR HGNC; HGNC:11306; SRPK2. DR HPA; ENSG00000135250; Tissue enhanced (testis). DR MIM; 602980; gene. DR neXtProt; NX_P78362; -. DR OpenTargets; ENSG00000135250; -. DR PharmGKB; PA36130; -. DR VEuPathDB; HostDB:ENSG00000135250; -. DR eggNOG; KOG1290; Eukaryota. DR GeneTree; ENSGT00940000154795; -. DR HOGENOM; CLU_000288_81_9_1; -. DR InParanoid; P78362; -. DR OMA; NHKGPNG; -. DR OrthoDB; 912242at2759; -. DR PhylomeDB; P78362; -. DR TreeFam; TF105334; -. DR PathwayCommons; P78362; -. DR Reactome; R-HSA-9694631; Maturation of nucleoprotein. DR SignaLink; P78362; -. DR SIGNOR; P78362; -. DR BioGRID-ORCS; 6733; 14 hits in 1162 CRISPR screens. DR ChiTaRS; SRPK2; human. DR EvolutionaryTrace; P78362; -. DR GeneWiki; SRPK2; -. DR GenomeRNAi; 6733; -. DR Pharos; P78362; Tchem. DR PRO; PR:P78362; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P78362; Protein. DR Bgee; ENSG00000135250; Expressed in sperm and 217 other cell types or tissues. DR ExpressionAtlas; P78362; baseline and differential. 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:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0071889; F:14-3-3 protein binding; ISS:BHF-UCL. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. 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:0001525; P:angiogenesis; ISS:BHF-UCL. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. 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:0035063; P:nuclear speck organization; ISS:BHF-UCL. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IGI:CACAO. DR GO; GO:0045787; P:positive regulation of cell cycle; ISS:BHF-UCL. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:BHF-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; ISS:BHF-UCL. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS: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:0062176; P:R-loop processing; IDA:UniProtKB. DR GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central. DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; TAS:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IDA:UniProtKB. DR GO; GO:0000245; P:spliceosomal complex assembly; IDA:UniProtKB. DR DisProt; DP02591; -. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2. 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 PANTHER; PTHR47634; PROTEIN KINASE DOMAIN-CONTAINING PROTEIN-RELATED; 1. DR PANTHER; PTHR47634:SF6; SRSF PROTEIN KINASE 2; 1. DR Pfam; PF00069; Pkinase; 2. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; P78362; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Chromosome; Cytoplasm; KW Differentiation; Kinase; mRNA processing; mRNA splicing; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1..688 FT /note="SRSF protein kinase 2" FT /id="PRO_0000086677" FT CHAIN 1..139 FT /note="SRSF protein kinase 2 N-terminal" FT /id="PRO_0000414751" FT CHAIN 140..688 FT /note="SRSF protein kinase 2 C-terminal" FT /id="PRO_0000414752" FT DOMAIN 81..684 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..65 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 239..277 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 329..444 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 469..501 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..16 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 18..45 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 46..60 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 329..345 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 346..370 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 377..391 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 395..419 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 421..436 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 214 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 87..95 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q9UPE1, FT ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 110 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:Q9UPE1, FT ECO:0000255|PROSITE-ProRule:PRU00159" FT SITE 139..140 FT /note="Cleavage; by caspase-3" FT /evidence="ECO:0000269|PubMed:21056976" FT SITE 403..404 FT /note="Cleavage; by caspase-3" FT /evidence="ECO:0000269|PubMed:21056976" FT MOD_RES 52 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 380 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569" FT MOD_RES 475 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O54781" FT MOD_RES 478 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O54781" FT MOD_RES 484 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O54781" FT MOD_RES 486 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O54781" FT MOD_RES 490 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O54781" FT MOD_RES 492 FT /note="Phosphothreonine; by PKB/AKT1" FT /evidence="ECO:0000269|PubMed:19592491" FT MOD_RES 494 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 497 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569" FT MOD_RES 588 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000250" FT VAR_SEQ 1..13 FT /note="MSVNSEKSSSSER -> MSSRKVLAIQARKRRPKREKHPKK (in FT isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_039386" FT VARIANT 43 FT /note="P -> L (in dbSNP:rs34699980)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041114" FT VARIANT 243 FT /note="G -> D (in a glioblastoma multiforme sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041115" FT VARIANT 426 FT /note="T -> P (in dbSNP:rs55743527)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041116" FT VARIANT 486 FT /note="S -> F (in dbSNP:rs56112661)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041117" FT VARIANT 515 FT /note="P -> T (in dbSNP:rs56017595)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_041118" FT VARIANT 608 FT /note="S -> N (in dbSNP:rs1050413)" FT /id="VAR_060390" FT VARIANT 615 FT /note="L -> I (in dbSNP:rs1050418)" FT /id="VAR_057111" FT CONFLICT 137 FT /note="P -> R (in Ref. 4; AAH68547)" FT /evidence="ECO:0000305" FT CONFLICT 236..237 FT /note="AT -> P (in Ref. 1; AAC05299)" FT /evidence="ECO:0000305" FT CONFLICT 521 FT /note="A -> R (in Ref. 1; AAC05299)" FT /evidence="ECO:0000305" FT CONFLICT 601 FT /note="H -> L (in Ref. 2; AAC29141)" FT /evidence="ECO:0000305" FT CONFLICT 608..609 FT /note="SI -> KV (in Ref. 2; AAC29141)" FT /evidence="ECO:0000305" FT CONFLICT 612..616 FT /note="HFALS -> KYAML (in Ref. 2; AAC29141)" FT /evidence="ECO:0000305" FT CONFLICT 621 FT /note="R -> K (in Ref. 2; AAC29141)" FT /evidence="ECO:0000305" FT CONFLICT 625..627 FT /note="NRR -> TRK (in Ref. 2; AAC29141)" FT /evidence="ECO:0000305" FT CONFLICT 640 FT /note="S -> G (in Ref. 4; AAH68547)" FT /evidence="ECO:0000305" FT CONFLICT 681 FT /note="Missing (in Ref. 1; AAC05299)" FT /evidence="ECO:0000305" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:7ZKX" FT STRAND 81..89 FT /evidence="ECO:0007829|PDB:7ZKX" FT STRAND 91..100 FT /evidence="ECO:0007829|PDB:7ZKX" FT TURN 101..104 FT /evidence="ECO:0007829|PDB:7ZKX" FT STRAND 105..112 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 116..134 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 140..144 FT /evidence="ECO:0007829|PDB:7ZKX" FT STRAND 150..154 FT /evidence="ECO:0007829|PDB:7ZKX" FT STRAND 161..166 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 173..179 FT /evidence="ECO:0007829|PDB:7ZKX" FT TURN 180..182 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 187..206 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 217..219 FT /evidence="ECO:0007829|PDB:7ZKX" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 226..234 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 518..523 FT /evidence="ECO:0007829|PDB:7ZKX" FT STRAND 526..528 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 531..533 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 548..550 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 553..557 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 564..579 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 594..606 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 611..614 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 620..623 FT /evidence="ECO:0007829|PDB:7ZKX" FT STRAND 630..632 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 641..647 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 653..663 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 664..667 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 671..673 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 677..681 FT /evidence="ECO:0007829|PDB:7ZKX" FT HELIX 684..686 FT /evidence="ECO:0007829|PDB:7ZKX" SQ 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 //