SRPK2_HUMAN
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 03-AUG-2022, entry version 199.
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
RC Testis {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 ---------------------------------------------------------------------------
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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 PDBsum; 2X7G; -.
DR PDBsum; 5MYV; -.
DR AlphaFoldDB; P78362; -.
DR SMR; P78362; -.
DR BioGRID; 112611; 614.
DR IntAct; P78362; 385.
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 GlyGen; P78362; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P78362; -.
DR PhosphoSitePlus; P78362; -.
DR BioMuta; SRPK2; -.
DR DMDM; 300669676; -.
DR EPD; P78362; -.
DR jPOST; P78362; -.
DR MassIVE; P78362; -.
DR MaxQB; P78362; -.
DR PaxDb; P78362; -.
DR PeptideAtlas; P78362; -.
DR PRIDE; P78362; -.
DR ProteomicsDB; 57591; -. [P78362-1]
DR ProteomicsDB; 57592; -. [P78362-2]
DR Antibodypedia; 17064; 169 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 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; NTTGKHV; -.
DR OrthoDB; 290680at2759; -.
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 1083 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 215 other tissues.
DR ExpressionAtlas; P78362; baseline and differential.
DR Genevisible; P78362; HS.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
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 disassembly; 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 InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Chromosome; 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:2X7G"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:2X7G"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:2X7G"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:2X7G"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 116..134
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:2X7G"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:2X7G"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:2X7G"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 187..206
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:2X7G"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:2X7G"
FT TURN 521..523
FT /evidence="ECO:0007829|PDB:2X7G"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 553..557
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 564..579
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 594..606
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 611..614
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 620..623
FT /evidence="ECO:0007829|PDB:2X7G"
FT STRAND 630..632
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 641..649
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 653..666
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 671..673
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 677..681
FT /evidence="ECO:0007829|PDB:2X7G"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:2X7G"
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
