GPKOW_HUMAN
ID GPKOW_HUMAN Reviewed; 476 AA.
AC Q92917; Q59EK5; Q9BQA8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=G-patch domain and KOW motifs-containing protein;
DE AltName: Full=G-patch domain-containing protein 5;
DE AltName: Full=Protein MOS2 homolog;
DE AltName: Full=Protein T54;
GN Name=GPKOW; Synonyms=GPATC5, GPATCH5, T54;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8938429; DOI=10.1101/gr.6.11.1056;
RA Schindelhauer D., Hellebrand H., Grimm L., Bader I., Meitinger T.,
RA Wehnert M., Ross M., Meindl A.;
RT "Long-range map of a 3.5-Mb region in Xp11.23-22 with a sequence-ready map
RT from a 1.1-Mb gene-rich interval.";
RL Genome Res. 6:1056-1069(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-476.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION.
RX PubMed=16271871; DOI=10.1016/j.cub.2005.09.038;
RA Zhang Y., Cheng Y.T., Bi D., Palma K., Li X.;
RT "MOS2, a protein containing G-patch and KOW motifs, is essential for innate
RT immunity in Arabidopsis thaliana.";
RL Curr. Biol. 15:1936-1942(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP INTERACTION WITH PRKX.
RX PubMed=16491121; DOI=10.1038/sj.onc.1209436;
RA Glesne D., Huberman E.;
RT "Smad6 is a protein kinase X phosphorylation substrate and is required for
RT HL-60 cell differentiation.";
RL Oncogene 25:4086-4098(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND THR-216, 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND THR-216, 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 [12]
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 [13]
RP PHOSPHORYLATION AT SER-27 AND THR-316, MUTAGENESIS OF SER-27 AND THR-316,
RP INTERACTION WITH PRKACB, AND SUBCELLULAR LOCATION.
RX PubMed=21880142; DOI=10.1186/1750-2187-6-10;
RA Aksaas A.K., Larsen A.C., Rogne M., Rosendal K., Kvissel A.K.,
RA Skaalhegg B.S.;
RT "G-patch domain and KOW motifs-containing protein, GPKOW; a nuclear RNA-
RT binding protein regulated by protein kinase A.";
RL J. Mol. Signal. 6:10-10(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35; SER-42 AND SER-115, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DHX16, AND MUTAGENESIS OF
RP 176-GLY--TRP-177 AND 259-GLY--LYS-260.
RX PubMed=25296192; DOI=10.1042/bsr20140142;
RA Zang S., Lin T.Y., Chen X., Gencheva M., Newo A.N., Yang L., Rossi D.,
RA Hu J., Lin S.B., Huang A., Lin R.J.;
RT "GPKOW is essential for pre-mRNA splicing in vitro and suppresses splicing
RT defect caused by dominant-negative DHX16 mutation in vivo.";
RL Biosci. Rep. 34:E00163-E00163(2014).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216; SER-471 AND THR-473, 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 [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: RNA-binding protein involved in pre-mRNA splicing.
CC {ECO:0000269|PubMed:25296192}.
CC -!- SUBUNIT: Interacts with PRKX (PubMed:16491121). Interacts with DHX16
CC (PubMed:25296192). Interacts with PRKACB (PubMed:21880142).
CC {ECO:0000269|PubMed:16491121, ECO:0000269|PubMed:21880142,
CC ECO:0000269|PubMed:25296192}.
CC -!- INTERACTION:
CC Q92917; Q9P291: ARMCX1; NbExp=3; IntAct=EBI-746309, EBI-2843626;
CC Q92917; Q9BRD0: BUD13; NbExp=12; IntAct=EBI-746309, EBI-2561235;
CC Q92917; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-746309, EBI-2808286;
CC Q92917; Q6P9H4: CNKSR3; NbExp=3; IntAct=EBI-746309, EBI-10253274;
CC Q92917; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-746309, EBI-742054;
CC Q92917; O60231: DHX16; NbExp=3; IntAct=EBI-746309, EBI-311446;
CC Q92917; Q92620: DHX38; NbExp=2; IntAct=EBI-746309, EBI-1043041;
CC Q92917; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-746309, EBI-2349927;
CC Q92917; Q96IJ6: GMPPA; NbExp=3; IntAct=EBI-746309, EBI-750953;
CC Q92917; Q08379: GOLGA2; NbExp=9; IntAct=EBI-746309, EBI-618309;
CC Q92917; P46439: GSTM5; NbExp=3; IntAct=EBI-746309, EBI-4312072;
CC Q92917; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-746309, EBI-10961706;
CC Q92917; O75031: HSF2BP; NbExp=3; IntAct=EBI-746309, EBI-7116203;
CC Q92917; Q9Y6K9: IKBKG; NbExp=3; IntAct=EBI-746309, EBI-81279;
CC Q92917; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-746309, EBI-2556193;
CC Q92917; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-746309, EBI-739832;
CC Q92917; Q9P2M1: LRP2BP; NbExp=3; IntAct=EBI-746309, EBI-18273118;
CC Q92917; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-746309, EBI-1216080;
CC Q92917; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-746309, EBI-742610;
CC Q92917; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-746309, EBI-16439278;
CC Q92917; Q14696: MESD; NbExp=3; IntAct=EBI-746309, EBI-6165891;
CC Q92917; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-746309, EBI-10172526;
CC Q92917; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-746309, EBI-11522433;
CC Q92917; O43189: PHF1; NbExp=3; IntAct=EBI-746309, EBI-530034;
CC Q92917; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-746309, EBI-14066006;
CC Q92917; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-746309, EBI-79165;
CC Q92917; P62487: POLR2G; NbExp=3; IntAct=EBI-746309, EBI-347928;
CC Q92917; P22694-2: PRKACB; NbExp=4; IntAct=EBI-746309, EBI-5258763;
CC Q92917; P31321: PRKAR1B; NbExp=3; IntAct=EBI-746309, EBI-2805516;
CC Q92917; P51817: PRKX; NbExp=2; IntAct=EBI-746309, EBI-4302903;
CC Q92917; O43172: PRPF4; NbExp=2; IntAct=EBI-746309, EBI-718395;
CC Q92917; Q6P2Q9: PRPF8; NbExp=2; IntAct=EBI-746309, EBI-538479;
CC Q92917; P98175: RBM10; NbExp=2; IntAct=EBI-746309, EBI-721525;
CC Q92917; Q04864-2: REL; NbExp=3; IntAct=EBI-746309, EBI-10829018;
CC Q92917; Q9HAT0: ROPN1; NbExp=6; IntAct=EBI-746309, EBI-1378139;
CC Q92917; Q6FGM0: SH3GL1; NbExp=3; IntAct=EBI-746309, EBI-10173690;
CC Q92917; Q99961: SH3GL1; NbExp=8; IntAct=EBI-746309, EBI-697911;
CC Q92917; O60504: SORBS3; NbExp=3; IntAct=EBI-746309, EBI-741237;
CC Q92917; A6NLX3: SPDYE4; NbExp=3; IntAct=EBI-746309, EBI-12047907;
CC Q92917; P23193: TCEA1; NbExp=3; IntAct=EBI-746309, EBI-2608271;
CC Q92917; Q15560: TCEA2; NbExp=7; IntAct=EBI-746309, EBI-710310;
CC Q92917; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-746309, EBI-750109;
CC Q92917; Q12933: TRAF2; NbExp=7; IntAct=EBI-746309, EBI-355744;
CC Q92917; P36406: TRIM23; NbExp=4; IntAct=EBI-746309, EBI-740098;
CC Q92917; P14373: TRIM27; NbExp=3; IntAct=EBI-746309, EBI-719493;
CC Q92917; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-746309, EBI-2799833;
CC Q92917; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-746309, EBI-12030590;
CC Q92917; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-746309, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21880142,
CC ECO:0000269|PubMed:25296192}.
CC -!- PTM: Phosphorylation regulates its ability to bind RNA.
CC {ECO:0000269|PubMed:21880142}.
CC -!- SIMILARITY: Belongs to the MOS2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB18640.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U66359; AAB18640.1; ALT_SEQ; mRNA.
DR EMBL; BC000397; AAH00397.1; -; mRNA.
DR EMBL; BC003148; AAH03148.1; -; mRNA.
DR EMBL; AB209806; BAD93043.1; -; mRNA.
DR CCDS; CCDS35251.1; -.
DR RefSeq; NP_056513.2; NM_015698.5.
DR PDB; 7DVQ; EM; 2.89 A; y=1-476.
DR PDBsum; 7DVQ; -.
DR AlphaFoldDB; Q92917; -.
DR SMR; Q92917; -.
DR BioGRID; 118086; 130.
DR IntAct; Q92917; 69.
DR MINT; Q92917; -.
DR STRING; 9606.ENSP00000156109; -.
DR GlyGen; Q92917; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q92917; -.
DR MetOSite; Q92917; -.
DR PhosphoSitePlus; Q92917; -.
DR BioMuta; GPKOW; -.
DR DMDM; 134048659; -.
DR EPD; Q92917; -.
DR jPOST; Q92917; -.
DR MassIVE; Q92917; -.
DR MaxQB; Q92917; -.
DR PaxDb; Q92917; -.
DR PeptideAtlas; Q92917; -.
DR PRIDE; Q92917; -.
DR ProteomicsDB; 75602; -.
DR Antibodypedia; 340; 181 antibodies from 28 providers.
DR DNASU; 27238; -.
DR Ensembl; ENST00000156109.7; ENSP00000156109.5; ENSG00000068394.11.
DR GeneID; 27238; -.
DR KEGG; hsa:27238; -.
DR MANE-Select; ENST00000156109.7; ENSP00000156109.5; NM_015698.6; NP_056513.2.
DR UCSC; uc004dmr.5; human.
DR CTD; 27238; -.
DR DisGeNET; 27238; -.
DR GeneCards; GPKOW; -.
DR HGNC; HGNC:30677; GPKOW.
DR HPA; ENSG00000068394; Low tissue specificity.
DR MalaCards; GPKOW; -.
DR MIM; 301003; gene.
DR neXtProt; NX_Q92917; -.
DR OpenTargets; ENSG00000068394; -.
DR Orphanet; 2570; Lethal intrauterine growth restriction-cortical malformation-congenital contractures syndrome.
DR PharmGKB; PA134956055; -.
DR VEuPathDB; HostDB:ENSG00000068394; -.
DR eggNOG; KOG4315; Eukaryota.
DR GeneTree; ENSGT00390000015154; -.
DR HOGENOM; CLU_045183_1_0_1; -.
DR InParanoid; Q92917; -.
DR OMA; VEGNRVM; -.
DR OrthoDB; 1427830at2759; -.
DR PhylomeDB; Q92917; -.
DR TreeFam; TF316786; -.
DR PathwayCommons; Q92917; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q92917; -.
DR SIGNOR; Q92917; -.
DR BioGRID-ORCS; 27238; 385 hits in 708 CRISPR screens.
DR GenomeRNAi; 27238; -.
DR Pharos; Q92917; Tbio.
DR PRO; PR:Q92917; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q92917; protein.
DR Bgee; ENSG00000068394; Expressed in paraflocculus and 193 other tissues.
DR Genevisible; Q92917; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:UniProtKB.
DR CDD; cd13152; KOW_GPKOW_A; 1.
DR CDD; cd13153; KOW_GPKOW_B; 1.
DR Gene3D; 2.30.30.30; -; 2.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR041993; GPKOW_KOW1.
DR InterPro; IPR041994; GPKOW_KOW2.
DR InterPro; IPR005824; KOW.
DR InterPro; IPR014722; Rib_L2_dom2.
DR InterPro; IPR045166; Spp2-like.
DR InterPro; IPR026822; Spp2/MOS2_G-patch.
DR PANTHER; PTHR15818; PTHR15818; 1.
DR Pfam; PF12656; G-patch_2; 1.
DR Pfam; PF00467; KOW; 1.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00739; KOW; 2.
DR PROSITE; PS50174; G_PATCH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..476
FT /note="G-patch domain and KOW motifs-containing protein"
FT /id="PRO_0000087559"
FT DOMAIN 164..210
FT /note="G-patch"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092"
FT DOMAIN 240..267
FT /note="KOW 1"
FT DOMAIN 415..442
FT /note="KOW 2"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 27
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:21880142"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 316
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000269|PubMed:21880142"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 473
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 5
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 27
FT /note="S->A: Reduced phosphorylation. Significant loss of
FT phosphorylation and increased RNA-binding; when associated
FT with A-316."
FT /evidence="ECO:0000269|PubMed:21880142"
FT MUTAGEN 176..177
FT /note="GW->AA: Significant loss of interaction with DHX16.
FT No loss of pre-mRNA splicing activity. Able to suppress the
FT splicing defect observed in dominant-negative DHX16 mutant
FT expressing cells."
FT /evidence="ECO:0000269|PubMed:25296192"
FT MUTAGEN 259..260
FT /note="GK->AA: No loss of interaction with DHX16. Reduced
FT pre-mRNA splicing activity. Decreased ability to suppress
FT the splicing defect observed in dominant-negative DHX16
FT mutant expressing cells."
FT /evidence="ECO:0000269|PubMed:25296192"
FT MUTAGEN 316
FT /note="T->A: Reduced phosphorylation. Significant loss of
FT phosphorylation and increased RNA-binding; when associated
FT with A-27."
FT /evidence="ECO:0000269|PubMed:21880142"
FT CONFLICT 317
FT /note="L -> F (in Ref. 3; BAD93043)"
FT /evidence="ECO:0000305"
FT STRAND 20..22
FT /evidence="ECO:0007829|PDB:7DVQ"
SQ SEQUENCE 476 AA; 52229 MW; 36F1C5771969897D CRC64;
MADSKEGVLP LTAASTAPIS FGFTRTSARR RLADSGDGAG PSPEEKDFLK TVEGRELQSV
KPQEAPKELV IPLIQNGHRR QPPARPPGPS TDTGALADGV VSQAVKELIA ESKKSLEERE
NAGVDPTLAI PMIQKGCTPS GEGADSEPRA ETVPEEANYE AVPVEAYGLA MLRGMGWKPG
EGIGRTFNQV VKPRVNSLRP KGLGLGANLT EAQALTPTGP SRMPRPDEEQ EKDKEDQPQG
LVPGGAVVVL SGPHRGLYGK VEGLDPDNVR AMVRLAVGSR VVTVSEYYLR PVSQQEFDKN
TLDLRQQNGT ASSRKTLWNQ ELYIQQDNSE RKRKHLPDRQ DGPAAKSEKA APRSQHWLHR
DLRVRFVDNM YKGGQYYNTK MIIEDVLSPD TCVCRTDEGR VLEGLREDML ETLVPKAEGD
RVMVVLGPQT GRVGHLLSRD RARSRALVQL PRENQVVELH YDAICQYMGP SDTDDD
