SFPQ_MOUSE
ID SFPQ_MOUSE Reviewed; 699 AA.
AC Q8VIJ6; A2A7U6; Q9ERW2;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Splicing factor, proline- and glutamine-rich;
DE AltName: Full=DNA-binding p52/p100 complex, 100 kDa subunit;
DE AltName: Full=Polypyrimidine tract-binding protein-associated-splicing factor;
DE Short=PSF;
DE Short=PTB-associated-splicing factor;
GN Name=Sfpq; Synonyms=Psf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone marrow;
RX PubMed=11514619; DOI=10.1091/mbc.12.8.2328;
RA Shav-Tal Y., Cohen M., Lapter S., Dye B., Patton J.G., Vandekerckhove J.,
RA Zipori D.;
RT "Nuclear relocalization of the pre-mRNA splicing factor PSF during
RT apoptosis involves hyperphosphorylation, masking of antigenic epitopes, and
RT changes in protein interactions.";
RL Mol. Biol. Cell 12:2328-2340(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 198-580, AND PROTEIN SEQUENCE OF 20-30; 47-55
RP AND 210-238.
RC TISSUE=Bone marrow;
RX PubMed=11008015; DOI=10.1016/s0301-472x(00)00510-5;
RA Shav-Tal Y., Lee B., Bar-Haim S., Vandekerckhove J., Zipori D.;
RT "Enhanced proteolysis of pre-mRNA splicing factors in myeloid cells.";
RL Exp. Hematol. 28:1029-1038(2000).
RN [5]
RP PROTEIN SEQUENCE OF 291-306; 312-322; 358-368 AND 472-485, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP INTERACTION WITH PSPC1.
RX PubMed=15140795; DOI=10.1095/biolreprod.104.028159;
RA Myojin R., Kuwahara S., Yasaki T., Matsunaga T., Sakurai T., Kimura M.,
RA Uesugi S., Kurihara Y.;
RT "Expression and functional significance of mouse paraspeckle protein 1 on
RT spermatogenesis.";
RL Biol. Reprod. 71:926-932(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-679, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP INTERACTION WITH PITX3 AND NR4A2.
RX PubMed=19144721; DOI=10.1242/dev.029769;
RA Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L., Burbach J.P.,
RA Smidt M.P.;
RT "Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation
RT through release of SMRT-mediated repression.";
RL Development 136:531-540(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-679, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION IN CIRCADIAN RHYTHMS, IDENTIFICATION IN A LARGE PER COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21680841; DOI=10.1126/science.1196766;
RA Duong H.A., Robles M.S., Knutti D., Weitz C.J.;
RT "A molecular mechanism for circadian clock negative feedback.";
RL Science 332:1436-1439(2011).
RN [11]
RP FUNCTION, AND INTERACTION WITH PER1 AND PER2.
RX PubMed=22966205; DOI=10.1128/mcb.00334-12;
RA Kowalska E., Ripperger J.A., Muheim C., Maier B., Kurihara Y., Fox A.H.,
RA Kramer A., Brown S.A.;
RT "Distinct roles of DBHS family members in the circadian transcriptional
RT feedback loop.";
RL Mol. Cell. Biol. 32:4585-4594(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [13]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-9; ARG-228; ARG-234; ARG-237;
RP ARG-673 AND ARG-685, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: DNA- and RNA binding protein, involved in several nuclear
CC processes. Essential pre-mRNA splicing factor required early in
CC spliceosome formation and for splicing catalytic step II, probably as a
CC heteromer with NONO. Binds to pre-mRNA in spliceosome C complex, and
CC specifically binds to intronic polypyrimidine tracts. Involved in
CC regulation of signal-induced alternative splicing. During splicing of
CC PTPRC/CD45, a phosphorylated form is sequestered by THRAP3 from the
CC pre-mRNA in resting T-cells; T-cell activation and subsequent reduced
CC phosphorylation is proposed to lead to release from THRAP3 allowing
CC binding to pre-mRNA splicing regulatotry elements which represses exon
CC inclusion. Interacts with U5 snRNA, probably by binding to a purine-
CC rich sequence located on the 3' side of U5 snRNA stem 1b. May be
CC involved in a pre-mRNA coupled splicing and polyadenylation process as
CC component of a snRNP-free complex with SNRPA/U1A. The SFPQ-NONO
CC heteromer associated with MATR3 may play a role in nuclear retention of
CC defective RNAs. SFPQ may be involved in homologous DNA pairing; in
CC vitro, promotes the invasion of ssDNA between a duplex DNA and produces
CC a D-loop formation. The SFPQ-NONO heteromer may be involved in DNA
CC unwinding by modulating the function of topoisomerase I/TOP1; in vitro,
CC stimulates dissociation of TOP1 from DNA after cleavage and enhances
CC its jumping between separate DNA helices. The SFPQ-NONO heteromer binds
CC DNA. The SFPQ-NONO heteromer may be involved in DNA non-homologous end
CC joining (NHEJ) required for double-strand break repair and V(D)J
CC recombination and may stabilize paired DNA ends; in vitro, the complex
CC strongly stimulates DNA end joining, binds directly to the DNA
CC substrates and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to
CC establish a functional preligation complex. SFPQ is involved in
CC transcriptional regulation. Functions as transcriptional activator (By
CC similarity). Transcriptional repression is mediated by an interaction
CC of SFPQ with SIN3A and subsequent recruitment of histone deacetylases
CC (HDACs). The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and
CC regulates basal and cAMP-dependent transcriptional activity. SFPQ
CC isoform Long binds to the DNA binding domains (DBD) of nuclear hormone
CC receptors, like RXRA and probably THRA, and acts as transcriptional
CC corepressor in absence of hormone ligands. Binds the DNA sequence 5'-
CC CTGAGTC-3' in the insulin-like growth factor response element (IGFRE)
CC and inhibits IGF-I-stimulated transcriptional activity (By similarity).
CC Regulates the circadian clock by repressing the transcriptional
CC activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Required for
CC the transcriptional repression of circadian target genes, such as PER1,
CC mediated by the large PER complex through histone deacetylation
CC (PubMed:21680841, PubMed:22966205). Required for the assembly of
CC nuclear speckles (By similarity). Plays a role in the regulation of DNA
CC virus-mediated innate immune response by assembling into the HDP-RNP
CC complex, a complex that serves as a platform for IRF3 phosphorylation
CC and subsequent innate immune response activation through the cGAS-STING
CC pathway (By similarity). {ECO:0000250|UniProtKB:P23246,
CC ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22966205}.
CC -!- SUBUNIT: Heterodimer with NONO. Monomer and component of the SFPQ-NONO
CC complex, which is probably a heterotetramer of two 52 kDa (NONO) and
CC two 100 kDa (SFPQ) subunits. The coiled coil domain mediates
CC interaction with NONO, and can also mediate formation of long, linear
CC homooligomers (in vitro). SFPQ is a component of spliceosome and U5.4/6
CC snRNP complexes. Interacts with SNRPA/U1A. Component of a snRNP-free
CC complex with SNRPA/U1A. Part of complex consisting of SFPQ, NONO and
CC MATR3. Interacts with polypyrimidine tract-binding protein 1/PTB. Part
CC of a complex consisting of SFPQ, NONO and NR5A1. Interacts with RXRA,
CC probably THRA, and SIN3A. Interacts with TOP1. Part of a complex
CC consisting of SFPQ, NONO and TOP1. Interacts with SNRNP70 in apoptotic
CC cells. Interacts with PSPC1 (PubMed:15140795). Interacts with RNF43 (By
CC similarity). Interacts with PITX3 and NR4A2/NURR1 (PubMed:19144721).
CC Interacts with PTK6. Interacts with THRAP3; the interaction is
CC dependent on SFPQ phosphorylation at 'Thr-687' and inhibits binding of
CC SFPQ to a ESS1 exonic splicing silencer element-containing RNA (By
CC similarity). The large PER complex involved in the histone
CC deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A
CC (PubMed:21680841). Interacts with PER1 and PER2 (PubMed:22966205). Part
CC of the HDP-RNP complex composed of at least HEXIM1, PRKDC, XRCC5,
CC XRCC6, paraspeckle proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and
CC NEAT1 RNA (By similarity). Interacts with PQBP1. Component of a
CC multiprotein complex with NONO and WASL (By similarity). Interacts with
CC ERCC6 (By similarity). {ECO:0000250|UniProtKB:P23246,
CC ECO:0000269|PubMed:15140795, ECO:0000269|PubMed:19144721,
CC ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22966205}.
CC -!- INTERACTION:
CC Q8VIJ6; O88609: Lmx1b; NbExp=5; IntAct=EBI-6094576, EBI-13951208;
CC Q8VIJ6; Q8R326: Pspc1; NbExp=2; IntAct=EBI-6094576, EBI-309927;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:P23246}.
CC Nucleus matrix {ECO:0000269|PubMed:21680841}. Cytoplasm
CC {ECO:0000250|UniProtKB:P23246}. Note=Predominantly in nuclear matrix.
CC {ECO:0000250|UniProtKB:P23246}.
CC -!- DOMAIN: The coiled coil domain mediates interaction with NONO, and can
CC also mediate formation of long, linear homooligomers (in vitro). The
CC coiled coil domain is required for optimal DNA binding, and optimal
CC transcription activation. {ECO:0000250|UniProtKB:P23246}.
CC -!- PTM: Phosphorylated on multiple serine and threonine residues during
CC apoptosis (By similarity). Phosphorylation of C-terminal tyrosines
CC promotes its cytoplasmic localization, impaired its binding to
CC polypyrimidine RNA and led to cell cycle arrest (By similarity). In
CC resting T-cells is phosphorylated at Thr-679 by GSK3B which is proposed
CC to promote association with THRAP and to prevent binding to PTPRC/CD45
CC pre-mRNA; T-cell activation leads to reduced phosphorylation at Thr-
CC 679. {ECO:0000250|UniProtKB:P23246}.
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DR EMBL; AY034062; AAK60397.1; -; mRNA.
DR EMBL; AL606985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC089305; AAH89305.1; -; mRNA.
DR EMBL; AF272847; AAG17365.1; -; mRNA.
DR CCDS; CCDS18662.1; -.
DR RefSeq; NP_076092.1; NM_023603.3.
DR AlphaFoldDB; Q8VIJ6; -.
DR SMR; Q8VIJ6; -.
DR BioGRID; 214752; 69.
DR IntAct; Q8VIJ6; 15.
DR MINT; Q8VIJ6; -.
DR STRING; 10090.ENSMUSP00000030623; -.
DR iPTMnet; Q8VIJ6; -.
DR PhosphoSitePlus; Q8VIJ6; -.
DR SwissPalm; Q8VIJ6; -.
DR REPRODUCTION-2DPAGE; Q8VIJ6; -.
DR EPD; Q8VIJ6; -.
DR jPOST; Q8VIJ6; -.
DR MaxQB; Q8VIJ6; -.
DR PaxDb; Q8VIJ6; -.
DR PeptideAtlas; Q8VIJ6; -.
DR PRIDE; Q8VIJ6; -.
DR ProteomicsDB; 261178; -.
DR Antibodypedia; 4083; 329 antibodies from 35 providers.
DR DNASU; 71514; -.
DR Ensembl; ENSMUST00000030623; ENSMUSP00000030623; ENSMUSG00000028820.
DR GeneID; 71514; -.
DR KEGG; mmu:71514; -.
DR UCSC; uc008utz.2; mouse.
DR CTD; 6421; -.
DR MGI; MGI:1918764; Sfpq.
DR VEuPathDB; HostDB:ENSMUSG00000028820; -.
DR eggNOG; KOG0115; Eukaryota.
DR GeneTree; ENSGT00940000156221; -.
DR HOGENOM; CLU_027185_1_0_1; -.
DR InParanoid; Q8VIJ6; -.
DR OMA; HKGGPGH; -.
DR OrthoDB; 1274880at2759; -.
DR PhylomeDB; Q8VIJ6; -.
DR TreeFam; TF315795; -.
DR Reactome; R-MMU-8849468; PTK6 Regulates Proteins Involved in RNA Processing.
DR BioGRID-ORCS; 71514; 27 hits in 115 CRISPR screens.
DR ChiTaRS; Sfpq; mouse.
DR PRO; PR:Q8VIJ6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8VIJ6; protein.
DR Bgee; ENSMUSG00000028820; Expressed in embryonic post-anal tail and 270 other tissues.
DR Genevisible; Q8VIJ6; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0042382; C:paraspeckles; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0002218; P:activation of innate immune response; ISO:MGI.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0051276; P:chromosome organization; IMP:MGI.
DR GO; GO:0098963; P:dendritic transport of messenger ribonucleoprotein complex; IDA:SynGO.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0070932; P:histone H3 deacetylation; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0042754; P:negative regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0045876; P:positive regulation of sister chromatid cohesion; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd12948; NOPS_PSF; 1.
DR CDD; cd12587; RRM1_PSF; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012975; NOPS.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034526; PSF_NOPS.
DR InterPro; IPR034525; PSF_RRM1.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF08075; NOPS; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Biological rhythms; Coiled coil; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA repair; DNA-binding; Immunity;
KW Innate immunity; Isopeptide bond; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; RNA-binding; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..699
FT /note="Splicing factor, proline- and glutamine-rich"
FT /id="PRO_0000081910"
FT REPEAT 9..11
FT /note="1"
FT REPEAT 19..21
FT /note="2"
FT REPEAT 25..27
FT /note="3"
FT DOMAIN 289..361
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 363..444
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 9..27
FT /note="3 X 3 AA repeats of R-G-G"
FT REGION 571..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 489..588
FT /evidence="ECO:0000255"
FT COMPBIAS 49..106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine; by MKNK2"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 9
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 9
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 200
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 228
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 234
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 237
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 275
FT /note="Phosphoserine; by MKNK2"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 285
FT /note="Phosphotyrosine; by ALK"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 306
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 311
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 330
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 360
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 413
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 464
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 563
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 673
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 679
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 683
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 685
FT /note="Dimethylated arginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT MOD_RES 685
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 687
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P23246"
FT CONFLICT 47
FT /note="M -> Q (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="S -> N (in Ref. 4; AAG17365)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 699 AA; 75442 MW; 714F786264C63AA0 CRC64;
MSRDRFRSRG GGGGGFHRRG GGGGRGGLHD FRSPPPGMGL NQNRGPMGPG PGGPKPPLPP
PPPHQQQQQP PPQQPPPQQP PPHQQPPPHQ PPHQQPPPPP QESKPVVPQG PGSAPGVSSA
PPPAVSAPPA NPPTTGAPPG PGPTPTPPPA VPSTAPGPPP PSTPSSGVST TPPQTGGPPP
PPAGGAGPGP KPGPGPGGPK GGKMPGGPKP GGGPGMGAPG GHPKPPHRGG GEPRGGRQHH
APYHQQHHQG PPPGGPGPRT EEKISDSEGF KANLSLLRRP GEKTYTQRCR LFVGNLPADI
TEDEFKRLFA KYGEPGEVFI NKGKGFGFIK LESRALAEIA KAELDDTPMR GRQLRVRFAT
HAAALSVRNL SPYVSNELLE EAFSQFGPIE RAVVIVDDRG RSTGKGIVEF ASKPAARKAF
ERCSEGVFLL TTTPRPVIVE PLEQLDDEDG LPEKLAQKNP MYQKERETPP RFAQHGTFEY
EYSQRWKSLD EMEKQQREQV EKNMKDAKDK LESEMEDAYH EHQANLLRQD LMRRQEELRR
MEELHSQEMQ KRKEMQLRQE EERRRREEEM MIRQREMEEQ MRRQREESYS RMGYMDPRER
DMRMGGGGTM NMGDPYGSGG QKFPPLGGGG GIGYEANPGV PPATMSGSMM GSDMRTERFG
QGGAGPVGGQ GPRGMGPGTP AGYGRGREEY EGPNKKPRF
