MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Splicing factor, proline- and glutamine-rich; AltName: Full=DNA-binding p52/p100 complex, 100 kDa subunit; AltName: Full=Polypyrimidine tract-binding protein-associated-splicing factor; Short=PSF; Short=PTB-associated-splicing factor; |
 |
|
| MyHits synonyms | SFPQ_MOUSE , Q8VIJ6 , A2A7U6 , Q9ERW2 , 714F786264C63AA0 |
 Legends: 1, Omega-N-methylated arginine. {ECO:0000250}; 2, Phosphoserine; by MKNK2. {ECO:0000250}; 3, Asymmetric dimethylarginine; alternate. {ECO:0000244|PubMed:24129315}; 4, Omega-N-methylarginine; alternate. {ECO:0000244|PubMed:24129315}; 5, Omega-N-methylated arginine; alternate. {ECO:0000250}; 6, Phosphoserine. {ECO:0000250|UniProtKB:P23246}; 7, N6-acetyllysine. {ECO:0000244|PubMed:23806337}; 8, Omega-N-methylarginine. {ECO:0000244|PubMed:24129315}; 9, Phosphotyrosine; by ALK. {ECO:0000250}; 10, N6,N6-dimethyllysine. {ECO:0000250|UniProtKB:P23246}; 11, N6-acetyllysine. {ECO:0000250|UniProtKB:P23246}; 12, N6-acetyllysine; alternate. {ECO:0000250|UniProtKB:P23246}; 13, Phosphothreonine. {ECO:0000250|UniProtKB:P23246}; 14, Dimethylated arginine. {ECO:0000250|UniProtKB:P23246}; 15, Phosphothreonine. {ECO:0000244|PubMed:17242355, ECO:0000244|PubMed:21183079}; 16, Phosphotyrosine. {ECO:0000250|UniProtKB:P23246}; 17, Dimethylated arginine; alternate. {ECO:0000250|UniProtKB:P23246}; 18, Omega-N-methylarginine. {ECO:0000250|UniProtKB:P23246}; 19, CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate. {ECO:0000250|UniProtKB:P23246}; 20, CONFLICT M -> Q (in Ref. 4; AA sequence). {ECO:0000305}; 21, CONFLICT S -> N (in Ref. 4; AAG17365). {ECO:0000305}; 22, REPEAT 1; 23, REPEAT 2; 24, REPEAT 3; 25, RRM 1. {ECO:0000255|PROSITE- ProRule:PRU00176}; 26, RRM 2. {ECO:0000255|PROSITE- ProRule:PRU00176}; 27, REGION 3 X 3 AA repeats of R-G-G; 28, COMPBIAS Poly-Gly; 29, COMPBIAS Poly-Pro; 30, COMPBIAS Poly-Gln; 31, COMPBIAS Poly-Arg; 32, ipfam:RRM_1 [T]; 33, ipfam:NOPS [T]; 34, iprf:RRM [T]; 35, ismart:RRM [T].
| |
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 02-NOV-2016, entry version 145.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; 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.,
RA Vandekerckhove J., Zipori D.;
RT "Nuclear relocalization of the pre-mRNA splicing factor PSF during
RT apoptosis involves hyperphosphorylation, masking of antigenic
RT epitopes, and 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.,
RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of
RT the 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
RT project: 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;
RP 47-55 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.,
RA Kimura M., Uesugi S., Kurihara Y.;
RT "Expression and functional significance of mouse paraspeckle protein 1
RT on spermatogenesis.";
RL Biol. Reprod. 71:926-932(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-679, AND IDENTIFICATION
RP BY 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.,
RA Burbach J.P., 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
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC Pancreas, 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
RT expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION IN CIRCADIAN RHYTHMS, IDENTIFICATION IN A LARGE PER COMPLEX,
RP AND 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.,
RA Fox A.H., Kramer A., Brown S.A.;
RT "Distinct roles of DBHS family members in the circadian
RT transcriptional feedback loop.";
RL Mol. Cell. Biol. 32:4585-4594(2012).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-200, AND IDENTIFICATION BY
RP MASS 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.,
RA Zhang Y., 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;
RP ARG-237; ARG-673 AND ARG-685, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE 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.,
RA Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
RA Vemulapalli V., 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
CC nuclear processes. Essential pre-mRNA splicing factor required
CC early in spliceosome formation and for splicing catalytic step II,
CC probably as a heteromer with NONO. Binds to pre-mRNA in
CC spliceosome C complex, and specifically binds to intronic
CC polypyrimidine tracts. Involved in regulation of signal-induced
CC alternative splicing. During splicing of PTPRC/CD45, a
CC phosphorylated form is sequestered by THRAP3 from the pre-mRNA in
CC resting T-cells; T-cell activation and subsequent reduced
CC phosphorylation is proposed to lead to release from THRAP3
CC allowing binding to pre-mRNA splicing regulatotry elements which
CC represses exon inclusion. Interacts with U5 snRNA, probably by
CC binding to a purine-rich sequence located on the 3' side of U5
CC snRNA stem 1b. May be involved in a pre-mRNA coupled splicing and
CC polyadenylation process as component of a snRNP-free complex with
CC SNRPA/U1A. The SFPQ-NONO heteromer associated with MATR3 may play
CC a role in nuclear retention of defective RNAs. SFPQ may be
CC involved in homologous DNA pairing; in vitro, promotes the
CC invasion of ssDNA between a duplex DNA and produces a D-loop
CC formation. The SFPQ-NONO heteromer may be involved in DNA
CC unwinding by modulating the function of topoisomerase I/TOP1; in
CC vitro, stimulates dissociation of TOP1 from DNA after cleavage and
CC enhances its jumping between separate DNA helices. The SFPQ-NONO
CC heteromer may be involved in DNA non-homologous end joining (NHEJ)
CC required for double-strand break repair and V(D)J recombination
CC and may stabilize paired DNA ends; in vitro, the complex strongly
CC stimulates DNA end joining, binds directly to the DNA substrates
CC and cooperates with the Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to
CC establish a functional preligation complex. SFPQ is involved in
CC transcriptional regulation. Transcriptional repression is mediated
CC by an interaction of SFPQ with SIN3A and subsequent recruitment of
CC histone deacetylases (HDACs). The SFPQ-NONO-NR5A1 complex binds to
CC the CYP17 promoter and regulates basal and cAMP-dependent
CC transcriptional avtivity. SFPQ isoform Long binds to the DNA
CC binding domains (DBD) of nuclear hormone receptors, like RXRA and
CC probably THRA, and acts as transcriptional corepressor in absence
CC of hormone ligands. Binds the DNA sequence 5'-CTGAGTC-3' in the
CC insulin-like growth factor response element (IGFRE) and inhibits
CC IGF-I-stimulated transcriptional activity. Regulates the circadian
CC clock by repressing the transcriptional activator activity of the
CC CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional
CC repression of circadian target genes, such as PER1, mediated by
CC the large PER complex through histone deacetylation.
CC {ECO:0000269|PubMed:21680841, ECO:0000269|PubMed:22966205}.
CC -!- SUBUNIT: Monomer and component of the SFPQ-NONO complex, which is
CC probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa
CC (SFPQ) subunits. SFPQ is a component of spliceosome and U5.4/6
CC snRNP complexes. Interacts with SNRPA/U1A. Component of a snRNP-
CC free complex with SNRPA/U1A. Part of complex consisting of SFPQ,
CC NONO and MATR3. Interacts with polypyrimidine tract-binding
CC protein 1/PTB. Part of a complex consisting of SFPQ, NONO and
CC NR5A1. Interacts with RXRA, probably THRA, and SIN3A. Interacts
CC with TOP1. Part of a complex consisting of SFPQ, NONO and TOP1.
CC Interacts with SNRNP70 in apoptotic cells. Interacts with PSPC1.
CC Interacts with RNF43. Interacts with PITX3 and NR4A2/NURR1.
CC Interacts with PTK6. Interacts with THRAP3; the interaction is
CC dependent on SFPQ phosphorylation at 'Thr-679' and inhibits
CC binding of SFPQ to a ESS1 exonic splicing silencer element-
CC containing RNA. The large PER complex involved in the histone
CC deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A.
CC Interacts with PER1 and PER2. {ECO:0000269|PubMed:15140795,
CC ECO:0000269|PubMed:19144721, ECO:0000269|PubMed:21680841,
CC ECO:0000269|PubMed:22966205}.
CC -!- SUBCELLULAR LOCATION: Nucleus matrix
CC {ECO:0000269|PubMed:21680841}. Cytoplasm
CC {ECO:0000250|UniProtKB:P23246}. Note=Predominantly in nuclear
CC matrix. {ECO:0000250|UniProtKB:P23246}.
CC -!- PTM: Phosphorylated on multiple serine and threonine residues
CC during apoptosis (By similarity). Phosphorylation of C-terminal
CC tyrosines promotes its cytoplasmic localization, impaired its
CC binding to polypyrimidine RNA and led to cell cycle arrest (By
CC similarity). In resting T-cells is phosphorylated at Thr-679 by
CC GSK3B which is proposed to promote association with THRAP and to
CC prevent binding to PTPRC/CD45 pre-mRNA; T-cell activation leads to
CC reduced phosphorylation at Thr-679. {ECO:0000250}.
CC -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC {ECO:0000255|PROSITE-ProRule:PRU00176}.
DR EMBL; AY034062; AAK60397.1; -; mRNA.
DR EMBL; AL606985; CAM15587.1; -; 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 UniGene; Mm.257276; -.
DR UniGene; Mm.482296; -.
DR ProteinModelPortal; Q8VIJ6; -.
DR SMR; Q8VIJ6; -.
DR BioGrid; 214752; 13.
DR IntAct; Q8VIJ6; 2.
DR MINT; MINT-4120373; -.
DR STRING; 10090.ENSMUSP00000030623; -.
DR iPTMnet; Q8VIJ6; -.
DR PhosphoSitePlus; Q8VIJ6; -.
DR SwissPalm; Q8VIJ6; -.
DR REPRODUCTION-2DPAGE; Q8VIJ6; -.
DR EPD; Q8VIJ6; -.
DR MaxQB; Q8VIJ6; -.
DR PaxDb; Q8VIJ6; -.
DR PeptideAtlas; Q8VIJ6; -.
DR PRIDE; Q8VIJ6; -.
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 eggNOG; KOG0115; Eukaryota.
DR eggNOG; ENOG410XQA0; LUCA.
DR GeneTree; ENSGT00390000005004; -.
DR HOGENOM; HOG000231095; -.
DR HOVERGEN; HBG009801; -.
DR InParanoid; Q8VIJ6; -.
DR KO; K13219; -.
DR OMA; GRQHHAP; -.
DR OrthoDB; EOG091G09T7; -.
DR PhylomeDB; Q8VIJ6; -.
DR TreeFam; TF315795; -.
DR Reactome; R-MMU-8849468; PTK6 Regulates Proteins Involved in RNA Processing.
DR ChiTaRS; Sfpq; mouse.
DR PRO; PR:Q8VIJ6; -.
DR Proteomes; UP000000589; Chromosome 4.
DR Bgee; ENSMUSG00000028820; -.
DR Genevisible; Q8VIJ6; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
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 factor complex; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:BHF-UCL.
DR GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0044822; F:poly(A) RNA binding; ISO:MGI.
DR GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:BHF-UCL.
DR GO; GO:0044212; F:transcription regulatory region DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
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:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0070932; P:histone H3 deacetylation; IMP:UniProtKB.
DR GO; GO:0042754; P:negative regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; 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:0051726; P:regulation of cell cycle; IMP:MGI.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012975; NOPS.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
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; Complete proteome;
KW Cytoplasm; Direct protein sequencing; DNA damage; DNA repair;
KW DNA-binding; 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 Splicing factor, proline- and glutamine-
FT rich.
FT /FTId=PRO_0000081910.
FT REPEAT 9 11 1.
FT REPEAT 19 21 2.
FT REPEAT 25 27 3.
FT DOMAIN 289 361 RRM 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00176}.
FT DOMAIN 363 444 RRM 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00176}.
FT REGION 9 27 3 X 3 AA repeats of R-G-G.
FT COMPBIAS 10 258 Gln/Glu/Pro-rich.
FT COMPBIAS 10 15 Poly-Gly.
FT COMPBIAS 20 27 Poly-Gly.
FT COMPBIAS 54 63 Poly-Pro.
FT COMPBIAS 65 69 Poly-Gln.
FT COMPBIAS 96 100 Poly-Pro.
FT COMPBIAS 158 161 Poly-Pro.
FT COMPBIAS 178 182 Poly-Pro.
FT COMPBIAS 563 566 Poly-Arg.
FT COMPBIAS 605 608 Poly-Gly.
FT COMPBIAS 627 633 Poly-Gly.
FT MOD_RES 7 7 Omega-N-methylated arginine.
FT {ECO:0000250}.
FT MOD_RES 8 8 Phosphoserine; by MKNK2. {ECO:0000250}.
FT MOD_RES 9 9 Asymmetric dimethylarginine; alternate.
FT {ECO:0000244|PubMed:24129315}.
FT MOD_RES 9 9 Omega-N-methylarginine; alternate.
FT {ECO:0000244|PubMed:24129315}.
FT MOD_RES 9 9 Omega-N-methylated arginine; alternate.
FT {ECO:0000250}.
FT MOD_RES 19 19 Omega-N-methylated arginine.
FT {ECO:0000250}.
FT MOD_RES 25 25 Omega-N-methylated arginine.
FT {ECO:0000250}.
FT MOD_RES 33 33 Phosphoserine.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 200 200 N6-acetyllysine.
FT {ECO:0000244|PubMed:23806337}.
FT MOD_RES 228 228 Omega-N-methylarginine.
FT {ECO:0000244|PubMed:24129315}.
FT MOD_RES 234 234 Omega-N-methylarginine.
FT {ECO:0000244|PubMed:24129315}.
FT MOD_RES 237 237 Omega-N-methylarginine.
FT {ECO:0000244|PubMed:24129315}.
FT MOD_RES 265 265 Phosphoserine.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 275 275 Phosphoserine; by MKNK2. {ECO:0000250}.
FT MOD_RES 285 285 Phosphotyrosine; by ALK. {ECO:0000250}.
FT MOD_RES 306 306 N6,N6-dimethyllysine.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 311 311 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 330 330 N6-acetyllysine; alternate.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 360 360 Phosphothreonine.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 366 366 Phosphoserine.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 371 371 Phosphoserine.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 413 413 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 464 464 N6-acetyllysine.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 488 488 Phosphoserine.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 563 563 Dimethylated arginine.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 618 618 Phosphoserine.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 673 673 Omega-N-methylarginine.
FT {ECO:0000244|PubMed:24129315}.
FT MOD_RES 679 679 Phosphothreonine.
FT {ECO:0000244|PubMed:17242355,
FT ECO:0000244|PubMed:21183079}.
FT MOD_RES 683 683 Phosphotyrosine.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 685 685 Dimethylated arginine; alternate.
FT {ECO:0000250|UniProtKB:P23246}.
FT MOD_RES 685 685 Omega-N-methylarginine; alternate.
FT {ECO:0000244|PubMed:24129315}.
FT MOD_RES 687 687 Omega-N-methylarginine.
FT {ECO:0000250|UniProtKB:P23246}.
FT CROSSLNK 330 330 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO2);
FT alternate.
FT {ECO:0000250|UniProtKB:P23246}.
FT CONFLICT 47 47 M -> Q (in Ref. 4; AA sequence).
FT {ECO:0000305}.
FT CONFLICT 546 546 S -> N (in Ref. 4; AAG17365).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 291 355 ipfam:RRM_1 [T]
FT MYHIT 436 487 ipfam:NOPS [T]
FT MYHIT 289 361 iprf:RRM [T]
FT MYHIT 290 357 ismart:RRM [T]
FT MYHIT 366 425 ipfam:RRM_1 [T]
FT MYHIT 364 440 ismart:RRM [T]
FT MYHIT 363 444 iprf:RRM [T]
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
//
| |