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- SASDFK3: Splicing factor, proline- and glutamine-rich (SFPQ) -

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Basic information

Entry
Database: SASBDB / ID: SASDFK3
SampleSplicing factor, proline- and glutamine-rich (SFPQ)
  • Splicing factor, proline- and glutamine-rich (protein), SFPQ, Homo sapiens
Function / homology
Function and homology information


PTK6 Regulates Proteins Involved in RNA Processing / negative regulation of circadian rhythm / alternative mRNA splicing, via spliceosome / Suppression of apoptosis / paraspeckles / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / activation of innate immune response / RNA splicing / double-strand break repair via homologous recombination / regulation of circadian rhythm ...PTK6 Regulates Proteins Involved in RNA Processing / negative regulation of circadian rhythm / alternative mRNA splicing, via spliceosome / Suppression of apoptosis / paraspeckles / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / activation of innate immune response / RNA splicing / double-strand break repair via homologous recombination / regulation of circadian rhythm / mRNA processing / nuclear matrix / histone deacetylase binding / RNA polymerase II transcription regulator complex / rhythmic process / transcription cis-regulatory region binding / nuclear speck / chromatin remodeling / innate immune response / negative regulation of DNA-templated transcription / chromatin binding / chromatin / regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / DNA binding / RNA binding / nucleoplasm / nucleus / cytosol
Similarity search - Function
PSF, RNA recognition motif 1 / PSF, NOPS domain / NOPS / NOPS (NUC059) domain / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Nucleotide-binding alpha-beta plait domain superfamily
Similarity search - Domain/homology
Splicing factor, proline- and glutamine-rich
Similarity search - Component
Biological speciesHomo sapiens (human)
CitationDate: 2019 Jun 1
Title: A new crystal structure and small-angle X-ray scattering analysis of the homodimer of human SFPQ
Authors: Hewage T / Caria S
Contact author
  • Sofia Caria (ANSTO, Australian Nuclear Science and Technology Organisation, Kirrawee DC, NSW 2232, Australia)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Models

Model #3006
Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 0.446
Search similar-shape structures of this assembly by Omokage search (details)
Model #3007
Type: mix / Radius of dummy atoms: 1.90 A / Chi-square value: 0.372
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Splicing factor, proline- and glutamine-rich (SFPQ) / Specimen concentration: 5 mg/ml
BufferName: 20 mM Tris-HCl, 250 mM NaCl, 5% (v/v) glycerol / pH: 7.5
Entity #1494Name: SFPQ / Type: protein / Description: Splicing factor, proline- and glutamine-rich / Formula weight: 30.049 / Num. of mol.: 2 / Source: Homo sapiens / References: UniProt: P23246
Sequence: GAMEGFKANL SLLRRPGEKT YTQRCRLFVG NLPADITEDE FKRLFAKYGE PGEVFINKGK GFGFIKLESR ALAEIAKAEL DDTPMRGRQL RVRFATHAAA LSVRNLSPYV SNELLEEAFS QFGPIERAVV IVDDRGRSTG KGIVEFASKP AARKAFERCS EGVFLLTTTP ...Sequence:
GAMEGFKANL SLLRRPGEKT YTQRCRLFVG NLPADITEDE FKRLFAKYGE PGEVFINKGK GFGFIKLESR ALAEIAKAEL DDTPMRGRQL RVRFATHAAA LSVRNLSPYV SNELLEEAFS QFGPIERAVV IVDDRGRSTG KGIVEFASKP AARKAFERCS EGVFLLTTTP RPVIVEPLEQ LDDEDGLPEK LAQKNPMYQK ERETPPRFAQ HGTFEYEYSQ RWKSLDEMEK QQREQVEKNM KDAKDKLESE MEDAYHEHQA NLL

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Experimental information

BeamInstrument name: Australian Synchrotron SAXS/WAXS / City: Melbourne / 国: Australia / Shape: Point / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.10332 Å / Dist. spec. to detc.: 2.68 mm
DetectorName: Pilatus 1M / Type: Dectris / Pixsize x: 172 mm
Scan
Title: Splicing factor, proline- and glutamine-rich (SFPQ) / Measurement date: Apr 19, 2018 / Cell temperature: 25 °C / Exposure time: 1 sec. / Number of frames: 4 / Unit: 1/A /
MinMax
Q0.0088 0.3518
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 823 /
MinMax
Q0.0173679 0.337796
P(R) point1 823
R0 82
Result
Type of curve: sec
Comments: CORAL was used to compare the scattering profile against the two PDB models of SFPQ in either P212121 or C2221 crystallographic space groups (CRYSOL fits to the data are shown; Coral models ...Comments: CORAL was used to compare the scattering profile against the two PDB models of SFPQ in either P212121 or C2221 crystallographic space groups (CRYSOL fits to the data are shown; Coral models and fits are included in the full entry zip archive).
ExperimentalStandardPorod
MW60.58 kDa60.58 kDa57 kDa
Volume--91 nm3

P(R)P(R) errorGuinierGuinier error
Forward scattering, I00.05871 0.00016 0.05911 0.00016
Radius of gyration, Rg2.731 nm0.008 2.77 nm0.01

MinMax
D-8.2
Guinier point8 106

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