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- SASDB32: Human Filamin A Ig-like domains 16-17 truncation (1782-1956) -

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Basic information

Entry
Database: SASBDB / ID: SASDB32
SampleHuman Filamin A Ig-like domains 16-17 truncation (1782-1956)
  • Human Filamin A Ig-like domains 16-17 (protein), FilaminA, Homo sapiens
Function / homology
Function and homology information


regulation of membrane repolarization during atrial cardiac muscle cell action potential / regulation of membrane repolarization during cardiac muscle cell action potential / establishment of Sertoli cell barrier / Myb complex / glycoprotein Ib-IX-V complex / adenylate cyclase-inhibiting dopamine receptor signaling pathway / formation of radial glial scaffolds / positive regulation of integrin-mediated signaling pathway / actin crosslink formation / blood coagulation, intrinsic pathway ...regulation of membrane repolarization during atrial cardiac muscle cell action potential / regulation of membrane repolarization during cardiac muscle cell action potential / establishment of Sertoli cell barrier / Myb complex / glycoprotein Ib-IX-V complex / adenylate cyclase-inhibiting dopamine receptor signaling pathway / formation of radial glial scaffolds / positive regulation of integrin-mediated signaling pathway / actin crosslink formation / blood coagulation, intrinsic pathway / tubulin deacetylation / OAS antiviral response / positive regulation of actin filament bundle assembly / positive regulation of neuron migration / protein localization to bicellular tight junction / Fc-gamma receptor I complex binding / Cell-extracellular matrix interactions / apical dendrite / positive regulation of potassium ion transmembrane transport / positive regulation of neural precursor cell proliferation / positive regulation of platelet activation / protein localization to cell surface / wound healing, spreading of cells / podosome / negative regulation of transcription by RNA polymerase I / megakaryocyte development / GP1b-IX-V activation signalling / SMAD binding / receptor clustering / cortical cytoskeleton / RHO GTPases activate PAKs / semaphorin-plexin signaling pathway / cilium assembly / mitotic spindle assembly / potassium channel regulator activity / negative regulation of DNA-binding transcription factor activity / release of sequestered calcium ion into cytosol / positive regulation of substrate adhesion-dependent cell spreading / protein sequestering activity / regulation of cell migration / dendritic shaft / protein localization to plasma membrane / actin filament / establishment of protein localization / mRNA transcription by RNA polymerase II / G protein-coupled receptor binding / cerebral cortex development / negative regulation of protein catabolic process / positive regulation of protein import into nucleus / small GTPase binding / platelet aggregation / kinase binding / Z disc / actin filament binding / cell-cell junction / Platelet degranulation / actin cytoskeleton / growth cone / GTPase binding / actin cytoskeleton organization / perikaryon / DNA-binding transcription factor binding / transmembrane transporter binding / positive regulation of canonical NF-kappaB signal transduction / postsynapse / protein stabilization / cadherin binding / focal adhesion / negative regulation of apoptotic process / nucleolus / perinuclear region of cytoplasm / glutamatergic synapse / protein homodimerization activity / RNA binding / extracellular exosome / extracellular region / nucleus / membrane / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Filamin family / Filamin/ABP280 repeat / Filamin-type immunoglobulin domains / Filamin/ABP280 repeat / Filamin/ABP280 repeat profile. / Filamin/ABP280 repeat-like / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Actinin-type actin-binding domain, conserved site / Calponin homology domain ...Filamin family / Filamin/ABP280 repeat / Filamin-type immunoglobulin domains / Filamin/ABP280 repeat / Filamin/ABP280 repeat profile. / Filamin/ABP280 repeat-like / Actinin-type actin-binding domain signature 1. / Actinin-type actin-binding domain signature 2. / Actinin-type actin-binding domain, conserved site / Calponin homology domain / Calponin homology (CH) domain / Calponin homology domain / CH domain superfamily / Calponin homology (CH) domain profile. / Immunoglobulin E-set / Immunoglobulin-like fold
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
CitationDate: 2017 Dec
Title: Skeletal Dysplasia Mutations Effect on Human Filamins’ Structure and Mechanosensing
Authors: Seppälä J / Bernardi R / Haataja T / Hellman M / Pentikäinen O / Schulten K / Permi P / Ylänne J
Contact author
  • Jonne Seppälä (University of Jyväskylä, Jyväskylän, Finland)

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Models

Model #382
Type: dummy / Radius of dummy atoms: 1.75 A / Chi-square value: 1.096
Search similar-shape structures of this assembly by Omokage search (details)

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Sample

SampleName: Human Filamin A Ig-like domains 16-17 truncation (1782-1956)
Specimen concentration: 1.00-5.00
BufferName: 20 mM Tris 50 mM NaCl 10 mM DTT / Concentration: 20.00 mM / Composition: 50mM NaCl, 10mM DTT
Entity #246Name: FilaminA / Type: protein / Description: Human Filamin A Ig-like domains 16-17 / Formula weight: 18.7 / Num. of mol.: 1 / Source: Homo sapiens / References: UniProt: P21333
Sequence:
GLDVTSLRPF DLVIPFTIKK GEITGEVRMP SGKVAQPTIT DNKDGTVTVR YAPSEAGLHE MDIRYDNMHI PGSPLQFYVD YVNCGHVTAY GPGLTHGVVN KPATFTVNTK DAGEGGLSLA IEGPSKAEIS CTDNQDGTCS VSYLPVLPGD YSILVKYNEQ HVPGSPFTAR VTGDD

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Experimental information

BeamInstrument name: ESRF BM29 / City: Grenoble / : France / Type of source: X-ray synchrotron / Wavelength: 0.93 Å / Dist. spec. to detc.: 2.43 mm
DetectorName: Pilatus 1M
Scan
Title: Human Filamin A Ig-like domains 16-17 / Measurement date: Sep 30, 2013 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 10 / Unit: 1/nm /
MinMax
Q0.0366 4.4631
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 374 /
MinMax
Q0.267 3.477
P(R) point54 427
R0 6.24
Result
Type of curve: merged
ExperimentalStandardPorodEstimatedEstimated method
MW20 kDa20 kDa18.1 kDa--
Volume--30.7 nm337.8 DAMMIN

P(R)Guinier
Forward scattering, I030.32 30.33
Radius of gyration, Rg1.83 nm1.83 nm

MinMax
D-6.2
Guinier point26 115

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