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- SASDFZ4: R16-24 human dystrophin fragment (Human dystrophin central domain... -
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Open data
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Basic information
Entry | ![]() |
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![]() | R16-24 human dystrophin fragment
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Function / homology | ![]() regulation of muscle system process / regulation of cellular response to growth factor stimulus / regulation of skeletal muscle contraction / syntrophin complex / synaptic signaling / cardiac muscle cell action potential / regulation of voltage-gated calcium channel activity / negative regulation of peptidyl-cysteine S-nitrosylation / positive regulation of sodium ion transmembrane transporter activity / dystrophin-associated glycoprotein complex ...regulation of muscle system process / regulation of cellular response to growth factor stimulus / regulation of skeletal muscle contraction / syntrophin complex / synaptic signaling / cardiac muscle cell action potential / regulation of voltage-gated calcium channel activity / negative regulation of peptidyl-cysteine S-nitrosylation / positive regulation of sodium ion transmembrane transporter activity / dystrophin-associated glycoprotein complex / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / peptide biosynthetic process / cell-substrate junction / motile cilium assembly / dystroglycan binding / vinculin binding / muscle cell development / costamere / neuron projection terminus / Striated Muscle Contraction / filopodium membrane / muscle organ development / structural constituent of muscle / muscle cell cellular homeostasis / maintenance of blood-brain barrier / myosin binding / nitric-oxide synthase binding / negative regulation of peptidyl-serine phosphorylation / Non-integrin membrane-ECM interactions / neuron development / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / cardiac muscle contraction / skeletal muscle tissue development / regulation of ryanodine-sensitive calcium-release channel activity / response to muscle stretch / positive regulation of neuron differentiation / regulation of heart rate / filopodium / protein localization / structural constituent of cytoskeleton / sarcolemma / positive regulation of neuron projection development / Z disc / actin binding / protein-containing complex assembly / postsynaptic membrane / cytoskeleton / membrane raft / synapse / cell surface / protein-containing complex / zinc ion binding / nucleus / plasma membrane / cytosol Similarity search - Function |
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Structure visualization
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Downloads & links
-Data source
SASBDB page | ![]() |
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-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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External links
Related items in Molecule of the Month |
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-Models
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Sample
![]() | Name: R16-24 human dystrophin fragment |
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Buffer | Name: NaP 20 mM, NaCl 300 mM, EDTA 1 mM, Glycérol 2% / pH: 7.5 |
Entity #1557 | Type: protein Description: Human dystrophin central domain R16-24 fragment Formula weight: 126.616 / Num. of mol.: 1 / References: UniProt: P11532 Sequence: MSYYHHHHHH DYDIPTTENL YFOGAMGRSL VPRGSLEISY VPSTYLTEIT HVSQALLEVE QLLNAPDLCA KDFEDLFKQE ESLKNIKDSL QQSSGRIDII HSKKTAALQS ATPVERVKLQ EALSQLDFQW EKVNKMYKDR QGRFDRSVEK WRRFHYDIKI FNQWLTEAEQ ...Sequence: MSYYHHHHHH DYDIPTTENL YFOGAMGRSL VPRGSLEISY VPSTYLTEIT HVSQALLEVE QLLNAPDLCA KDFEDLFKQE ESLKNIKDSL QQSSGRIDII HSKKTAALQS ATPVERVKLQ EALSQLDFQW EKVNKMYKDR QGRFDRSVEK WRRFHYDIKI FNQWLTEAEQ FLRKTQIPEN WEHAKYKWYL KELQDGIGQR QTVVRTLNAT GEEIIQQSSK TDASILQEKL GSLNLRWQEV CKQLSDRKKR LEEQKNILSE FQRDLNEFVL WLEEADNIAS IPLEPGKEQQ LKEKLEQVKL LVEELPLRQA GILKQLNETG GPVLVSAPIS PEEQDKLENK LKQTNLQWIK VSRALPEKQG EIEAQIKDLG QLEKKLEDLE EQLNHLLLWL SPIRNQLEIY NQPNQEGPFD VQETEIAVQA KQPDVEEILS KGQHLYKEKP ATQPVKRKLE DLSSEWKAVN RLLQELRAKQ PDLAPGLTTI GASPTQTVTL VTQPVVTKET AISKLEMPSS LMLEVPALAD FNRAWTELTD WLSLLDQVIK SQRVMVGDLE DINEMIIKQK ATMQDLEQRR PQLEELITAA QNLKNKTSNQ EARTIITDRI ERIQNQWDEV QEHLQNRRQQ LNEMLKDSTQ WLEAKEEAEQ VLGQARAKLE SWKEGPYTVD AIQKKITETK QLAKDLRQWQ TNVDVANDLA LKLLRDYSAD DTRKVHMITE NINASWRSIH KRVSEREAAL EETHRLLQQF PLDLEKFLAW LTEAETTANV LQDATRKERL LEDSKGVKEL MKQWQDLQGE IEAHTDVYHN LDENSQKILR SLEGSDDAVL LQRRLDNMNF KWSELRKKSL NIRSHLEASS DQWKRLHLSL QELLVWLQLK DDELSRQAPI GGDFPAVQKQ NDVHRAFKRE LKTKEPVIMS TLETVRIFLT EQPLEGLEKL YQEPRELPPE ERAQNVTRLL RKQAEEVNTE WEKLNLHSAD WQRKIDETLE RLQELQEATD ELDLKLRQAE VIKGSWQPVG DLLIDSLQDH LEKVKALRGE IAPLKENVSH VNDLARQLTT LGIQLSPYNL STLEDLNTRW KLLQVAVEDR VRQLHE |
-Experimental information
Beam | Instrument name: SOLEIL SWING ![]() ![]() | ||||||||||||
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Detector | Name: AVIEX PCCD170170 / Type: CCD | ||||||||||||
Scan |
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Distance distribution function P(R) |
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Result | Comments: SEC-SAXS was performed at 20°C using the following parameters: Column: BioSEC5-500Å (4.6 mm id * 300 mm); Flow rate: 0.3 mL/min; Sample injection concentration: 4.5 mg/mL; Injection ...Comments: SEC-SAXS was performed at 20°C using the following parameters: Column: BioSEC5-500Å (4.6 mm id * 300 mm); Flow rate: 0.3 mL/min; Sample injection concentration: 4.5 mg/mL; Injection volume: 50μL. The data were collected through the SEC peak of the protein as a series of 38 x 0.75 second exposures. The experimental molecular weight was determined from SEC-MALS (130 kDa).
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