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9B3Q

The structure of the human cardiac F-actin mutant A331P

Functional Information from GO Data
ChainGOidnamespacecontents
A0000146molecular_functionmicrofilament motor activity
A0000166molecular_functionnucleotide binding
A0005200molecular_functionstructural constituent of cytoskeleton
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005884cellular_componentactin filament
A0005925cellular_componentfocal adhesion
A0007015biological_processactin filament organization
A0009410biological_processresponse to xenobiotic stimulus
A0010628biological_processpositive regulation of gene expression
A0015629cellular_componentactin cytoskeleton
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0017022molecular_functionmyosin binding
A0030017cellular_componentsarcomere
A0030027cellular_componentlamellipodium
A0030048biological_processactin filament-based movement
A0030175cellular_componentfilopodium
A0030240biological_processskeletal muscle thin filament assembly
A0031032biological_processactomyosin structure organization
A0031674cellular_componentI band
A0033275biological_processactin-myosin filament sliding
A0044297cellular_componentcell body
A0045202cellular_componentsynapse
A0045471biological_processresponse to ethanol
A0055003biological_processcardiac myofibril assembly
A0055008biological_processcardiac muscle tissue morphogenesis
A0060047biological_processheart contraction
A0060048biological_processcardiac muscle contraction
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
A0090131biological_processmesenchyme migration
A0098978cellular_componentglutamatergic synapse
D0000146molecular_functionmicrofilament motor activity
D0000166molecular_functionnucleotide binding
D0005200molecular_functionstructural constituent of cytoskeleton
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005615cellular_componentextracellular space
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005856cellular_componentcytoskeleton
D0005884cellular_componentactin filament
D0005925cellular_componentfocal adhesion
D0007015biological_processactin filament organization
D0009410biological_processresponse to xenobiotic stimulus
D0010628biological_processpositive regulation of gene expression
D0015629cellular_componentactin cytoskeleton
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
D0017022molecular_functionmyosin binding
D0030017cellular_componentsarcomere
D0030027cellular_componentlamellipodium
D0030048biological_processactin filament-based movement
D0030175cellular_componentfilopodium
D0030240biological_processskeletal muscle thin filament assembly
D0031032biological_processactomyosin structure organization
D0031674cellular_componentI band
D0033275biological_processactin-myosin filament sliding
D0044297cellular_componentcell body
D0045202cellular_componentsynapse
D0045471biological_processresponse to ethanol
D0055003biological_processcardiac myofibril assembly
D0055008biological_processcardiac muscle tissue morphogenesis
D0060047biological_processheart contraction
D0060048biological_processcardiac muscle contraction
D0070062cellular_componentextracellular exosome
D0072562cellular_componentblood microparticle
D0090131biological_processmesenchyme migration
D0098978cellular_componentglutamatergic synapse
E0000146molecular_functionmicrofilament motor activity
E0000166molecular_functionnucleotide binding
E0005200molecular_functionstructural constituent of cytoskeleton
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005615cellular_componentextracellular space
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0005856cellular_componentcytoskeleton
E0005884cellular_componentactin filament
E0005925cellular_componentfocal adhesion
E0007015biological_processactin filament organization
E0009410biological_processresponse to xenobiotic stimulus
E0010628biological_processpositive regulation of gene expression
E0015629cellular_componentactin cytoskeleton
E0016020cellular_componentmembrane
E0016787molecular_functionhydrolase activity
E0017022molecular_functionmyosin binding
E0030017cellular_componentsarcomere
E0030027cellular_componentlamellipodium
E0030048biological_processactin filament-based movement
E0030175cellular_componentfilopodium
E0030240biological_processskeletal muscle thin filament assembly
E0031032biological_processactomyosin structure organization
E0031674cellular_componentI band
E0033275biological_processactin-myosin filament sliding
E0044297cellular_componentcell body
E0045202cellular_componentsynapse
E0045471biological_processresponse to ethanol
E0055003biological_processcardiac myofibril assembly
E0055008biological_processcardiac muscle tissue morphogenesis
E0060047biological_processheart contraction
E0060048biological_processcardiac muscle contraction
E0070062cellular_componentextracellular exosome
E0072562cellular_componentblood microparticle
E0090131biological_processmesenchyme migration
E0098978cellular_componentglutamatergic synapse
Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR53-GLY63

site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WISKqEYDE
ChainResidueDetails
ATRP356-GLU364

site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU104-ARG116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsModified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68033","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsModified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"30626964","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"23673617","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsCross-link: {"description":"Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-272); by Vibrio toxins RtxA and VgrG1","evidences":[{"source":"UniProtKB","id":"P60709","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsCross-link: {"description":"Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-52); by Vibrio toxins RtxA and VgrG1","evidences":[{"source":"UniProtKB","id":"P60709","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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