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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9SZR

shutdown state non-muscle myosin 2A heads region

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0000146molecular_functionmicrofilament motor activity
A0000166molecular_functionnucleotide binding
A0000902biological_processcell morphogenesis
A0001525biological_processangiogenesis
A0001618molecular_functionvirus receptor activity
A0001725cellular_componentstress fiber
A0001726cellular_componentruffle
A0001772cellular_componentimmunological synapse
A0001778biological_processplasma membrane repair
A0001931cellular_componenturopod
A0003723molecular_functionRNA binding
A0003774molecular_functioncytoskeletal motor activity
A0003779molecular_functionactin binding
A0005178molecular_functionintegrin binding
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005819cellular_componentspindle
A0005826cellular_componentactomyosin contractile ring
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005903cellular_componentbrush border
A0005912cellular_componentadherens junction
A0005925cellular_componentfocal adhesion
A0005938cellular_componentcell cortex
A0006509biological_processmembrane protein ectodomain proteolysis
A0006911biological_processphagocytosis, engulfment
A0007010biological_processcytoskeleton organization
A0007155biological_processcell adhesion
A0007229biological_processintegrin-mediated signaling pathway
A0008180cellular_componentCOP9 signalosome
A0008360biological_processregulation of cell shape
A0009898cellular_componentcytoplasmic side of plasma membrane
A0009986cellular_componentcell surface
A0015031biological_processprotein transport
A0015629cellular_componentactin cytoskeleton
A0016020cellular_componentmembrane
A0016459cellular_componentmyosin complex
A0016460cellular_componentmyosin II complex
A0019904molecular_functionprotein domain specific binding
A0030029biological_processactin filament-based process
A0030036biological_processactin cytoskeleton organization
A0030048biological_processactin filament-based movement
A0030154biological_processcell differentiation
A0030220biological_processplatelet formation
A0030224biological_processmonocyte differentiation
A0030863cellular_componentcortical cytoskeleton
A0031032biological_processactomyosin structure organization
A0031252cellular_componentcell leading edge
A0031410cellular_componentcytoplasmic vesicle
A0031594cellular_componentneuromuscular junction
A0032154cellular_componentcleavage furrow
A0032418biological_processlysosome localization
A0032506biological_processcytokinetic process
A0032970biological_processregulation of actin filament-based process
A0032982cellular_componentmyosin filament
A0032991cellular_componentprotein-containing complex
A0042641cellular_componentactomyosin
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0043495molecular_functionprotein-membrane adaptor activity
A0043531molecular_functionADP binding
A0043534biological_processblood vessel endothelial cell migration
A0045055biological_processregulated exocytosis
A0045296molecular_functioncadherin binding
A0046718biological_processsymbiont entry into host cell
A0050900biological_processleukocyte migration
A0051015molecular_functionactin filament binding
A0060471biological_processcortical granule exocytosis
A0060473cellular_componentcortical granule
A0070062cellular_componentextracellular exosome
A0070527biological_processplatelet aggregation
A0097513cellular_componentmyosin II filament
A0099512cellular_componentsupramolecular fiber
A1903919biological_processnegative regulation of actin filament severing
A1903923biological_processpositive regulation of protein processing in phagocytic vesicle
A1905684biological_processregulation of plasma membrane repair
B0000146molecular_functionmicrofilament motor activity
B0000166molecular_functionnucleotide binding
B0000902biological_processcell morphogenesis
B0001525biological_processangiogenesis
B0001618molecular_functionvirus receptor activity
B0001725cellular_componentstress fiber
B0001726cellular_componentruffle
B0001772cellular_componentimmunological synapse
B0001778biological_processplasma membrane repair
B0001931cellular_componenturopod
B0003723molecular_functionRNA binding
B0003774molecular_functioncytoskeletal motor activity
B0003779molecular_functionactin binding
B0005178molecular_functionintegrin binding
B0005515molecular_functionprotein binding
B0005516molecular_functioncalmodulin binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005794cellular_componentGolgi apparatus
B0005819cellular_componentspindle
B0005826cellular_componentactomyosin contractile ring
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0005903cellular_componentbrush border
B0005912cellular_componentadherens junction
B0005925cellular_componentfocal adhesion
B0005938cellular_componentcell cortex
B0006509biological_processmembrane protein ectodomain proteolysis
B0006911biological_processphagocytosis, engulfment
B0007010biological_processcytoskeleton organization
B0007155biological_processcell adhesion
B0007229biological_processintegrin-mediated signaling pathway
B0008180cellular_componentCOP9 signalosome
B0008360biological_processregulation of cell shape
B0009898cellular_componentcytoplasmic side of plasma membrane
B0009986cellular_componentcell surface
B0015031biological_processprotein transport
B0015629cellular_componentactin cytoskeleton
B0016020cellular_componentmembrane
B0016459cellular_componentmyosin complex
B0016460cellular_componentmyosin II complex
B0019904molecular_functionprotein domain specific binding
B0030029biological_processactin filament-based process
B0030036biological_processactin cytoskeleton organization
B0030048biological_processactin filament-based movement
B0030154biological_processcell differentiation
B0030220biological_processplatelet formation
B0030224biological_processmonocyte differentiation
B0030863cellular_componentcortical cytoskeleton
B0031032biological_processactomyosin structure organization
B0031252cellular_componentcell leading edge
B0031410cellular_componentcytoplasmic vesicle
B0031594cellular_componentneuromuscular junction
B0032154cellular_componentcleavage furrow
B0032418biological_processlysosome localization
B0032506biological_processcytokinetic process
B0032970biological_processregulation of actin filament-based process
B0032982cellular_componentmyosin filament
B0032991cellular_componentprotein-containing complex
B0042641cellular_componentactomyosin
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0043495molecular_functionprotein-membrane adaptor activity
B0043531molecular_functionADP binding
B0043534biological_processblood vessel endothelial cell migration
B0045055biological_processregulated exocytosis
B0045296molecular_functioncadherin binding
B0046718biological_processsymbiont entry into host cell
B0050900biological_processleukocyte migration
B0051015molecular_functionactin filament binding
B0060471biological_processcortical granule exocytosis
B0060473cellular_componentcortical granule
B0070062cellular_componentextracellular exosome
B0070527biological_processplatelet aggregation
B0097513cellular_componentmyosin II filament
B0099512cellular_componentsupramolecular fiber
B1903919biological_processnegative regulation of actin filament severing
B1903923biological_processpositive regulation of protein processing in phagocytic vesicle
B1905684biological_processregulation of plasma membrane repair
C0000146molecular_functionmicrofilament motor activity
C0000287molecular_functionmagnesium ion binding
C0005515molecular_functionprotein binding
C0005829cellular_componentcytosol
C0005859cellular_componentmuscle myosin complex
C0008307molecular_functionstructural constituent of muscle
C0016459cellular_componentmyosin complex
C0016460cellular_componentmyosin II complex
C0030239biological_processmyofibril assembly
C0031032biological_processactomyosin structure organization
C0032036molecular_functionmyosin heavy chain binding
C0042641cellular_componentactomyosin
C0043531molecular_functionADP binding
C0045159molecular_functionmyosin II binding
C0051015molecular_functionactin filament binding
C0097513cellular_componentmyosin II filament
D0000146molecular_functionmicrofilament motor activity
D0000287molecular_functionmagnesium ion binding
D0005515molecular_functionprotein binding
D0005829cellular_componentcytosol
D0005859cellular_componentmuscle myosin complex
D0008307molecular_functionstructural constituent of muscle
D0016459cellular_componentmyosin complex
D0016460cellular_componentmyosin II complex
D0030239biological_processmyofibril assembly
D0031032biological_processactomyosin structure organization
D0032036molecular_functionmyosin heavy chain binding
D0042641cellular_componentactomyosin
D0043531molecular_functionADP binding
D0045159molecular_functionmyosin II binding
D0051015molecular_functionactin filament binding
D0097513cellular_componentmyosin II filament
E0000146molecular_functionmicrofilament motor activity
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005938cellular_componentcell cortex
E0016459cellular_componentmyosin complex
E0016460cellular_componentmyosin II complex
E0031032biological_processactomyosin structure organization
E0032036molecular_functionmyosin heavy chain binding
E0042641cellular_componentactomyosin
E0046872molecular_functionmetal ion binding
E0051015molecular_functionactin filament binding
E0097513cellular_componentmyosin II filament
F0000146molecular_functionmicrofilament motor activity
F0005737cellular_componentcytoplasm
F0005856cellular_componentcytoskeleton
F0005938cellular_componentcell cortex
F0016459cellular_componentmyosin complex
F0016460cellular_componentmyosin II complex
F0031032biological_processactomyosin structure organization
F0032036molecular_functionmyosin heavy chain binding
F0042641cellular_componentactomyosin
F0046872molecular_functionmetal ion binding
F0051015molecular_functionactin filament binding
F0097513cellular_componentmyosin II filament
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DQNRDGFIDkeDL
ChainResidueDetails
EASP41-LEU53
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues100
DetailsDomain: {"description":"Myosin N-terminal SH3-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU01190","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues58
DetailsDomain: {"description":"IQ","evidences":[{"source":"PROSITE-ProRule","id":"PRU00116","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues44
DetailsRegion: {"description":"Actin-binding"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues248
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2178
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues94
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues14
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys R."]}}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues20
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P35580","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues14
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q8VDD5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q8VDD5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8VDD5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q61879","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q61879","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17487921","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18088087","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18318008","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19367720","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues140
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues140
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues64
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"N-acetylcysteine","evidences":[{"source":"PubMed","id":"6870825","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by MLCK, CIT and ROCK2","evidences":[{"source":"UniProtKB","id":"P24844","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by CDC42BP, CIT, MLCK, PAK1, ROCK1, ROCK2, DAPK1, DAPK2 and ZIPK/DAPK3","evidences":[{"source":"UniProtKB","id":"P24844","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

248636

PDB entries from 2026-02-04

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