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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8W41

Cryo-EM structure of Myosin VI in the autoinhibited state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000146molecular_functionmicrofilament motor activity
A0000166molecular_functionnucleotide binding
A0001726cellular_componentruffle
A0003774molecular_functioncytoskeletal motor activity
A0003779molecular_functionactin binding
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005768cellular_componentendosome
A0005776cellular_componentautophagosome
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0005884cellular_componentactin filament
A0005886cellular_componentplasma membrane
A0005902cellular_componentmicrovillus
A0005905cellular_componentclathrin-coated pit
A0005938cellular_componentcell cortex
A0006886biological_processintracellular protein transport
A0006897biological_processendocytosis
A0007015biological_processactin filament organization
A0007266biological_processRho protein signal transduction
A0007605biological_processsensory perception of sound
A0008104biological_processintracellular protein localization
A0015031biological_processprotein transport
A0015629cellular_componentactin cytoskeleton
A0016020cellular_componentmembrane
A0016459cellular_componentmyosin complex
A0016461cellular_componentunconventional myosin complex
A0030048biological_processactin filament-based movement
A0030136cellular_componentclathrin-coated vesicle
A0030139cellular_componentendocytic vesicle
A0030175cellular_componentfilopodium
A0030330biological_processDNA damage response, signal transduction by p53 class mediator
A0030665cellular_componentclathrin-coated vesicle membrane
A0031106biological_processseptin ring organization
A0031410cellular_componentcytoplasmic vesicle
A0031941cellular_componentfilamentous actin
A0031965cellular_componentnuclear membrane
A0032587cellular_componentruffle membrane
A0042472biological_processinner ear morphogenesis
A0042491biological_processinner ear auditory receptor cell differentiation
A0043531molecular_functionADP binding
A0045334cellular_componentclathrin-coated endocytic vesicle
A0048471cellular_componentperinuclear region of cytoplasm
A0051015molecular_functionactin filament binding
A0051046biological_processregulation of secretion
A0060001molecular_functionminus-end directed microfilament motor activity
A0070062cellular_componentextracellular exosome
B0000086biological_processG2/M transition of mitotic cell cycle
B0000785cellular_componentchromatin
B0000922cellular_componentspindle pole
B0001975biological_processresponse to amphetamine
B0002027biological_processregulation of heart rate
B0005246molecular_functioncalcium channel regulator activity
B0005509molecular_functioncalcium ion binding
B0005513biological_processdetection of calcium ion
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005819cellular_componentspindle
B0005829cellular_componentcytosol
B0005876cellular_componentspindle microtubule
B0006897biological_processendocytosis
B0007259biological_processcell surface receptor signaling pathway via JAK-STAT
B0008076cellular_componentvoltage-gated potassium channel complex
B0008179molecular_functionadenylate cyclase binding
B0010856molecular_functionadenylate cyclase activator activity
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
B0016240biological_processautophagosome membrane docking
B0019855molecular_functioncalcium channel inhibitor activity
B0019901molecular_functionprotein kinase binding
B0019904molecular_functionprotein domain specific binding
B0030017cellular_componentsarcomere
B0030235molecular_functionnitric-oxide synthase regulator activity
B0030426cellular_componentgrowth cone
B0030672cellular_componentsynaptic vesicle membrane
B0031432molecular_functiontitin binding
B0031514cellular_componentmotile cilium
B0031800molecular_functiontype 3 metabotropic glutamate receptor binding
B0031966cellular_componentmitochondrial membrane
B0032465biological_processregulation of cytokinesis
B0032991cellular_componentprotein-containing complex
B0034704cellular_componentcalcium channel complex
B0035458biological_processcellular response to interferon-beta
B0043209cellular_componentmyelin sheath
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0043548molecular_functionphosphatidylinositol 3-kinase binding
B0044305cellular_componentcalyx of Held
B0044325molecular_functiontransmembrane transporter binding
B0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0050998molecular_functionnitric-oxide synthase binding
B0051412biological_processresponse to corticosterone
B0051592biological_processresponse to calcium ion
B0051649biological_processestablishment of localization in cell
B0055117biological_processregulation of cardiac muscle contraction
B0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
B0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
B0071346biological_processcellular response to type II interferon
B0072542molecular_functionprotein phosphatase activator activity
B0090150biological_processestablishment of protein localization to membrane
B0090151biological_processestablishment of protein localization to mitochondrial membrane
B0097225cellular_componentsperm midpiece
B0097720biological_processcalcineurin-mediated signaling
B0098685cellular_componentSchaffer collateral - CA1 synapse
B0098901biological_processregulation of cardiac muscle cell action potential
B0099523cellular_componentpresynaptic cytosol
B0099524cellular_componentpostsynaptic cytosol
B0140056biological_processorganelle localization by membrane tethering
B0140238biological_processpresynaptic endocytosis
B0150034cellular_componentdistal axon
B1900242biological_processregulation of synaptic vesicle endocytosis
B1901842biological_processnegative regulation of high voltage-gated calcium channel activity
B1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
B1902494cellular_componentcatalytic complex
B1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
B2000300biological_processregulation of synaptic vesicle exocytosis
I0000086biological_processG2/M transition of mitotic cell cycle
I0000785cellular_componentchromatin
I0000922cellular_componentspindle pole
I0001975biological_processresponse to amphetamine
I0002027biological_processregulation of heart rate
I0005246molecular_functioncalcium channel regulator activity
I0005509molecular_functioncalcium ion binding
I0005513biological_processdetection of calcium ion
I0005515molecular_functionprotein binding
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005737cellular_componentcytoplasm
I0005813cellular_componentcentrosome
I0005819cellular_componentspindle
I0005829cellular_componentcytosol
I0005876cellular_componentspindle microtubule
I0006897biological_processendocytosis
I0007259biological_processcell surface receptor signaling pathway via JAK-STAT
I0008076cellular_componentvoltage-gated potassium channel complex
I0008179molecular_functionadenylate cyclase binding
I0010856molecular_functionadenylate cyclase activator activity
I0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
I0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
I0016240biological_processautophagosome membrane docking
I0019855molecular_functioncalcium channel inhibitor activity
I0019901molecular_functionprotein kinase binding
I0019904molecular_functionprotein domain specific binding
I0030017cellular_componentsarcomere
I0030235molecular_functionnitric-oxide synthase regulator activity
I0030426cellular_componentgrowth cone
I0030672cellular_componentsynaptic vesicle membrane
I0031432molecular_functiontitin binding
I0031514cellular_componentmotile cilium
I0031800molecular_functiontype 3 metabotropic glutamate receptor binding
I0031966cellular_componentmitochondrial membrane
I0032465biological_processregulation of cytokinesis
I0032991cellular_componentprotein-containing complex
I0034704cellular_componentcalcium channel complex
I0035458biological_processcellular response to interferon-beta
I0043209cellular_componentmyelin sheath
I0043539molecular_functionprotein serine/threonine kinase activator activity
I0043548molecular_functionphosphatidylinositol 3-kinase binding
I0044305cellular_componentcalyx of Held
I0044325molecular_functiontransmembrane transporter binding
I0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
I0046872molecular_functionmetal ion binding
I0048306molecular_functioncalcium-dependent protein binding
I0050998molecular_functionnitric-oxide synthase binding
I0051412biological_processresponse to corticosterone
I0051592biological_processresponse to calcium ion
I0051649biological_processestablishment of localization in cell
I0055117biological_processregulation of cardiac muscle contraction
I0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
I0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
I0071346biological_processcellular response to type II interferon
I0072542molecular_functionprotein phosphatase activator activity
I0090150biological_processestablishment of protein localization to membrane
I0090151biological_processestablishment of protein localization to mitochondrial membrane
I0097225cellular_componentsperm midpiece
I0097720biological_processcalcineurin-mediated signaling
I0098685cellular_componentSchaffer collateral - CA1 synapse
I0098901biological_processregulation of cardiac muscle cell action potential
I0099523cellular_componentpresynaptic cytosol
I0099524cellular_componentpostsynaptic cytosol
I0140056biological_processorganelle localization by membrane tethering
I0140238biological_processpresynaptic endocytosis
I0150034cellular_componentdistal axon
I1900242biological_processregulation of synaptic vesicle endocytosis
I1901842biological_processnegative regulation of high voltage-gated calcium channel activity
I1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
I1902494cellular_componentcatalytic complex
I1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
I2000300biological_processregulation of synaptic vesicle exocytosis
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
BASP21-LEU33
BASP57-PHE69
BASP94-LEU106
BASP130-PHE142
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues70
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues70
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues70
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"4HEX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ZLK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18034455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues20
DetailsDomain: {"description":"IQ","evidences":[{"source":"UniProtKB","id":"Q29122","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues44
DetailsRegion: {"description":"Responsible for slow ATPase activity","evidences":[{"source":"UniProtKB","id":"Q29122","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues7
DetailsRegion: {"description":"Actin-binding","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues28
DetailsRegion: {"description":"Required for binding calmodulin","evidences":[{"source":"UniProtKB","id":"Q29122","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues81
DetailsRegion: {"description":"Three-helix bundle","evidences":[{"source":"UniProtKB","id":"Q29122","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues67
DetailsRegion: {"description":"SAH","evidences":[{"source":"PubMed","id":"18511944","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues21
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsRegion: {"description":"Interaction with OPTN","evidences":[{"source":"UniProtKB","id":"Q9I8D1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q64331","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

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