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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9UG2

Severed and capped actin fragment by two G1G3 domains of gelsolin

Functional Information from GO Data
ChainGOidnamespacecontents
C0000287molecular_functionmagnesium ion binding
C0001725cellular_componentstress fiber
C0003785molecular_functionactin monomer binding
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005523molecular_functiontropomyosin binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005865cellular_componentstriated muscle thin filament
C0005884cellular_componentactin filament
C0010628biological_processpositive regulation of gene expression
C0016887molecular_functionATP hydrolysis activity
C0019904molecular_functionprotein domain specific binding
C0030027cellular_componentlamellipodium
C0030041biological_processactin filament polymerization
C0030175cellular_componentfilopodium
C0030240biological_processskeletal muscle thin filament assembly
C0031013molecular_functiontroponin I binding
C0031432molecular_functiontitin binding
C0031941cellular_componentfilamentous actin
C0032036molecular_functionmyosin heavy chain binding
C0032432cellular_componentactin filament bundle
C0042802molecular_functionidentical protein binding
C0044297cellular_componentcell body
C0048306molecular_functioncalcium-dependent protein binding
C0048741biological_processskeletal muscle fiber development
C0051017biological_processactin filament bundle assembly
C0090131biological_processmesenchyme migration
C0098723cellular_componentskeletal muscle myofibril
C0140660molecular_functioncytoskeletal motor activator activity
D0000287molecular_functionmagnesium ion binding
D0001725cellular_componentstress fiber
D0003785molecular_functionactin monomer binding
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005523molecular_functiontropomyosin binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005865cellular_componentstriated muscle thin filament
D0005884cellular_componentactin filament
D0010628biological_processpositive regulation of gene expression
D0016887molecular_functionATP hydrolysis activity
D0019904molecular_functionprotein domain specific binding
D0030027cellular_componentlamellipodium
D0030041biological_processactin filament polymerization
D0030175cellular_componentfilopodium
D0030240biological_processskeletal muscle thin filament assembly
D0031013molecular_functiontroponin I binding
D0031432molecular_functiontitin binding
D0031941cellular_componentfilamentous actin
D0032036molecular_functionmyosin heavy chain binding
D0032432cellular_componentactin filament bundle
D0042802molecular_functionidentical protein binding
D0044297cellular_componentcell body
D0048306molecular_functioncalcium-dependent protein binding
D0048741biological_processskeletal muscle fiber development
D0051017biological_processactin filament bundle assembly
D0090131biological_processmesenchyme migration
D0098723cellular_componentskeletal muscle myofibril
D0140660molecular_functioncytoskeletal motor activator activity
E0000287molecular_functionmagnesium ion binding
E0001725cellular_componentstress fiber
E0003785molecular_functionactin monomer binding
E0005509molecular_functioncalcium ion binding
E0005515molecular_functionprotein binding
E0005523molecular_functiontropomyosin binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005865cellular_componentstriated muscle thin filament
E0005884cellular_componentactin filament
E0010628biological_processpositive regulation of gene expression
E0016887molecular_functionATP hydrolysis activity
E0019904molecular_functionprotein domain specific binding
E0030027cellular_componentlamellipodium
E0030041biological_processactin filament polymerization
E0030175cellular_componentfilopodium
E0030240biological_processskeletal muscle thin filament assembly
E0031013molecular_functiontroponin I binding
E0031432molecular_functiontitin binding
E0031941cellular_componentfilamentous actin
E0032036molecular_functionmyosin heavy chain binding
E0032432cellular_componentactin filament bundle
E0042802molecular_functionidentical protein binding
E0044297cellular_componentcell body
E0048306molecular_functioncalcium-dependent protein binding
E0048741biological_processskeletal muscle fiber development
E0051017biological_processactin filament bundle assembly
E0090131biological_processmesenchyme migration
E0098723cellular_componentskeletal muscle myofibril
E0140660molecular_functioncytoskeletal motor activator activity
F0000287molecular_functionmagnesium ion binding
F0001725cellular_componentstress fiber
F0003785molecular_functionactin monomer binding
F0005509molecular_functioncalcium ion binding
F0005515molecular_functionprotein binding
F0005523molecular_functiontropomyosin binding
F0005737cellular_componentcytoplasm
F0005856cellular_componentcytoskeleton
F0005865cellular_componentstriated muscle thin filament
F0005884cellular_componentactin filament
F0010628biological_processpositive regulation of gene expression
F0016887molecular_functionATP hydrolysis activity
F0019904molecular_functionprotein domain specific binding
F0030027cellular_componentlamellipodium
F0030041biological_processactin filament polymerization
F0030175cellular_componentfilopodium
F0030240biological_processskeletal muscle thin filament assembly
F0031013molecular_functiontroponin I binding
F0031432molecular_functiontitin binding
F0031941cellular_componentfilamentous actin
F0032036molecular_functionmyosin heavy chain binding
F0032432cellular_componentactin filament bundle
F0042802molecular_functionidentical protein binding
F0044297cellular_componentcell body
F0048306molecular_functioncalcium-dependent protein binding
F0048741biological_processskeletal muscle fiber development
F0051017biological_processactin filament bundle assembly
F0090131biological_processmesenchyme migration
F0098723cellular_componentskeletal muscle myofibril
F0140660molecular_functioncytoskeletal motor activator activity
Functional Information from PROSITE/UniProt
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
CTYR53-GLY63
site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
CTRP356-GLU364
site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
CLEU104-ARG116
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues164
DetailsRepeat: {"description":"Gelsolin-like 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues144
DetailsRepeat: {"description":"Gelsolin-like 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues144
DetailsRepeat: {"description":"Gelsolin-like 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsRegion: {"description":"Actin-actin interfilament contact point"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues38
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues30
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19666512","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FFK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues30
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by SRC; in vitro","evidences":[{"source":"PubMed","id":"10210201","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues64
DetailsRegion: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

254587

PDB entries from 2026-06-03

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